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        <title>Chembiochem 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 'Chembiochem' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Chembiochem&t=Chembiochem&s=Search&f=source]]></link>
        <lastBuildDate>Mon, 06 Feb 2012 13:31:37 +0100</lastBuildDate>
        <item>
            <title>In-Cell Solid-State NMR as a Tool to Study Proteins in Large Complexes.</title>
            <link>http://www.medworm.com/index.php?rid=5654689&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22298299%26dopt%3DAbstract</link>
            <description>Authors: Reckel S, Lopez JJ, Löhr F, Glaubitz C, Dötsch V
    Abstract
    A major limitation of solution NMR is molecular tumbling, which is often too slow for detection. Here we demonstrate that solid-state NMR spectroscopy in combination with flash freezing of cells can be used to detect proteins in the cellular environment and provides information on backbone chemical shifts.
    PMID: 22298299 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5654689</comments>
            <pubDate>Wed, 01 Feb 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Sequence Determinants Governing the Topology and Biological Activity of a Lasso Peptide, Microcin J25.</title>
            <link>http://www.medworm.com/index.php?rid=5654692&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22287061%26dopt%3DAbstract</link>
            <description>In this study, we rationally designed and performed site-specific mutations in order to pinpoint the sequence determinants of the lasso topology. Structures of the resulting variants were analysed by a combination of methods (mass spectrometry, NMR spectroscopy, enzymatic digestion), and correlated to the antibacterial activity. The selected mutations resulted in the production of branched-cyclic or lasso variants. The C-terminal residues below the ring (Tyr20, Gly21) and the size of the macrolactam ring were revealed to be critical for both the lasso scaffold and bioactivity, while shortening the loop region (Tyr9-Ser18) or extending the C-terminal tail below the ring did not alter the lasso structure, but differentially affected the antibacterial activity. These results provide new insig...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5654692</comments>
            <pubDate>Fri, 27 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5654692</guid>        </item>
        <item>
            <title>An Enzyme Catalyzing O-Prenylation of the Glucose Moiety of Fusicoccin A, a Diterpene Glucoside Produced by the Fungus Phomopsis amygdali.</title>
            <link>http://www.medworm.com/index.php?rid=5654690&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22287087%26dopt%3DAbstract</link>
            <description>In this study, we identified for the first time, from a genome database of P. amygdali, a gene (papt) encoding a prenyltransferase that reversibly transfers dimethylallyl diphosphate (DMAPP) to the 6'-hydroxy group of the glucose moiety of FC A to yield an O-prenylated sugar. An in vitro assay with a recombinant enzyme was also developed. Detailed analyses with recombinant PAPT showed that the enzyme is likely to be a monomer and requires no divalent cations. The optimum pH and temperature were 8.0 and 50 °C, respectively. K(m) values were calculated as 0.49±0.037 μM for FC P (a plausible intermediate of FC A biosynthesis) and 8.3±0.63 μM for DMAPP, with a k(cat) of 55.3±3.3×10(-3) s. The enzyme did not act on representative substrates of the above-mentioned three types of prenylt...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5654690</comments>
            <pubDate>Fri, 27 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5654690</guid>        </item>
        <item>
            <title>Discovery of the Rhizopodin Biosynthetic Gene Cluster in Stigmatella aurantiaca Sg a15 by Genome Mining.</title>
            <link>http://www.medworm.com/index.php?rid=5636563&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22278953%26dopt%3DAbstract</link>
            <description>Authors: Pistorius D, Müller R
    Abstract
    The field of bacterial natural product research is currently undergoing a paradigm change concerning the discovery of natural products. Previously most efforts were based on isolation of the most abundant compound in an extract, or on tracking bioactivity. However, traditional activity-guided approaches are limited by the available test panels and frequently lead to the rediscovery of already known compounds. The constantly increasing availability of bacterial genome sequences provides the potential for the discovery of a huge number of new natural compounds by in silico identification of biosynthetic gene clusters. Examination of the information on the biosynthetic machinery can further prevent rediscovery of known compounds, and can help i...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636563</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636563</guid>        </item>
        <item>
            <title>Redundant Pathways of Sunscreen Biosynthesis in a Cyanobacterium.</title>
            <link>http://www.medworm.com/index.php?rid=5636562&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22278966%26dopt%3DAbstract</link>
            <description>Authors: Spence E, Dunlap WC, Shick JM, Long PF
    Abstract
    Route of the sun block: According to empirical evidence, sun-screening mycosporine-like amino acids (MAAs) in Eukarya originate from the shikimic acid pathway, whereas in cyanobacteria, biosynthesis of the MAA shinorine reportedly occurs through the pentose phosphate pathway. However, gene deletion shows that the cyanobacterium Anabaena variabilis ATCC 29143 does not biosynthesise shinorine exclusively by this route.
    PMID: 22278966 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636562</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636562</guid>        </item>
        <item>
            <title>NMR as an Effective Tool for the Structure Determination of Lasso Peptides.</title>
            <link>http://www.medworm.com/index.php?rid=5636561&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22278977%26dopt%3DAbstract</link>
            <description>Authors: Xie X, Marahiel MA
    Abstract
    Lasso peptides: unique structure and unusual stability: The highly ordered structures of lasso peptides comprising 16-21 amino acids render them unusually stable. The extremely neat 2D NMR spectra obtained in organic solvents makes NMR a powerful tool for determining these lasso structures.
    PMID: 22278977 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636561</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636561</guid>        </item>
        <item>
            <title>A FlAsH Reporter for Protein-Dimerization Triggers.</title>
            <link>http://www.medworm.com/index.php?rid=5636560&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22278994%26dopt%3DAbstract</link>
            <description>Authors: Stafforst T
    Abstract
    A FlAsH of potential: The specific binding of the biarsenical probe to the tetracysteine motif has matured as a tool for cell biology studies. Combining two such binders in one probe generates a useful reporter of protein dimerization events. The current state of art and the perspective for future developments are highlighted.
