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        <title>Biochimica et Biophysica Acta via MedWorm.com</title>
        <description>MedWorm.com provides a medical RSS filtering service. Over 6000 RSS medical sources are combined and output via different filters. This feed contains the latest items from the 'Biochimica et Biophysica Acta' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Biochimica+et+Biophysica+Acta&t=Biochimica+et+Biophysica+Acta&s=Search&f=source]]></link>
        <lastBuildDate>Sun, 21 Mar 2010 16:57:38 +0100</lastBuildDate>
        <item>
            <title>A surface view on membrane structure, dynamics and applications.</title>
            <link>http://www.medworm.com/index.php?rid=3347079&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20206732%26dopt%3DAbstract</link>
            <description>Authors: P&amp;#xE9;rez-Gil J
    
    PMID: 20206732 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3347079</comments>
            <pubDate>Tue, 09 Mar 2010 22:50:06 +0100</pubDate>
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        <item>
            <title>The alternative complex iii of Rhodothermus marinus and its structural and functional association with caa(3) oxygen reductase.</title>
            <link>http://www.medworm.com/index.php?rid=3347082&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20206595%26dopt%3DAbstract</link>
            <description>Authors: Refojo PN, Teixeira M, Pereira MM
    An alternative complex III (ACIII) is a respiratory complex with quinol: electron acceptor oxidoreductase activity. It is the only example of an enzyme performing complex III function that does not belong to bc(1) complex family. ACIII from Rhodothermus (R.) marinus was the first enzyme of this type to be isolated and characterized, and in this work we deepen its characterization. We addressed its interaction with quinol substrate and with the caa(3) oxygen reductase, whose coding gene cluster follows that of the ACIII. There is at least, one quinone binding site present in R. marinus ACIII as observed by fluorescence quenching titration of HQNO, a quinone analogue inhibitor. Furthermore, electrophoretic and spectroscopic evidence, taken toget...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3347082</comments>
            <pubDate>Wed, 03 Mar 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Modulation of intracellular chloride channels by ATP and Mg(2+).</title>
            <link>http://www.medworm.com/index.php?rid=3347081&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20206596%26dopt%3DAbstract</link>
            <description>We report the effects of ATP and Mg(2+) on the activity of intracellular chloride channels. Mitochondrial and lysosomal membrane vesicles isolated from rat hearts were incorporated into bilayer lipid membranes, and single chloride channel currents were measured. The observed chloride channels (n=112) possessed wide variation in single channel parameters and sensitivities to ATP. ATP (0.5-2mmol/l) modulated and/or inhibited the chloride channel activities (n=38/112) in a concentration-dependent manner. The inhibition effect was irreversible (n=5/93) or reversible (n=15/93). The non-hydrolysable ATP analogue AMP-PNP had a similar inhibition effect as ATP, indicating that phosphorylation did not play a role in the ATP inhibition effect. ATP modulated the gating properties of the channels (n=6...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3347081</comments>
            <pubDate>Wed, 03 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3347081</guid>        </item>
        <item>
            <title>Differences in RNA processing underlie the tissue specific phenotype of ISCU myopathy.</title>
            <link>http://www.medworm.com/index.php?rid=3347080&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20206689%26dopt%3DAbstract</link>
            <description>Authors: Sanaker PS, Toompuu M, Hogan VE, He L, Tzoulis C, Chrzanowska-Lightowlers ZM, Taylor RW, Bindoff LA
    Hereditary myopathy with lactic acidosis, or Myopathy with exercise intolerance, Swedish type (OMIM #255125) is caused by mutations in the iron-sulfur cluster scaffold (ISCU) gene. The g.7044G&amp;gt;C ISCU mutation induces a splicing error in the pre-mRNA that strengthens a weak intronic splice site leading to inclusion of a new exon and subsequent loss of mRNA and protein. While ISCU is widely expressed, homozygosity for this particular intronic mutation gives rise to a pure myopathy. In order to investigate tissue specificity and disease mechanism, we studied muscle, myoblasts, fibroblasts and blood cells from the first non-Swedish case of this disease. Consistent with the recogn...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3347080</comments>
            <pubDate>Wed, 03 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3347080</guid>        </item>
        <item>
            <title>Substitution of Chloride by Bromide Modifies the Low-Temperature Tyrosine Z Oxidation in Active Photosystem II.</title>
            <link>http://www.medworm.com/index.php?rid=3347086&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20206122%26dopt%3DAbstract</link>
            <description>Authors: Ren Y, Zhang C, Zhao J
    Chloride is an essential cofactor for photosynthetic water oxidation. However, its location and functional roles in active photosystem II are still a matter of debate. We have investigated this issue by studying the effects of Cl(-) replacement by Br(-) in active PSII. In Br(-) substituted samples, Cl(-) is effectively replaced by Br(-) in the presence of 1.2 M NaBr under room light with protection of anaerobic atmosphere followed by dialysis. Following results have been obtained. i) The oxygen evolving activities of the Br(-) -PSII samples are significantly lower than that of the Cl(-) -PSII samples; ii) The same S(2) multiline EPR signals are observed in both Br(-) and Cl(-) -PSII samples; iii) The amplitudes of the visible light induced S(1)Tyr(Z)() a...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3347086</comments>
            <pubDate>Tue, 02 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3347086</guid>        </item>
        <item>
            <title>Oscillations in energy metabolism.</title>
            <link>http://www.medworm.com/index.php?rid=3347085&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20206123%26dopt%3DAbstract</link>
            <description>Authors: Iotti S, Borsari M, Bendahan D
    Organisation of mitochondrial metabolism is a quintessential example of a complex dissipative system which can display dynamic instabilities. Several findings have indicated that the conditions inducing instabilities are within the physiological range and that mild perturbations could elicit oscillations. Different mathematical models have been put forth in order to explain the genesis of oscillations in energy metabolism. One model considers mitochondria as an organised network of oscillators and indicates that communication between mitochondria involves mitochondrial reactive oxygen species (ROS) production acting as synchronisers of the energy status of the whole population of mitochondria. An alternative model proposes that extra-mitochondria...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3347085</comments>
            <pubDate>Tue, 02 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3347085</guid>        </item>
        <item>
            <title>Absence of uncoupling protein-3 leads to greater activation of an adenine nucleotide translocase-mediated proton conductance in skeletal muscle mitochondria from calorie restricted mice.</title>
            <link>http://www.medworm.com/index.php?rid=3347084&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20206124%26dopt%3DAbstract</link>
            <description>Authors: Bevilacqua L, Seifert EL, Estey C, Gerrits MF, Harper ME
    Calorie restriction (CR), without malnutrition, consistently increases lifespan in all species tested, and reduces age-associated pathologies in mammals. Alterations in mitochondrial content and function are thought to underlie some of the effects of CR. Previously, we reported that rats subjected to variable durations of 40% CR demonstrated a rapid and sustained decrease in maximal leak-dependent respiration in skeletal muscle mitochondria. This was accompanied by decreased mitochondrial reactive oxygen species generation and increased uncoupling protein-3 protein (UCP3) expression. The aim of the present study was to determine the contribution of UCP3, as well as the adenine nucleotide translocas to these functional ch...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3347084</comments>
            <pubDate>Tue, 02 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3347084</guid>        </item>
        <item>
            <title>Quinolinate phosphoribosyl transferase, a key enzyme in de novo NAD(+) synthesis, suppresses spontaneous cell death by inhibiting overproduction of active-caspase-3.</title>
            <link>http://www.medworm.com/index.php?rid=3347083&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20206212%26dopt%3DAbstract</link>
            <description>This study was designed to elucidate the functions of QPRT protein in addition to NAD(+) synthesis. QPRT was identified as a caspase-3 binding protein using double layer fluorescent zymography, but was not a substrate for caspase-3. Surface plasmon resonance analysis using recombinant proteins showed interaction of QPRT with active-caspase-3 in a dose dependent manner at 55 nM of the dissociation constant. The interaction was also confirmed by immunoprecipitation analysis of actinomycin D-treated QPRT-FLAG expressing cells using anti-FLAG-agarose. QPRT-depleted cells showed increased sensitivity to spontaneous cell death, upregulated caspase-3 activity and strong active-caspase-3 signals. Considered together, the results suggested that QPRT protein acts as an inhibitor of spontaneous cell ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3347083</comments>
            <pubDate>Tue, 02 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3347083</guid>        </item>
        <item>
            <title>Modulation of transcription factor function by O-GlcNAc modification.</title>
            <link>http://www.medworm.com/index.php?rid=3347087&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20202486%26dopt%3DAbstract</link>
            <description>Authors: Ozcan S, Andrali SS, Cantrell JE
    O-linked beta-N-acetylglucosamine (O-GlcNAc) modification of nuclear and cytoplasmic proteins is important for many cellular processes, and the number of proteins that contain this modification is steadily increasing. This modification is dynamic and reversible, and in some cases competes for phosphorylation of the same residues. O-GlcNAc modification of proteins is regulated by cell cycle, nutrient metabolism, and other extracellular signals. Compared to protein phosphorylation, which is mediated by a large number of kinases, O-GlcNAc modification is catalyzed only by one enzyme called O-linked N-acetylglucosaminyl transferase or OGT. Removal of O-GlcNAc from proteins is catalyzed by the enzyme beta-N-acetylglucosaminidase (O-GlcNAcase or OGA)...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3347087</comments>
            <pubDate>Mon, 01 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3347087</guid>        </item>
        <item>
            <title>Mitochondrial research and medicine.</title>
            <link>http://www.medworm.com/index.php?rid=3302905&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20171500%26dopt%3DAbstract</link>
            <description>Authors: Wei YH
    
    PMID: 20171500 [PubMed - in process] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3302905</comments>
            <pubDate>Wed, 24 Feb 2010 20:20:06 +0100</pubDate>
            <guid isPermaLink="false">3302905</guid>        </item>
        <item>
            <title>Inhibitors of the Abl kinase directed at either the ATP- or myristate-binding site.</title>
            <link>http://www.medworm.com/index.php?rid=3276665&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20152788%26dopt%3DAbstract</link>
            <description>Authors: Fabbro D, Manley PW, Jahnke W, Liebetanz J, Szyttenholm A, Fendrich G, Strauss A, Zhang J, Gray NS, Adrian F, Warmuth M, Pelle X, Grotzfeld R, Berst F, Marzinzik A, Cowan-Jacob SW, Furet P, Mestan J
    The ATP-competitive inhibitors dasatinib and nilotinib, which bind to catalytically different conformations of the Abl kinase domain, have recently been approved for the treatment of imatinib-resistant CML. These two new drugs, albeit very efficient against most of the imatinib-resistant mutants of Bcr-Abl, fail to effectively suppress the Bcr-Abl activity of the T315I (or gatekeeper) mutation. Generating new ATP site-binding drugs that target the T315I in Abl has been hampered, amongst others, by target selectivity, which is frequently an issue when developing ATP-competitive inhi...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276665</comments>
            <pubDate>Wed, 17 Feb 2010 08:27:37 +0100</pubDate>
            <guid isPermaLink="false">3276665</guid>        </item>
        <item>
            <title>Cholesterol and peroxidized cardiolipin in mitochondrial membrane properties, permeabilization and cell death.</title>
            <link>http://www.medworm.com/index.php?rid=3276647&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153716%26dopt%3DAbstract</link>
            <description>Authors: Montero J, Mari M, Colell A, Morales A, Basa&amp;#xF1;ez G, Garcia-Ruiz C, Fern&amp;#xE1;ndez-Checa JC
    Mitochondria are known to actively regulate cell death with the final phenotype of demise being determined by the metabolic and energetic status of the cell. Mitochondrial membrane permeabilization (MMP) is a critical event in cell death, as it regulates the degree of mitochondrial dysfunction and the release of intermembrane proteins that function in the activation and assembly of caspases. In addition to the crucial role of proapoptotic members of the Bcl-2 family, the lipid composition of the mitochondrial membranes is increasingly recognized to modulate MMP and hence cell death. The unphysiological accumulation of cholesterol in mitochondrial membranes regulates their physical pr...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276647</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276647</guid>        </item>
        <item>
            <title>Hypoxia and mitochondrial oxidative metabolism.</title>
            <link>http://www.medworm.com/index.php?rid=3276646&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153717%26dopt%3DAbstract</link>
            <description>Authors: Solaini G, Baracca A, Lenaz G, Sgarbi G
    It is now clear that mitochondrial defects are associated with a large variety of clinical phenotypes. This is the result of the mitochondria's central role in energy production, reactive oxygen species homeostasis, and cell death. These processes are interdependent and may occur under various stressing conditions, among which low oxygen levels (hypoxia) is certainly prominent. Cells exposed to hypoxia respond acutely with endogenous metabolites and proteins promptly regulating metabolic pathways, but if low oxygen levels are prolonged, cells activate adapting mechanisms, the master switch being the hypoxia-inducible factor 1 (HIF-1). Activation of this factor is strictly bound to the mitochondrial function, which in turn is related with...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276646</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276646</guid>        </item>
        <item>
            <title>Pore-forming properties of the Bacillus thuringiensis toxin Cry9Ca in Manduca sexta brush border membrane vesicles.</title>
            <link>http://www.medworm.com/index.php?rid=3276645&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153718%26dopt%3DAbstract</link>
            <description>Authors: Brunet JF, Vachon V, Juteau M, Van Rie J, Larouche G, Vincent C, Schwartz JL, Laprade R
    The toxicity and pore-forming ability of the Bacillus thuringiensis Cry9Ca insecticidal toxin, its single-site mutants, R164A and R164K, and the 55-kDa fragment resulting from its proteolytic cleavage at residue 164 were investigated using Manduca sexta neonate larvae and fifth-instar larval midgut brush border membrane vesicles, respectively. Neither the mutations nor the proteolytic cleavage altered Cry9Ca toxicity. Compared with Cry1Ac, Cry9Ca and its mutants formed large poorly selective pores in the vesicles. Pore formation was highly dependent on pH, however, especially for wild-type Cry9Ca and both mutants. Increasing pH from 6.5 to 10.5 resulted in an irregular step-wise decrease in...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276645</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276645</guid>        </item>
        <item>
            <title>Erythrocyte Death in vitro Induced by Starvation in the Absence of Ca(2+).</title>
            <link>http://www.medworm.com/index.php?rid=3276644&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153719%26dopt%3DAbstract</link>
            <description>Authors: Pompeo G, Girasole M, Cricenti A, Boumis G, Bellelli A, Amiconi S
    Human erythrocytes (RBCs), stored at 4 degrees C under nominal absence of external energy sources and calcium ions, show a gradual decrease in membrane roughness (R(rms)) at the end of which the appearance of morphological phenomena (spicules, vesicles and spherocytes) is observed on the cell membrane, phenomena that can mainly be ascribed to the ATP-dependent disconnection of the cortical cytoskeleton from the lipid bilayer. After depletion of the intracellular energy sources obtained under the extreme conditions chosen, treatment with a minimal rejuvenation solution makes it possible the following remarks : (i) RBCs are able to regenerate adenosine triphosphate (ATP) and 2,3-bisphosphoglycerate only up to 4 da...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276644</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276644</guid>        </item>
        <item>
            <title>Influence of the nature of the sterol on the behavior of palmitic acid/sterol mixtures and their derived liposomes.</title>
            <link>http://www.medworm.com/index.php?rid=3276643&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153720%26dopt%3DAbstract</link>
            <description>Authors: Cui ZK, Bastiat G, Jin C, Keyvanloo A, Lafleur M
    The phase behavior of mixtures formed with palmitic acid (PA) and one of the following sterols (dihydrocholesterol, ergosterol, 7-dehydrocholesterol, stigmasterol and stigmastanol), in a PA/sterol molar ratio of 3/7, has been characterized by IR and (2)H NMR spectroscopy at different pH. Our study shows that it is possible to form liquid-ordered (lo) lamellar phases with these binary non-phospholipid mixtures. The characterization of alkyl chain dynamics of PA in these systems revealed the large ordering effect of the sterols. It was possible to extrude these systems, using standard extrusion techniques, to form large unilamellar vesicles (LUVs), except in the case of ergosterol-containing mixture. The resulting LUVs displayed a...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276643</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276643</guid>        </item>
        <item>
            <title>A conserved function for Inp2 in peroxisome inheritance.</title>
            <link>http://www.medworm.com/index.php?rid=3276642&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153784%26dopt%3DAbstract</link>
            <description>Authors: Saraya R, Cepi&amp;#x144;ska MN, Kiel JA, Veenhuis M, van der Klei IJ
    In budding yeast Saccharomyces cerevisiae, the peroxisomal protein Inp2 is required for inheritance of peroxisomes to the bud, by connecting the organelles to the motor protein Myo2 and the actin cytoskeleton. Recent data suggested that the function of Inp2 may not be conserved in other yeast species. Using in silico analyses we have identified a weakly conserved Inp2-related protein in 18 species of budding yeast and analysed the role of the identified protein in the methylotrophic yeast Hansenula polymorpha in peroxisome inheritance. Our data show that H. polymorpha Inp2 locates to peroxisomes, interacts with Myo2, and is essential for peroxisome inheritance.
    PMID: 20153784 [PubMed - as supplied by publish...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276642</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276642</guid>        </item>
        <item>
            <title>Muscle transfection and permeabilization induced by electrotransfer or pluronic((R)) L64. Paired study by optical imaging and MRI.</title>
            <link>http://www.medworm.com/index.php?rid=3276641&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153812%26dopt%3DAbstract</link>
            <description>Conclusion and general significance It is possible to use successively on the same animals MRI and optical imaging for paired studies of muscle transfection and permeabilization. Permeabilization is possibly not related to gene transfer but it indicates membrane modification related to transfection by the electrotransfer or coinjection of DNA with the L64.
