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        <title>BMC Biochemistry 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 'BMC Biochemistry' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=BMC+Biochemistry&t=BMC+Biochemistry&s=Search&f=source]]></link>
        <lastBuildDate>Thu, 18 Mar 2010 16:19:34 +0100</lastBuildDate>
        <item>
            <title>Identification and molecular characterization of a novel flavin-free NADPH preferred azoreductase encoded by azoB in Pigmentiphaga kullae K24</title>
            <link>http://www.medworm.com/index.php?rid=3369595&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F11%2F13</link>
            <description>Conclusion:
The biochemical and structural properties of AzoB from P. kullae K24 revealed its preference for NADPH over NADH and it is a member of the monomeric flavin-free azoreductase group. Our studies show the substrate specificity of AzoB based on structure and cofactor requirement and the phylogenetic relationship among azoreductase groups. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3369595</comments>
            <pubDate>Tue, 16 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3369595</guid>        </item>
        <item>
            <title>Specific fibre composition and metabolism of the rectus abdominis muscle of bovine Charolais cattle</title>
            <link>http://www.medworm.com/index.php?rid=3337835&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F11%2F12</link>
            <description>Conclusions:
RA muscle has some particularities in comparison to the LT and TB muscles, especially concerning the unusual large cross-section surface of SO fibres and the very low oxidative activity of intermediate IIA fibres. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3337835</comments>
            <pubDate>Fri, 05 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3337835</guid>        </item>
        <item>
            <title>Characterization of rubber particles and rubber chain elongation in Taraxacum koksaghyz</title>
            <link>http://www.medworm.com/index.php?rid=3287155&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F11%2F11</link>
            <description>Conclusions:
T. koksaghyz rubber particles are similar to those described for H. brasiliensis. They contain very pure, high molecular mass poly(cis-1,4-isoprene) and the chain elongation process can be studied ex vivo. Because of their localization on rubber particles and their activity in yeast, we propose that the recently described T. koksaghyz CPTs are the major rubber chain elongating enzymes in this species. T. koksaghyz is amenable to genetic analysis and modification, and therefore could be used as a model species for the investigation and comparison of rubber biosynthesis. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3287155</comments>
            <pubDate>Fri, 19 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3287155</guid>        </item>
        <item>
            <title>Biochemical characterization of three putative ATPases from a new type IV secretion system of Aeromonas veronii plasmid pAC3249A</title>
            <link>http://www.medworm.com/index.php?rid=3258174&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F11%2F10</link>
            <description>Conclusions:
This is the first biochemical characterization of conjugative transport ATPases encoded by a conjugative plasmid from Aeromonas. Our study demonstrated that the three ATPases of a newly reported TFSS of A. veronii plasmid pAc3249A are functional in both ATP hydrolysis and ATP binding. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3258174</comments>
            <pubDate>Tue, 09 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3258174</guid>        </item>
        <item>
            <title>The Thiamine diphosphate dependent Enzyme Engineering Database: A tool for the systematic analysis of sequence and structure relations</title>
            <link>http://www.medworm.com/index.php?rid=3230762&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F11%2F9</link>
            <description>Conclusions:
The online accessible version of the TEED has been designed to serve as a navigation and analysis tool for the large and diverse family of ThDP-dependent enzymes. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3230762</comments>
            <pubDate>Mon, 01 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3230762</guid>        </item>
        <item>
            <title>Orthophosphate binding at the dimer interface of Corynebacterium callunae starch phosphorylase: mutational analysis of its role for activity and stability of the enzyme</title>
            <link>http://www.medworm.com/index.php?rid=3219769&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F11%2F8</link>
            <description>Conclusions:
The phosphate sites at the subunit-subunit interface of C. callunae starch phosphorylase appear to be cooperatively functional in conferring extra kinetic stability to the native dimer structure of the active enzyme. The molecular strategy exploited for quaternary structure stabilization is to our knowledge novel among dimeric proteins. It can be distinguished clearly from the co-solute effect of orthophosphate on protein thermostability resulting from (relatively weak) interactions of the ligand with protein surface residues. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3219769</comments>
            <pubDate>Fri, 29 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3219769</guid>        </item>
        <item>
            <title>Rapid determination of tricarboxylic acid cycle enzyme activities in biological samples</title>
            <link>http://www.medworm.com/index.php?rid=3215739&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F11%2F5</link>
            <description>Conclusion:
This set of assays is rapid and simple to use and can immediately detect even partial defects, as the activity of each enzyme can be readily compared with one or more other activities measured in the same sample. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3215739</comments>
            <pubDate>Thu, 28 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3215739</guid>        </item>
        <item>
            <title>NMR characterisation of the minimal interacting regions of centrosomal proteins 4.1R and NuMA1: effect of phosphorylation</title>
            <link>http://www.medworm.com/index.php?rid=3215738&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F11%2F7</link>
            <description>Conclusions:
These changes in the interaction derived from the phosphorylation state of NuMA1 suggest that phosphorylation can act as subtle mechanism of temporal and spatial regulation of the complex 4.1R-NuMA1 and therefore of the processes where both proteins play a role. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3215738</comments>
            <pubDate>Thu, 28 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3215738</guid>        </item>
        <item>
            <title>Thioredoxins function as deglutathionylase enzymes in the yeast Saccharomyces cerevisiae</title>
            <link>http://www.medworm.com/index.php?rid=3175162&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F11%2F3</link>
            <description>Conclusions:
There is increasing evidence that the thioredoxin and glutathione redox systems have overlapping functions and these present data indicate that the thioredoxin system plays a key role in regulating the modification of proteins by the glutathione system. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3175162</comments>
            <pubDate>Thu, 14 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3175162</guid>        </item>
        <item>
            <title>Mechanism of attenuation of leptin signaling under chronic ligand stimulation</title>
            <link>http://www.medworm.com/index.php?rid=3152815&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F11%2F2</link>
            <description>Conclusions:
Both Tyr985 and Tyr1077 contribute to the negative regulation of LEPRb signaling. The inhibitory effects of SOCS1 and SOCS3 differ in the dependence on the tyrosine residues in the intracellular domain of LEPRb. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3152815</comments>
            <pubDate>Fri, 08 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3152815</guid>        </item>
        <item>
            <title>Cloning and characterization of Escherichia coli DUF299: a bifunctional ADP-dependent kinase - phosphate-dependent pyrophosphorylase from bacteria.</title>
            <link>http://www.medworm.com/index.php?rid=3138708&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F11%2F1</link>
            <description>Conclusion:
This paper represents the first report of a bifunctional regulatory enzyme catalysing an ADP-dependent phosphorylation and a Pi-dependent pyrophosphorylation reaction in bacteria. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3138708</comments>
            <pubDate>Sun, 03 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3138708</guid>        </item>
        <item>
            <title>Identification of four novel phosphorylation sites in estrogen receptor alpha: impact on receptor-dependent gene expression and phosphorylation by protein kinase CK2.</title>
            <link>http://www.medworm.com/index.php?rid=3135223&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F36</link>
            <description>Conclusion:
These novel ERalpha phosphorylation sites represent new means for modulation of ERalpha activity. S559 represents the first phosphorylation site identified in the extreme C-terminus (F domain) of a steroid receptor. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3135223</comments>
            <pubDate>Thu, 31 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3135223</guid>        </item>
        <item>
            <title>The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains</title>