    PMID: 22278994 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636560</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636560</guid>        </item>
        <item>
            <title>Effects of Single Genetic Damage in Carbohydrate-Recognizing Proteins in Mouse Serum N-Glycan Profile Revealed by Simple Glycotyping Analysis.</title>
            <link>http://www.medworm.com/index.php?rid=5636571&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22271523%26dopt%3DAbstract</link>
            <description>Authors: Amano M, Hashimoto R, Nishimura SI
    Abstract
    Gene knock-out of C-type lectin receptors expressed in dendritic cells induced significant alteration of serum N-glycans compared with that of gender-matched controls. Glycotyping analysis suggested that putative-core fucosylation is strongly influenced by differences in the dominant mechanisms after carbohydrate recognition by pattern-recognition receptors, endocytosis of ligands, or induction of cytokines/chemokines. However, the loss of galectin-9, a ligand for T-helper type 1-specific cell-surface molecule, did not affect most N-glycan profiles. Interestingly, lack of the Chst3 gene (chondroitin 6-sulfotransferase) appeared to influence markedly the expression of most N-glycans, especially highly modified glycoforms bearing m...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636571</comments>
            <pubDate>Tue, 24 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636571</guid>        </item>
        <item>
            <title>A Single Active Site Mutation Inverts Stereoselectivity of 16-Hydroxylation of Testosterone Catalyzed by Engineered Cytochrome P450 BM3.</title>
            <link>http://www.medworm.com/index.php?rid=5636564&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22275147%26dopt%3DAbstract</link>
            <description>Authors: Venkataraman H, de Beer SB, van Bergen LA, van Essen N, Geerke DP, Vermeulen NP, Commandeur JN
    Abstract
    Inversion of stereoselectivity: screening of a minimal mutant library revealed a cytochrome P450 BM3 variant M01 A82W S72I capable of producing 16 α-OH-testosterone. Remarkably, a single active site mutation S72I in M01 A82W inverted the stereoselectivity of hydroxylation from 16 β to 16 α. Introduction of S72I mutation in another 16 β-OH-selective variant M11 V87I, also resulted in similar inversion of stereoselectivity.
    PMID: 22275147 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636564</comments>
            <pubDate>Tue, 24 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636564</guid>        </item>
        <item>
            <title>The Myxobacterial Compounds Spirangien A and Spirangien M522 are Potent Inhibitors of IL-8 Expression.</title>
            <link>http://www.medworm.com/index.php?rid=5636570&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22271561%26dopt%3DAbstract</link>
            <description>Authors: Reboll MR, Ritter B, Sasse F, Niggemann J, Frank R, Nourbakhsh M
    Abstract
    Elevated expression of interleukin-8 (IL-8) has been implicated in inflammatory diseases, in tumor growth, and in angiogenesis. The aim of this study was to identify natural or synthetic compounds that suppress IL-8 production in response to interleukin-1 (IL-1), the natural inflammatory stimulus of the IL-8 gene. We therefore developed an IL-1-inducible cell-based screening assay by stable integration of an IL-8 reporter gene into HeLa S3 cells. The screening of heterogeneous compound libraries revealed several compounds that displayed an inhibitory effect on the reporter gene expression. Following hit validation, we focused on the most efficient compound, spirangien A, and its chemical derivate spi...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636570</comments>
            <pubDate>Mon, 23 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636570</guid>        </item>
        <item>
            <title>Base Pairing at the Abasic Site in DNA Duplexes and Its Application in Adenosine Aptasensors.</title>
            <link>http://www.medworm.com/index.php?rid=5636569&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22271570%26dopt%3DAbstract</link>
            <description>Authors: Pang Y, Xu Z, Sato Y, Nishizawa S, Teramae N
    Abstract
    The binding of nucleosides to abasic site (AP site)-containing DNA duplexes (AP-DNAs) carrying complementary nucleosides opposite the AP site was investigated by thermal denaturation and isothermal titration calorimetric (ITC) experiments. Purine nucleosides show high affinities (K(d) =14.1 μM for adenosine and 41.8 μM for guanosine) for binding to the AP-DNAs, and the interactions are driven primarily by the enthalpy change, similarly to the case of DNA intercalators. In contrast, pyrimidine nucleosides do not show noticeable binding to the AP-DNAs, thus suggesting that stacking interaction at the AP site plays a key role in the binding of purine nucleosides to the AP-DNAs, as revealed by ITC measurements. Next, to a...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636569</comments>
            <pubDate>Mon, 23 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636569</guid>        </item>
        <item>
            <title>Photocaged DNA Provides New Levels of Transcription Control.</title>
            <link>http://www.medworm.com/index.php?rid=5636568&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22271631%26dopt%3DAbstract</link>
            <description>Authors: Ceo LM, Koh JT
    Abstract
    Spot lit: Photocaged nucleic acids have been used to regulate gene expression through the action of light. Whereas most methods target mRNAs, DNA decoys have recently been used to target DNA transcription by targeting specific DNA-transcription-factor interactions. This has allowed researchers to &quot;turn-off&quot; transcription through the action of light on caged nucleic acids for the first time.