    PMID: 20153812 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276641</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276641</guid>        </item>
        <item>
            <title>Functional analysis of H. sapiens DNA polymerase gamma spacer mutation W748S with and without common variant E1143G.</title>
            <link>http://www.medworm.com/index.php?rid=3276640&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153822%26dopt%3DAbstract</link>
            <description>Authors: Palin EJ, Lesonen A, Farr CL, Euro L, Suomalainen A, Kaguni LS
    Mitochondrial DNA polymerase, POLG, is the sole DNA polymerase found in animal mitochondria. In humans, POLGalpha W748S in cis with an E1143G mutation has been linked to a new type of recessive ataxia, MIRAS, which is the most common inherited ataxia in Finland. We investigated the biochemical phenotypes of the W748S amino acid change, using recombinant human POLG. We measured processive and non-processive DNA polymerase activity, DNA binding affinity, enzyme processivity, and subunit interaction with recombinant POLGbeta. In addition, we studied the effects of the W748S and E1143G mutations in primary human cell cultures using retroviral transduction. Here, we examined cell viability, mitochondrial DNA copy number...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276640</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276640</guid>        </item>
        <item>
            <title>ISG15 and Immune Diseases.</title>
            <link>http://www.medworm.com/index.php?rid=3276639&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153823%26dopt%3DAbstract</link>
            <description>Authors: Jeon YJ, Yoo HM, Chung CH
    ISG15, the product of interferon (IFN)-stimulated gene 15, is the first identified ubiquitin-like protein, consisting of two ubiquitin-like domains. ISG15 is synthesized as a precursor in certain mammals, and therefore needs to be processed to expose the C-terminal glycine residue prior to conjugation to target proteins. A set of three-step cascade enzymes, an E1 enzyme (UBE1L), an E2 enzyme (UbcH8), and one of several E3 ligases (e.g., EFP and HERC5), catalyzes ISG15 conjugation (ISGylation) of a specific protein. These enzymes are unique among the cascade enzymes for ubiquitin and other ubiquitin-like proteins in that all of them are induced by type-I IFNs or other stimuli, such as exposure to viruses and lipopolysaccharide. Mass spectrometric analy...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276639</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276639</guid>        </item>
        <item>
            <title>Dopamine and G protein-coupled receptor kinase 4 in the kidney: Role in blood pressure regulation.</title>
            <link>http://www.medworm.com/index.php?rid=3276638&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153824%26dopt%3DAbstract</link>
            <description>Authors: Jose PA, Soares-da-Silva P, Eisner GM, Felder RA
    Complex interactions between genes and environment result in a sodium-induced elevation in blood pressure (salt sensitivity) and/or hypertension that lead to significant morbidity and mortality affecting up to 25% of the middle-aged adult population worldwide. Determining the etiology of genetic and/or environmentally-induced high blood pressure has been difficult because of the many interacting systems involved. Two main pathways have been implicated as principal determinants of blood pressure since they are located in the kidney (the key organ responsible for blood pressure regulation), and have profound effects on sodium balance: the dopaminergic and renin-angiotensin systems. These systems counteract or modulate each other, ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276638</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276638</guid>        </item>
        <item>
            <title>Mitochondrial bioenergetics and dynamics interplay in complex i-deficient fibroblasts.</title>
            <link>http://www.medworm.com/index.php?rid=3276637&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153825%26dopt%3DAbstract</link>
            <description>CONCLUSION: Our main finding was that severe CI-deficiency in patients harbouring mutations in the NDUFA1 and NDUFV1 genes is linked to a delayed mitochondrial network recovery after cccp treatment. However, the CI deficiency is neither associated with massive mitochondrial fragmentation nor with increased ROS levels. The different genetic backgrounds of patients with OXPHOS disorders would explain, at least partially, differences in the pathophysiological manifestations of CI deficiency.
    PMID: 20153825 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276637</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276637</guid>        </item>
        <item>
            <title>Limited cholesterol depletion causes aggregation of plasma membrane lipid rafts inducing T cell activation.</title>
            <link>http://www.medworm.com/index.php?rid=3276636&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153839%26dopt%3DAbstract</link>
            <description>Authors: Mahammad S, Dinic J, Adler J, Parmryd I
    Acute cholesterol depletion is generally associated with decreased or abolished T cell signalling but it can also cause T cell activation. This anomaly has been addressed in Jurkat T cells using progressive cholesterol depletion with methyl-beta-cyclodextrin (MBCD). At depletion levels higher than 50% there is substantial cell death, which explains reports of signalling inhibition. At 10-20% depletion levels, tyrosine phosphorylation is increased, ERK is activated and there is a small increase in cytoplasmic Ca(2+). Peripheral actin polymerisation is also triggered by limited cholesterol depletion. Strikingly, the lipid raft marker GM1 aggregates upon cholesterol depletion and these aggregated domains concentrate the signalling proteins ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276636</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276636</guid>        </item>
        <item>
            <title>Apolipoprotein A-V associates with intrahepatic lipid droplets and influences triglyceride accumulation.</title>
            <link>http://www.medworm.com/index.php?rid=3276635&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153840%26dopt%3DAbstract</link>
            <description>Authors: Shu X, Nelbach L, Ryan RO, Forte TM
    Apolipoprotein A-V (apoA-V), secreted solely by the liver, is a low abundance protein that strongly influences plasma triglyceride (TG) levels. In vitro, in transfected hepatoma cell lines apoA-V is largely retained within the cell in association with cytosolic lipid droplets (LD). To evaluate if this is true in vivo, in the present study the amount of apoA-V in the plasma compartment versus liver tissue was determined in APOA5 transgenic (Tg) mice. The majority of total apoA-V ( approximately 80%) was in the plasma compartment. Injection of APOA5 Tg mice with heparin increased plasma apoA-V protein levels by approximately 25% indicating the existence of a heparin-releasable pool. Intrahepatic apoA-V was associated with LD isolated from live...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276635</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276635</guid>        </item>
        <item>
            <title>Cell biology meets biophysics to unveil the different mechanisms of penetratin internalization in cells.</title>
            <link>http://www.medworm.com/index.php?rid=3276664&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20152795%26dopt%3DAbstract</link>
            <description>Authors: Alves ID, Jiao CY, Aubry S, Aussedat B, Burlina F, Chassaing G, Sagan S
    Although cell-penetrating peptides are widely used as molecular devices to cross membranes and transport molecules or nanoparticles inside cells, the underlying internalization mechanism for such behavior is still studied and discussed. One of the reasons for such debate is the wide panel of chemically different cell-penetrating peptides or cargo that is used. Indeed the intrinsic physico-chemical properties of CPP and conjugates strongly affect the cell membrane recognition and therefore the internalization pathways. Altogether, the mechanisms described so far should be shared between two general pathways: endocytosis and direct translocation. As it is established now that one cell-penetrating peptide can...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276664</comments>
            <pubDate>Wed, 10 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276664</guid>        </item>
        <item>
            <title>Stearoyl-CoA desaturase and insulin signaling - what is the molecular switch?</title>
            <link>http://www.medworm.com/index.php?rid=3276657&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153289%26dopt%3DAbstract</link>
            <description>Authors: Dobrzyn P, Jazurek M, Dobrzyn A
    Increasing evidence suggests that stearoyl-CoA desaturase (SCD), the rate limiting enzyme of monounsaturated fatty acid biosynthesis, is an important factor in the pathogenesis of lipid-induced insulin resistance. Mice with a targeted disruption of the SCD1 gene have improved glucose tolerance compared to wild-type mice, despite lower fasting plasma insulin levels. Increased SCD activity has been found in insulin resistant humans and animals, whereas SCD1 deficiency attenuates both diet- and genetically- induced impairment of insulin action. Phosphorylation of serine and threonine residues on insulin receptor, insulin receptor substrates (IRS1 and IRS2), and on Akt has been shown to be the major step in insulin signaling that is altered due to t...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276657</comments>
            <pubDate>Wed, 10 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276657</guid>        </item>
        <item>
            <title>Role of Calcineurin, hnRNPA2 and Akt in mitochondrial respiratory stress-mediated transcription activation of nuclear gene targets.</title>
            <link>http://www.medworm.com/index.php?rid=3276656&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153290%26dopt%3DAbstract</link>
            <description>We report here that mitochondrial stress leads to induced expression and activation of serine threonine kinase Akt1. Interestingly, we observe that Akt1 phosphorylates hnRNPA2 under mitochondrial stress conditions, which is a crucial step for the recruitment of this coactivator to the stress target promoters and culmination in mitochondrial stress-mediated transcription activation of target genes. We propose that mitochondrial stress plays an important role in tumor progression and emergence of invasive phenotypes.
    PMID: 20153290 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276656</comments>
            <pubDate>Wed, 10 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276656</guid>        </item>
        <item>
            <title>Role of FtsH2 in the repair of Photosystem II in mutants of the cyanobacterium Synechocystis PCC 6803 with impaired assembly or stability of the CaMn(4) cluster.</title>
            <link>http://www.medworm.com/index.php?rid=3276655&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153291%26dopt%3DAbstract</link>
            <description>Authors: Komenda J, Knoppov&amp;#xE1; J, Krynick&amp;#xE1; V, Nixon PJ, Tich&amp;#xFD; M
    The FtsH2 protease, encoded by the slr0228 gene, plays a key role in the selective degradation of photodamaged D1 protein during the repair of Photosystem II (PSII) in the cyanobacterium Synechocystis sp. PCC 6803. To test whether additional proteases might be involved in D1 degradation during high rates of photodamage, we have studied the synthesis and degradation of the D1 protein in DeltaPsbO and DeltaPsbV mutants, in which the CaMn(4) cluster catalyzing oxygen evolution is less stable, and in the D1 processing mutants, D1-S345P and DeltaCtpA, which are unable to assemble a functional cluster. All four mutants exhibited a dramatically increased rate of D1 degradation in high light compared to the wild type....</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276655</comments>
            <pubDate>Wed, 10 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276655</guid>        </item>
        <item>
            <title>Specific motifs of the V-ATPase a2-subunit isoform interact with catalytic and regulatory domains of ARNO.</title>
            <link>http://www.medworm.com/index.php?rid=3276654&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153292%26dopt%3DAbstract</link>
            <description>Authors: Merkulova M, Bakulina A, Thaker YR, Gr&amp;#xFC;ber G, Marshansky V
    We have previously shown that the V-ATPase a2-subunit isoform interacts specifically, and in an intra-endosomal acidification-dependent manner, with the Arf-GEF ARNO. In the present study, we examined the molecular mechanism of this interaction using synthetic peptides and purified recombinant proteins in protein-association assays. In these experiments, we revealed the involvement of multiple sites on the N-terminus of the V-ATPase a2-subunit (a2N) in the association with ARNO. While six a2N-derived peptides interact with wild-type ARNO, only two of them (named a2N-01 and a2N-03) bind to its catalytic Sec7 domain. However, of these, only the a2N-01 peptide (MGSLFRSESMCLAQLFL) showed specificity towards the Sec7 d...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276654</comments>
            <pubDate>Wed, 10 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276654</guid>        </item>
        <item>
            <title>Interaction of the N-terminal segment of HCV protein NS5A with model membranes.</title>
            <link>http://www.medworm.com/index.php?rid=3276653&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153293%26dopt%3DAbstract</link>
            <description>We report the identification in NS5A of a highly membranotropic region located at the suggested membrane association domain of the protein. We report the binding and interaction with model membranes of two peptides patterned after this segment, peptides 1A and 1B, derived from the strains 1a_H77 and 1b_HC-4J respectively. We show that they insert into phospholipid membranes, interact with them, and are located in a shallow position in the membrane. The NS5A region where this segment resides might have an essential role in the membrane replication and/or assembly of the viral particle through the modulation of the replication complex, and consequently, directly implicated in the HCV life cycle.
    PMID: 20153293 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276653</comments>
            <pubDate>Wed, 10 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276653</guid>        </item>
        <item>
            <title>Unravelling the molecular basis of the selectivity of the HIV-1 fusion inhibitor sifuvirtide towards phosphatidylcholine-rich rigid membranes.</title>
            <link>http://www.medworm.com/index.php?rid=3276652&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153294%26dopt%3DAbstract</link>
            <description>Authors: Franquelim HG, Veiga AS, Weissm&amp;#xFC;ller G, Santos NC, Castanho MA
    Sifuvirtide, a 36 amino acid negatively charged peptide, is a novel HIV-1 fusion inhibitor with improved antiretroviral activity. In this work we evaluated the physical chemistry foundation of the interaction of sifuvirtide with biomembrane model systems. Since this peptide has aromatic residues, fluorescence spectroscopy techniques were mostly used. The interaction was assessed by partition and quenching experiments. Results showed no significant interaction with large unilamellar vesicles composed by sphingomyelin and ceramide. In contrast, sifuvirtide presented selectivity towards vesicles composed by phosphatidylcholines (PC) in the gel phase, in opposition to fluid phase PC vesicles. The interaction of th...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276652</comments>
            <pubDate>Wed, 10 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276652</guid>        </item>
        <item>
            <title>Radiolabelled Proteins for Positron Emission Tomography: Pros and cons of labelling methods.</title>
            <link>http://www.medworm.com/index.php?rid=3276651&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153401%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: Factors such as matching biological and physical half-lives, availability of the nuclide, labelling yields, and influences of labelling on targeting properties (affinity, charge and lipophilicity, cellular processing and retention of catabolites) should be considered when selecting a labelling strategy for each proteinaceous tracer. GENERAL SIGNIFICANCE: The labelling strategy used can make all the difference between success and failure in a tracer application. This review emphasizes chemical, biological and pharmacological considerations in labelling proteins with positron emitting radionuclides.
    PMID: 20153401 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276651</comments>
            <pubDate>Wed, 10 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276651</guid>        </item>
        <item>
            <title>Altered lipid a structures and polymyxin hypersensitivity of rhizobium etli mutants lacking the LpxE and LpxF phosphatases.</title>
            <link>http://www.medworm.com/index.php?rid=3276650&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153447%26dopt%3DAbstract</link>
            <description>Authors: Ingram BO, Sohlenkamp C, Geiger O, Raetz CR
    The lipid A of Rhizobium etli, a nitrogen-fixing plant endosymbiont, displays significant structural differences when compared to that of Escherichia coli. An especially striking feature of R. etli lipid A is that it lacks both the 1- and 4'-phosphate groups. The 4'-phosphate moiety of the distal glucosamine unit is replaced with a galacturonic acid residue. The dephosphorylated proximal unit is present as a mixture of the glucosamine hemiacetal and an oxidized 2-aminogluconate derivative. Distinct lipid A phosphatases directed to the 1 or the 4'-positions have been identified previously in extracts of R. etli and Rhizobium leguminosarum. The corresponding structural genes, lpxE and lpxF respectively, have also been identified. Here ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276650</comments>
            <pubDate>Wed, 10 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276650</guid>        </item>
        <item>
            <title>DmsD, a Tat system specific chaperone, interacts with other general chaperones and proteins involved in the molybdenum cofactor biosynthesis.</title>
            <link>http://www.medworm.com/index.php?rid=3276649&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153451%26dopt%3DAbstract</link>
            <description>In this study, we identified several potential interacting partners of DmsD by using several in vitro protein-protein interaction screening approaches, including affinity chromatography, co-precipitation, and cross-linking. Candidate hits from these in vitro findings were analyzed by in vivo methods of bacterial two-hybrid (BACTH) and bimolecular fluorescence complementation (BiFC). From these data, DmsD was confirmed to interact with the general molecular chaperones DnaK, DnaJ, GrpE, GroEL, Tig and Ef-Tu. In addition, DmsD was also found to interact with proteins involved in the molybdenum cofactor biosynthesis pathway. Our data suggests that DmsD may play a role as a &quot;node&quot; in escorting its substrate through a cascade of chaperone assisted protein-folding maturation events.