            <link>http://www.medworm.com/index.php?rid=3133150&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F35</link>
            <description>Conclusions:
Identification of the A-domains as IDPs will be important for determining their precise function(s), and suggests a role in protein-protein interactions, which may explain how these proteins serve as receptors for such a wide variety of preprotein substrates. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3133150</comments>
            <pubDate>Wed, 30 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3133150</guid>        </item>
        <item>
            <title>Comparison of the receptor FGFRL1 from sea urchins and humans illustrates evolution of a zinc binding motif in the intracellular domain</title>
            <link>http://www.medworm.com/index.php?rid=3104471&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F33</link>
            <description>Conclusion:
The FGFRL1 gene has evolved much earlier than previously assumed. A comparison of the intracellular domain between sea urchin and human FGFRL1 provides interesting insights into the shaping of a novel zinc binding domain. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3104471</comments>
            <pubDate>Fri, 18 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3104471</guid>        </item>
        <item>
            <title>Analysis of the stoichiometric metal activation of methionine aminopeptidase</title>
            <link>http://www.medworm.com/index.php?rid=3096007&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F32</link>
            <description>Conclusions:
Considering different scenarios of MetAP activation by one or two metal ions, it is concluded that E. coli MetAP is fully active as a monometalated enzyme. Our approach can be of value in proper determination of the number of cations needed for catalysis by metalloenzymes. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3096007</comments>
            <pubDate>Thu, 17 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3096007</guid>        </item>
        <item>
            <title>Biochemical evidence for the tyrosine involvement in cationic intermediate stabilization in mouse beta-carotene 15, 15'-monooxygenase.</title>
            <link>http://www.medworm.com/index.php?rid=3088654&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F31</link>
            <description>Conclusions:
Our data are consistent with the formation of a substrate carbocation intermediate and cation-pi stabilization of this intermediate by two aromatic residues in the substrate-binding cleft of BCMO1. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3088654</comments>
            <pubDate>Mon, 14 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3088654</guid>        </item>
        <item>
            <title>Ghrelin-like peptide with fatty acid modification and O-glycosylation in the red stingray, Dasyatis akajei</title>
            <link>http://www.medworm.com/index.php?rid=3084301&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F30</link>
            <description>Conclusions:
This study reveals the structural diversity of GRLN and GRLN-LP in vertebrates. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3084301</comments>
            <pubDate>Mon, 14 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3084301</guid>        </item>
        <item>
            <title>Prion protein self-peptides modulate prion interactions and conversion</title>
            <link>http://www.medworm.com/index.php?rid=3039135&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F29</link>
            <description>Conclusions:
This study identified the putative PrP core binding domain that facilitates the PrPC-PrPSc interaction (not conversion), likely important in the species-barrier and/or scrapie susceptibility. The octarepeats can be involved in PrPC-PrPSc stabilization, whereas the N-terminal glycosaminoglycan binding motif and the amyloidogenic motif indirectly affected conversion. Binding domain 2 and the C-terminal domain are directly implicated in PrPC self-interaction during the conversion process and may prove to be prime targets in new therapeutic strategy development, potentially retaining PrPC function. These results emphasize the importance of probable PrPC-PrPC and required PrPC-PrPSc interactions during PrP conversion. All interactions are probably part of the complex process in whi...</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3039135</comments>
            <pubDate>Mon, 30 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3039135</guid>        </item>
        <item>
            <title>The Cytochrome P450 Engineering Database: integration of biochemical properties</title>
            <link>http://www.medworm.com/index.php?rid=2988329&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F27</link>
            <description>Conclusions:
The online accessible version of the CYPED at http://www.cyped.uni-stuttgart.de provides a valuable tool for the analysis of sequences, structures and their relationships to biochemical properties. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2988329</comments>
            <pubDate>Thu, 12 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2988329</guid>        </item>
        <item>
            <title>Biosynthesis of the proteasome inhibitor syringolin A: the ureido group joining two amino acids originates from bicarbonate</title>
            <link>http://www.medworm.com/index.php?rid=2934078&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F26</link>
            <description>Conclusions:
The results show that no additional syringolin A-specific genes were needed for the biosynthesis of the enigmatic ureido group joining two amino acids. They reveal the source of the ureido carbonyl group to be bicarbonate/carbon dioxide, which we hypothesize is incorporated by carbamylation of valine mediated by the sylC gene product(s). A similar mechanism may also play a role in the biosynthesis of other ureido-group-containing NRPS products known largely from cyanobacteria. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2934078</comments>
            <pubDate>Wed, 28 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2934078</guid>        </item>
        <item>
            <title>Ser170 of Bacillus thuringiensis Cry1Ab delta-endotoxin becomes anchored in a hydrophobic moiety upon insertion of this protein into Manduca sexta brush border membranes</title>
            <link>http://www.medworm.com/index.php?rid=2908024&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F25</link>
            <description>Conclusions:
Ion transport data for L157, S170, and S176, along with the mobility of the spin-labels, structural characterization of the resulting proteins, and toxicity assays against a target insect, suggest that the toxin undergoes conformational changes upon protein translocation into the midgut membrane. These conformational changes result in the midregion of the alpha-helix 5 being exposed to a hydrophobic-like environment. The location of these three residues in the toxin suggests that the entire alpha-helix becomes inserted in the insect midgut membrane. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2908024</comments>
            <pubDate>Sun, 18 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2908024</guid>        </item>
        <item>
            <title>Mapping of protein phosphatase-6 association with its SAPS domain regulatory subunit using a model of helical repeats</title>
            <link>http://www.medworm.com/index.php?rid=2901360&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F24</link>
            <description>Conclusions:
The conserved SAPS domain in PP6R3 forms helical repeats similar to those in golgin p115 and negatively charged residues in interhelical loops are used to associate specifically with PP6. The results advance understanding of how distinctive helical repeat subunits uniquely distribute and differentially regulate closely related Ser/Thr phosphatases. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2901360</comments>
            <pubDate>Thu, 15 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2901360</guid>        </item>
        <item>
            <title>Monitoring compartment-specific substrate cleavage by cathepsins B, K, L, and S at physiological pH and redox conditions</title>
            <link>http://www.medworm.com/index.php?rid=2818904&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F23</link>
            <description>Conclusions:
The results revealed distinct cleavage patterns at all conditions analyzed, indicating compartment-specific processing of thyroglobulin by cysteine cathepsins. In particular, proteolytic activity of cathepsin S towards the substrate thyroglobulin can now be understood as instrumental for extracellular thyroid hormone liberation. Our study emphasizes that the proteolytic functions of cysteine cathepsins in the thyroid are not restricted to endo-lysosomes but include pivotal roles in extracellular substrate utilization. We conclude that understanding of the interplay and fine adjustment of protease networks in vivo is better approachable by simulating physiological conditions in protease activity assays. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2818904</comments>
            <pubDate>Mon, 21 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2818904</guid>        </item>
        <item>
            <title>Identification of a nuclear localization motif in the serine/arginine protein kinase PSRPK of physarum polycephalum</title>
            <link>http://www.medworm.com/index.php?rid=2729450&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F22</link>
            <description>Conclusions:
This study demonstrated that the 318PKKGDKYDKTD328 peptides localized in the C-terminal conserved domain of PSRPK with the Omega-loop structure could play a crucial role in the NLS function of PSRPK. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2729450</comments>