    PMID: 22271631 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636568</comments>
            <pubDate>Mon, 23 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636568</guid>        </item>
        <item>
            <title>Stereoselective Hydride Transfer by Aryl-Alcohol Oxidase, a Member of the GMC Superfamily.</title>
            <link>http://www.medworm.com/index.php?rid=5636567&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22271643%26dopt%3DAbstract</link>
            <description>Authors: Hernández-Ortega A, Ferreira P, Merino P, Medina M, Guallar V, Martínez AT
    Abstract
    Primary alcohol oxidation by aryl-alcohol oxidase (AAO), a flavoenzyme providing H(2) O(2) to ligninolytic peroxidases, is produced by concerted proton and hydride transfers, as shown by substrate and solvent kinetic isotope effects (KIEs). Interestingly, when the reaction was investigated with synthesized (R)- and (S)-α-deuterated p-methoxybenzyl alcohol, a primary KIE (≈6) was observed only for the R enantiomer, revealing that the hydride transfer is highly stereoselective. Docking of p-methoxybenzyl alcohol at the buried crystal active site, together with QM/MM calculations, showed that this stereoselectivity is due to the position of the hydride- and proton-receiving atoms (flavin ...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636567</comments>
            <pubDate>Mon, 23 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636567</guid>        </item>
        <item>
            <title>An Adaptable Luminescence Resonance Energy Transfer Assay for Measuring and Screening Protein-Protein Interactions and their Inhibition.</title>
            <link>http://www.medworm.com/index.php?rid=5636566&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22271654%26dopt%3DAbstract</link>
            <description>Authors: Yapici E, Reddy DR, Miller LW
    Abstract
    Protein-protein interactions (PPIs) are central to biological processes and represent an important class of therapeutic targets. Here we show that the interaction between FK506-binding protein 12 fused to green fluorescent protein (GFP-FKBP) and the rapamycin-binding domain of mTor fused to Escherichia coli dihydrofolate reductase (FRB-eDHFR) can be sensitively detected (signal-to-background ratio (S/B)&amp;gt;100) and accurately quantified within an impure cell lysate matrix using a luminescence resonance energy transfer (LRET) assay. Ascomycin-mediated inhibition of GFP-FKBP-rapamycin-FRB-eDHFR complex formation was also detected at high S/B ratio (&amp;gt;80) and Z'-factor (0.89). The method leverages the selective, stable binding of trime...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636566</comments>
            <pubDate>Mon, 23 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636566</guid>        </item>
        <item>
            <title>Identification of Hydrophobic Tags for the Degradation of Stabilized Proteins.</title>
            <link>http://www.medworm.com/index.php?rid=5636565&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22271667%26dopt%3DAbstract</link>
            <description>In this report, we employed a chemical approach to extend this hydrophobic tagging methodology to highly stabilized proteins by synthesizing and evaluating a library of HyTs, which led to the identification of HyT36.
    PMID: 22271667 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636565</comments>
            <pubDate>Mon, 23 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636565</guid>        </item>
        <item>
            <title>Abstracts.</title>
            <link>http://www.medworm.com/index.php?rid=5618501&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246811%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22246811 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618501</comments>
            <pubDate>Sun, 22 Jan 2012 17:31:19 +0100</pubDate>
            <guid isPermaLink="false">5618501</guid>        </item>
        <item>
            <title>Preview: ChemBioChem 3/2012.</title>
            <link>http://www.medworm.com/index.php?rid=5618500&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246812%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22246812 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618500</comments>
            <pubDate>Sun, 22 Jan 2012 17:31:10 +0100</pubDate>
            <guid isPermaLink="false">5618500</guid>        </item>
        <item>
            <title>Imaging the Sialome during Zebrafish Development with Copper-Free Click Chemistry.</title>
            <link>http://www.medworm.com/index.php?rid=5618495&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22262667%26dopt%3DAbstract</link>
            <description>Authors: Dehnert KW, Baskin JM, Laughlin ST, Beahm BJ, Naidu NN, Amacher SL, Bertozzi CR
    Abstract
    The sialome is comprised of sialylated glycoproteins and glycolipids that play essential roles in cell-cell communication. Using azide-modified molecular precursors of sialic acids and copper-free click chemistry, we visualized the spatiotemporal dynamics of the sialome in live zebrafish embryos.
    PMID: 22262667 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618495</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618495</guid>        </item>
        <item>
            <title>Cell Interaction Study of Amyloid by Using Luminescent Conjugated Polythiophene: Implication that Amyloid Cytotoxicity Is Correlated with Prolonged Cellular Binding.</title>
            <link>http://www.medworm.com/index.php?rid=5618497&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22262644%26dopt%3DAbstract</link>
            <description>Authors: Zako T, Sakono M, Kobayashi T, Sörgjerd K, Nilsson KP, Hammarström P, Lindgren M, Maeda M
    Abstract
    Needles and noodles: Studying amyloid toxicity is important for understanding protein misfolding diseases. Using a luminescent conjugated polythiophene, we found that cell binding of nontoxic filamentous amyloids of insulin and β2-microglobulin was less efficient than that of toxic fibrillar amyloids; this suggests a correlation between amyloid toxicity and cell binding.
    PMID: 22262644 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618497</comments>
            <pubDate>Thu, 19 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618497</guid>        </item>
        <item>
            <title>5-Thiomannosides Block the Biosynthesis of Dolichol-Linked Oligosaccharides and Mimic Class I Congenital Disorders of Glycosylation.</title>
            <link>http://www.medworm.com/index.php?rid=5618496&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22262650%26dopt%3DAbstract</link>
            <description>Authors: Zandberg WF, Gao N, Kumarasamy J, Lehrman MA, Seidah NG, Pinto BM
    Abstract
    In a cell-based assay for novel inhibitors, we have discovered that two glycosides of 5-thiomannose, each containing an interglycosidic nitrogen atom, prevented the correct zymogen processing of the prohormone proopiomelanocortinin (POMC) and the transcription factor sterol-regulatory element-binding protein-2 (SREBP-2) in mouse pituitary cells and Chinese hamster ovary (CHO) cells, respectively. In the case of SREBP-2, these effects were correlated with the altered N-linked glycosylation of subtilisin/kexin-like isozyme-1 (SKI-1), the protease responsible for SREBP-2 processing under sterol-limiting conditions. Further examination of the effects of these compounds in CHO cells showed that they caus...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618496</comments>
            <pubDate>Thu, 19 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618496</guid>        </item>
        <item>
            <title>&quot;Clicking&quot; on the Lights To Reveal Bacterial Social Networking.</title>
            <link>http://www.medworm.com/index.php?rid=5618494&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22262670%26dopt%3DAbstract</link>
            <description>&quot;Clicking&quot; on the Lights To Reveal Bacterial Social Networking.