    PMID: 201...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276649</comments>
            <pubDate>Wed, 10 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276649</guid>        </item>
        <item>
            <title>Sp1 and Sp3 regulate transcription of the chicken GAS41 gene.</title>
            <link>http://www.medworm.com/index.php?rid=3276648&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153453%26dopt%3DAbstract</link>
            <description>In this study, we have localized the GAS 41 promoter to this narrow region. Electrophoretic mobility shift assays and chromatin immunoprecipitation analyses revealed that Sp1 and Sp3 bind to this promoter. Mapping by a technique of indirect end-labelling demonstrated that the Sp1 binding sites contained in this region exactly co-map with two previously identified DNase I hypersensitive (HS) sites, which suggests the important role of Sp1 binding in maintaining an open chromatin structure of the GAS41 promoter. We further found that Sp1 as well as Sp3 strongly activate CAT expression controlled by the putative GAS41 promoter in Drosophila Schneider S2 cells and that deletion of the Sp1 sites resulted in a loss of promoter activity in chicken HD11 cells. The results indicate that transcripti...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276648</comments>
            <pubDate>Wed, 10 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276648</guid>        </item>
        <item>
            <title>Arylsulfatase B Regulates Interaction of Chondroitin 4-Sulfate and Kininogen in Renal Epithelial Cells.</title>
            <link>http://www.medworm.com/index.php?rid=3276663&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20152898%26dopt%3DAbstract</link>
            <description>In this report, we present the role of ASB in regulation of the kininogen-bradykinin axis, due to its effect on chondroitin-4-sulfation and the interaction of C4S with kininogen. Silencing or overexpression of ASB in normal rat kidney epithelial cells in tissue culture modified the content of total sulfated glycosaminoglycans (sGAG), C4S, kininogen, and bradykinin in spent media and cell lysates. Treatment of the cultured cells with chondroitinase ABC also increased the secretion of bradykinin into the spent media and reduced the C4S-associated kininogen. When ASB was overexpressed, the cellular kininogen that associated with C4S declined, suggesting a vital role for chondroitin 4-sulfation in regulating the kininogen - C4S interaction. These findings suggest that ASB, due to its effect on...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276663</comments>
            <pubDate>Tue, 09 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276663</guid>        </item>
        <item>
            <title>Beta Sheet 2 - Alpha Helix C Loop of Cytochrome P450 Reductase Serves as a Docking Site for Redox Partners.</title>
            <link>http://www.medworm.com/index.php?rid=3276662&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20152939%26dopt%3DAbstract</link>
            <description>Authors: Jang HH, Jamakhandi AP, Sullivan SZ, Yun CH, Hollenberg PF, Miller GP
    As a promiscuous redox partner, the biological role of cytochrome P450 reductase (CPR) depends significantly on protein-protein interactions. We tested a hypothesized CPR docking site by mutating D113, E115, and E116 to alanine and assaying activity toward various electron acceptors as a function of ionic strength. Steady-state cytochrome c studies demonstrated the mutations improved catalytic efficiency and decreased the impact of ionic strength on catalytic parameters when compared to wild type. Based on activity toward 7-ethoxy-4-trifluoro-methylcoumarin, CYP2B1 and CPR favored formation of an active CYP2B1*CPR complex and inactive (CYP2B1)(2)*CPR complex until higher ionic strength whereby only the binar...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276662</comments>
            <pubDate>Tue, 09 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276662</guid>        </item>
        <item>
            <title>Protein disulfide isomerase-P5, down-regulated in the final stage of boar epididymal sperm maturation, catalyses disulfide formation to inhibit protein function in oxidative refolding of reduced denatured lysozyme.</title>
            <link>http://www.medworm.com/index.php?rid=3276661&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20152940%26dopt%3DAbstract</link>
            <description>We examined the expression profiles of proteins from boar epididymal caput, corpus, and cauda sperm by two-dimensional gel electrophoresis and peptide mass fingerprinting. Our results indicated that protein disulfide isomerase-P5 (PDI-P5) human homolog was down-regulated from the epididymal corpus to cauda sperm, in contrast to the constant expression of protein disulfide isomerase A3 (PDIA3) human homolog. To examine the functions of PDIA3 and PDI-P5, we cloned and sequenced cDNAs of pig PDIA3 and PDI-P5 protein precursors. Each recombinant pig mature PDIA3 and PDI-P5 expressed in Escherichia coli showed thiol-dependent disulfide reductase activities in insulin turbidity assay. Although PDIA3 showed chaperone activity to promote oxidative refolding of reduced denatured lysozyme, PDI-P5 ex...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276661</comments>
            <pubDate>Tue, 09 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276661</guid>        </item>
        <item>
            <title>Effects on human plasminogen conformation and activation rate caused by interaction with VEK-30, a peptide derived from the group a streptococcal m-like protein (PAM).</title>
            <link>http://www.medworm.com/index.php?rid=3276660&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20152941%26dopt%3DAbstract</link>
            <description>Authors: Figuera-Losada M, Ranson M, Sanderson-Smith ML, Walker MJ, Castellino FJ, Prorok M
    In vertebrates, fibrinolysis is primarily carried out by the serine protease plasmin (Pm), which is derived from activation of the zymogen precursor, plasminogen (Pg). One of the most distinctive features of Pg/Pm is the presence of five homologous kringle (K) domains. These structural elements possess conserved Lys-binding sites (LBS) that facilitate interactions with substrates, activators, inhibitors and receptors. In human Pg (hPg), K2 displays weak Lys affinity, however the LBS of this domain has been implicated in an atypical interaction with the N-terminal region of a bacterial surface protein known as PAM (Pg-binding group A streptococcal M-like protein). A direct correlation has been es...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276660</comments>
            <pubDate>Tue, 09 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276660</guid>        </item>
        <item>
            <title>Alkaline pH dependent differential unfolding characteristics of mesophilic and thermophilic homologs of dimeric serine hydroxymethyltransferase.</title>
            <link>http://www.medworm.com/index.php?rid=3276659&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20152942%26dopt%3DAbstract</link>
            <description>Authors: Bhatt AN, Bhakuni V, Kumar A, Khan MY, Siddiqi MI
    Environmental variables such as pH can significantly influence the folding and stability of a protein molecule. In present investigation, we compared the alkaline pH induced unfolding of two homologous serine hydroxymethyltransferase from mesophilic Bacillus subtilis (bsSHMT) and thermophilic Bacillus stearothermophilus (bstSHMT) using various biophysical techniques. The thermophilic enzyme bstSHMT was found to be more resistant to alkaline denaturation compared to its mesosphilic counterpart, bsSHMT. Unfolding studies using domain swapped chimera, constructed by swapping the C-terminal domain of these two wild type proteins, revealed that C-terminal domain play a pivotal role in the folding, stability and subunit interaction o...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276659</comments>
            <pubDate>Tue, 09 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276659</guid>        </item>
        <item>
            <title>Site-directed chemical modification of archaeal Thermococcus litoralis Sh1B DNA polymerase: Acquired ability to read through template-strand uracils.</title>
            <link>http://www.medworm.com/index.php?rid=3276658&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20152943%26dopt%3DAbstract</link>
            <description>We present site-directed chemical modification (SDCM), a new tool for engineering U-resistant archaeal DNA polymerases of family B. The Thermococcus litoralis Sh1B DNA polymerase (GenBank: GQ891548) was choosen as the object of the study. Similar to D.Tok, Kod1, Pfu, Tgo and other archaeal members of this family, the T.litoralis Sh1B DNA polymerase is a domain structured, proofreading-proficient enzyme that has the polymerization and 3'--&amp;gt;5' DNA exonucleolytic activities and contains N-terminally located highly conserved template-strand U-binding pocket. The tight binding of template uracil in the enzyme pocket during polymerization blocks the replication of DNA containing uracils. This effect can be alleviated by mutations in key amino acids of the U-binding pocket. We altered T.litora...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276658</comments>
            <pubDate>Tue, 09 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276658</guid>        </item>
        <item>
            <title>Biogenesis Of Tartrate-Resistant Acid Phosphatase Isoforms 5a and 5b in stably transfected MDA-MB-231 breast cancer epithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=3268418&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20149826%26dopt%3DAbstract</link>
            <description>In conclusion, these data provide evidence that distinct monomeric TRAP populations are diverted early in the secretory pathway either giving rise to a secreted, monomeric 5a-like TRAP isoform or to an intracellular, proteolytically processed 5b-like TRAP isoform.
    PMID: 20149826 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3268418</comments>
            <pubDate>Mon, 08 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3268418</guid>        </item>
        <item>
            <title>The dopamine-D2-receptor agonist ropinirole dose-dependently blocks the Ca(2+)-triggered permeability transition of mitochondria.</title>
            <link>http://www.medworm.com/index.php?rid=3262979&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20144882%26dopt%3DAbstract</link>
            <description>In conclusion, our data suggest that the neuroprotective activity of ropinirole is due to the blockade of the the Ca(2+)-triggered permeability transition.
    PMID: 20144882 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262979</comments>
            <pubDate>Sat, 06 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262979</guid>        </item>
        <item>
            <title>Restoring the charge and surface activity of bovine lung extract surfactants with cationic and anionic polysaccharides.</title>
            <link>http://www.medworm.com/index.php?rid=3262978&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20144883%26dopt%3DAbstract</link>
            <description>Authors: Acosta EJ, Policova Z, Lee S, Dang A, Hair ML, Neumann AW
    Chitosan, a cationic polysaccharide, has been found to improve the surface activity of lung surfactant extracts in the presence of various inhibitors. It has been proposed that chitosan binds to anionic lipids (e.g. phosphatidyl glycerols) in lung surfactants, producing stable lipid films at the air-water interface. This binding also reverses the net charge of the surfactant aggregates, from negative to positive. Unfortunately, positively charged aggregates may adsorb or interact with the negatively charged epithelial tissue, leading to poor surfactant performance. To address this issue an anionic polysaccharide, dextran sulfate (dexS), was used as a secondary coating to reverse the charge of chitosan-lung surfactant ex...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262978</comments>
            <pubDate>Sat, 06 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262978</guid>        </item>
        <item>
            <title>Moonlighting proteins: An intriguing mode of multitasking.</title>
            <link>http://www.medworm.com/index.php?rid=3262977&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20144902%26dopt%3DAbstract</link>
            <description>Authors: Huberts DH, van der Klei IJ
    Proteins are macromolecules, which perform a large variety of functions. Most of them have only a single function, but an increasing number of proteins are being identified as multifunctional. Moonlighting proteins form a special class of multifunctional proteins. They perform multiple autonomous and often unrelated functions without partitioning these functions into different domains of the protein. Striking examples are enzymes, which in addition to their catalytic function are involved in fully unrelated processes such as autophagy, protein transport or DNA maintenance. In this contribution we present an overview of our current knowledge of moonlighting proteins and discuss the significant implications for biomedical and fundamental research.
   ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262977</comments>
            <pubDate>Sat, 06 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262977</guid>        </item>
        <item>
            <title>The regulation of OXPHOS by extramitochondrial calcium.</title>
            <link>http://www.medworm.com/index.php?rid=3262986&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20144582%26dopt%3DAbstract</link>
            <description>Authors: Gellerich FN, Gizatullina Z, Trumbeckaite S, Nguyen HP, Pallas T, Arandarcikaite O, Vielhaber S, Seppet E, Striggow F
    Despite extensive research, the regulation of mitochondrial function is still not understood completely. Ample evidence shows that cytosolic Ca(2+) has a strategic task in co-ordinating the cellular work load and the regeneration of ATP by mitochondria. Currently, the paradigmatic view is that Ca(2+)(cyt) taken up by the Ca(2+) uniporter activates the matrix enzymes pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase and isocitrate dehydrogenase. However, we have recently found that Ca(2+) regulates the glutamate-dependent state 3 respiration by the supply of glutamate to mitochondria via aralar, a mitochondrial glutamate/aspartate carrier. Since this act...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262986</comments>
            <pubDate>Fri, 05 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262986</guid>        </item>
        <item>
            <title>Kinetic model of the inhibition of respiration by endogenous nitric oxide in intact cells.</title>
            <link>http://www.medworm.com/index.php?rid=3262985&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20144583%26dopt%3DAbstract</link>
            <description>We present a kinetic model of CcO inhibition by NO that efficiently predicts experimentally determined respiration at physiological O(2) and NO concentrations and under hypoxia, and accurately predicts the respiratory responses under hyperoxia. The model invokes competitive and uncompetitive inhibition by binding of NO to the reduced and oxidized forms of CcO, respectively, and suggests that dissociation of NO from reduced CcO may involve its O(2)-dependent oxidation. It also explains the non-linear dependence of IC(50) on O(2) concentration, and the hyperbolic increase of c(50) as a function of NO concentration.
    PMID: 20144583 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262985</comments>
            <pubDate>Fri, 05 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262985</guid>        </item>
        <item>
            <title>4Pi microscopy reveals an impaired three-dimensional mitochondrial network of pancreatic islet beta-cells, an experimental model of type-2 diabetes.</title>
            <link>http://www.medworm.com/index.php?rid=3262984&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20144584%26dopt%3DAbstract</link>
            <description>Authors: Dlaskov&amp;#xE1; A, Spa&amp;#x10D;ek T, Santorov&amp;#xE1; J, Plecit&amp;#xE1;-Hlavat&amp;#xE1; L, Berkov&amp;#xE1; Z, Saudek F, Lessard M, Bewersdorf J, Je&amp;#x17E;ek P
    Insulin production in pancreatic beta-cells is critically linked to mitochondrial oxidative phosphorylation. Increased ATP production triggered by blood glucose represents the beta-cells' glucose sensor. Type 2 diabetes mellitus results from insulin resistance in peripheral tissues and impaired insulin secretion. Pathology of diabetic beta-cells might be reflected by the altered morphology of mitochondrial network. Its characterization is however hampered by the complexity and density of the three-dimensional (3D) mitochondrial tubular networks in these cell types. Conventional confocal microscopy does not provide sufficient axial res...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262984</comments>
            <pubDate>Fri, 05 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262984</guid>        </item>
        <item>
            <title>Overexpression of gamma-tocopherol methyl transferase gene in transgenic Brassica juncea plants alleviates abiotic stress: Physiological and chlorophyll a fluorescence measurements.</title>
            <link>http://www.medworm.com/index.php?rid=3262983&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20144585%26dopt%3DAbstract</link>
            <description>Authors: Yusuf MA, Kumar D, Rajwanshi R, Strasser RJ, Tsimilli-Michael M, Govindjee , Sarin NB
    Tocopherols (vitamin E) are lipid soluble antioxidants synthesized by plants and some cyanobacteria. We have earlier reported that overexpression of the gamma-tocopherol methyl transferase (gamma-TMT) gene from Arabidopsis thaliana in transgenic Brassica juncea plants resulted in an over six-fold increase in the level of alpha-tocopherol, the most active form of all the tocopherols. Tocopherol levels have been shown to increase in response to a variety of abiotic stresses. In the present study on Brassica juncea, we found that salt, heavy metal and osmotic stress induced an increase in the total tocopherol levels. Measurements of seed germination, shoot growth and leaf disc senescence showed ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262983</comments>
            <pubDate>Fri, 05 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262983</guid>        </item>
        <item>
            <title>Communication between mitochondria and nucleus: putative role for VDAC in reduction/oxidation mechanism.</title>
            <link>http://www.medworm.com/index.php?rid=3262982&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20144586%26dopt%3DAbstract</link>
            <description>Authors: Galganska H, Karachitos A, Wojtkowska M, Stobienia O, Budzinska M, Kmita H
    Voltage dependent anion channel (VDAC) was identified in 1976 and since that time has been extensively studied. It is well known that VDAC transports metabolites across the outer mitochondrial membrane. The simple transport function is indispensable for proper mitochondria functions and, consequently for cell activity, and makes VDAC crucial for a range of cellular processes including ATP rationing, Ca(2+) homeostasis and apoptosis execution. Here, we review recent data obtained for Saccharomyces cerevisiae cells used as a model system concerning the putative role of VDAC in communication between mitochondria and the nucleus. The S. cerevisiae VDAC isoform known as VDAC1 (termed here YVDAC) mediates the...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262982</comments>
            <pubDate>Fri, 05 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262982</guid>        </item>
        <item>
            <title>Delivering cargoes into cancer cells using DNA aptamers targeting internalized surface portals.</title>
            <link>http://www.medworm.com/index.php?rid=3262981&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20144587%26dopt%3DAbstract</link>
            <description>Authors: Orava EW, Cicmil N, Gari&amp;#xE9;py J
    Many evolving treatments for cancer patients are based on the targeted delivery of therapeutic cargoes to and into cancer cells. The advent of monoclonal antibodies and the use of peptide hormones, growth factors and cytokines have historically provided a spectrum of ligands needed to selectively target tumor-associated antigens on cancer cells. However, issues linked to the size, cost and immunogenicity of protein-based ligands have led to the search for alternate ligand families. The advent of short synthetic oligonucleotide ligands known as aptamers now provides a simple strategy to select for membrane-impermeant aptamers tailored to precisely target internalized surface markers present on cancer cells. Here we described how 25-base long, ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262981</comments>
            <pubDate>Fri, 05 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262981</guid>        </item>
        <item>
            <title>The sodium pump and cardiotonic steroids-induced signal transduction protein kinases and calcium signaling microdomain in regulation of transporter trafficking.</title>
            <link>http://www.medworm.com/index.php?rid=3262980&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20144708%26dopt%3DAbstract</link>
            <description>Authors: Liu J, Xie ZJ
    The Na/K-ATPase was discovered as an energy transducing ion pump. A major difference between the Na/K-ATPase and other P-type ATPases is its ability to bind a group of chemicals called cardiotonic steroids (CTS). The plant-derived CTS such as digoxin are valuable drugs for the management of cardiac diseases, whereas ouabain and marinobufagenin (MBG) have been identified as a new class of endogenous hormones. Recent studies have demonstrated that the endogenous CTS are important regulators of renal Na(+) excretion and blood pressure. The Na/K-ATPase is not only an ion pump, but also an important receptor that can transduce the ligand-like effect of CTS on intracellular protein kinases and Ca(2+) signaling. Significantly, these CTS-provoked signaling events are cap...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262980</comments>
            <pubDate>Fri, 05 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262980</guid>        </item>
        <item>
            <title>Characterization of human VDAC isoforms: A peculiar function for VDAC3?</title>
            <link>http://www.medworm.com/index.php?rid=3262991&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138821%26dopt%3DAbstract</link>
            <description>Authors: De Pinto V, Guarino F, Guarnera A, Messina A, Reina S, Tomasello FM, Palermo V, Mazzoni C
    VDACs are a family of pore-forming proteins mainly located in the mitochondrial outer membrane. In mammals three isoforms exist. In this work we review the information available about them with the addition of new results. We have compared the human VDACs transformed in a yeast strain lacking the endogenous porin. VDAC1 and 2 are able to complement the lack of porin in mitochondrial respiration and modulation of ROS. VDAC3 has a limited ability to support the mitochondrial respiration and has no influence in the control of ROS production. The over-expression of VDAC isoforms in wild type yeast strain strain led to a dramatic sensitivity to oxidative stress, especially for VDAC3, and a sho...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262991</comments>