            <pubDate>Mon, 24 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2729450</guid>        </item>
        <item>
            <title>Biochemical characterization of malate synthase G of P. aeruginosa</title>
            <link>http://www.medworm.com/index.php?rid=2503489&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F20</link>
            <description>Conclusions:
The implication of the glyoxylate bypass in the pathology of various microorganisms makes malate synthase G an attractive new target for antibacterial therapy. The purification procedure and biochemical characterization assist in the development of antibacterial components directed against this target in P. aeruginosa. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2503489</comments>
            <pubDate>Tue, 23 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2503489</guid>        </item>
        <item>
            <title>Insights into the role of Val45 and Gln182 of Escherichia coli MutY in DNA substrate binding and specificity</title>
            <link>http://www.medworm.com/index.php?rid=2503490&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F19</link>
            <description>Conclusion:
The substrate specificities are altered in V45A, Q182L, and V45A/Q182L EcMutY mutants. V45A and Q182L mutants had reduced binding and glycosylase activities for A/G and A/8-oxoG mismatches and increased affinities towards T/G mismatch. However, in contrast to a previous report that Mig.MthI thymine DNA glycosylase can be converted to a MutY-like adenine glycosylase by replacing two residues (A50V and L187Q), both V45A and Q182L EcMutY mutants did not exhibit any T/G or T/8-oxoG glycosylase activity. The dominant negative phenotype of V45A EcMutY mutant protein is probably caused by its increased binding affinity to T/G mismatch and thus inhibiting other repair pathways. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2503490</comments>
            <pubDate>Thu, 11 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2503490</guid>        </item>
        <item>
            <title>DNA binding kinetics of two response regulators, PlnC and PlnD, from the bacteriocin regulon of Lactobacillus plantarum C11</title>
            <link>http://www.medworm.com/index.php?rid=2503492&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F17</link>
            <description>Conclusion:
We have characterised the DNA binding kinetics of the two regulators PlnC and PlnD from the bacteriocin locus in L. plantarum C11. Our data show that PlnC and PlnD, despite their strong homology to each other, differ greatly from each other in terms of binding affinity and cooperativity to the different promoters of the pln regulon. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2503492</comments>
            <pubDate>Wed, 10 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2503492</guid>        </item>
        <item>
            <title>Analysis of DNA relaxation and cleavage activities of recombinant Mycobacterium tuberculosis DNA topoisomerase I from a new expression and purification protocol</title>
            <link>http://www.medworm.com/index.php?rid=2503491&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F18</link>
            <description>Conclusions:
Recombinant M. tuberculosis DNA topoisomerase I can be expressed as a soluble protein and purified in high yield from E. coli host with a new protocol. Analysis of DNA cleavage with M. tuberculosis DNA substrate showed that the preferred DNA cleavage sites have a C nucleotide in the -4 position. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2503491</comments>
            <pubDate>Wed, 10 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2503491</guid>        </item>
        <item>
            <title>TIPT2 and geminin interact with basal transcription factors to synergize in transcriptional regulation</title>
            <link>http://www.medworm.com/index.php?rid=2521662&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F16</link>
            <description>Conclusion:
Together, our study introduces a novel transcriptional regulator and its function in cooperation with chromatin associated factors and the basal transcription machinery. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2521662</comments>
            <pubDate>Tue, 09 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2521662</guid>        </item>
        <item>
            <title>TIPT2 and geminin interact with basal transcription factors to synergize in transcriptional regulation</title>
            <link>http://www.medworm.com/index.php?rid=2503493&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2Fbmcbiochem%2F</link>
            <description>Conclusions:
Together, our study introduces a novel transcriptional regulator and its function in cooperation with chromatin associated factors and the basal transcription machinery. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2503493</comments>
            <pubDate>Tue, 09 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2503493</guid>        </item>
        <item>
            <title>A novel human NatA N-alpha-terminal acetyltransferase complex: hNaa16p-hNaa10p (hNat2-hArd1)</title>
            <link>http://www.medworm.com/index.php?rid=2446197&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F15</link>
            <description>Conclusions:
At least two distinct NatA protein N-alpha-terminal acetyltransferases coexist in human cells potentially creating a more complex and flexible system for N-alpha-terminal acetylation as compared to lower eukaryotes. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2446197</comments>
            <pubDate>Fri, 29 May 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2446197</guid>        </item>
        <item>
            <title>The endocannabinoid anandamide is a precursor for the signaling lipid N-arachidonyl glycine through two distinct pathways</title>
            <link>http://www.medworm.com/index.php?rid=2426893&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F14</link>
            <description>Conclusions:
These data support the hypothesis that the signaling lipid NAGly is a metabolic product of AEA by both oxidative metabolism of the AEA ethanolamine moiety and through the conjugation of glycine to AA that is released during AEA hydrolysis by FAAH. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2426893</comments>
            <pubDate>Thu, 21 May 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2426893</guid>        </item>
        <item>
            <title>Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI)</title>
            <link>http://www.medworm.com/index.php?rid=2422660&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F13</link>
            <description>Conclusion:
The findings presented here suggest that the properties of these two orthologous proteins are similar and that conclusions reached using the bovine TAFI may be extrapolated to the human protein. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2422660</comments>
            <pubDate>Tue, 05 May 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2422660</guid>        </item>
        <item>
            <title>Biochemical characterization of bovine plasma thrombin-activatable fibrinolysis inhibitor (TAFI).</title>
            <link>http://www.medworm.com/index.php?rid=2396692&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F13</link>
            <description>Conclusions:
These findings suggest that the properties of these two orthologous proteins are similar and that conclusions reached using the bovine TAFI may be extrapolated to the human protein. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2396692</comments>
            <pubDate>Tue, 05 May 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2396692</guid>        </item>
        <item>
            <title>Exploring the functional interaction between POSH and Alix and the relevance to HIV-1 release</title>
            <link>http://www.medworm.com/index.php?rid=2363615&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F12</link>
            <description>Conclusions:
Thus, the cumulative results identified ALIX as an ubiquitination substrate of POSH and indicate that POSH and ALIX cooperate to facilitate efficient virus release. However, while ALIX is obligatory for the release of YPXnL-dependent HIV-1, POSH, albeit rate-limiting, may be functionally interchangeable. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2363615</comments>
            <pubDate>Fri, 24 Apr 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2363615</guid>        </item>
        <item>
            <title>Identification of distinct SET/TAF-Ibeta domains required for core histone binding and quantitative characterisation of the interaction</title>
            <link>http://www.medworm.com/index.php?rid=2325205&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F10</link>
            <description>Conclusions:
This type of analysis allowed us to assess the relative affinities of SET/TAF-Ibeta for different histones and identify the domains of the protein required for effective histone recognition. Our findings are consistent with recent structural studies of SET/TAF-Ibeta and can be valuable to understand the role of SET/TAF-Ibeta in chromatin function. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2325205</comments>
            <pubDate>Thu, 09 Apr 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2325205</guid>        </item>
        <item>
            <title>alpha-Sarcin catalytic activity is not required for cytotoxicity</title>
            <link>http://www.medworm.com/index.php?rid=2325207&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F9</link>
            <description>Conclusions:
We conclude that although protein synthesis inhibition likely contributes to cell death, it is not required. Thus, our results suggest that alpha-sarcin can promote cell death through a previously unappreciated mechanism that is independent of rRNA cleavage and JNK activation. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2325207</comments>