    Chembiochem. 2012 Jan 19;
    Authors: Clevenger KD, Fast W
    Abstract
    &quot;No man is an island.&quot;([1]) With apologies to John Donne, the same could be said for a bacterium. The discovery of bacterial quorum sensing and its relevance to microbial ecology and pathogenesis have fueled the increasing scrutiny of the molecular mechanisms responsible for the apparent group behavior of microbes.([2]) A number of chemically diverse small molecules act as diffusible signaling molecules that regulate gene expression in a population-dependent manner. Some of these signals, such as the N-acyl-L-homoserine lactones, are produced and sensed by others in the same or closely related species, and other chemical classes of signals are use...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618494</comments>
            <pubDate>Thu, 19 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618494</guid>        </item>
        <item>
            <title>The Importance of Peripheral Sequences in Determining the Metal Selectivity of an in Vitro-Selected Co(2+) -Dependent DNAzyme.</title>
            <link>http://www.medworm.com/index.php?rid=5618499&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22250000%26dopt%3DAbstract</link>
            <description>Authors: Nelson KE, Ihms HE, Mazumdar D, Bruesehoff PJ, Lu Y
    Abstract
    DNAzymes are catalytically active DNA molecules that use metal cofactors for their enzymatic functions. While a growing number of DNAzymes with diverse functions and metal selectivities have been reported, the relationships between metal ion selectivity, conserved sequences and structures responsible for selectivity remain to be elucidated. To address this issue, we report biochemical assays of a family of previously reported in vitro selected DNAzymes. This family includes the clone 11 DNAzyme, which was isolated by positive and negative selection, and the clone 18 DNAzyme, which was isolated by positive selection alone. The clone 11 DNAzyme has a higher selectivity for Co(2+) over Pb(2+) compared with clone 18....</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618499</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618499</guid>        </item>
        <item>
            <title>Monocillin II Inhibits Human Breast Cancer Growth Partially by Inhibiting MAPK Pathways and CDK2 Thr160 Phosphorylation.</title>
            <link>http://www.medworm.com/index.php?rid=5618498&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22253097%26dopt%3DAbstract</link>
            <description>Authors: Wei H, Xu L, Yu M, Zhang L, Wang H, Wei X, Ruan Y
    Abstract
    Twenty-two β-resorcylic acid lactones (RALs) were evaluated for cytotoxicity against human breast cancer cells to find their structure-activity relationship (SAR). Monocillin II, a trans-enone RAL without epoxy and conjugated dienone, was found to have higher activity in inhibiting tumor cell growth in both in vitro experiment and in vivo nude xenografted mice model than its analogue radicicol, an anticancer lead compound. We demonstrated for the first time that monocillin II could arrest breast cancer cell cycle in G1 phase, which might partially be the result of its inhibition effect on the phosphorylation of the Thr160 residue of cyclin dependent kinase 2 (CDK2), a key enzyme in cell-cycle regulation. Moreover,...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618498</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618498</guid>        </item>
        <item>
            <title>Tuning the Activity of Mitochondria-Penetrating Peptides for Delivery or Disruption.</title>
            <link>http://www.medworm.com/index.php?rid=5595056&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22238158%26dopt%3DAbstract</link>
            <description>This study illustrates that the activity of a mitochondria-localizing agent can be controlled through alterations in peptide hydrophobicity and dosing concentrations.
    PMID: 22238158 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5595056</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5595056</guid>        </item>
        <item>
            <title>Natural and Engineered Plasmin Inhibitors: Applications and Design Strategies.</title>
            <link>http://www.medworm.com/index.php?rid=5595055&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22238174%26dopt%3DAbstract</link>
            <description>Authors: Swedberg JE, Harris JM
    Abstract
    The serine protease plasmin is ubiquitously expressed throughout the human body in the form of the zymogen plasminogen. Conversion to active plasmin occurs through enzymatic cleavage by plasminogen activators. The plasminogen activator/plasmin system has a well-established function in the removal of intravascular fibrin deposition through fibrinolysis and the inhibition of plasmin activity; this has found widespread clinical use in reducing perioperative bleeding. Increasing evidence also suggests diverse, although currently less defined, roles for plasmin in a number of physiological and pathological processes relating to extracellular matrix degradation, cell migration and tissue remodelling. In particular, dysregulation of plasmin has bee...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5595055</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5595055</guid>        </item>
        <item>
            <title>Colorful Calcium Sensors.</title>
            <link>http://www.medworm.com/index.php?rid=5595057&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22234942%26dopt%3DAbstract</link>
            <description>Authors: Lindenburg L, Merkx M
    Abstract
    (R)evolution of protein-based calcium sensors: Expanding the toolbox of genetically encoded calcium sensors with new colors and traits is important for understanding calcium signaling and its relation to other intracellular pathways. Campbell and co-workers have used a new directed-evolution strategy to develop a rich palette of new sensors, including the first red-shifted, genetically encoded calcium sensor.
    PMID: 22234942 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5595057</comments>
            <pubDate>Tue, 10 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5595057</guid>        </item>
        <item>
            <title>A New Concept for Glycosyltransferase Inhibitors: Nonionic Mimics of the Nucleotide Donor of the Human Blood Group B Galactosyltransferase.</title>
            <link>http://www.medworm.com/index.php?rid=5576417&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22223604%26dopt%3DAbstract</link>
            <description>Authors: Schaefer K, Albers J, Sindhuwinata N, Peters T, Meyer B
    Abstract
    Glycosyltransferases play an important role in the formation of oligosaccharides and glycoconjugates. To find suitable and selective inhibitors for this class of enzymes is still challenging. Here, we describe a novel concept that allows the design of inhibitors based on the structure of the donor substrate binding pocket. As a first step we describe the design, synthesis and analysis of inhibitors of the human blood group B galactosyltransferase (GTB). This enzyme served as a model system to study the concept, which can be used for easy access of glycosyltransferase inhibitors in general. In silico docking of bicyclic heteroaromatic ligands to GTB and experimental verification of binding affinities by satura...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576417</comments>
            <pubDate>Thu, 05 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576417</guid>        </item>
        <item>
            <title>Simultaneous Purification and Site-Specific Modification of Pyrroline-Carboxy-Lysine Proteins.</title>
            <link>http://www.medworm.com/index.php?rid=5576416&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22223621%26dopt%3DAbstract</link>
            <description>Authors: Chiu HP, Grünewald J, Hao X, Brock A, Okach L, Uno T, Geierstanger BH
    Abstract
    Sticky residue: Pyrroline-carboxy-lysine (Pcl) can be readily incorporated into proteins expressed in E. coli and mammalian cells by using the pyrrolysyl tRNA/tRNA synthetase pair. Pcl can be used as a single amino acid purification tag and can be site-specifically modified with functional probes during the elution process.