            <pubDate>Thu, 04 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262991</guid>        </item>
        <item>
            <title>Interaction between CFTR and prestin (SLC26A5).</title>
            <link>http://www.medworm.com/index.php?rid=3262990&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138822%26dopt%3DAbstract</link>
            <description>Authors: Homma K, Miller KK, Anderson CT, Sengupta S, Du GG, Agui&amp;#xF1;aga S, Cheatham M, Dallos P, Zheng J
    Cystic fibrosis transmembrane conductance regulator (CFTR) is a cAMP-activated chloride channel that is present in a variety of epithelial cell types, and usually expressed in the luminal membrane. In contrast, prestin (SLC26A5) is a voltage-dependent motor protein, which is present in the basolateral membrane of cochlear outer hair cells (OHCs), and plays an important role in the frequency selectivity and sensitivity of mammalian hearing. By using in situ hybridization and immunofluorescence, we found that both mRNA and protein of CFTR are present in OHCs, and that CFTR localizes in both the apical and the lateral membranes. CFTR was not detected in the lateral membrane of inner...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262990</comments>
            <pubDate>Thu, 04 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262990</guid>        </item>
        <item>
            <title>A novel bifunctional peptidic aspartic protease inhibitor inhibits chitinase a from Serratia marcescens: Kinetic analysis of inhibition and binding affinity.</title>
            <link>http://www.medworm.com/index.php?rid=3262989&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138972%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: The peptide has an amino acid sequence Asp-Leu-Tyr-Asp-Gly-Trp-Lys-His-Glu-Ala-Glu-Cys-Ile. The ChiA-API kinetic interactions reveal noncompetitive, irreversible and tight binding nature of API with I(50)=600 nM and K(i)=510 nM in the presence of chromogenic substrate p-nitrophenyl-N,N'-diacetyl-beta-chitobioside[p-NP-(GlcNAc)(2)]. The inhibition progress curves show a two step slow tight binding inhibition mechanism with the rate constant k(5)=8.7+/-1x10(-3)s(-1) and k(6)=7.3+/-0.6x10(-5)s(-1). CD-spectra and tryptophanyl fluorescence analysis of ChiA incubated with increasing API concentrations confirms conformational changes in enzyme structure which may be due to irreversible denaturation of enzyme upon binding of API. Chemical modifications by WRK abolished the anti-chiti...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262989</comments>
            <pubDate>Thu, 04 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262989</guid>        </item>
        <item>
            <title>Tryptase promotes human monocyte-derived macrophage foam cell formation by suppressing LXRalpha activation.</title>
            <link>http://www.medworm.com/index.php?rid=3262988&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20139031%26dopt%3DAbstract</link>
            <description>Authors: Yeong P, Ning Y, Xu Y, Li X, Yin L
    Accumulated mast cells in atherosclerotic plaques secrete a high level of tryptase that may participate in the pathogenesis of atherosclerotic disease by diverse pathways. However, the role of tryptase in the lipid metabolism of macrophages remains to be defined. In the present study, we found that the addition of tryptase into THP-1-derived macrophages increased both intracellular lipid accumulation and total cholesterol level. Tryptase promoting foam cell formation was also observed by transmission electron microscope. These effects were resisted by APC366, a selective inhibitor of mast cell tryptase. Tryptase dramatically resisted 22RHC induced activation of LXRalpha protein expression, which can be reversed by SAM-11 (a PAR-2-specific neu...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262988</comments>
            <pubDate>Thu, 04 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262988</guid>        </item>
        <item>
            <title>Chromatin dynamics during herpes simplex virus-1 lytic infection.</title>
            <link>http://www.medworm.com/index.php?rid=3262987&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20139038%26dopt%3DAbstract</link>
            <description>Authors: Placek BJ, Berger SL
    Herpes simplex virus type 1 is a DNA virus that can establish lytic infections in epithelial cells and latent infections in sensory neurons. Upon entry into the nucleus the genome of HSV-1 rapidly associates with histone proteins. Similar to the genomes of the cellular host, HSV-1 is subject to chromatin-based regulation of transcription and replication. However, unlike the host genome, nucleosomes appear to be underrepresented on the HSV genome. During lytic infection, when the genome is transcribed, the HSV-1 chromatin structure appears to be disorganized, and characterized by histone variant sub-types and post-translational modifications representative of active chromatin. In contrast, during latency, when the majority of the viral genome is transcripti...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262987</comments>
            <pubDate>Thu, 04 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262987</guid>        </item>
        <item>
            <title>Mitochondrial generated nitric oxide protects against permeability transition via formation of membrane protein S-nitrosothiols.</title>
            <link>http://www.medworm.com/index.php?rid=3263000&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138021%26dopt%3DAbstract</link>
            <description>Authors: Leite AC, Oliveira HC, Utino FL, Garcia R, Alberici LC, Fernandes MP, Castilho RF, Vercesi AE
    Mitochondria generated nitric oxide (NO(*)) regulates several cell functions including energy metabolism, cell cycling, and cell death. Here we report that the NO(*) synthase inhibitors (L-NAME, L-NNA and L-NMMA) administered either in vitro or in vivo induce Ca(2+)-dependent mitochondrial permeability transition (MPT) in rat liver mitochondria via a mechanism independent on changes in the energy state of the organelle. MPT was determined by the occurrence of cyclosporin A sensitive mitochondrial membrane potential disruption followed by mitochondrial swelling and Ca(2+) release. In in vitro experiments, the effect of NOS inhibitors was dose dependent (1 to 50microM). In addition to c...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3263000</comments>
            <pubDate>Wed, 03 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3263000</guid>        </item>
        <item>
            <title>Effects of protons on macroscopic and single-channel currents mediated by the human P2X7 receptor.</title>
            <link>http://www.medworm.com/index.php?rid=3262999&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138022%26dopt%3DAbstract</link>
            <description>Authors: Flittiger B, Klapperst&amp;#xFC;ck M, Schmalzing G, Markwardt F
    Human P2X7 receptors (hP2X7Rs) belong to the P2X family, which opens an intrinsic cation channel when challenged by extracellular ATP. hP2X7Rs are expressed in cells of the inflammatory and immune system. During inflammation, ATP and protons are secreted into the interstitial fluid. Therefore, we investigated the effect of protons on the activation of hP2X7Rs. hP2X7Rs were expressed in Xenopus laevis oocytes and activated by the agonists ATP or benzoyl-benzoyl-ATP (BzATP) at different pH values. The protons reduced the hP2X7R-dependent cation current amplitude and slowed the current deactivation depending on the type and concentration of the agonist used. These effects can be explained by (i) the protonation of ATP, w...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262999</comments>
            <pubDate>Wed, 03 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262999</guid>        </item>
        <item>
            <title>Biogenesis of membrane bound respiratory complexes in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=3262997&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138092%26dopt%3DAbstract</link>
            <description>Authors: Price CE, Driessen AJ
    Escherichia coli is one of the preferred bacteria for studies on the energetics and regulation of respiration. Respiratory chains consist of primary dehydrogenases and of terminal reductases or oxidases linked by quinones. In order to assemble this complex arrangement of protein complexes, synthesis of the subunits occurs in the cytoplasm followed by assembly in the cytoplasm and/or membrane, the incorporation of metal or organic cofactors and the anchoring of the complex to the membrane. In the case of exported metalloproteins, synthesis, assembly and incorporation of metal cofactors must be completed before translocation across the cytoplasmic membrane. Coordination data on these processes is, however, scarce. In this review, we discuss the various proc...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262997</comments>
            <pubDate>Wed, 03 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262997</guid>        </item>
        <item>
            <title>The multifaceted capacity of Dps proteins to combat bacterial stress conditions: detoxification of iron and hydrogen peroxide and DNA binding.</title>
            <link>http://www.medworm.com/index.php?rid=3262996&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138126%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: The state of the art is that the response to oxidative and peroxide-mediated stress is mediated directly by Dps proteins via their ferritin-like activity. In contrast, the response to other stress conditions derives from the concerted interplay of diverse interactions that Dps proteins may establish with DNA and with other DNA-binding proteins.
    PMID: 20138126 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262996</comments>
            <pubDate>Wed, 03 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262996</guid>        </item>
        <item>
            <title>Antioxidant defence systems and generation of reactive oxygen species in osteosarcoma cells with defective mitochondria; effect of selenium.</title>
            <link>http://www.medworm.com/index.php?rid=3262994&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138159%26dopt%3DAbstract</link>
            <description>This study was aimed to elucidate effects of selenium on ROS and antioxidant system of NARP cybrid cells with 98% of T8993G mutation load. We found that selenium decreased ROS generation and increased the level and activity of antioxidant enzymes such as glutathione peroxidase (GPx) and thioredoxin reductase (TrxR). Therefore, we propose selenium to be a promising therapeutic agent not only in the case of NARP syndrome but also other diseases associated with mitochondrial dysfunctions and oxidative stress.
    PMID: 20138159 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262994</comments>
            <pubDate>Wed, 03 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262994</guid>        </item>
        <item>
            <title>Cytosolic phospholipase A(2)-alpha enhances induction of endoplasmic reticulum stress.</title>
            <link>http://www.medworm.com/index.php?rid=3262993&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138193%26dopt%3DAbstract</link>
            <description>Authors: Ren G, Takano T, Papillon J, Cybulsky AV
    Induction of endoplasmic reticulum (ER) stress by the complement membrane attack complex is enhanced by activation of cytosolic phospholipase A(2)-alpha (cPLA(2)). To address mechanisms by which cPLA(2) may modulate ER stress, we produced a mutant cPLA(2), containing an ER-targeting domain (cPLA(2)-ERmut). After transfection and fractionation of COS-1 cells, cPLA(2)-ERmut was present mainly in the membrane fraction, whereas wild type (wt) cPLA(2) was principally in the cytosol. By fluorescence microscopy, cPLA(2)-ERmut was enriched in a perinuclear distribution under basal conditions, colocalizing with the ER protein, calnexin, while cPLA(2)-wt was mainly cytosolic. Both forms of cPLA(2) transiently expressed in COS cells showed basal p...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262993</comments>
            <pubDate>Wed, 03 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262993</guid>        </item>
        <item>
            <title>Activation of TM7SF2 promoter by SREBP-2 depends on a new sterol regulatory element, a GC-box, and an inverted CCAAT-box.</title>
            <link>http://www.medworm.com/index.php?rid=3262992&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138239%26dopt%3DAbstract</link>
            <description>Authors: Schiavoni G, Bennati AM, Castelli M, Della Fazia MA, Beccari T, Servillo G, Roberti R
    TM7SF2 gene encodes 3beta-hydroxysterol Delta(14)-reductase, responsible for the reduction of C14-unsaturated sterols in cholesterol biosynthesis. TM7SF2 gene expression is controlled by cell sterol levels through the SREBP-2. The motifs of TM7SF2 promoter responsible for activation by SREBP-2 have not been characterized. Using electrophoretic mobility shift assays and mutation analysis, we identified a new SRE motif, 60% identical to an inverted SRE-3, able to bind SREBP-2 in vitro and in vivo. Co-transfection of promoter-luciferase reporter constructs in HepG2 cells showed that the binding of SREBP-2 to SRE produced approximately 26-fold promoter activation, whereas mutation of the SRE moti...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262992</comments>
            <pubDate>Wed, 03 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262992</guid>        </item>
        <item>
            <title>Cell-penetrating peptide exploited syndecans.</title>
            <link>http://www.medworm.com/index.php?rid=3262998&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138023%26dopt%3DAbstract</link>
            <description>Authors: Letoha T, Keller A, Kusz E, Kolozsi C, Bozs&amp;#xF3; Z, T&amp;#xF3;th G, Vizler C, Ol&amp;#xE1;h Z, Szil&amp;#xE1;k L
    Cell-penetrating peptides (CPPs) are short peptides capable of translocating across the plasma membrane of live cells and transporting conjugated compounds intracellularly. Fifteen years after discovering the first model cationic CPPs, penetratin and TAT, CPP internalization is still challenging many questions. Particularly it has been unknown whether CPPs enter the cells with or without mediation of a specific surface receptor. Here we report that syndecan-4, the universally expressed isoform of the syndecan family of transmembrane proteoglycans, binds and mediates transport of the three most frequently utilized cationic CPPs (penetratin, octaarginine and TAT) into the cells...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262998</comments>
            <pubDate>Tue, 02 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262998</guid>        </item>
        <item>
            <title>Conserved and divergent features of the structure and function of La and La-related proteins (LARPs).</title>
            <link>http://www.medworm.com/index.php?rid=3262995&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138158%26dopt%3DAbstract</link>
            <description>Authors: Bayfield MA, Yang R, Maraia RJ
    Genuine La proteins contain two RNA binding motifs, a La motif (LAM) followed by a RNA recognition motif (RRM), arranged in a unique way to bind RNA. These proteins interact with an extensive variety of cellular RNAs and exhibit activities in two broad categories: i) to promote the metabolism of nascent pol III transcripts, including precursor-tRNAs, by binding to their common, UUU-3'OH containing ends, and ii) to modulate the translation of certain mRNAs involving an unknown binding mechanism. Characterization of several La-RNA crystal structures as well as biochemical studies reveal insight into their unique two-motif domain architecture and how the LAM recognizes UUU-3'OH while the RRM binds other parts of a pre-tRNA. Recent studies of members...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3262995</comments>
            <pubDate>Tue, 02 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3262995</guid>        </item>
        <item>
            <title>Mutation of His 834 in human anion exchanger 1 affects substrate binding.</title>
            <link>http://www.medworm.com/index.php?rid=3248870&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20132789%26dopt%3DAbstract</link>
            <description>Authors: Takazaki S, Abe Y, Yamaguchi T, Yagi M, Ueda T, Kang D, Hamasaki N
    Anion exchanger 1 (AE1 or band 3) is responsible for Cl(-)-HCO(3)(-) exchange on erythrocyte membrane. Previously, we showed that band 3 is fixed in an inward-facing conformation by specific modification of His 834 with DEPC, resulting in a strong inhibition of its anion transport activity. To clarify the physiological role of His 834, we evaluated the sulfate transport activities of various band 3 mutants: different mutants at His 834 and alanine mutants of peripheral residues around 834 (Lys 829 approximately Phe 836) in yeast cell membranes. The Km values of the His 834 mutants were 4-10 times higher than that of the wild type, while their Vmax values were barely lower than that of wild type. Meanwhile, the ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3248870</comments>
            <pubDate>Mon, 01 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3248870</guid>        </item>
        <item>
            <title>Interaction of the exported malaria protein Pf332 with the red blood cell membrane skeleton.</title>
            <link>http://www.medworm.com/index.php?rid=3248869&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20132790%26dopt%3DAbstract</link>
            <description>Authors: Waller KL, Stubberfield LM, Dubljevic V, Buckingham DW, Mohandas N, Coppel RL, Cooke BM
    Intra-erythrocytic Plasmodium falciparum malaria parasites synthesize and export numerous proteins into the red blood cell (RBC) cytosol, where some bind to the RBC membrane skeleton. These interactions are responsible for the altered antigenic, morphological and functional properties of parasite-infected red blood cells (IRBCs). Plasmodium falciparum protein 332 (Pf332) is a large parasite protein that associates with the membrane skeleton and who's function has recently been elucidated. Using recombinant fragments of Pf332 in in vitro interaction assays, we have localised the specific domain within Pf332 that binds to the RBC membrane skeleton to an 86 residue sequence proximal to the C-t...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3248869</comments>
            <pubDate>Mon, 01 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3248869</guid>        </item>
        <item>
            <title>Membrane simulations mimicking acidic pH reveal increased thickness and negative curvature in a bilayer consisting of lysophosphatidylcholines and free fatty acids.</title>
            <link>http://www.medworm.com/index.php?rid=3248868&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20132791%26dopt%3DAbstract</link>
            <description>Authors: L&amp;#xE4;hdesm&amp;#xE4;ki K, Ollila OH, Koivuniemi A, Kovanen PT, Hyv&amp;#xF6;nen MT
    Phospholipids are key components of biological membranes and their lipolysis with phospholipase A(2) (PLA(2)) enzymes occurs in different cellular pH environments. Since no studies are available on the effect of pH on PLA(2)-modified phospholipid membranes, we performed 50-ns atomistic molecular dynamics simulations at three different pH conditions (pH 9.0, 7.5, and 5.5) using a fully PLA(2)-hydrolyzed phosphatidylcholine (PC) bilayer which consists solely of lysophosphatidylcholine and free fatty acid molecules. We found that a decrease in pH results in lateral squeezing of the membrane, i.e. in decreased surface area per headgroup. Thus, at the decreased pH, the lipid hydrocarbon chains had larger S...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3248868</comments>
            <pubDate>Mon, 01 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3248868</guid>        </item>
        <item>
            <title>Structure and function of the molecular chaperone Trigger Factor.</title>
            <link>http://www.medworm.com/index.php?rid=3248867&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20132842%26dopt%3DAbstract</link>
            <description>We describe recent progress on structural and dynamic aspects of Trigger Factor s interactions with the ribosome and substrates and discuss how these interactions affect co-translational protein folding. In addition, we discuss the newly proposed ribosome-independent function of Trigger Factor as assembly factor of multi-subunit protein complexes. Finally, we cover the functional cooperation between Trigger Factor, DnaK and GroEL in folding of cytosolic proteins and the interplay between Trigger Factor and other ribosome-associated factors acting in enzymatic processing and translocation of nascent polypeptide chains.
    PMID: 20132842 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3248867</comments>
            <pubDate>Mon, 01 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3248867</guid>        </item>
        <item>
            <title>Evidence for proteolytic processing and stimulated organelle redistribution of iPLA(2)beta.</title>
            <link>http://www.medworm.com/index.php?rid=3248866&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20132906%26dopt%3DAbstract</link>
            <description>Authors: Song H, Bao S, Lei X, Jin C, Zhang S, Turk J, Ramanadham S
    Over the past decade, important roles for the 84-88 kDa Group VIA Ca(2+)-independent phospholipase A(2) (iPLA(2)beta) in various organs have been described. We demonstrated that iPLA(2)beta participates in insulin secretion, insulinoma cells and native pancreatic islets express full-length and truncated isoforms of iPLA(2)beta, and certain stimuli promote perinuclear localization of iPLA(2)beta. To gain a better understanding of its mobilization, iPLA(2)beta was expressed in INS-1 cells as a fusion protein with EGFP, enabling detection of subcellular localization of iPLA(2)beta by monitoring EGFP fluorescence. Cells stably-transfected with fusion protein expressed nearly 5-fold higher catalytic iPLA(2)beta activity tha...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3248866</comments>
            <pubDate>Mon, 01 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3248866</guid>        </item>
        <item>
            <title>Sirtuin Chemical Mechanisms.</title>
            <link>http://www.medworm.com/index.php?rid=3248865&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20132909%26dopt%3DAbstract</link>
            <description>Authors: Sauve AA
    Sirtuins are ancient proteins widely distributed in all lifeforms of earth. These proteins are universally able to bind NAD(+), and activate it to effect ADP-ribosylation of cellular nucleophiles. The most commonly observed sirtuin reaction, is the ADPribosylation of acetyllysine, which leads to NAD(+)-dependent deacetylation. Other types of ADP-ribosylation have also been observed, including protein ADP-ribosylation, NAD(+) solvolysis and ADP-ribosyltransfer to 5,6-dimethylbenzimidazole, a reaction involved in eubacterial cobalamin biosynthesis. This review broadly surveys the chemistries and chemical mechanisms of these enzymes.