            <pubDate>Fri, 03 Apr 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2325207</guid>        </item>
        <item>
            <title>Characterisation of the paralytic shellfish toxin biosynthesis gene clusters in Anabaena circinalis AWQC131C and Aphanizomenon sp. NH-5</title>
            <link>http://www.medworm.com/index.php?rid=2325209&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F8</link>
            <description>Conclusions:
The PST biosynthesis gene cluster presents a mosaic structure, whereby genes have apparently transposed in segments of varying size, resulting in different gene arrangements in all three sxt clusters sequenced so far. The gene cluster organizational structure and sequence similarity seems to reflect the phylogeny of the producer organisms, indicating that the gene clusters have an ancient origin, or that their lateral transfer was also an ancient event. The knowledge we gain from the characterisation of the PST biosynthesis gene clusters, including the identity and sequence of the genes involved in the biosynthesis, may also afford the identification of these gene clusters in dinoflagellates, the cause of human mortalities and significant financial loss to the tourism and shel...</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2325209</comments>
            <pubDate>Mon, 30 Mar 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2325209</guid>        </item>
        <item>
            <title>The roles of aldehyde dehydrogenases (ALDHs) in the PDH bypass of Arabidopsis</title>
            <link>http://www.medworm.com/index.php?rid=2296321&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F7</link>
            <description>Conclusions:
The PDH bypass is active in sporophytic tissue of plants. Blocking this pathway via triple ALDH mutants does not uncover obvious visible phenotypes. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2296321</comments>
            <pubDate>Wed, 25 Mar 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2296321</guid>        </item>
        <item>
            <title>A novel method for screening the glutathione transferase inhibitors</title>
            <link>http://www.medworm.com/index.php?rid=2268507&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F6</link>
            <description>Conclusion:
It appears that the F2 peptide can be used as a new potent specific GST inhibitor. It is proposed that the novel method, described in this report, might be useful for screening the inhibitors of not only GST but also other enzymes. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2268507</comments>
            <pubDate>Mon, 16 Mar 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2268507</guid>        </item>
        <item>
            <title>Human Rad51 mediated DNA unwinding is facilitated by conditions that favour Rad51-dsDNA aggregation</title>
            <link>http://www.medworm.com/index.php?rid=2089555&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F10%2F2</link>
            <description>Conclusions:
RAD52 itself being a highly aggregated protein perhaps acts as scaffold to bring together RAD51 and DNA molecules into large co-aggregates of RAD52-RAD51-DNA complexes to promote RAD51 mediated DNA unwinding reaction, when appropriate nucleotide cofactors are available, presumably through macromolecular crowding effects. Our work highlights the functional link between aggregation of protein-DNA complexes and DNA unwinding in RAD51 system. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2089555</comments>
            <pubDate>Fri, 09 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2089555</guid>        </item>
        <item>
            <title>Modification of carbonic anhydrase II with acetaldehyde, the first metabolite of ethanol, leads to decreased enzyme activity</title>
            <link>http://www.medworm.com/index.php?rid=1989714&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F32</link>
            <description>Conclusions:
The acetaldehyde-derived modifications in CA II molecule may have physiological consequences in alcoholic patients. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1989714</comments>
            <pubDate>Thu, 27 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1989714</guid>        </item>
        <item>
            <title>Lipid bilayer composition influences small multidrug transporters</title>
            <link>http://www.medworm.com/index.php?rid=1989715&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F31</link>
            <description>Conclusions These findings show that the physical state of the membrane modifies drug transport and that substrate translocation is dependent on in vitro lipid composition. Multidrug transport activity seems to respond to alterations in the lateral forces exerted upon the transport proteins by the bilayer. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1989715</comments>
            <pubDate>Tue, 25 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1989715</guid>        </item>
        <item>
            <title>The FF domains of yeast U1 snRNP protein Prp40 mediate interactions with Luc7 and Snu71</title>
            <link>http://www.medworm.com/index.php?rid=1951338&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F29</link>
            <description>Conclusions:
Prp40, Luc7, and Snu71 appear to form a subcomplex within the yeast U1snRNP. Our data suggests that the N-terminal FF domains are critical for these interactions. Crystallization of Prp40, Luc7, and Snu71 have failed so far but co-crystallization of pairs or the whole tri-complex may facilitate crystallographic and further functional analysis. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1951338</comments>
            <pubDate>Tue, 11 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1951338</guid>        </item>
        <item>
            <title>Displacement affinity chromatography of protein phosphatase one (PP1) complexes</title>
            <link>http://www.medworm.com/index.php?rid=1946790&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F28</link>
            <description>Conclusions:
This modification of the microcystin-Sepharose technique offers an effective means of purifying novel PP1 regulatory subunits and provides a simple method to uncover a link between PP1 and additional cellular processes. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1946790</comments>
            <pubDate>Mon, 10 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1946790</guid>        </item>
        <item>
            <title>Immunoaffinity purification and characterization of mitochondrial membrane-bound D-3-hydroxybutyrate dehydrogenase from Jaculus orientalis</title>
            <link>http://www.medworm.com/index.php?rid=1900844&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F26</link>
            <description>Conclusion:
This study applies immunoaffinity chromatography to purify BDH, the membrane-bound and lipid-dependent enzyme, as a 31 kDa single polypeptide chain. In addition, bacterial BDH isolation was achieved in a two-step purification procedure, improving the knowledge of an enzyme involved in the lipid metabolism of a unique hibernating mammal. Sequence alignment revealed conserved putative amino acids for possible NAD+ interaction. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1900844</comments>
            <pubDate>Tue, 30 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1900844</guid>        </item>
        <item>
            <title>Immuno-affinity purification and characterization of the mitochondrial membrane bound D-3-hydroxybutyrate dehydrogenase from Jaculus orientalis</title>
            <link>http://www.medworm.com/index.php?rid=1840533&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F26</link>
            <description>Conclusions:
This study applies immunoaffinity chromatography to purify BDH, the membrane-bound and lipid-dependent enzyme, as a 31 kDa single polypeptide chain. In addition, bacterial BDH isolation was achieved in a two-step purification procedure, improving the knowledge of an enzyme involved in the lipid metabolism of a unique hibernating mammal. Sequence alignment revealed conserved putative amino acids for possible NAD+ interaction. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1840533</comments>
            <pubDate>Tue, 30 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1840533</guid>        </item>
        <item>
            <title>The serine/threonine kinase Stk33 exhibits autophosphorylation and 
phosphorylates the intermediate filament protein Vimentin</title>
            <link>http://www.medworm.com/index.php?rid=1824354&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F25</link>
            <description>Conclusions:
We hypothesize that Stk33 is involved in the in vivo dynamics of the intermediate filament cytoskeleton by phosphorylating vimentin. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1824354</comments>
            <pubDate>Tue, 23 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1824354</guid>        </item>
        <item>
            <title>YB-1 promotes microtubule assembly in vitro through interaction with tubulin and microtubules</title>
            <link>http://www.medworm.com/index.php?rid=1794016&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F23</link>
            <description>Conclusions:
These results suggest that YB-1 may regulate microtubule assembly in vivo and that its interaction with tubulin may contribute to the control of mRNA translation. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1794016</comments>
            <pubDate>Mon, 15 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1794016</guid>        </item>
        <item>