    PMID: 22223621 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576416</comments>
            <pubDate>Thu, 05 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576416</guid>        </item>
        <item>
            <title>The Thorny Way to the Mechanism of Ribosomal Peptide-Bond Formation.</title>
            <link>http://www.medworm.com/index.php?rid=5576419&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22213275%26dopt%3DAbstract</link>
            <description>Authors: Pech M, Nierhaus KH
    Abstract
    Per aspera ad astra: Kinetic isotope effects have indicated a new and comprehensive picture of the central ribosomal enzymatic activity, peptide-bond formation. To this end, isotopes were incorporated in the positions highlighted in red.
    PMID: 22213275 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576419</comments>
            <pubDate>Mon, 02 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576419</guid>        </item>
        <item>
            <title>A New Chemical Handle for Protein AMPylation at the Host-Pathogen Interface.</title>
            <link>http://www.medworm.com/index.php?rid=5576418&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22213418%26dopt%3DAbstract</link>
            <description>Authors: Broncel M, Serwa RA, Tate EW
    Abstract
    Tagging protein AMPylation: A new chemical reporter for AMPylation, recently identified as a key post-translational modification during bacterial infection, is a robust tool for detecting and identifying AMPylated proteins in vitro.
    PMID: 22213418 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576418</comments>
            <pubDate>Mon, 02 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576418</guid>        </item>
        <item>
            <title>Editorial.</title>
            <link>http://www.medworm.com/index.php?rid=5544453&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22190442%26dopt%3DAbstract</link>
            <description>Authors: Neal A, Gölitz P
    PMID: 22190442 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544453</comments>
            <pubDate>Wed, 28 Dec 2011 06:13:04 +0100</pubDate>
            <guid isPermaLink="false">5544453</guid>        </item>
        <item>
            <title>Abstracts.</title>
            <link>http://www.medworm.com/index.php?rid=5544452&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22190443%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22190443 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544452</comments>
            <pubDate>Wed, 28 Dec 2011 06:12:54 +0100</pubDate>
            <guid isPermaLink="false">5544452</guid>        </item>
        <item>
            <title>Preview: ChemBioChem 2/2012.</title>
            <link>http://www.medworm.com/index.php?rid=5544451&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22190444%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22190444 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544451</comments>
            <pubDate>Wed, 28 Dec 2011 06:12:44 +0100</pubDate>
            <guid isPermaLink="false">5544451</guid>        </item>
        <item>
            <title>Towards Quantitative Computer-Aided Studies of Enzymatic Enantioselectivity: The Case of Candida antarctica Lipase A.</title>
            <link>http://www.medworm.com/index.php?rid=5544450&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22190449%26dopt%3DAbstract</link>
            <description>Authors: Frushicheva MP, Warshel A
    Abstract
    The prospect for consistent computer-aided refinement of stereoselective enzymes is explored by simulating the hydrolysis of enantiomers of an α-substituted ester by wild-type and mutant Candida antarctica lipase A, using several strategies. In particular, we focused on the use of the empirical valence bond (EVB) method in a quantitative screening for enantioselectivity, and evaluate both k(cat) and k(cat) /K(M) of the R and S stereoisomers. We found that an extensive sampling is essential for obtaining converging results. This requirement points towards possible problems with approaches that use a limited conformational sampling. However, performing the proper sampling appears to give encouraging results and to offer a powerful tool for...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544450</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5544450</guid>        </item>
        <item>
            <title>Direct Observation of Metabolic Differences in Living Escherichia Coli Strains K-12 and BL21.</title>
            <link>http://www.medworm.com/index.php?rid=5544449&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22190455%26dopt%3DAbstract</link>
            <description>Authors: Meier S, Jensen PR, Duus JO
    Abstract
    Direct observation of metabolism on a timescale of seconds shows altered usage, due to genomic differences, of one specific reaction in living E. coli K-12 and BL21. The resulting phenotypic data vary strongly when directly detecting biochemical reactions at work.
    PMID: 22190455 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544449</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5544449</guid>        </item>
        <item>
            <title>Incorporation of Manganese Complexes into Xylanase: New Artificial Metalloenzymes for Enantioselective Epoxidation.</title>
            <link>http://www.medworm.com/index.php?rid=5544448&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22190469%26dopt%3DAbstract</link>
            <description>Authors: Allard M, Dupont C, Muñoz Robles V, Doucet N, Lledós A, Maréchal JD, Urvoas A, Mahy JP, Ricoux R
    Abstract
    Here we report the best artificial metalloenzyme to date for the selective oxidation of aromatic alkenes; it was obtained by noncovalent insertion of Mn(III) -meso-tetrakis(p-carboxyphenyl)porphyrin [Mn(TpCPP), 1-Mn] into a host protein, xylanase 10A from Streptomyces lividans (Xln10A). Two metallic complexes-N,N'-ethylene bis(2-hydroxybenzylimine)-5,5'-dicarboxylic acid Mn(III) [(Mn-salen), 2-Mn] and 1-Mn-were associated with Xln10A, and the two hybrid biocatalysts were characterised by UV-visible spectroscopy, circular dichroism and molecular modelling. Only the artificial metalloenzyme based on 1-Mn and Xln10A was studied for its catalytic properties in the oxida...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544448</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5544448</guid>        </item>
        <item>
            <title>Abstracts.</title>
            <link>http://www.medworm.com/index.php?rid=5525366&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22162213%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22162213 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525366</comments>
            <pubDate>Fri, 16 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525366</guid>        </item>
        <item>
            <title>Autoproteolytic fragments are intermediates in the oligomerization/aggregation of the Parkinson's disease protein alpha-synuclein as revealed by ion mobility mass spectrometry.</title>
            <link>http://www.medworm.com/index.php?rid=5525365&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22162214%26dopt%3DAbstract</link>
            <description>Authors: Vlad C, Lindner K, Karreman C, Schildknecht S, Leist M, Tomczyk N, Rontree J, Langridge J, Danzer K, Ciossek T, Petre A, Gross ML, Hengerer B, Przybylski M
    Abstract
    Gas-phase protein separation by ion mobility: With its ability to separate the Parkinson's disease protein α-synuclein and its autoproteolytic products-despite the small concentrations of the latter-ion-mobility MS has enabled the characterization of intermediate fragments in in vitro oligomerization-aggregation. In particular, a possible key fragment, the highly aggregating C-terminal fragment, αSyn(72-140), has been revealed.