    PMID: 20132909 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3248865</comments>
            <pubDate>Mon, 01 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3248865</guid>        </item>
        <item>
            <title>Enzymatic catalysis with rapid turnover-carbonic anhydrase and superoxide dismutase.</title>
            <link>http://www.medworm.com/index.php?rid=3244643&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20129395%26dopt%3DAbstract</link>
            <description>Authors: Silverman DN
    
    PMID: 20129395 [PubMed - in process] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3244643</comments>
            <pubDate>Mon, 01 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3244643</guid>        </item>
        <item>
            <title>Nucleocytoplasmic glycosylation.</title>
            <link>http://www.medworm.com/index.php?rid=3236653&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20117275%26dopt%3DAbstract</link>
            <description>Authors: West CM
    
    PMID: 20117275 [PubMed - in process] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3236653</comments>
            <pubDate>Mon, 01 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3236653</guid>        </item>
        <item>
            <title>Special issue on &quot;Membrane Protein Dynamics: Correlating Structure to Function&quot;.</title>
            <link>http://www.medworm.com/index.php?rid=3219572&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20103412%26dopt%3DAbstract</link>
            <description>Authors: Veglia G, Ramamoorthy A
    
    PMID: 20103412 [PubMed - in process] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3219572</comments>
            <pubDate>Fri, 29 Jan 2010 15:50:06 +0100</pubDate>
            <guid isPermaLink="false">3219572</guid>        </item>
        <item>
            <title>Fifteen formins for an actin filament A molecular view on the regulation of human formins.</title>
            <link>http://www.medworm.com/index.php?rid=3219573&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20102729%26dopt%3DAbstract</link>
            <description>Authors: Sch&amp;#xF6;nichen A, Geyer M
    The regulation of the actin cytoskeleton is a key process for the stability and motility of eukaryotic cells. Besides the Arp2/3 complex and its nucleation promoting factors, WH2 domain containing proteins and a diverse family of formin proteins have recently been recognized as actin nucleators and potent polymerization factors of actin filaments. Formins are defined by the presence of a catalytic formin homology 2 (FH2) domain, yet, the modular domain architecture appears significantly different for the eight formin families identified in humans. A diverse picture of protein localization, interaction partners and cell specific regulation emerged, suggesting various functions of formins in the building and maintenance of actin filaments. This review ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3219573</comments>
            <pubDate>Sat, 23 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3219573</guid>        </item>
        <item>
            <title>Specific interaction between E2F1 and Sp1 regulates the expression of murine CTP:phosphocholine cytidylyltransferase alpha during the S phase.</title>
            <link>http://www.medworm.com/index.php?rid=3212820&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20096375%26dopt%3DAbstract</link>
            <description>In conclusion, the present results allowed us to portray the clearest picture of the CCTalpha-gene expression in proliferating cells, and understand the mechanism by which cells coordinate cell cycle progression with the requirement for phosphatidylcholine.
    PMID: 20096375 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212820</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212820</guid>        </item>
        <item>
            <title>Biophysical characterization and mutational analysis of the antibiotic resistance protein NimA from Deinococcus radiodurans.</title>
            <link>http://www.medworm.com/index.php?rid=3212818&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20096385%26dopt%3DAbstract</link>
            <description>Authors: Leiros HK, Brandsdala BO, McSweeney SM
    Metronidazole (MTZ) is an antibiotic commonly used to treat anaerobic bacterial infections in humans and animals. Antibiotic resistance toward this class of 5-nitroimidazole (5-Ni) drug derivatives has been related to the Nim genes thought to encode a reductase. Here we report the biophysical characteristics of the NimA protein from Deinococcus radiodurans (DrNimA) binding to MTZ and three other 5-Ni drugs. The interaction energies of the protein and antibiotic are studied by isothermal titration calorimetry (ITC) and with free energy and linear interaction energy (LIE) calculations, where the latter method revealed that the antibiotic binding is mainly of hydrophobic character. ITC measurements further found that one DrNimA dimer has two...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212818</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212818</guid>        </item>
        <item>
            <title>Energy conservation by Rhodothermus marinus respiratory complex I.</title>
            <link>http://www.medworm.com/index.php?rid=3212808&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100453%26dopt%3DAbstract</link>
            <description>Authors: Batista AP, Fernandes AS, Louro RO, Steuber J, Pereira MM
    A sodium ion efflux, together with a proton influx and an inside-positive DeltaPsi, was observed during NADH-respiration by Rhodothermus marinus membrane vesicles. Proton translocation was monitored by fluorescence spectroscopy and sodium ion transport by (23)Na-NMR spectroscopy. Specific inhibitors of complex I (rotenone) and of the dioxygen reductase (KCN) inhibited the proton and the sodium ion transport, but the KCN effect was totally reverted by the addition of menaquinone analogues, indicating that both transports were catalyzed by complex I. We concluded that the coupling ion of the system is proton and that neither the catalytic reaction nor the establishment of the delta-pH are dependent on sodium, but the pres...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212808</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212808</guid>        </item>
        <item>
            <title>Ceramide channels and their role in mitochondria-mediated apoptosis.</title>
            <link>http://www.medworm.com/index.php?rid=3212807&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100454%26dopt%3DAbstract</link>
            <description>Authors: Colombini M
    A key, decision-making step in apoptosis is the release of proteins from the mitochondrial intermembrane space. Ceramide can self-assemble in the mitochondrial outer membrane to form large stable channels capable of releasing said proteins. Ceramide levels measured in mitochondria early in apoptosis are sufficient to form ceramide channels in the outer membrane. The channels are in dynamic equilibrium with non-conducting forms of ceramide in the membrane. This equilibrium can be strongly influenced by other sphingolipids and Bcl-2 family proteins. The properties of ceramide channels formed in a defined system, planar phospholipid membranes, demonstrate that proteins are not required for channel formation. In addition, experiments in the defined system reveal struct...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212807</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212807</guid>        </item>
        <item>
            <title>Detection and manipulation of mitochondrial reactive oxygen species in mammalian cells.</title>
            <link>http://www.medworm.com/index.php?rid=3212806&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100455%26dopt%3DAbstract</link>
            <description>Authors: Forkink M, Smeitink JA, Brock R, Willems PH, Koopman WJ
    Reactive oxygen species (ROS) are formed upon incomplete reduction of molecular oxygen (O(2)) as an inevitable consequence of mitochondrial metabolism. Because ROS can damage biomolecules, cells contain elaborate antioxidant defense systems to prevent oxidative stress. In addition to their damaging effect, ROS can also operate as intracellular signaling molecules. Given the fact that mitochondrial ROS appear to be only generated at specific sites and that particular ROS species display a unique chemistry and have specific molecular targets, mitochondria-derived ROS might constitute local regulatory signals. The latter would allow individual mitochondria to auto-regulate their metabolism, shape and motility, enabling them ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212806</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212806</guid>        </item>
        <item>
            <title>Mutation of the Heme Axial Ligand of Escherichia coli Succinate-Quinone Reductase: Implications for Heme Ligation in Mitochondrial Complex II from Yeast.</title>
            <link>http://www.medworm.com/index.php?rid=3212805&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100456%26dopt%3DAbstract</link>
            <description>In this report, the role of Cys residues for heme coordination in the complex II family of enzymes is addressed. Cys was substituted to the SdhD-71 position and the yeast Tyr71Cys72 motif also recreated. The Cys71 variant retained heme, although it was high spin, while the Tyr71Cys72 mutant lacked heme. Previously the presence of heme in S. cerevisiae was detected by a spectral peak in fumarate-oxidized, dithionite-reduced mitochondria. Here it is shown that this method must be used with caution. Comparison of bovine and yeast mitochondrial membranes shows that fumarate induced reoxidation of cytochromes in both SQR and the bc(1) complex (ubiquinol-cytochrome c reductase). Thus, this report raises a concern about the presence of low spin heme b in S. cerevisiae complex II.
    PMID: 201004...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212805</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212805</guid>        </item>
        <item>
            <title>The Membrane Insertion of Helical Antimicrobial Peptides from the N-Terminus of Helicobacter pylori Ribosomal Protein L1.</title>
            <link>http://www.medworm.com/index.php?rid=3212804&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100457%26dopt%3DAbstract</link>
            <description>Authors: Lee TH, Hall KN, Swann MJ, Popplewell JF, Unabia S, Park Y, Hahm KS, Aguilar MI
    The interaction of two helical antimicrobial peptides, HPA3 and HPA3P with planar supported lipid membranes was quantitatively analysed using two complementary optical biosensors. The peptides are analogues of Hp(2-20) derived from the N-terminus of Helicobacter pylori ribosomal protein L1 (RpL1). The binding of these two peptide analogues to zwitterionic dimyristoyl-phosphatidylcholine (DMPC) and negatively charged membranes composed of DMPC/dimyristoylphosphatidylglycerol (DMPG) (4:1) was determined using surface plasmon resonance (SPR) and dual polarisation interferometry (DPI). Using SPR analysis, it was shown that the proline substitution in HPA3P resulted in much lower binding for both zwitte...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212804</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212804</guid>        </item>
        <item>
            <title>Liquid ordered phase in cell membranes evidenced by a hydration-sensitive probe: Effects of cholesterol depletion and apoptosis.</title>
            <link>http://www.medworm.com/index.php?rid=3212803&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100458%26dopt%3DAbstract</link>
            <description>Authors: Oncul S, Klymchenko AS, Kucherak OA, Demchenko AP, Martin S, Dontenwill M, Arntz Y, Didier P, Duportail G, M&amp;#xE9;ly Y
    Herein, using a recently developed hydration-sensitive ratiometric biomembrane probe based on 3-hydroxyflavone (F2N12S) that binds selectively to the outer leaflet of plasma membranes, we compared plasma membranes of living cells and lipid vesicles as model membranes. Through the spectroscopic analysis of the probe response, we characterized the membranes in terms of hydration and polarity (electrostatics). The hydration parameter value in cell membranes was in between the values obtained with liquid ordered (Lo) and liquid disordered (Ld) phases in model membranes, suggesting that cell plasma membranes exhibit a significant fraction of Lo phase in their outer...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212803</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212803</guid>        </item>
        <item>
            <title>Protein import into chloroplasts: The Tic complex and its regulation.</title>
            <link>http://www.medworm.com/index.php?rid=3212802&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100520%26dopt%3DAbstract</link>
            <description>Authors: Kov&amp;#xE1;cs-Bogd&amp;#xE1;n E, Soll J, B&amp;#xF6;lter B
    Chloroplasts like mitochondria derived from an endosymbiontic event. Due to the massive gene transfer to the nucleus during endosymbiosis, only a limited number of chloroplastic proteins are still encoded for in the plastid genome. Most of the nuclear-encoded plastidic proteins are post-translationally translocated back to the chloroplast via the general import pathway through distinct outer and inner envelope membrane protein complexes, the Toc and Tic translocons (Translocon at the outer/inner envelope membrane of chloroplasts). Eight Tic subunits have been described so far, including two potential channel proteins (Tic110 and Tic20), the &quot;motor complex&quot; (Tic40 associated with the stromal chaperone Hsp93) and the &quot;redox regulo...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212802</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212802</guid>        </item>
        <item>
            <title>Conserved amino acid residues in C-terminus of PERIOD 2 are involved in interaction with CRYPTOCHROME 1.</title>
            <link>http://www.medworm.com/index.php?rid=3212801&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100521%26dopt%3DAbstract</link>
            <description>Authors: Tomita T, Miyazaki K, Onishi Y, Honda S, Ishida N, Oishi K
    We investigated the amino acid sequences of rat PERIOD2 (rPER2) that are required for interaction with CRYPTOCHROME1 (CRY1) to understand the molecular mechanism of the circadian clock. Co-immunoprecipitation assays using various C-terminal fragments of rPER2 with internal deletions revealed that amino acid residues 1179-1198 are necessary for interaction with CRY1. To identify precisely which amino acid residues are responsible for the interaction, we substituted alanine for residues conserved among PER isoforms and species. We found that more than three mutations of conserved PER2 residues impaired not only binding to CRY1 but also subsequent nuclear translocation, although mutations of non-conserved residues did not...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212801</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212801</guid>        </item>
        <item>
            <title>Viruses as vesicular carriers of the viral genome: A functional module perspective.</title>
            <link>http://www.medworm.com/index.php?rid=3212800&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100522%26dopt%3DAbstract</link>
            <description>Authors: Thaa B, Hofmann KP, Veit M
    Enveloped viruses and cellular transport vesicles share obvious morphological and functional properties. Both are composed of a closed membrane, which is lined with coat-proteins and encases cargo. Transmembrane proteins inserted into the membrane define the target membrane area with which the vesicle or virus is destined to fuse. Here we discuss recent insight into the functioning of enveloped viruses in the framework of the &quot;functional module&quot; concept. Vesicular transport is an exemplary case of a functional module, as defined as a part of the proteome that assembles to perform a specific autonomous function in a living cell. Cellular vesicles serve to transport cargo between membranous organelles inside the cell, while enveloped viruses can be see...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212800</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212800</guid>        </item>
        <item>
            <title>On the mechanism of preprotein import by the mitochondrial presequence translocase.</title>
            <link>http://www.medworm.com/index.php?rid=3212799&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100523%26dopt%3DAbstract</link>
            <description>Authors: van der Laan M, Hutu DP, Rehling P
    Mitochondria are organelles of endosymbiontic origin that contain more than one thousand different proteins. The vast majority of these proteins is synthesized in the cytosol and imported into one of four mitochondrial subcompartments: outer membrane, intermembrane space, inner membrane and matrix. Several import pathways exist and are committed to different classes of precursor proteins. The presequence translocase of the inner mitochondrial membrane (TIM23 complex) mediates import of precursor proteins with cleavable amino-terminal presequences. Presequences direct precursors across the inner membrane. The combination of this presequence with adjacent regions determines if a precursor is fully translocated into the matrix or laterally sorte...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212799</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212799</guid>        </item>
        <item>
            <title>Influence of different estrogens on neuroplasticity and cognition in the hippocampus.</title>
            <link>http://www.medworm.com/index.php?rid=3212798&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100545%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: Different forms of estrogens modulate neuroplasticity and cognition in complex and intriguing ways. Specifically, estrogens upregulate adult hippocampal neurogenesis (via cell proliferation) and synaptic protein levels in the hippocampus in a time- and dose-dependent manner. Low levels of estradiol facilitate spatial working memory and contextual fear conditioning while high levels of estradiol impair spatial working, spatial reference memory and contextual fear conditioning. In addition, estrone impairs contextual fear conditioning. GENERAL SIGNIFICANCE: Advances in our knowledge of how estrogens exert their effects on the brain may ultimately lead to refinements in targeted therapies for cognitive impairments at all stages of life. However caution should be taken in interpre...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212798</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212798</guid>        </item>
        <item>
            <title>Phytoferritin and its implications for human health and nutrition.</title>
            <link>http://www.medworm.com/index.php?rid=3212797&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100546%26dopt%3DAbstract</link>
            <description>This study focuses on the relationship between structure and function of phytoferritin and the recent progress in the use of phytoferritin as iron supplement.
    PMID: 20100546 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212797</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212797</guid>        </item>
        <item>
            <title>Enhanced thermal and ultrasonic stability of a fungal protease encapsulated within biomimetically generated silicate nanospheres.</title>
            <link>http://www.medworm.com/index.php?rid=3212796&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100547%26dopt%3DAbstract</link>
            <description>CONCLUSION: PAMAM dendrimer generation 0 could be effectively used for rapid encapsulation of a fungal protease from Aspegilus Oryzae. GENERAL SIGNIFICANCE: Encapsulation significantly enhances the thermal and ultrasonic stabilities of enzymes, suggesting a range of diverse applications for them.
    PMID: 20100547 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212796</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212796</guid>        </item>
        <item>
            <title>The critical period hypothesis of estrogen effects on cognition: Insights from basic research.</title>
            <link>http://www.medworm.com/index.php?rid=3212795&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100548%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: Results of basic research provide support for the critical period hypothesis. Furthermore, results of work in rodent models suggest mechanisms by which the response to estrogen is altered if treatment is initiated following long-term ovarian hormone deprivation. GENERAL SIGNIFICANCE: Understanding if and under what conditions hormone administration following the loss of ovarian function positively affects the brain and behavior could have important implications with regard to female cognitive aging. Results of basic research can contribute to this understanding and provide insight into the complex mechanisms by which estrogen affects cognition.