            <title>The central proline rich region of POB1/REPS2 plays a regulatory role in epidermal growth factor receptor endocytosis by binding to 14-3-3 and SH3 domain-containing proteins</title>
            <link>http://www.medworm.com/index.php?rid=1679186&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F21</link>
            <description>Conclusion:
Our findings are relevant to the characterization of the molecular mechanism underlying the involvement of POB1/REPS2, SH3 and 14-3-3 proteins in receptor endocytosis, suggesting that 14-3-3 could work by bridging the EGF receptor and the scaffold protein POB1/REPS2. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1679186</comments>
            <pubDate>Tue, 22 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1679186</guid>        </item>
        <item>
            <title>Functional and biochemical characterization of the 20S proteasome in a yeast temperature-sensitive mutant, rpt6-1</title>
            <link>http://www.medworm.com/index.php?rid=1642235&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F20</link>
            <description>Conclusion:
Two alpha-subunits (alpha1 and alpha7) of the 20S proteasome in the rpt6-1 mutant differed from their wild-type counterparts and peptidase activities were found to be lower in the mutant than in the wild-type strain. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1642235</comments>
            <pubDate>Mon, 21 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1642235</guid>        </item>
        <item>
            <title>Modulation of the pharmacological effects of enzymatically-active PLA2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga</title>
            <link>http://www.medworm.com/index.php?rid=1575157&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F16</link>
            <description>Conclusion:
The unexpected results observed for the PLA2-BTL-2 complex strongly suggest that the pharmacological activity of this PLA2 is not solely dependent on the presence of enzymatic activity, and that other pharmacological regions may also be involved. In addition, we describe for the first time an interaction between two different molecules, which form a stable complex with significant changes in their original biological action. This opens new possibilities for understanding the function and action of crude venom, an extremely complex mixture of different molecules. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1575157</comments>
            <pubDate>Fri, 06 Jun 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1575157</guid>        </item>
        <item>
            <title>Isolation, characterization and molecular cloning of Duplex-Specific Nuclease from the hepatopancreas of the Kamchatka crab</title>
            <link>http://www.medworm.com/index.php?rid=1460746&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F14</link>
            <description>Conclusion:
We describe a new DSN from Kamchatka crab hepatopancreas, determining its primary structure and developing a preparative method for its purification. We found that DSN had unique substrate specificity, cleaving only DNA duplexes longer than 8 base pairs, or DNA in DNA-RNA hybrids. Interestingly, the DSN primary structure is homologous to well-known Serratia-like non-specific nucleases structures, but the properties of DSN are distinct. The unique substrate specificity of DSN should prove valuable in certain molecular biology applications. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1460746</comments>
            <pubDate>Wed, 21 May 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1460746</guid>        </item>
        <item>
            <title>The Mycobacterium tuberculosis Rv2540c DNA sequence encodes a bifunctional chorismate synthase</title>
            <link>http://www.medworm.com/index.php?rid=1406626&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F13</link>
            <description>Conclusions:
This is the first report showing that a bacterial CS is bifunctional. Primary deuterium kinetic isotope effects show that C4-proS hydrogen is being transferred during the reduction of FMNox by NADH and that hydride transfer contributes significantly to the rate-limiting step of FMN reduction reaction. Solvent kinetic isotope effects and proton inventory results indicate that proton transfer from solvent partially limits the rate of FMN reduction and that a single proton transfer gives rise to the observed solvent isotope effect. Multiple isotope effects suggest a stepwise mechanism for the reduction of FMNox. The results on enzyme kinetics described here provide evidence for the mode of action of MtCS and should thus pave the way for the rational design of antitubercular agent...</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1406626</comments>
            <pubDate>Tue, 29 Apr 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1406626</guid>        </item>
        <item>
            <title>Regulation of 5'-adenosine monophosphate deaminase in the freeze tolerant wood frog, Rana sylvatica</title>
            <link>http://www.medworm.com/index.php?rid=1390806&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F12</link>
            <description>Conclusion:
Maintenance of long term viability under the ischemic conditions in frozen muscle requires attention to the control of cellular energetics. Differential regulatory controls on AMPD by mechanisms including binding to muscle proteins, actions of allosteric effectors, glucose and temperature effects, and reversible phosphorylation adjust enzyme function for an optimal role in controlling cellular adenylate levels in ischemic frozen muscle. Stable modification of AMPD properties via freeze-responsive phosphorylation may contribute both to AMPD control and to coordinating AMPD function with other enzymes of energy metabolism in cold ischemic muscle. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1390806</comments>
            <pubDate>Tue, 22 Apr 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1390806</guid>        </item>
        <item>
            <title>A new classification system for bacterial Rieske non-heme iron aromatic ring-hydroxylating oxygenases</title>
            <link>http://www.medworm.com/index.php?rid=1349277&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F11</link>
            <description>Conclusion:
The new classification system provides the following features. First, the new classification system analyzes RHO enzymes as a whole. Second, the new classification system is not static but responds dynamically to the growing pool of RHO enzymes. Third, our classification can be applied reliably to the classification of incomplete RHOs. Fourth, the classification has direct applicability to experimental work. Fifth, the system provides new insights into the evolution of RHO systems based on enzyme interaction. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1349277</comments>
            <pubDate>Thu, 03 Apr 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1349277</guid>        </item>
        <item>
            <title>Pro-protein convertases control the maturation and processing of the iron-regulatory protein, RGMc/hemojuvelin</title>
            <link>http://www.medworm.com/index.php?rid=1346087&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F9</link>
            <description>Conclusions:
Our results support a key role for PCs in maturation of RGMc that has implications for the physiological actions of this critical iron-regulatory protein. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1346087</comments>
            <pubDate>Wed, 02 Apr 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1346087</guid>        </item>
        <item>
            <title>The pyrroloquinoline quinone biosynthesis pathway revisited: 
a structural approach</title>
            <link>http://www.medworm.com/index.php?rid=1331236&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F8</link>
            <description>Conclusion:
PQQ is derived from the two amino acids glutamate and tyrosine encoded in the precursor peptide PqqA. Five reactions are necessary to form this quinone cofactor. The PqqA peptide is recognised by PqqE, which links the C9 and C9a, afterwards it is accepted by PqqF which cuts out the linked amino acids. The next reaction (Schiff base) is spontaneous, the following dioxygenation is catalysed by an unknown enzyme. The last cyclization and oxidation steps are catalysed by PqqC. Taken together the known facts of the different proteins we assign a putative function to all six proteins in PQQ biosynthesis pathway. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1331236</comments>
            <pubDate>Thu, 27 Mar 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1331236</guid>        </item>
        <item>
            <title>Functional role of the additional domains in inulosucrase (IslA) from Leuconostoc citreum CW28.</title>
            <link>http://www.medworm.com/index.php?rid=1191160&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F6</link>
            <description>Conclusion:
The C-terminal domain may have been acquired to anchor inulosucrase to the cell surface. Furthermore, the acquired domains in IslA interact with the catalytic core resulting in a new conformation that renders the enzyme more stable and switch the specificity from a hydrolytic to a transglycosylase mechanism. Based on these results, chimeric constructions may become a strategy to stabilize and modulate biocatalysts based on FTF activity. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1191160</comments>
            <pubDate>Thu, 31 Jan 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1191160</guid>        </item>
        <item>
            <title>Components of the ubiquitin-proteasome pathway compete for surfaces on Rad23 family proteins</title>
            <link>http://www.medworm.com/index.php?rid=1188342&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F4</link>
            <description>Conclusions:
We conclude that the competition of ubiquitin-proteasome pathway components for surfaces on Rad23 is important for the role of the Rad23 family proteins in proteasomal targeting. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1188342</comments>
            <pubDate>Wed, 30 Jan 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1188342</guid>        </item>
        <item>
            <title>Thermal dependency of RAG1 self-association properties</title>
            <link>http://www.medworm.com/index.php?rid=1188341&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F5</link>
            <description>Conclusions:
Together these results confirm that the functional form of RAG1 in V(D)J recombination is in the dimeric state, and that its stability under physiological conditions likely requires complex formation with RAG2. Additionally, in future structural and functional studies of RAG1, it will be important to take into account the temperature-dependent self-association properties of RAG1 described in this study. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1188341</comments>
            <pubDate>Wed, 30 Jan 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1188341</guid>        </item>
        <item>
            <title>Blocking Binding of Bacillus thuringiensis Cry1Aa to Bombyx mori Cadherin Receptor Results in Only a Minor Reduction of Toxicity</title>
            <link>http://www.medworm.com/index.php?rid=1174770&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F3</link>
            <description>Conclusion:
The results identify a novel receptor-binding epitope and demonstrate that virtual elimination of binding to cadherin BR-175 does not completely remove toxicity in the case of B. mori. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1174770</comments>
            <pubDate>Thu, 24 Jan 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1174770</guid>        </item>
        <item>
            <title>Association of SAP130/SF3b-3 with Cullin-RING ubiquitin ligase complexes and its regulation by the COP9 signalosome</title>
            <link>http://www.medworm.com/index.php?rid=1128454&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F9%2F1</link>
            <description>Conclusions:
SAP130 is a cullin binding protein that is likely involved in the Nedd8 pathway. The association of SAP130 with various cullin member proteins such as Cul1, Cul2 and Cul4A is modulated by CAND1 and CSN. As an established component of transcription and RNA processing complexes, we hypothesis that SAP130 may link CRL mediated ubiquitination to gene expression. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1128454</comments>
            <pubDate>Thu, 03 Jan 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1128454</guid>        </item>
        <item>
            <title>Binding to DPF-motif by the POB1 EH domain is responsible for POB1-Eps15 interaction</title>
            <link>http://www.medworm.com/index.php?rid=1111379&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F29</link>
            <description>Conclusions:
In the present study we have analysed the binding specificity of the POB1 EH domain. We show that it differs from other EH domains since it interacts with both NPF- and DPF-containing sequences. These unusual binding properties could be attributed to a different conformation of the binding pocket that allows to accommodate negative charges; moreover, we identified a cluster of solvent exposed Lys residues, which are only found in the EH domain of POB1, and influence binding to both NPF and DPF motifs. The characterization of structures of the DPF ligands described in this study and the POB1 EH domain will clearly determine the involvement of the positive patch and the rationalization of our findings. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1111379</comments>
            <pubDate>Fri, 21 Dec 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1111379</guid>        </item>
        <item>
            <title>Downregulation of COP9 signalosome subunits differentially affects CSN complex and target protein stability</title>
            <link>http://www.medworm.com/index.php?rid=1105958&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F27</link>
            <description>Conclusions:
There exists a coordinated downregulation of CSN subunits in the CSN1 and CSN3 knockdowns. The underlying regulatory mechanisms are obscure. CSN5 seems to possess a specific status in HeLa cells. Its reduction is not connected with coordinated downregulation of other subunits. CSN knockdowns confirm that the stabilization of the CRL component Rbx1 is a major CSN function. In addition, downregulation of CSN subunits influences the stability of important cellular regulators such as c-Jun and p27. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1105958</comments>
            <pubDate>Wed, 19 Dec 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1105958</guid>        </item>
        <item>
            <title>Glutathionylation of beta-actin via a cysteinyl
sulfenic acid intermediary</title>
            <link>http://www.medworm.com/index.php?rid=1084057&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F26</link>
            <description>Conclusions:
We conclude that glutathionylation of beta-actin may occur via spontaneous oxidation of a cysteinyl residue to a sulfenic acid that readily reacts with GSH to form a mixed disulfide. We also show that the reactivity and oxidation to a reactive protein thiol intermediary differ between different actin isoforms. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1084057</comments>
            <pubDate>Mon, 10 Dec 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1084057</guid>        </item>
        <item>
            <title>Metabolic signature of breast cancer cell line MCF-7: 
profiling of modified nucleosides via LC-IT MS coupling</title>
            <link>http://www.medworm.com/index.php?rid=1059765&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F25</link>
            <description>Conclusion:
The obtained results are discussed against the background of pathological changes in cell metabolism, resulting in new perspectives for modified nucleosides and related metabolites as possible biomedical markers for breast carcinoma in vivo. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1059765</comments>
            <pubDate>Thu, 29 Nov 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1059765</guid>        </item>
        <item>
            <title>Membrane binding of the neuronal calcium sensor recoverin - modulatory role of the charged carboxy-terminus</title>
            <link>http://www.medworm.com/index.php?rid=1045886&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F24</link>
            <description>Conclusions:
Our data indicate a small, but evident electrostatic contribution to the overall binding energy of recoverin association with lipid bilayer. Properties of the charged carboxy-terminus are consistent with a role of this region as an internal effector region that prolongs the time recoverin stays on the membrane by influencing its Ca2+-sensitivity. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1045886</comments>
            <pubDate>Thu, 22 Nov 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1045886</guid>        </item>
        <item>
            <title>The FTO (fat mass and obesity associated) gene codes for a novel member of the non-heme dioxygenase superfamily</title>
            <link>http://www.medworm.com/index.php?rid=1014746&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F23</link>
            <description>Conclusions:
Our analysis suggests that human FTO is a member of the non-heme dioxygenase (Fe(II)- and 2-oxoglutarate-dependent dioxygenases) superfamily. Amino acid conservation patterns support this hypothesis and indicate that both 2-oxoglutarate and iron should be important for FTO function. This computational prediction of the function of FTO should suggest further steps for its experimental characterization and help to formulate hypothesis about the mechanisms by which it relates to obesity in humans. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1014746</comments>
            <pubDate>Thu, 08 Nov 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1014746</guid>        </item>
        <item>
            <title>Recognition of essential purines by the U1A protein</title>
            <link>http://www.medworm.com/index.php?rid=1000596&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F22</link>
            <description>Conclusions:
These investigations identify different roles that hydrogen bond donors and acceptors on bases in both cognate and non-cognate RNA play in the specific recognition of RNA by the U1A protein. Taken together with investigations of other RNA-RRM complexes, the results contribute to a general understanding of the origins of RNA-RRM specificity and highlight, in particular, the contribution of steric and electrostatic repulsion to binding specificity. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1000596</comments>
            <pubDate>Fri, 02 Nov 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1000596</guid>        </item>
        <item>
            <title>Aminopeptidase B, a glucagon-processing enzyme: site directed mutagenesis of the Zn2+-binding motif and molecular modelling</title>
            <link>http://www.medworm.com/index.php?rid=994690&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F21</link>
            <description>Conclusions:
Alignment of the primary structures of the M1 family members clearly demonstrates the existence of different sub-families and highlights crucial residues in the enzymatic activity of the whole family. E. coli recombinant enzyme and Ap-B structural model constitute powerful tools for investigating the importance and possible roles of these conserved residues in Ap-B, LTA4H and M1 aminopeptidase catalytic sites and to gain new insight into their physiological functions. Analysis of Ap-B structural model indicates that several interactions between Ap-B and proteins can occur and suggests that endopeptidases might form a complex with Ap-B during hormone processing. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=994690</comments>