    PMID: 22162214 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525365</comments>
            <pubDate>Fri, 16 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525365</guid>        </item>
        <item>
            <title>Detection of Cytochrome P450 Substrates by Using a Small-Molecule Droplet Array on an NADH-Immobilized Solid Surface.</title>
            <link>http://www.medworm.com/index.php?rid=5525364&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22162215%26dopt%3DAbstract</link>
            <description>Authors: Takayama H, Takahashi S, Moriya T, Osada H, Iwabuchi Y, Kanoh N
    Abstract
    Seeing below the surface: A small-molecule droplet array platform on an NADH-immobilized solid surface and a biotinylated acetophenone derivative were developed to identify the substrate candidates for soluble P450 enzymes of interest. This methodology is thought to be easily applicable to other class I P450 systems, including those that use NADPH as cofactor.
    PMID: 22162215 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525364</comments>
            <pubDate>Fri, 16 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525364</guid>        </item>
        <item>
            <title>Targeting Zinc Finger Domains with Small Molecules: Solution Structure and Binding Studies of the RanBP2-Type Zinc Finger of RBM5.</title>
            <link>http://www.medworm.com/index.php?rid=5525363&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22162216%26dopt%3DAbstract</link>
            <description>Authors: Farina B, Fattorusso R, Pellecchia M
    Abstract
    The RNA binding motif protein 5 (RBM5), also known as Luca15 or H37, is a component of prespliceosomal complexes that regulates the alternative splicing of several mRNAs, such as Fas and caspase-2. The RBM5 gene is located at the 2p21.3 chromosomal region, which is strongly associated with lung cancer and many other cancers. Both increased and decreased levels of RBM5 can play a role in tumor progression. In particular, downregulation of rbm5 is involved in lung cancer and other cancers upon Ras activation, and, also, represents a molecular signature associated with metastasis in various solid tumors. On the other hand, upregulation of RBM5 occurs in breast and ovarian cancer. Moreover, RBM5 was also found to be involved in the...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525363</comments>
            <pubDate>Fri, 16 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525363</guid>        </item>
        <item>
            <title>Preview: ChemBioChem 1/2012.</title>
            <link>http://www.medworm.com/index.php?rid=5525362&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22162217%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22162217 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525362</comments>
            <pubDate>Fri, 16 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525362</guid>        </item>
        <item>
            <title>Phosphorylation as a Tool To Modulate Aggregation Propensity and To Predict Fibril Architecture.</title>
            <link>http://www.medworm.com/index.php?rid=5525356&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22174034%26dopt%3DAbstract</link>
            <description>Authors: Valette NM, Radford SE, Harris SA, Warriner SL
    Abstract
    Despite the importance of post-translational modifications in controlling the solubility and conformational properties of proteins and peptides, precisely how the aggregation propensity of different peptide sequences is modulated by chemical modification remains unclear. Here we have investigated the effect of phosphorylation on the aggregation propensity of a 13-residue synthetic peptide incorporating one or more phosphate groups at seven different sites at various pH values. Fibril formation was shown to be inhibited when a single phosphate group was introduced at all seven locations in the peptide sequence at pH 7.5, when the phosphate group is fully charged. By contrast, when the same peptides were analysed at pH ...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525356</comments>
            <pubDate>Thu, 15 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525356</guid>        </item>
        <item>
            <title>Rapid Synthesis of New DNMT Inhibitors Derivatives of Procainamide.</title>
            <link>http://www.medworm.com/index.php?rid=5525357&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22170584%26dopt%3DAbstract</link>
            <description>Authors: Halby L, Champion C, Sénamaud-Beaufort C, Ajjan S, Drujon T, Rajavelu A, Ceccaldi A, Jurkowska R, Lequin O, Nelson WG, Guy A, Jeltsch A, Guianvarc'h D, Ferroud C, Arimondo PB
    Abstract
    DNA methyltransferases (DNMTs) are responsible for DNA methylation, an epigenetic modification involved in gene regulation. Families of conjugates of procainamide, an inhibitor of DNMT1, were conceived and produced by rapid synthetic pathways. Six compounds resulted in potent inhibitors of the murine catalytic Dnmt3A/3L complex and of human DNMT1, at least 50 times greater than that of the parent compounds. The inhibitors showed selectivity for C5 DNA methyltransferases. The cytotoxicity of the inhibitors was validated on two tumour cell lines (DU145 and HCT116) and correlated with the DNMT ...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525357</comments>
            <pubDate>Wed, 14 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525357</guid>        </item>
        <item>
            <title>Cloning and Heterologous Expression of Three Type II PKS Gene Clusters from Streptomyces bottropensis.</title>
            <link>http://www.medworm.com/index.php?rid=5525361&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22162248%26dopt%3DAbstract</link>
            <description>Authors: Yan X, Probst K, Linnenbrink A, Arnold M, Paululat T, Zeeck A, Bechthold A
    Abstract
    Mensacarcin is a potent cytotoxic agent isolated from Streptomyces bottropensis. It possesses a high content of oxygen atoms and two epoxide groups, and shows cytostatic and cytotoxic activity comparable to that of doxorubicin, a widely used drug for antitumor therapy. Another natural compound, rishirilide A, was also isolated from the fermentation broth of S. bottropensis. Screening a cosmid library of S. bottropensis with minimal PKS-gene-specific primers revealed the presence of three different type II polyketide synthase (PKS) gene clusters in this strain: the msn cluster (mensacarcin biosynthesis), the rsl cluster (rishirilide biosynthesis), and the mec cluster (putative spore pigment ...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525361</comments>
            <pubDate>Mon, 12 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525361</guid>        </item>
        <item>