    PMID: 20100548 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212795</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212795</guid>        </item>
        <item>
            <title>Critical role of interfaces and agitation on the nucleation of Abeta amyloid fibrils at low concentrations of Abeta monomers.</title>
            <link>http://www.medworm.com/index.php?rid=3212794&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100601%26dopt%3DAbstract</link>
            <description>Authors: Morinaga A, Hasegawa K, Nomura R, Ookoshi T, Ozawa D, Goto Y, Yamada M, Naiki H
    Amyloid deposits are pathological hallmarks of various neurodegenerative diseases including Alzheimer's disease (AD), where amyloid beta-peptide (Abeta) polymerizes into amyloid fibrils by a nucleation-dependent polymerization mechanism. The biological membranes or other interfaces as well as the convection of the extracellular fluids in the brain may influence Abeta amyloid fibril formation in vivo. Here, we examined the polymerization kinetics of 2.5, 5, 10 and 20muM Abeta in the presence or absence of air-water interface (AWI) using fluorescence spectroscopy and florescence microscopy with the amyloid specific dye, thioflavin T. When the solutions were incubated with AWI and in quiescence, amylo...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212794</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212794</guid>        </item>
        <item>
            <title>Evolutionary conservation of heavy chain protein transfer between glycosaminoglycans.</title>
            <link>http://www.medworm.com/index.php?rid=3212793&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100602%26dopt%3DAbstract</link>
            <description>Authors: Sanggaard KW, Hansen L, Scavenius C, Wisniewski HG, Kristensen T, Th&amp;#xF8;gersen IB, Enghild JJ
    The bikunin proteins are composed of heavy chains (HCs) covalently linked to a chondroitin sulfate chain originating from Ser-10 of bikunin. Tumor necrosis factor stimulated gene-6 protein (TSG-6) / heavy chain 2 (HC2) cleaves this unique cross-link and transfers the HCs to hyaluronan and other glycosaminoglycans via a covalent HC*TSG-6 intermediate. In the present study, we have investigated if this reaction is evolutionary conserved based on the hypothesis that it is of fundamental importance. The results revealed that plasma/serum samples from mammal, bird, and reptile were able to form TSG-6 complexes suggesting the presence of proteins with the same function as the human bikuni...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212793</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212793</guid>        </item>
        <item>
            <title>PONDR-FIT: A meta-predictor of intrinsically disordered amino acids.</title>
            <link>http://www.medworm.com/index.php?rid=3212792&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100603%26dopt%3DAbstract</link>
            <description>Authors: Xue B, Dunbrack RL, Williams RW, Dunker AK, Uversky VN
    Protein intrinsic disorder is becoming increasingly recognized in proteomics research. While lacking structure, many regions of disorder have been associated with biological function. There are many different experimental methods for characterizing intrinsically disordered proteins and regions; nevertheless, the prediction of intrinsic disorder from amino acid sequence remains a useful strategy especially for many large-scale proteomics investigations. Here we introduced a consensus artificial neural network (ANN) prediction method, which was developed by combining the outputs of several individual disorder predictors. By eight-fold cross-validation, this meta-predictor, called PONDR-FIT, was found to improve the predictio...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212792</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212792</guid>        </item>
        <item>
            <title>hnRNP H1 and intronic G runs in the splicing control of the human rpL3 gene.</title>
            <link>http://www.medworm.com/index.php?rid=3212791&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100605%26dopt%3DAbstract</link>
            <description>Authors: Russo A, Siciliano G, Catillo M, Giangrande C, Amoresano A, Pucci P, Pietropaolo C, Russo G
    By generating mRNA containing a premature termination codon (PTC), alternative splicing (AS) can quantitatively regulate the expression of genes that are degraded by nonsense-mediated mRNA decay (NMD). We previously demonstrated that AS-induced retention of part of intron 3 of rpL3 pre-mRNA produces an mRNA isoform that contains a PTC and is targeted for decay by NMD. We also demonstrated that overexpression of rpL3 downregulates canonical splicing and upregulates the alternative splicing of its pre-mRNA. We are currently investigating the molecular mechanism underlying rpL3 autoregulation. Here we report that the heterogeneous nuclear ribonucleoprotein (hnRNP) H1 is a transacting facto...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212791</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212791</guid>        </item>
        <item>
            <title>Structural characterization of H3K56Q nucleosomes and nucleosomal arrays.</title>
            <link>http://www.medworm.com/index.php?rid=3212790&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100606%26dopt%3DAbstract</link>
            <description>Authors: Watanabe S, Resch M, Lilyestrom W, Clark N, Hansen JC, Peterson C, Luger K
    The posttranslational modification of histones is a key mechanism for the modulation of DNA accessibility. Acetylated lysine 56 in histone H3 is associated with nucleosome assembly during replication and DNA repair, and is thus likely to predominate in regions of chromatin containing nucleosome free regions. Here we show by x-ray crystallography that mutation of H3 lysine 56 to glutamine (to mimic acetylation) or glutamate (to cause a charge reversal) has no detectable effects on the structure of the nucleosome. At the level of higher order chromatin structure, the K to Q substitution has no effect on the folding of model nucleosomal arrays in cis, regardless of the degree of nucleosome density. In cont...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212790</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212790</guid>        </item>
        <item>
            <title>Photosystem I light-harvesting complex Lhca4 adopts multiple conformations: Red forms and excited-state quenching are mutually exclusive.</title>
            <link>http://www.medworm.com/index.php?rid=3212817&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20097154%26dopt%3DAbstract</link>
            <description>Authors: Passarini F, Wientjes E, van Amerongen H, Croce R
    In this work we have investigated the origin of the mutiexponential fluorescence decay and of the short excited-state lifetime of Lhca4. Lhca4 is the antenna complex of Photosystem I which accommodates the red-most chlorophyll forms and it has been proposed that these chlorophylls can play a role in the flourescence quenching. Here we have compared the fluorescence decay of Lhca4 with that of several Lhca4 mutants that are affected in their red-form content. The results show that neither the multiexponentiality of the decay nor the fluorescence quenching are due to the red forms. The data indicate that Lhca4 exists in multiple conformations. The presence of the red forms, which are very sensitive to changes in the environment, ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212817</comments>
            <pubDate>Thu, 21 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212817</guid>        </item>
        <item>
            <title>Horseradish peroxidase catalyzed oxidation of chlorophyll a with hydrogen peroxide. Characterization of the products and mechanism of the reaction.</title>
            <link>http://www.medworm.com/index.php?rid=3212816&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20097155%26dopt%3DAbstract</link>
            <description>Authors: Hynninen PH, Kaartinen V, Kolehmainen E
    Horseradish peroxidase was verified to catalyze, without any phenol, the hydrogen peroxide oxidation of chlorophyll a (Chl a), solubilized with Triton X-100. The 13(2)(S) and 13(2)(R) diastereomers of 13(2)-hydroxyChl a were characterized as major oxidation products (ca. 60%) by TLC on sucrose, UV-vis, (1)H, and (13)C NMR spectra, as well as fast-atom bombardment MS. A minor amount of the 15(2)-methyl, 17(3)-phytyl ester of Mg-unstable chlorin was identified on the basis of its UV-vis spectrum and reactivity with diazomethane, which converted it to the 13(1),15(2)-dimethyl, 17(3)-phytyl ester of Mg-purpurin 7. The side products (ca. 10%) were suggested to include the 17(3)-phytyl ester of Mg-purpurin 18, which is known to form easily fro...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212816</comments>
            <pubDate>Thu, 21 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212816</guid>        </item>
        <item>
            <title>Photoconsumption of molecular oxygen on both donor and acceptor sides of photosystem II in Mn-depleted subchloroplast membrane fragments.</title>
            <link>http://www.medworm.com/index.php?rid=3212815&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20097156%26dopt%3DAbstract</link>
            <description>Authors: Yanykin DV, Khorobrykh AA, Khorobrykh SA, Klimov VV
    Oxygen consumption in Mn-depleted photosystem II (PSII) preparations under continuous and pulsed illumination is investigated. It is shown that removal of manganese from the water-oxidizing complex (WOC) by high pH treatment leads to a 6-fold increase in the rate of O(2) photoconsumption. The use of exogenous electron acceptors and donors to PSII shows that in Mn-depleted PSII preparations along with the well-known effect of O(2) photoreduction on the acceptor side of PSII, there is light-induced O(2) consumption on the donor side of PSII (nearly 30% and 70%, respectively). It is suggested that the light-induced O(2) uptake on the donor side of PSII is related to interaction of O(2) with radicals produced by photooxidation of...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212815</comments>
            <pubDate>Thu, 21 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212815</guid>        </item>
        <item>
            <title>Clearance of Rhodopsin(P23H) aggregates requires the ERAD effector VCP.</title>
            <link>http://www.medworm.com/index.php?rid=3212814&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20097236%26dopt%3DAbstract</link>
            <description>Authors: Griciuc A, Aron L, Piccoli G, Ueffing M
    Dominant mutations in the visual pigment Rhodopsin (Rh) cause retinitis pigmentosa (RP) characterized by progressive blindness and retinal degeneration. The most common Rh mutation, Rh(P23H) forms aggregates in the endoplasmic reticulum (ER) and impairs the proteasome; however, the mechanisms linking Rh aggregate formation to proteasome dysfunction and photoreceptor cell loss remain unclear. Using mammalian cell cultures, we provide the first evidence that misfolded Rh(P23H) is a substrate of the ERAD effector VCP, an ATP-dependent chaperone that extracts misfolded proteins from the ER and escorts them for proteasomal degradation. VCP co-localizes with misfolded Rh(P23H) in retinal cells and requires functional N-terminal and D1 ATPase d...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212814</comments>
            <pubDate>Thu, 21 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212814</guid>        </item>
        <item>
            <title>Contributions of estrogen receptor-alpha and estrogen receptor-beta to the regulation of behavior.</title>
            <link>http://www.medworm.com/index.php?rid=3212813&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20097268%26dopt%3DAbstract</link>
            <description>Authors: Tetel MJ, Pfaff DW
    
    PMID: 20097268 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212813</comments>
            <pubDate>Thu, 21 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212813</guid>        </item>
        <item>
            <title>Residue 234 is a Master Switch of the Alternative-Substrates Activity Profile of Human and Rodent Theta Class Glutathione Transferase T1-1.</title>
            <link>http://www.medworm.com/index.php?rid=3212812&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20097269%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: H-site residue 234 has a key role in governing the activity and substrate selectivity profile of GST T1-1. GENERAL SIGNIFICANCE: The functional divergence between human and rodent Theta class GST demonstrates that a single point mutation can enable or suppress enzyme activities with different substrates.
    PMID: 20097269 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212812</comments>
            <pubDate>Thu, 21 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212812</guid>        </item>
        <item>
            <title>Increased SOD1 association with chromatin, DNA damage, p53 activation, and apoptosis in a cellular model of SOD1-linked ALS.</title>
            <link>http://www.medworm.com/index.php?rid=3212811&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20097285%26dopt%3DAbstract</link>
            <description>Authors: Barbosa LF, Cerqueira FM, Macedo AF, Garcia CC, Angeli JP, Schumacher RI, Sogayar MC, Augusto O, Carr&amp;#xEC; MT, Di Mascio P, Medeiros MH
    Mutations in the gene encoding cytosolic Cu,Zn-superoxide dismutase (SOD1) have been linked to familial amyotrophic lateral sclerosis (FALS). However the molecular mechanisms of motor neuron death are multi-factorial and remain unclear. Here we examined DNA damage, p53 activity and apoptosis in SH-SY5Y human neuroblastoma cells transfected to achieve low-level expression of either wild-type or mutant Gly(93)--&amp;gt; Ala (G93A) SOD1, typical of FALS. DNA damage was investigated by evaluating the levels of 8-oxo-7,8-dihydro-2 -deoxyguanosine (8-oxodGuo) and DNA strand breaks. Significantly higher levels of DNA damage, increased p53 activity, and ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212811</comments>
            <pubDate>Thu, 21 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212811</guid>        </item>
        <item>
            <title>Expression proteomics of acute promyelocytic leukaemia cells treated with methotrexate.</title>
            <link>http://www.medworm.com/index.php?rid=3212810&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20097313%26dopt%3DAbstract</link>
            <description>Authors: Agarwal NK, Mueller GA, Mueller CA, Streich JH, Asif AR, Dihazi H
    Methotrexate was first introduced as a cytotoxic agent that inhibits nucleotide biosynthesis in various cancer disorders; its molecular mechanism remains elusive. To understand the molecular mechanism by which methotrexate induces apoptosis, we analyzed the resulting intracellular protein changes in methotrexate-treated acute promyelocytic leukaemia (HL-60) cells by cysteine-labeled differential in-gel electrophoresis (CL-DIGE) combined with mass spectrometry. Initial CL-DIGE analysis revealed that 24 proteins were differentially expressed (p&amp;lt;0.05) in the HL-60 cell proteome after treatment with 2.5microM methotrexate for 72h. We found that three structural alpha4, alpha5, alpha7 proteasome subunits, a non-ca...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212810</comments>
            <pubDate>Thu, 21 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212810</guid>        </item>
        <item>
            <title>Translocation by multi-subunit RNA polymerases.</title>
            <link>http://www.medworm.com/index.php?rid=3212809&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20097318%26dopt%3DAbstract</link>
            <description>Authors: Kireeva M, Kashlev M, Burton ZF
    DNA template and RNA/DNA hybrid movement through RNA polymerase (RNAP) is referred to as &quot;translocation&quot;. Because nucleic acid movement is coupled to NTP loading, pyrophosphate release, and conformational changes, the precise ordering of events during bond addition is consequential. Moreover, based on several lines of experimental evidence, translocation, pyrophosphate release or an associated conformational change may determine the transcription elongation rate. In this review we discuss various models of translocation, the data supporting the hypothesis that translocation rate determines transcription elongation rate and also data that may be inconsistent with this point of view. A model of the nucleotide addition cycle accommodating available...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212809</comments>
            <pubDate>Thu, 21 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212809</guid>        </item>
        <item>
            <title>Preferential insertion of lactose permease in phospholipid domains: AFM observations.</title>
            <link>http://www.medworm.com/index.php?rid=3212821&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20096263%26dopt%3DAbstract</link>
            <description>We report the insertion of a transmembrane protein, lactose permease (LacY) from Escherichia coli (E. coli), in supported lipid bilayers (SLBs) of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol (POPG), in biomimetic molar proportions. We provide evidence of the preferential insertion of LacY in the fluid domains. Analysis of the self-assembled protein arrangements showed that LacY: (i) is inserted as a monomer within fluid domains of SLBs of POPE:POPG (3:1, mol/mol), (ii) has a diameter of approx. 7.8nm; and (iii) keeps an area of phospholipids surrounding the protein that is compatible with shells of phospholipids.
    PMID: 20096263 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212821</comments>
            <pubDate>Wed, 20 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212821</guid>        </item>
        <item>
            <title>Structure-function relationships in feedback regulation of energy fluxes in vivo in health and disease: Mitochondrial interactosome.</title>
            <link>http://www.medworm.com/index.php?rid=3212823&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20096261%26dopt%3DAbstract</link>
            <description>Authors: Valdur S, Rita G, Natalja T, Kersti T, Minna V, Claire M, Nathalie B, Tuuli K, Andrey K, Lumme K, Eimre M, Enn S
    The aim of this review is to analyze the results of experimental research of mechanisms of regulation of mitochondrial respiration in cardiac and skeletal muscle cells in vivo obtained by using the permeabilized cell technique. Such an analysis in the framework of Molecular Systems Bioenergetics shows that the mechanisms of regulation of energy fluxes depend on structural organization of the cells and interaction of mitochondria with cytoskeletal elements. Two types of cells of cardiac phenotype with very different structure were analyzed: adult cardiomyocytes and continuously dividing cancerous HL-1 cells. In cardiomyocytes mitochondria are arranged very regularly,...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212823</comments>
            <pubDate>Tue, 19 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212823</guid>        </item>
        <item>
            <title>A study of cytochrome bo(3) in a tethered bilayer lipid membrane.</title>
            <link>http://www.medworm.com/index.php?rid=3212822&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20096262%26dopt%3DAbstract</link>
            <description>Authors: Weiss SA, Bushby RJ, Evans SD, Jeuken LJ
    An assay has been developed in which the activity of an ubiquinol oxidase from Escherichia coli, cytochrome bo(3) (cbo(3)), is determined as a function of the hydrophobic substrate ubiquinol-10 (UQ-10) in tethered lipid bilayers membranes (tBLMs). UQ-10 was added in situ, while the enzyme activity and the UQ-10 concentration in the membrane have been determined by cyclic voltammetry. Cbo(3) is inhibited by UQ-10 at concentrations above 5-10pmol/cm(2), while product inhibition is absent. Cyclic voltammetry has also been used to characterise the effects of three inhibitors; Cyanide, inhibiting oxygen reduction; 2-n-Heptyl-4-hydroxyquinoline N-oxide (HQNO), inhibiting the quinone oxidation and Zn(II), thought to block the proton channels r...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212822</comments>
            <pubDate>Tue, 19 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212822</guid>        </item>
        <item>
            <title>Mutagenesis and subsite mapping underpin the importance for substrate specificity of the aglycon subsites of glycoside hydrolase family 11 xylanases.</title>
            <link>http://www.medworm.com/index.php?rid=3212819&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20096384%26dopt%3DAbstract</link>
            <description>Authors: Pollet A, Lagaert S, Eneyskaya E, Kulminskaya A, Delcour JA, Courtin CM
    Glycoside hydrolase family (GH) 11 xylanase A from Bacillus subtilis (BsXynA) was subjected to site-directed mutagenesis to probe the role of aglycon active site residues with regard to activity, binding of decorated substrates and hydrolysis product profile. Targets were those amino acid identified to be important by 3D structure analysis of BsXynA in complex with substrate bound in the glycon subsites and the +1 aglycon subsite. Several aromatic residues in the aglycon subsites that make strong substrate-protein interactions and that are indispensable for enzyme activity, were also important for the specificity of the xylanase. In the +2 subsite of BsXynA, Tyr65 and Trp129 were identified as residues tha...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3212819</comments>
            <pubDate>Tue, 19 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3212819</guid>        </item>
        <item>
            <title>Mitochondria isolated in nearly isotonic KCl buffer: Focus on cardiolipin and organelle morphology.</title>
            <link>http://www.medworm.com/index.php?rid=3200971&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20093104%26dopt%3DAbstract</link>
            <description>Authors: Corcelli A, Saponetti MS, Zaccagnino P, Lopalco P, Mastrodonato MG, Liquori GE, Lorusso M
    Rat liver mitochondria were isolated in parallel in two different isolation buffers: a standard buffer containing mannitol/sucrose and a nearly physiological KCl based solution. The two different organelle preparations were comparatively characterized by respiratory activity, heme content, microsomal and Golgi contamination, electron microscopy and lipid analyses. The substitution of saccharides with KCl in the isolation buffer does not induce the formation of mitoplasts or disruption of mitochondria. Mitochondria isolated in KCl buffer are coupled and able to maintain a stable transmembrane charge separation. A number of biochemical and functional differences between the two organelle pr...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3200971</comments>
            <pubDate>Mon, 18 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3200971</guid>        </item>
        <item>
            <title>Restoring the activity of serum-inhibited bovine lung extract surfactant (BLES) using cationic additives.</title>
            <link>http://www.medworm.com/index.php?rid=3200970&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20093105%26dopt%3DAbstract</link>
            <description>Authors: Acosta EJ, Policova Z, Lee S, Dang A, Hair ML, Neumann AW
    In this work four cationic additives were used to improve the surface activity of lung surfactants, particularly in the presence of bovine serum that was used as a model surfactant inhibitor. Two of those additives were chitosan in its soluble hydrochloride form with average molecular weights of 113KDa and 213KDa. The other two additives were cationic peptides, polylysine 50KDa and polymyxin B. These additives were added to bovine lipid extract surfactant (BLES) and the optimal additive-surfactant ratio was determined based on the minimum surface tension upon dynamic compression carried out in a constrained sessile drop (CSD) device in the presence of 50mul/ml serum. At the optimal ratio all the BLES-additive mixtures w...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3200970</comments>
            <pubDate>Mon, 18 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3200970</guid>        </item>
        <item>
            <title>Evolution and disease converge in the mitochondrion.</title>
            <link>http://www.medworm.com/index.php?rid=3177851&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20074547%26dopt%3DAbstract</link>
            <description>Authors: Mishmar D, Zhidkov I
    Mitochondrial DNA (mtDNA) mutations are long known to cause diseases but also underlie tremendous population divergence in humans. It was assumed that the two types of mutations differ in one major trait: functionality. However, evidence from disease association studies, cell culture and animal models support the functionality of common mtDNA genetic variants, leading to the hypothesis that disease-causing mutations and mtDNA genetic variants share considerable common features. Here we provide evidence showing that the two types of mutations obey the rules of evolution, including random genetic drift and natural selection. This similarity does not only converge at the principle level; rather, disease- causing mutations could recapitulate the ancestral DNA ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3177851</comments>
            <pubDate>Mon, 11 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3177851</guid>        </item>
        <item>
            <title>Palmitoylation of R-Ras by human DHHC19, a palmitoyl transferase with a CaaX box.</title>
            <link>http://www.medworm.com/index.php?rid=3177850&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20074548%26dopt%3DAbstract</link>
            <description>Authors: Baumgart F, Corral-Escariz M, P&amp;#xE9;rez-Gil J, Rodr&amp;#xED;guez-Crespo I
    Mammalian proteins that contain an aspartate-histidine-histidine-cysteine-(DHHC) motif have been recently identified as a group of membrane-associated palmitoyl acyltransferases (PATs). Among the several protein substrates known to become palmitoylated by DHHC PATs are small GTPases prenylated at their carboxy-terminal end, such as H-Ras or N-Ras, eNOS, kinases myristoylated at their N-terminal end, such as Lck, and many transmembrane proteins and channels. We have focused our studies on the product of the human gene DHHC19, a putative palmitoyl transferase that, interestingly, displays a conserved CaaX box at its carboxy terminal end. We show herein that the amino acid sequence present at the carboxy-term...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3177850</comments>
            <pubDate>Mon, 11 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3177850</guid>        </item>
        <item>
            <title>DARPP-32 binds to tra2-beta1 and influences alternative splicing.</title>
            <link>http://www.medworm.com/index.php?rid=3177849&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20074680%26dopt%3DAbstract</link>
            <description>Authors: Benderska N, Becker K, Girault JA, Becker CM, Andreadis A, Stamm S
    The majority of human genes undergo alternative splicing, which is frequently altered in response to physiological stimuli. DARPP-32 (Dopamine and cAMP regulated phosphoprotein, 32 kD) is a component of PKA-dependent signaling pathways. Here we show that DARPP-32 binds directly to the splicing factor tra2-beta1 (transformer 2). DARPP-32 changes the usage of tra2-beta1 dependent alternative exons in a concentration dependent manner, suggesting that the DARPP-32:tra2-beta1 interaction is a molecular link between signaling pathways and pre-mRNA processing.