            <pubDate>Wed, 31 Oct 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">994690</guid>        </item>
        <item>
            <title>A study on the two binding sites of hexokinase on brain mitochondria</title>
            <link>http://www.medworm.com/index.php?rid=965111&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F20</link>
            <description>Conclusion:
Use of very low concentrations of KSCN at about 10% of the level previously 
reported to cause total release of HK-I from the G6P- insensitive site, caused partial 
release from this site in a reproducible manner. In contrast to site A, no 
rebinding of the enzyme takes place on site B, suggesting that site A is ` the only 
physiologically-important site in relation to the release-rebinding of the enzyme which occur in response to the energy requirements of the brain. Based on the results presented, a possible physiological role for distribution of the enzyme between the two sites on the mitochondrion is proposed. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=965111</comments>
            <pubDate>Sat, 20 Oct 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">965111</guid>        </item>
        <item>
            <title>The subunit composition of human extracellular superoxide dismutase (EC-SOD) regulates enzymatic activity</title>
            <link>http://www.medworm.com/index.php?rid=950812&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F19</link>
            <description>Conclusion:
This finding shows that the aEC-SOD and iEC-SOD subunits combine in all 3 possible ways supporting the presence of tetrameric enzymes with variable enzymatic activity. This variation may regulate the antioxidant level in the extracellular space and represent a novel way of modulating enzymatic activity in general. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=950812</comments>
            <pubDate>Mon, 15 Oct 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">950812</guid>        </item>
        <item>
            <title>R7-binding protein targets the G protein beta5/R7-regulator of G protein signaling complex to lipid rafts in neuronal cells and brain</title>
            <link>http://www.medworm.com/index.php?rid=885142&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F18</link>
            <description>Conclusions:
A fraction of Gbeta5/R7-RGS/R7BP protein complexes is targeted to low-density, detergent-resistant membrane lipid rafts in PC12 cells and brain. In cultured cells, the palmitoylation status of R7BP regulated the lipid raft targeting of endogenous or co-expressed Gbeta5/R7-RGS proteins. Taken together with recent evidence that the kinetic effects of the Gbeta5 complex on GPCR signaling are greatly enhanced by R7BP palmitoylation through a membrane-anchoring mechanism, our data suggest the targeting of the Gbeta5/R7-RGS/R7BP complex to lipid rafts in neurons and brain, where G proteins and their effectors are concentrated, may be central to the G protein regulatory function of the complex. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=885142</comments>
            <pubDate>Wed, 19 Sep 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">885142</guid>        </item>
        <item>
            <title>Thiamine diphosphate adenylyl transferase from E. coli:
functional characterization of the enzyme synthesizing adenosine thiamine triphosphate</title>
            <link>http://www.medworm.com/index.php?rid=803366&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F17</link>
            <description>Conclusion:
This is the first demonstration of an enzyme activity transferring a nucleotidyl group on thiamine diphosphate to produce AThTP. The existence of a mechanism for the enzymatic synthesis of this compound is in agreement with the hypothesis of a non-cofactor role for thiamine derivatives in living cells. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=803366</comments>
            <pubDate>Thu, 16 Aug 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">803366</guid>        </item>
        <item>
            <title>C-terminal processing of yeast Spt7 occurs in the absence 
of functional SAGA complex</title>
            <link>http://www.medworm.com/index.php?rid=788004&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F16</link>
            <description>Conclusion:
We conclude that truncation of Spt7 occurs early in the biosynthesis of distinct Spt7 containing complexes rather than being a dynamic process linked to the action of the SAGA complex in transcriptional regulation. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=788004</comments>
            <pubDate>Wed, 08 Aug 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">788004</guid>        </item>
        <item>
            <title>Module structure of interphotoreceptor retinoid-binding protein (IRBP) may provide bases for its complex role in the visual cycle - structure / function study of Xenopus IRBP</title>
            <link>http://www.medworm.com/index.php?rid=778429&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F15</link>
            <description>Conclusions:
Although its four modules are homologous and each capable of supporting ligand-binding activity, structural differences between their ligand-binding domains, and interactions between the modules themselves will be critical to understanding IRBP's complex role in the visual cycle. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=778429</comments>
            <pubDate>Sat, 04 Aug 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">778429</guid>        </item>
        <item>
            <title>ExplorEnz: a MySQL database of the IUBMB enzyme nomenclature</title>
            <link>http://www.medworm.com/index.php?rid=762875&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F14</link>
            <description>Conclusions:
ExplorEnz has powerful and flexible search capabilities and provides the scientific community with the most up-to-date version of the IUBMB Enzyme List. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=762875</comments>
            <pubDate>Fri, 27 Jul 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">762875</guid>        </item>
        <item>
            <title>Effects of the deletion of the Escherichia coli frataxin homologue CyaY on the respiratory NADH:ubiquinone oxidoreductase</title>
            <link>http://www.medworm.com/index.php?rid=755510&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F13</link>
            <description>Conclusions:
CyaY plays a non-essential role in the assembly of complex I in E. coli. It is not a structural component but may transiently interact with the complex. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=755510</comments>
            <pubDate>Tue, 24 Jul 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">755510</guid>        </item>
        <item>
            <title>Comparison of interactions between beta-hairpin decapeptides and SDS/DPC micelles from experimental and simulation data</title>
            <link>http://www.medworm.com/index.php?rid=737419&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F11</link>
            <description>Conclusions:
We demonstrate here the accuracy of molecular dynamics simulations methods through comparison with experiments, and have used the simulation results to enhance the understanding of how these two peptides interact with the two types of micelles. We find agreement between simulation and experimental results in the final structure of the peptides and in the peptides final conformation with respect to the micelle. Looking in depth at the peptide interactions, we find differences in the interactions between the two peptides from the simulation data; Leu-1 on PC-72 interacts strongly with the SDS micelle, though the interaction is not persistent - the residue withdraws and inserts into the micelle throughout the simulation. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=737419</comments>
            <pubDate>Mon, 16 Jul 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">737419</guid>        </item>
        <item>
            <title>Presence of thiamine pyrophosphate in mammalian peroxisomes</title>
            <link>http://www.medworm.com/index.php?rid=699141&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F10</link>
            <description>Conclusions:
Our results clearly indicate that mammalian peroxisomes do contain TPP but that no pyrophosphorylation of thiamine occurs in these organelles, implying that thiamine must enter the peroxisome already pyrophosphorylated. Consequently, TPP entry may depend on a specific transport system or, in a bound form, on HACL1 translocation. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=699141</comments>
            <pubDate>Wed, 27 Jun 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">699141</guid>        </item>
        <item>
            <title>Role of the linker region in the expression of Rhizopus oryzae glucoamylase</title>
            <link>http://www.medworm.com/index.php?rid=694078&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F9</link>
            <description>Conclusions:
Our data provide direct evidence that the length, composition, and glycosylation of the interdomain linker play a central role in the structure and function of RoGA. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=694078</comments>
            <pubDate>Mon, 25 Jun 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">694078</guid>        </item>
        <item>
            <title>Revalidation and rationale for high pKa values of unconjugated bilirubin.</title>
            <link>http://www.medworm.com/index.php?rid=596059&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F7</link>
            <description>Conclusions:
These results support the high pKa values of unconjugated bilirubin, above 8.0, derived from our earlier solvent partition study. In both studies, our measurements were based on the rapid analysis of clearly under-saturated solutions of highly-purified bilirubin over a wide pH range, using properly purified and preserved solvents. No previous direct estimate of the aqueous pKa values of unconjugated bilirubin meets all these preconditions. Three theoretical factors acting in combination, each related to the unique, extensive internal H-bonding of the -COOH groups, are proposed to support high pKa values of unconjugated bilirubin in water: a) donation of an H-bond from the -OH moiety of the -COOH group, which is broken on ionization; b) hindered solvation of the -COO- group aft...</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=596059</comments>
            <pubDate>Wed, 02 May 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">596059</guid>        </item>
        <item>
            <title>Mapping of possible prion protein self interaction domains using peptide arrays</title>
            <link>http://www.medworm.com/index.php?rid=542994&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F6</link>
            <description>Conclusions:
Binding of MBP-PrP to PrP-specific sequences indicate that several specific self interactions between individual PrP molecules can occur and suggest that an array of interactions between PrPC-PrPC as well as PrPC-PrPSc may be possible, which ultimately lead to variations in species barrier and strain differences. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=542994</comments>
            <pubDate>Thu, 12 Apr 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">542994</guid>        </item>
        <item>
            <title>A novel bifunctional N-acetylglutamate synthase-kinase from Xanthomonas campestris that is closely related to mammalian N-acetylglutamate synthase</title>
            <link>http://www.medworm.com/index.php?rid=542995&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F4</link>
            <description>Conclusion:
The close phylogenetic relationship and similar biochemical properties of xanthomonad NAGS-K and mammalian NAGS suggest that we have identified a close relative to the bacterial antecedent of mammalian NAGS and that the enzyme from X. campestris could become a good model for mammalian NAGS in structural, biochemical and biophysical studies. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=542995</comments>
            <pubDate>Tue, 10 Apr 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">542995</guid>        </item>
        <item>
            <title>Expression and localization of estrogenic type 12 17beta-hydroxysteroid dehydrogenase in the cynomolgus monkey</title>
            <link>http://www.medworm.com/index.php?rid=404057&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F2</link>
            <description>Conclusions:
These results strongly suggest that the Macaca fascicularis 17beta-HSD12 is an essential partner of aromatase in the biosynthesis of estradiol (E2). It strongly suggests that in the estradiol biosynthesis pathway, the step of 17-ketoreduction comes after the step of the aromatization (the aromatization of 4-androstendione to estrone followed by the conversion of estrone into estradiol by estrogen specific 17beta-HSDs) which is in contrast with the hypothesis suggesting that 4-androstenedione is converted to testosterone followed by the aromatization of testosterone. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=404057</comments>
            <pubDate>Mon, 05 Feb 2007 07:00:00 +0100</pubDate>
            <guid isPermaLink="false">404057</guid>        </item>
        <item>
            <title>Expression and localization of estrogenic type 12 17β-hydroxysteroid dehydrogenase in the cynomolgus monkey</title>
            <link>http://www.medworm.com/index.php?rid=456265&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F8%2F2</link>
            <description>Conclusion:
These results strongly suggest that the Macaca fascicularis 17β-HSD12 is an essential partner of aromatase in the biosynthesis of estradiol (E2). It strongly suggests that in the estradiol biosynthesis pathway, the step of 17-ketoreduction comes after the step of the aromatization (the aromatization of 4-androstendione to estrone followed by the conversion of estrone into estradiol by estrogen specific l7β-HSDs) which is in contrast with the hypothesis suggesting that 4-androstenedione is converted to testosterone followed by the aromatization of testosterone. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=456265</comments>
            <pubDate>Mon, 05 Feb 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">456265</guid>        </item>
        <item>
            <title>Characterization of a β-glucanase produced by Rhizopus microsporus var. microsporus, and its potential for application in the brewing industry</title>
            <link>http://www.medworm.com/index.php?rid=343986&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F7%2F23</link>
            <description>Conclusion:
The zygomycete microfungus R. microsporus var. microsporus produced a 1,3-1,4-β-D-glucan 4-glucanhydrolase (EC 3.2.1.73) which is able to hydrolyze β-D-glucan that contains both the 1,3- and 1,4-bonds (barley β-glucans). Its molecular mass was 33.7 kDa. Maximum activity was detected at pH values in the range of 4–5, and temperatures in the range of 50–60°C. The enzyme was able to reduce both the viscosity of the brewer mash and the filtration time, indicating its potential value for the brewing industry. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=343986</comments>
            <pubDate>Tue, 05 Dec 2006 07:00:00 +0100</pubDate>
            <guid isPermaLink="false">343986</guid>        </item>
        <item>
            <title>The DNA polymerase activity of Pol ε holoenzyme is required for rapid and efficient chromosomal DNA replication in Xenopus egg extracts</title>
            <link>http://www.medworm.com/index.php?rid=343987&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F7%2F21</link>
            <description>Conclusion:
These results indicate that the DNA polymerase activity of Pol ε holoenzyme plays an essential role in normal chromosomal DNA replication in Xenopus egg extracts. These are the first biochemical data to show the DNA polymerase activity of Pol ε holoenzyme is essential for chromosomal DNA replication in higher eukaryotes, unlike in yeasts. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=343987</comments>
            <pubDate>Tue, 22 Aug 2006 06:00:00 +0100</pubDate>
            <guid isPermaLink="false">343987</guid>        </item>
        <item>
            <title>Identification, cloning and characterization of a novel 47 kDa murine PKA C subunit homologous to human and bovine Cβ2</title>
            <link>http://www.medworm.com/index.php?rid=343988&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F7%2F20</link>
            <description>Conclusion:
Murine lymphoid tissues express a protein that is a homologue of human and bovine Cβ2. The murine Cβ gene encodes the splice variants Cβ1, Cβ2, Cβ3 and Cβ4, as is the case with the human Cβ gene. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=343988</comments>
            <pubDate>Fri, 04 Aug 2006 06:00:00 +0100</pubDate>
            <guid isPermaLink="false">343988</guid>        </item>
        <item>
            <title>Influence of simulated microgravity on the activation of the small GTPase Rho involved in cytoskeletal formation – molecular cloning and sequencing of bovine leukemia-associated guanine nucleotide exchange factor</title>
            <link>http://www.medworm.com/index.php?rid=343989&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F7%2F19</link>
            <description>Conclusion:
The activation of the small GTPase Rho was influenced by simulated microgravity generated by a three-dimensional (3D) clinostat. Furthermore, the full-length cDNA of bovine LARG, a member of the Rho guanine nucleotide exchange factor (GEF) family, was identified, and its gene expression was observed to be downregulated under clinorotation. This downregulation subsequently resulted in the repression of RhoA activation. These results indicated that the disorganization of the actin fibers was caused by the inhibition of Rho activation by 3D clinorotation. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=343989</comments>
            <pubDate>Wed, 28 Jun 2006 06:00:00 +0100</pubDate>
            <guid isPermaLink="false">343989</guid>        </item>
        <item>
            <title>Calcium adsorption and displacement: characterization of lipid monolayers and their interaction with membrane-active peptides/proteins</title>
            <link>http://www.medworm.com/index.php?rid=343990&amp;cid=s_34019_60_f&amp;fid=34019&amp;url=http%3A%2F%2Fwww.biomedcentral.com%2F1471-2091%2F7%2F15</link>
            <description>Conclusion:
To characterize the electrical properties of negatively charged phospholipids and LPSs and their electrostatic interaction with various polycationic peptides/proteins, the adsorption of calcium to and displacement from lipid monolayers is a suitable parameter. Using the calcium displacement method, the binding of peptides to monolayers can be determined even if they do not intercalate. The interpretation of ζ-potential data is difficulty for LPS aggregates, because of the complex three-dimensional structure of the LPS molecules. However, the influence of peptides/proteins on the ζ-potential can be used to characterize the underlying interaction mechanisms. (Source: BMC Biochemistry)</description>
            <author>BMC Biochemistry</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=343990</comments>
            <pubDate>Wed, 03 May 2006 06:00:00 +0100</pubDate>
            <guid isPermaLink="false">343990</guid>        </item>
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