            <title>Enzymatic Recognition of 2'-Modified Ribonucleoside 5'-Triphosphates: Towards the Evolution of Versatile Aptamers.</title>
            <link>http://www.medworm.com/index.php?rid=5525359&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22162282%26dopt%3DAbstract</link>
            <description>Authors: Rothnagel JA, Lauridsen LH, Veedu RN
    Abstract
    The quest for effective, selective and nontoxic nucleic-acid-based drugs has led to designing modifications of naturally occurring nucleosides. A number of modified nucleic acids have been made in the past decades in the hope that they would prove useful in target-validation studies and therapeutic applications involving antisense, RNAi, aptamer, and ribozyme-based technologies. Since their invention in the early 1990s, aptamers have emerged as a very promising class of therapeutics, with one drug entering the market for the treatment of age-related macular degeneration. To combat the limitations of aptamers containing naturally occurring nucleotides, chemically modified nucleotides have to be used. In order to apply modified n...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525359</comments>
            <pubDate>Mon, 12 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525359</guid>        </item>
        <item>
            <title>Novel Cell-Penetrating Peptides Based on α-Aminoxy Acids.</title>
            <link>http://www.medworm.com/index.php?rid=5525358&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22162305%26dopt%3DAbstract</link>
            <description>Authors: Ma Y, Yang D, Ma Y, Zhang YH
    Abstract
    The remarkable ability of cell-penetrating peptides (CPPs) to deliver cell-impermeable compounds into living cells makes them attractive transporters for use in biology and medicine. Despite their highly efficient cellular uptake, CPPs consisting of natural amino acids always suffer from degradation and endosomal entrapment, thereby greatly limiting their application in vivo. Here, we describe the preparation of novel CPPs incorporating α-aminoxy acid residues and their cellular uptake behavior. We demonstrate that introducing α-aminoxy acids into the backbones of CPPs enhances their diffuse cytosolic distribution after direct membrane translocation. We also reveal a hybrid peptide, consisting of D-α-aminoxy acids and L-α-amino aci...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525358</comments>
            <pubDate>Mon, 12 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525358</guid>        </item>
        <item>
            <title>Synthesis and Evaluation of a Fluorescent Non-Peptidic Cholecystokinin-B/Gastrin Receptor Specific Antagonist for Cancer Cell Imaging.</title>
            <link>http://www.medworm.com/index.php?rid=5525360&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22162268%26dopt%3DAbstract</link>
            <description>Authors: Kumari S, Chowdhury J, Mishra AK, Chandna S, Saluja D, Chopra M
    Abstract
    Fluorescent labeling has enabled a better understanding of the relationships between receptor location, function, and life cycle. Each of these perspectives contributes new insights into drug action, particularly for G protein-coupled receptors (GPCRs). The aim of this study was to develop a fluorescein derivative, FLUO-QUIN-a novel antagonist of the cholecystokinin-B/gastrin receptor. A radioligand-binding experiment revealed an IC(50) of 4.79 nm, and the antagonist inhibited gastric acid secretion in an isolated lumen-perfused mouse stomach assay (up to 51 % at 100 nm). The fluorescence properties altered upon binding to the receptor, and the fluorophore was quenched to a greater extent when free ...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525360</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525360</guid>        </item>
        <item>
            <title>Inhibition of Heat Shock Transcription Factor Binding by a Linear Polyamide Binding in an Unusual 1:1 Mode.</title>
            <link>http://www.medworm.com/index.php?rid=5488663&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22134972%26dopt%3DAbstract</link>
            <description>Authors: Wang RE, Pandita RK, Cai J, Hunt CR, Taylor JS
    Abstract
    Heat shock proteins (HSPs) are known to protect cells from heat, oxidative stress, and the cytotoxic effects of drugs, and thus can enhance cancer cell survival. As a result, HSPs are a newly emerging class of protein targets for chemotherapy. Among the various HSPs, the HSP70 family is the most highly conserved and prevalent. Herein we describe the development of a β-alanine rich linear polyamide that binds the GGA heat shock elements (HSEs) 3 and 4 in the HSP70 promoter in an unusual 1:1 mode and inhibits heat shock transcription factor 1 (HSF1) binding in vitro.
    PMID: 22134972 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488663</comments>
            <pubDate>Thu, 01 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488663</guid>        </item>
        <item>
            <title>Glycine Fluoromethylketones as SENP-Specific Activity Based Probes.</title>
            <link>http://www.medworm.com/index.php?rid=5488662&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22134988%26dopt%3DAbstract</link>
            <description>We report here the synthesis and biochemical properties of a new peptidyl activity-based probe 1 for SUMO proteases, SENPs. The activity-based probe has at its C terminus a glycine-derived fluoromethylketone moiety as a reactive group designed to target the active-site cysteine of SENPs. Based on a study of the interactions between SENPs and SUMOs, we introduced further design elements that allow the activity-based probe to selectively target SENPs at low micromolar to high nanomolar concentrations. Moreover, 1 out-competes SUMO1 from the reversible SUMO1-SENP1 complex, thus suggesting that 1 and SUMO1 share a common binding site on SENP1.
    PMID: 22134988 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488662</comments>
            <pubDate>Thu, 01 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488662</guid>        </item>
        <item>
            <title>Sequence-Unrestricted, Watson-Crick Recognition of Double Helical B-DNA by (R)-MiniPEG-γPNAs.</title>
            <link>http://www.medworm.com/index.php?rid=5488661&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22135012%26dopt%3DAbstract</link>
            <description>Authors: Bahal R, Sahu B, Rapireddy S, Lee CM, Ly DH
    Abstract
    Invasion of the strand snatchers: We have synthesized chiral γ-peptide nucleic acids containing miniPEG side chains. Using gel shift assays we show that this particular type of nucleic acid mimic can invade any sequence of double helical B-form DNA, and this recognition occurs through direct Watson-Crick base pairing.