    PMID: 20074680 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3177849</comments>
            <pubDate>Mon, 11 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3177849</guid>        </item>
        <item>
            <title>Tissue-specific forkhead protein foxa2 up-regulates sox14 gene expression.</title>
            <link>http://www.medworm.com/index.php?rid=3177848&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20074681%26dopt%3DAbstract</link>
            <description>Authors: Popovic J, Klajn A, Petrovic I, Stevanovic M
    The expression of Sox14 gene in spinal cord explants was found to be regulated by Sonic hedgehog (SHH) in a dose-dependent manner, indicating that this signaling molecule might act as an regulator of Sox14-expressing interneuron differentiation. In the present study we identified the positive control element and provided the first evidence that FOXA2 is involved in up-regulation of SOX14 expression in HepG2 and U87MG cell lines. By functional analysis we demonstrated that mutation in FOXA2 binding site reduced the SOX14 reporter construct activity, and that FOXA2 over-expression increased endogenous SOX14 protein expression. Further, we have shown that human SOX14 expression is GLI1 depended in U87MG cells and SHH-N dependent in U87...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3177848</comments>
            <pubDate>Mon, 11 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3177848</guid>        </item>
        <item>
            <title>Identification of a slowly inducible zeaxanthin-dependent component of non-photochemical quenching of chlorophyll fluorescence generated under steady state conditions in Arabidopsis.</title>
            <link>http://www.medworm.com/index.php?rid=3172311&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20067757%26dopt%3DAbstract</link>
            <description>Authors: Nilkens M, Kress E, Lambrev P, Miloslavina Y, M&amp;#xFC;ller M, Holzwarth AR, Jahns P
    The induction and relaxation of non-photochemical quenching (NPQ) under steady state conditions, i.e. during up to 90min of illumination at saturating light intensities, was studied in Arabidopsis thaliana. Besides the well-characterized fast qE and the very slow qI component of NPQ, the analysis of the NPQ dynamics identified a zeaxanthin (Zx) dependent component which we term qZ. The formation (rise time 10-15min) and relaxation (life time 10-15min) of qZ correlated with the synthesis and epoxidation of Zx, respectively. Comparative analysis of different NPQ mutants from Arabidopsis showed that qZ was clearly not related to qE, qT or qI and thus represents a separate, Zx dependent NPQ componen...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3172311</comments>
            <pubDate>Sat, 09 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3172311</guid>        </item>
        <item>
            <title>Taking another look with fluorescence microscopy: Image processing techniques in langmuir monolayers for the twenty-first century.</title>
            <link>http://www.medworm.com/index.php?rid=3172310&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20067758%26dopt%3DAbstract</link>
            <description>Authors: Stottrup BL, Nguyen AH, T&amp;#xFC;zel E
    Fluorescence microscopy has become a powerful and standard complementary technique in the study of amphiphilic films at the air-water interface. For nearly three decades the coupling of traditional thermodynamic measurements with direct visualization has provided a better understanding of self-assembled Langmuir monolayers and their application in the study of the physical properties of membranes and interfaces. As an introduction we provide a brief overview of this established technique and demonstrate its continued utility in the recent observation of novel phase behavior in monolayers of 25-hydroxycholesterol (25-OH) and 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC). We then focus our review on new analysis techniques which take adv...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3172310</comments>
            <pubDate>Sat, 09 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3172310</guid>        </item>
        <item>
            <title>The action of Sphingomyelinase in lipid monolayers as revealed by microscopic image analysis.</title>
            <link>http://www.medworm.com/index.php?rid=3172309&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20067759%26dopt%3DAbstract</link>
            <description>Authors: Fanani ML, Hartel S, Maggio B, De Tullio L, Jara J, Olmos F, Oliveira RG
    In recent years, new evidence in biomembrane research brought about a holistic, supramolecular view on membrane-mediated signal transduction. The consequences of sphingomyelinase (SMase) driven formation of ceramide (Cer) at the membrane interface involves reorganization of the lateral membrane structure of lipids and proteins from the nm to the mum level. In this review, we present recent insights about mechanisms and features of the SMase-mediated formation of Cer-enriched domains in model membranes, which have been elucidated through a combination of microscopic techniques with advanced image processing algorithms. This approach extracts subtle morphological and pattern information beyond the visual pe...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3172309</comments>
            <pubDate>Sat, 09 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3172309</guid>        </item>
        <item>
            <title>Role of glycine residues highly conserved in the S2-S3 linkers of domains I and II of voltage-gated calcium channel alpha(1) subunits.</title>
            <link>http://www.medworm.com/index.php?rid=3172308&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20067760%26dopt%3DAbstract</link>
            <description>Authors: Teng J, Iida K, Ito M, Izumi-Nakaseko H, Kojima I, Adachi-Akahane S, Iida H
    The pore-forming component of voltage-gated calcium channels, alpha(1) subunit, contains four structurally conserved domains (I-IV), each of which contains six transmembrane segments (S1-S6). We have shown previously that a Gly residue in the S2-S3 linker of domain III is completely conserved from yeasts to humans and important for channel activity. The Gly residues in the S2-S3 linkers of domains I and II, which correspond positionally to the Gly in the S2-S3 linker of domain III, are also highly conserved. Here, we investigated the role of the Gly residues in the S2-S3 linkers of domains I and II of Ca(v)1.2. Each of the Gly residues was replaced with Glu or Gln to produce mutant Ca(v)1.2s; G182E, G1...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3172308</comments>
            <pubDate>Sat, 09 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3172308</guid>        </item>
        <item>
            <title>Mitochondrial energy metabolism and ageing.</title>
            <link>http://www.medworm.com/index.php?rid=3172315&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20064485%26dopt%3DAbstract</link>
            <description>Authors: Bratic I, Trifunovic A
    Ageing can be defined as &quot;a progressive, generalized impairment of function, resulting in an increased vulnerability to environmental challenge and a growing risk of disease and death&quot;. Ageing is likely a multifactorial process caused by accumulated damage to a variety of cellular components. During the last 20years, gerontological studies have revealed different molecular pathways involved in the ageing process and pointed out mitochondria as one of the key regulator of longevity. Increasing age in mammals correlates with increased levels of mitochondrial DNA (mtDNA) mutations and a deteriorating respiratory chain function. Experimental evidence in the mouse has linked increased levels of somatic mtDNA mutations to a variety of ageing phenotypes, such a...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3172315</comments>
            <pubDate>Fri, 08 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3172315</guid>        </item>
        <item>
            <title>The molecular structure of the IsiA-Photosystem I supercomplex, modelled from high-resolution, crystal structures of Photosystem I and the CP43 protein.</title>
            <link>http://www.medworm.com/index.php?rid=3172314&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20064486%26dopt%3DAbstract</link>
            <description>In conclusion, our model allows us to explain how the IsiA-PSI supercomplex may act as an efficient light-harvesting structure under low-light conditions and as an efficient dissipater of excess energy under high-light conditions.
    PMID: 20064486 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3172314</comments>
            <pubDate>Fri, 08 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3172314</guid>        </item>
        <item>
            <title>Plagiochin E, an antifungal active macrocyclic bis(bibenzyl), induced apoptosis in Candida albicans through a metacaspase-dependent apoptotic pathway.</title>
            <link>http://www.medworm.com/index.php?rid=3172313&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20064588%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: PLE induced apoptosis in C. albicans through a metacaspase-dependent apoptotic pathway. GENERAL SIGNIFICANCE: In this study, we reported for the first time that PLE induced apoptosis in C. albicans through activating the metacaspase. These results would conduce to elucidate its underlying antifungal mechanism.
    PMID: 20064588 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3172313</comments>
            <pubDate>Fri, 08 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3172313</guid>        </item>
        <item>
            <title>Peroxisomes, lipid metabolism and lipotoxicity.</title>
            <link>http://www.medworm.com/index.php?rid=3172312&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20064629%26dopt%3DAbstract</link>
            <description>Authors: Wanders RJ, Ferdinandusse S, Brites P, Kemp S
    Peroxisomes play an essential role in cellular lipid metabolism as exemplified by the existence of a number of genetic diseases in humans caused by the impaired function of one of the peroxisomal enzymes involved in lipid metabolism. Key pathways in which peroxisomes are involved include: (1.) fatty acid beta-oxidation; (2.) etherphospholipid biosynthesis, and (3.) fatty acid alpha oxidation. In this paper we will describe these different pathways in some detail and will provide an overview of peroxisomal disorders of metabolism and in addition discuss the toxicity of the intermediates of peroxisomal metabolism as they accumulate in the different peroxisomal deficiencies.
    PMID: 20064629 [PubMed - as supplied by publisher] (Sour...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3172312</comments>
            <pubDate>Fri, 08 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3172312</guid>        </item>
        <item>
            <title>Diversity of mechanisms involved in aromatase regulation and estrogen action in the brain.</title>
            <link>http://www.medworm.com/index.php?rid=3164296&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20060879%26dopt%3DAbstract</link>
            <description>Authors: Charlier TD, Cornil CA, Ball GF, Balthazart J
    The mechanisms through which estrogens modulate neuronal physiology, brain morphology, and behavior in recent years have proven to be far more complex than previously thought. For example, a second nuclear estrogen receptor has been identified, a new family of coregulatory proteins regulating steroid-dependent gene transcriptions was discovered and, finally, it has become clear that estrogens have surprisingly rapid effects based on their actions on cell membranes, which in turn results in the modulation of intracellular signaling cascades. This paper presents a selective review of new findings in this area related to work in our laboratories, focusing on the role of estrogens in the activation of male sexual behavior. Two separate...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164296</comments>
            <pubDate>Thu, 07 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164296</guid>        </item>
        <item>
            <title>Regulation of GPCR signaling in Hypertension.</title>
            <link>http://www.medworm.com/index.php?rid=3164295&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20060896%26dopt%3DAbstract</link>
            <description>Authors: Brinks HL, Eckhart AD
    Hypertension represents a complex, multifactorial disease and contributes to the major causes of morbidity and mortality in industrialized countries: ischemic and hypertensive heart disease, stroke, peripheral atherosclerosis and renal failure. Current pharmacological therapy of essential hypertension focuses on the regulation of vascular resistance by inhibition of hormones such as catecholamines and angiotensin II, blocking them from receptor activation. Interaction of G-protein coupled receptor kinases (GRKs) and Regulator of G-Protein Signaling (RGS) proteins with activated G-protein coupled receptors (GPCRs) effect the phosphorylation state of the receptor leading to desensitization and can profoundly impair signalling. Defects in GPCR regulation via...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164295</comments>
            <pubDate>Thu, 07 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164295</guid>        </item>
        <item>
            <title>The role of the autonomic nervous liver innervation in the control of energy metabolism.</title>
            <link>http://www.medworm.com/index.php?rid=3164294&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20060897%26dopt%3DAbstract</link>
            <description>Authors: Yi CX, la Fleur SE, Fliers E, Kalsbeek A
    Despite a longstanding research interest ever since the early work by Claude Bernard, the functional significance of autonomic liver innervation, either sympathetic or parasympathetic, is still ill defined. This scarcity of information not only holds for the brain control of hepatic metabolism, but also for the metabolic sensing function of the liver and the way in which this metabolic information from the liver affects the brain. Clinical information from the bedside suggests that successful human liver transplantation (implying a complete autonomic liver denervation) causes no life threatening metabolic derangements, at least in the absence of severe metabolic challenges such as hypoglycemia. However, from the benchside, data are accu...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164294</comments>
            <pubDate>Thu, 07 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164294</guid>        </item>
        <item>
            <title>In-vivo visualization of key molecular processes involved in Alzheimer's disease pathogenesis: Insights from neuroimaging research in humans and rodent models.</title>
            <link>http://www.medworm.com/index.php?rid=3164293&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20060898%26dopt%3DAbstract</link>
            <description>Authors: Higuchi M, Maeda J, Ji B, Maruyama M, Okauchi T, Tokunaga M, Ono M, Suhara T
    Diverse age-associated neurodegenerative disorders are featured at a molecular level by depositions of self-aggregating molecules, as represented by amyloid beta peptides (Abeta) and tau proteins in Alzheimer's disease, and cascade-type chain reactions are supposedly commenced with biochemical aberrancies of these amyloidogenic components. Mutagenesis and multiplication of the genes encoding Abeta, tau and other pathogenic initiators may accelerate the incipient process at the cascade top, rationalizing generations of transgenic and knock-in animal models of these illnesses. Meanwhile, these genetic manipulations do not necessarily compress the timelines of crucial intermediate events linking amyloido...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164293</comments>
            <pubDate>Thu, 07 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164293</guid>        </item>
        <item>
            <title>Lipid raft disruption protects mature neurons against amyloid oligomer toxicity.</title>
            <link>http://www.medworm.com/index.php?rid=3164292&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20060899%26dopt%3DAbstract</link>
            <description>Authors: Malchiodi-Albedi F, Contrusciere V, Raggi C, Fecchi K, Rainaldi G, Paradisi S, Matteucci A, Santini MT, Sargiacomo M, Frank C, Gaudiano MC, Diociaiuti M
    A specific neuronal vulnerability to amyloid protein toxicity may account for brain susceptibility to protein misfolding diseases. To investigate this issue, we compared the effects induced by oligomers from salmon calcitonin (sCTOs), a neurotoxic amyloid protein, on cells of different histogenesis: mature and immature primary hippocampal neurons, primary astrocytes, MG63 osteoblasts and NIH-3T3 fibroblasts. In mature neurons, sCTOs increased apoptosis and induced neuritic and synaptic damages similar to those caused by amyloid beta oligomers. Immature neurons and the other cell types showed no cytotoxicity. CTOs caused cytoso...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164292</comments>
            <pubDate>Thu, 07 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164292</guid>        </item>
        <item>
            <title>Prolyl-peptidyl isomerase, Pin1, phosphorylation is compromised in association with the expression of the HFE polymorphic allele, H63D.</title>
            <link>http://www.medworm.com/index.php?rid=3164291&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20060900%26dopt%3DAbstract</link>
            <description>Authors: Hall EC, Lee SY, Simmons Z, Neely EB, Nandar W, Connor JR
    There is substantial interest in HFE gene variants as putative risk factors in neurodegenerative diseases such as Alzheimer disease (AD). Previous studies in cell models have shown the H63D HFE variant to result in increased cellular iron, oxidative stress, glutamate dyshomeostasis, and an increase in tau phosphorylation; all processes thought to contribute to AD pathology. Pin1 is a prolyl-peptidyl cis/trans isomerase that can regulate the dephosphorylation of the amyloid and tau proteins. Hyperphosphorylation of these later proteins are implicated in the pathogenesis of AD and Pin1 levels are reportedly decreased in AD brains. Because of the relationship between Pin1 loss of function by oxidative stress and the increa...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164291</comments>
            <pubDate>Thu, 07 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164291</guid>        </item>
        <item>
            <title>Compared effects of missense mutations in Very-Long-Chain Acyl-CoA Dehydrogenase deficiency: Combined analysis by structural, functional and pharmacological approaches.</title>
            <link>http://www.medworm.com/index.php?rid=3164290&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20060901%26dopt%3DAbstract</link>
            <description>Authors: Gobin-Limballe S, McAndrew RP, Djouadi F, Kim JJ, Bastin J
    Very-Long-Chain Acyl-CoA Dehydrogenase deficiency (VLCADD) is an autosomal recessive disorder considered as one of the more common ss-oxidation defects, possibly associated with neonatal cardiomyopathy, infantile hepatic coma, or adult-onset myopathy. Numerous gene missense mutations have been described in these VLCADD phenotypes, but only few of them have been structurally and functionally analyzed, and the molecular basis of disease variability is still poorly understood. To address this question, we first analyzed fourteen disease-causing amino acid changes using the recently described crystal structure of VLCAD. The predicted effects varied from the replacement of amino acid residues lining the substrate binding ca...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164290</comments>
            <pubDate>Thu, 07 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164290</guid>        </item>
        <item>
            <title>The Paf1 Complex: Platform or Player in RNA Polymerase II Transcription?</title>
            <link>http://www.medworm.com/index.php?rid=3164289&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20060942%26dopt%3DAbstract</link>
            <description>Authors: Jaehning JA
    The Paf1 complex (Paf1C), composed of the proteins Paf1, Ctr9, Cdc73, Rtf1, and Leo1, accompanies RNA polymerase II (pol II) from the promoter to the 3' end formation site of mRNA and snoRNA encoding genes; it is also found associated with RNA polymerase I (pol I) on rDNA. The Paf1C is found in simple and complex eukaryotes; in human cells hSki8 is also part of the complex. The Paf1C has been linked to a large and growing list of transcription related processes including: communication with transcriptional activators; recruitment and activation of histone modification factors; facilitation of elongation on chromatin templates; and the recruitment of 3' end processing factors necessary for accurate termination of transcription. Absence of, or mutations in, Paf1C fac...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164289</comments>
            <pubDate>Thu, 07 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164289</guid>        </item>
        <item>
            <title>Liquid-ordered phases induced by cholesterol: A compendium of binary phase diagrams.</title>
            <link>http://www.medworm.com/index.php?rid=3164301&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20060378%26dopt%3DAbstract</link>
            <description>Authors: Marsh D
    Mixtures of phospholipids with cholesterol are able to form liquid-ordered phases that are characterised by short-range orientational order and long-range translational disorder. These L(o)-phases are distinct from the liquid-disordered, fluid L(alpha)-phases and the solid-ordered, gel L(beta)-phases that are assumed by the phospholipids alone. The liquid-ordered phase can produce spatially separated in-plane fluid domains, which, in the form of lipid rafts, are thought to act as platforms for signalling and membrane sorting in cells. The areas of domain formation are defined by the regions of phase coexistence in the phase diagrams for the binary mixtures of lipid with cholesterol. In this paper, the available binary phase diagrams of lipid-cholesterol mixtures are al...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164301</comments>
            <pubDate>Wed, 06 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164301</guid>        </item>
        <item>
            <title>Oxidatively modified fatty acyl chain determines physicochemical properties of aggregates of oxidized phospholipids.</title>
            <link>http://www.medworm.com/index.php?rid=3164300&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20060379%26dopt%3DAbstract</link>
            <description>In this study we have compared the properties of four closely related tOx-PLs which differ only in the type of modified fatty acyl chain present at the sn-2 position: 1-palmitoyl-2-azelaoyl-sn-glycero-3 phosphocholine (PazePC), 1-palmitoyl-2-(9'-oxo-nonanoyl)-sn-glycero-3-phosphocholine (PoxnoPC), 1-palmitoyl-2-glutaroyl-sn-glycero-3-phosphocholine (PGPC), and 1 palmitoyl-2-(5'-oxo-valeroyl)-sn-glycero-3-phosphocholine (POVPC). Aggregates of individual tOx-PL in aqueous solution were characterized by fluorescence spectroscopy, size exclusion chromatography, native polyacrylamide and agarose gel electrophoresis. The data suggest that aggregates of four closely related tOx-PLs forms micelle-like particles of considerably different properties. Our result provides first direct evidence that be...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164300</comments>
            <pubDate>Wed, 06 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164300</guid>        </item>
        <item>
            <title>Are optimal levels of testosterone associated with better cognitive function in healthy older women and men?</title>
            <link>http://www.medworm.com/index.php?rid=3164299&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20060437%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: Results replicate earlier cross sectional findings that high levels of sex steroids are not associated with better cognitive function in older people. In men, age accelerated endocrinological change could be associated with dementia pathology. GENERAL SIGNIFICANCE: These data do not support increasing testosterone levels to prevent cognitive decline in men and women over 65years of age.
    PMID: 20060437 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164299</comments>
            <pubDate>Wed, 06 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164299</guid>        </item>
        <item>
            <title>The bile acid sensor FXR regulates insulin transcription and secretion.</title>
            <link>http://www.medworm.com/index.php?rid=3164298&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20060466%26dopt%3DAbstract</link>
            <description>Authors: Renga B, Mencarelli A, Vavassori P, Brancaleone V, Fiorucci S
    Farnesoid X Receptor plays an important role in maintaining bile acid, cholesterol homeostasis and glucose metabolism. Here we investigated whether FXR is expressed by pancreatic beta-cells and regulates insulin signaling in pancreatic beta-cell line and human islets. We found that FXR activation induces a positive regulatory effects on glucose-induced insulin transcription and secretion by genomic and non-genomic activities. Genomic effects of FXR activation relays on the induction of the glucose regulated transcription factor KLF11. Indeed, results from silencing experiments of KLF11 demonstrates that this transcription factor is essential for FXR activity on glucose-induced insulin gene transcription. In addition...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164298</comments>
            <pubDate>Wed, 06 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164298</guid>        </item>
        <item>
            <title>Mitochondrial Sirtuins.</title>
            <link>http://www.medworm.com/index.php?rid=3164297&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20060508%26dopt%3DAbstract</link>
            <description>Authors: Huang JY, Hirschey MD, Shimazu T, Ho L, Verdin E
    Sirtuins have emerged as important proteins in aging, stress resistance and metabolic regulation. Three sirtuins, SIRT3, 4 and 5, are located within the mitochondrial matrix. SIRT3 and SIRT5 are NAD(+)-dependent deacetylases that remove acetyl groups from acetyllysine-modified proteins and yield 2'-O-acetyl-ADP ribose and nicotinamide. SIRT4 can transfer the ADP-ribose group from NAD(+) onto acceptor proteins. Recent findings reveal that a large fraction of mitochondrial proteins is acetylated and that mitochondrial protein acetylation is modulated by nutritional status. This and the identification of targets for SIRT3, 4 and 5 support the model that mitochondrial sirtuins are metabolic sensors that modulate the activity of meta...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164297</comments>
            <pubDate>Wed, 06 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164297</guid>        </item>
        <item>
            <title>Purification and kinetic characterization of recombinant alternative oxidase from Trypanosoma brucei brucei.</title>
            <link>http://www.medworm.com/index.php?rid=3157873&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20056101%26dopt%3DAbstract</link>
            <description>Authors: Kido Y, Sakamoto K, Nakamura K, Harada M, Suzuki T, Yabu Y, Saimoto H, Yamakura F, Ohmori D, Moore A, Harada S, Kita K
    
    PMID: 20056101 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157873</comments>
            <pubDate>Mon, 04 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3157873</guid>        </item>
        <item>
            <title>Sodium-translocating NADH:Quinone oxidoreductase as a redox-driven ion pump.</title>
            <link>http://www.medworm.com/index.php?rid=3157872&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20056102%26dopt%3DAbstract</link>
            <description>Authors: Verkhovsky MI, Bogachev AV
    The Na(+)-translocating NADH:ubiquinone oxidoreductase (Na(+)-NQR) is a component of the respiratory chain of various bacteria. This enzyme is an analogous but not homologous counterpart of mitochondrial Complex I. Na(+)-NQR drives the same chemistry and also uses released energy to translocate ions across the membrane, but it pumps Na(+) instead of H(+). Most likely the mechanism of sodium pumping is quite different from that of proton pumping (for example, it could not accommodate the Grotthuss mechanism of ion movement); this is why the enzyme structure, subunits and prosthetic groups are completely special. This review summarizes modern knowledge on the structural and catalytic properties of bacterial Na(+)-translocating NADH:quinone oxidoreducta...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157872</comments>
            <pubDate>Mon, 04 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3157872</guid>        </item>
        <item>
            <title>Consequences of the pathogenic T9176C mutation of human mitochondrial DNA on yeast mitochondrial ATP synthase.</title>
            <link>http://www.medworm.com/index.php?rid=3157870&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20056103%26dopt%3DAbstract</link>
            <description>Authors: Kucharczyk R, Ezkurdia N, Couplan E, Procaccio V, Ackerman SH, Blondel M, di Rago JP
    Several human neurological disorders have been associated with various mutations affecting mitochondrial enzymes involved in cellular ATP production. One of these mutations, T9176C in the mitochondrial DNA (mtDNA), changes a highly conserved leucine residue into proline at position 217 of the mitochondrially encoded Atp6p (or a) subunit of the F(1)F(O)-ATP synthase. The consequences of this mutation on the mitochondrial ATP synthase are still poorly defined. To gain insight into the primary pathogenic mechanisms induced by T9176C, we have investigated the consequences of this mutation on the ATP synthase of yeast where Atp6p is also encoded by the mtDNA. In vitro, yeast atp6-T9176C mitochondri...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157870</comments>
            <pubDate>Mon, 04 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3157870</guid>        </item>
        <item>
            <title>Differential mechanism of light-induced and oxygen-dependent restoration of the high-potential form of cytochrome b(559) in Tris-treated Photosystem II membranes.</title>
            <link>http://www.medworm.com/index.php?rid=3157869&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20056104%26dopt%3DAbstract</link>
            <description>Authors: Posp&amp;#xED;&amp;#x161;il P, Tiwari A
    The effect of illumination and molecular oxygen on the redox and the redox potential changes of cytochrome b(559) (cyt b(559)) has been studied in Tris-treated spinach photosystem II (PSII) membranes. It has been demonstrated that the illumination of Tris-treated PSII membranes induced the conversion of the intermediate potential form (IP) of cyt b(559) to the reduced high-potential (HP(Fe2+)) form, whereas the removal of molecular oxygen resulted in the conversion of the IP form to the oxidized high-potential (HP(Fe3+)) form of cyt b(559). Light-induced conversion of cyt b(559) from the IP to the HP form was completely inhibited above pH 8 or by the modification of histidine ligand that prevents its protonation. Interestingly, no effect of high...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157869</comments>
            <pubDate>Mon, 04 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3157869</guid>        </item>
        <item>
            <title>Maintenance and expression of the S. cerevisiae mitochondrial genome - from genetics to evolution and systems biology.</title>
            <link>http://www.medworm.com/index.php?rid=3157868&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20056105%26dopt%3DAbstract</link>
            <description>Authors: Lipinski KA, Kaniak-Golik A, Golik P
    As a legacy of their endosymbiotic eubacterial origin, mitochondria possess a residual genome, encoding only a few proteins and dependent on a variety of factors encoded by the nuclear genome for its maintenance and expression. As a facultative anaerobe with well understood genetics and molecular biology, S. cerevisiae is the model system of choice for studying nucleo-mitochondrial genetic interactions. Maintenance of the mitochondrial genome is controlled by a set of nuclear-coded factors forming intricately interconnected circuits responsible for replication, recombination, repair and transmission to buds. Expression of the yeast mitochondrial genome is regulated mostly at the post-transcriptional level, and involves many general and gene...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157868</comments>
            <pubDate>Mon, 04 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3157868</guid>        </item>
        <item>
            <title>Detection of lipid domains in model and cell membranes by fluorescence lifetime imaging microscopy.</title>
            <link>http://www.medworm.com/index.php?rid=3157867&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20056106%26dopt%3DAbstract</link>
            <description>Authors: St&amp;#xF6;ckl MT
    The discovery that the lipids constituting the plasma membrane are not randomly distributed, but instead are able to form laterally segregated lipid domains with different properties has given hints how the formation of such lipid domains influences and regulates many processes occurring at the plasma membrane. While in model systems these lipid domains can be easily accessed and their properties studied, it is still challenging to determine the properties of cholesterol lipid domains, the so called &quot;Rafts&quot;, in the plasma membrane of living cells due to their small size and transient nature. One promising technique to address such issues is fluorescence lifetime imaging (FLIM) microscopy, as spatially resolved images make the visualization of the lateral lipid d...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157867</comments>
            <pubDate>Mon, 04 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3157867</guid>        </item>
        <item>
            <title>Functional impact of serial deletions at the C-terminus of the human GABArho1 receptor.</title>
            <link>http://www.medworm.com/index.php?rid=3157866&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20056107%26dopt%3DAbstract</link>
            <description>This study reveals that GABArho1 can tolerate removal of several residues that form the fourth transmembrane segment up to a critical point, signaled by W475, beyond which the mutant protein is translated but does not form functional receptors. A comparative study is presented of some electrophysiological and pharmacological properties of the deletion mutants that were able to generate GABA-currents.
    PMID: 20056107 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157866</comments>
            <pubDate>Mon, 04 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3157866</guid>        </item>
        <item>
            <title>CD44 and hyaluronan promote invasive growth of B35 neuroblastoma cells into brain.</title>
            <link>http://www.medworm.com/index.php?rid=3157865&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20056122%26dopt%3DAbstract</link>
            <description>This study examines how CD44 regulates the motility and invasive growth of B35 neuroblastoma cells into a hyaluronan-rich environment. A comprehensive experimental approach was used encompassing biochemical techniques, single molecule microscopy, correlative confocal and scanning electron microscopy, morphometry of cellular extensions, live-cell imaging and tracking, transplantation onto organotypic brain slices, two-photon imaging and invasion assays. We found that CD44-GFP fusion protein was localized in filopodia and in focal bleb-like protrusions where it provided binding sites for hyaluronan. Transient expression of CD44-GFP was sufficient to increase the length of filopodia, to enhance cell migration and to promote invasive growth into hyaluronan-rich brain tissue. Thus, CD44 control...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157865</comments>
            <pubDate>Mon, 04 Jan 2010 00:00:00 +0100</pubDate>
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            <title>Insulin alters the expression of components of the Wnt signaling pathway including TCF-4 in the intestinal cells.</title>
            <link>http://www.medworm.com/index.php?rid=3157864&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20056134%26dopt%3DAbstract</link>
            <description>Authors: Sun J, Wang D, Jin T
    BACKGROUND: Epidemiological and experimental evidence that support the correlation between Type 2 diabetes mellitus (T2D) and increased risks of colorectal cancer formation have led us to hypothesize the existence of molecular crosstalk between insulin and canonical Wnt signaling pathways. Insulin was shown to stimulate Wnt target gene expression, utilizing the effector of the Wnt signaling pathway. Whether insulin affects expression of components of Wnt pathway has not been extensively examined. METHODS: cDNA microarray was utilized to assess the effect of insulin on gene expression profile in the rat intestinal non-cancer IEC-6 cell line, followed by real time RT-PCR, Western blotting and reporter gene analyses in intestinal cancer and non-cancer cells. ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157864</comments>
            <pubDate>Mon, 04 Jan 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Neurogenesis in mouse models of Alzheimer's disease.</title>
            <link>http://www.medworm.com/index.php?rid=3157863&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20056145%26dopt%3DAbstract</link>
            <description>Authors: Chuang TT
    The brains of the adult mouse and human possess neural stem cells (NSCs) that retain the capacity to generate new neurons through the process of neurogenesis. They share the same anatomical locations of stem cell niches in the brain, as well as the prominent feature of rostral migratory stream formed by neuroblasts migrating from the lateral ventricles towards the olfactory bulb. Therefore the mouse possesses some fundamental features that may qualify it as a relevant model for adult human neurogenesis. Adult born young hippocampal neurons in the mouse display the unique property of enhanced plasticity, and can integrate physically and functionally into existing neural circuits in the brain. Such crucial properties of neurogenesis may at least partially underlie the ...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157863</comments>
            <pubDate>Mon, 04 Jan 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Obese and anorexic yeasts: Experimental models to understand the metabolic syndrome and lipotoxicity.</title>
            <link>http://www.medworm.com/index.php?rid=3157862&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20056167%26dopt%3DAbstract</link>
            <description>Authors: Kohlwein SD
    Lipotoxicity is the pathological consequence of lipid overflow in non-adipose tissue, mediated through reactive lipid moieties which may even lead to lipid-induced cell death (lipoapoptosis). This derailment of cellular and organismal fat homeostasis is the consequence of obesity due to continued over-feeding, and contributes substantially to the pathogenesis of insulin resistance, type 2 diabetes mellitus and cardiovascular disease, which are all components of the metabolic syndrome. Now, does yeast, a single-celled eukaryote, ever suffer from the metabolic syndrome and what can we potentially learn from studies in this organism about the underlying molecular mechanism that lead to lipid-associated pathologies in human cells? In this review I will summarize the re...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157862</comments>
            <pubDate>Mon, 04 Jan 2010 00:00:00 +0100</pubDate>
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            <title>Modulation of plasma TG lipolysis by Angiopoietin-like proteins and GPIHBP-1.</title>
            <link>http://www.medworm.com/index.php?rid=3157861&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20056168%26dopt%3DAbstract</link>
            <description>Authors: Lichtenstein L, Kersten S
    There is evidence that elevated plasma triglycerides (TG) serve as an independent risk factor for coronary heart disease. Plasma TG levels are determined by the balance between the rate of production of chylomicrons and VLDL in intestine and liver, respectively, and their rate of clearance in peripheral tissues. Lipolytic processing of TG-rich lipoproteins is mediated by the enzyme lipoprotein lipase (LPL), which is tethered to the capillary endothelium via heparin sulphate proteoglycans. In recent years the Angiopoietin-like proteins ANGPTL3 and ANGPTL4 have emerged as novel modulators of LPL activity. Studies in transgenic animals supported by in vitro experiments have demonstrated that ANGPTL3 and ANGPTL4 impair plasma TG clearance by inhibiting LP...</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3157861</comments>
            <pubDate>Mon, 04 Jan 2010 00:00:00 +0100</pubDate>
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            <title>Adipose tissue expandability, lipotoxicity and the Metabolic Syndrome - an allostatic perspective.</title>
            <link>http://www.medworm.com/index.php?rid=3157860&amp;cid=s_34400_60_f&amp;fid=34400&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20056169%26dopt%3DAbstract</link>
            <description>This article discusses the links between adipokines, inflammation, adipose tissue expandability and lipotoxicity. Finally, we will discuss how considering the concept of allostasis may enable a better understanding of how diabetes develops and allow the rational design of new anti diabetic treatments.
    PMID: 20056169 [PubMed - as supplied by publisher] (Source: Biochimica et Biophysica Acta)</description>
            <author>Biochimica et Biophysica Acta</author>
            <type>journals</type>
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            <pubDate>Mon, 04 Jan 2010 00:00:00 +0100</pubDate>
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