    PMID: 22135012 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488661</comments>
            <pubDate>Thu, 01 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488661</guid>        </item>
        <item>
            <title>Stereochemical Studies of the Type II Isopentenyl Diphosphate-Dimethylallyl Diphosphate Isomerase Implicate the FMN Coenzyme in Substrate Protonation.</title>
            <link>http://www.medworm.com/index.php?rid=5488660&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22135039%26dopt%3DAbstract</link>
            <description>Authors: Calveras J, Thibodeaux CJ, Mansoorabadi SO, Liu HW
    Abstract
    The type II isopentenyl diphosphate: Dimethylallyl diphosphate isomerase (IDI-2) is a flavoenzyme catalyzing the interconversion of IPP and DMAPP. Chiral methyl analysis and proton inventory studies were used to probe the stereochemical course of this reaction. The results suggest that FMN acts as both the acid and base in IDI-2 catalysis.
    PMID: 22135039 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488660</comments>
            <pubDate>Thu, 01 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488660</guid>        </item>
        <item>
            <title>Mechanism-Oriented Redesign of an Isomaltulose Synthase to an Isomelezitose Synthase by Site-Directed Mutagenesis.</title>
            <link>http://www.medworm.com/index.php?rid=5488666&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22124943%26dopt%3DAbstract</link>
            <description>Authors: Görl J, Timm M, Seibel J
    Abstract
    An isomelezitose synthase was redesigned out of the sucrose isomerase from Protaminobacter rubrum for the synthesis of isomelezitose (6-O(F) -glucosylsucrose), a potential nutraceutical. The variants F297A, F297P, R333K, F321A_F319A and E428D catalyze the formation of isomelezitose in up to 70 % yield.
    PMID: 22124943 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488666</comments>
            <pubDate>Tue, 29 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488666</guid>        </item>
        <item>
            <title>Inactivation of Glucosamine-6-Phosphate Synthase by N(3) -Oxoacyl Derivatives of L-2,3-Diaminopropanoic Acid.</title>
            <link>http://www.medworm.com/index.php?rid=5488665&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22125025%26dopt%3DAbstract</link>
            <description>Authors: Jędrzejczak R, Wojciechowski M, Andruszkiewicz R, Sowiński P, Kot-Wasik A, Milewski S
    Abstract
    N(3) -Oxoacyl derivatives of L-2,3-diaminopropanoic acid 1-4, containing either an epoxide group or a conjugated double bond system, inactivate Saccharomyces cerevisiae glucosamine-6-phosphate (GlcN-6-P) synthase in a time- and concentration dependent manner. The results of kinetics studies on inactivation suggested a biphasic course, with formation of the enzyme-ligand complex preceding irreversible modification of the enzyme. The examined compounds differed markedly in their affinity to the enzyme active site. Inhibitors containing a phenyl ketone moiety bound much more strongly than their methyl ketone counterparts. The molecular mechanism of enzyme inactivation by phenyl ke...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488665</comments>
            <pubDate>Mon, 28 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488665</guid>        </item>
        <item>
            <title>Two-Step, PCR-Free Telomerase Detection by Using Exonuclease III-Aided Target Recycling.</title>
            <link>http://www.medworm.com/index.php?rid=5488664&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22125097%26dopt%3DAbstract</link>
            <description>We report the sensitive detection of telomerase activity by using exonuclease III-aided target recycling to amplify the signal produced by a chimeric LNA-DNA molecular beacon. We demonstrate the specific detection of as few as 30 telomerase-positive breast cancer cells in a single-measurement fluorescence assay that avoids the problematic PCR and gel analysis of the current &quot;gold-standard&quot; assay.
    PMID: 22125097 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488664</comments>
            <pubDate>Mon, 28 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488664</guid>        </item>
        <item>
            <title>Abstracts.</title>
            <link>http://www.medworm.com/index.php?rid=5488683&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22102380%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22102380 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488683</comments>
            <pubDate>Fri, 25 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488683</guid>        </item>
        <item>
            <title>Preview: ChemBioChem 18/2011.</title>
            <link>http://www.medworm.com/index.php?rid=5488682&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22102381%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22102381 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488682</comments>
            <pubDate>Fri, 25 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488682</guid>        </item>
        <item>
            <title>Mechanistic Insight into the Catalytic Activity of ββα-Metallonucleases from Computer Simulations: Vibrio vulnificus Periplasmic Nuclease as a Test Case.</title>
            <link>http://www.medworm.com/index.php?rid=5488672&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22114054%26dopt%3DAbstract</link>
            <description>Authors: Bueren-Calabuig JA, Coderch C, Rico E, Jiménez-Ruiz A, Gago F
    Abstract
    Using information from wild-type and mutant Vibrio vulnificus nuclease (Vvn) and I-PpoI homing endonuclease co-crystallized with different oligodeoxynucleotides, we have built the complex of Vvn with a DNA octamer and carried out a series of simulations to dissect the catalytic mechanism of this metallonuclease in a stepwise fashion. The distinct roles played in the reaction by individual active site residues, the metal cation and water molecules have been clarified by using a combination of classical molecular dynamics simulations and quantum mechanical calculations. Our results strongly support the most parsimonious catalytic mechanism, namely one in which a single water molecule from bulk solvent is...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488672</comments>
            <pubDate>Fri, 25 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488672</guid>        </item>
        <item>
            <title>Identification of Late-Stage Glycosylation Steps in the Biosynthetic Pathway of the Anthracycline Nogalamycin.</title>
            <link>http://www.medworm.com/index.php?rid=5488669&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22120896%26dopt%3DAbstract</link>
            <description>Authors: Siitonen V, Claesson M, Patrikainen P, Aromaa M, Mäntsälä P, Schneider G, Metsä-Ketelä M
    Abstract
    Nogalamycin is an anthracycline antibiotic that has been shown to exhibit significant cytotoxicity. Its biological activity requires two deoxysugar moieties: nogalose and nogalamine, which are attached at C7 and C1, respectively, of the aromatic polyketide aglycone. Curiously, the aminosugar nogalamine is also connected through a CC bond between C2 and C5''. Despite extensive molecular genetic characterization of early biosynthetic steps, nogalamycin glycosylation has not been investigated in detail. Here we show that expression of the majority of the gene cluster in Streptomyces albus led to accumulation of three new anthracyclines, which unexpectedly included nogalam...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488669</comments>
            <pubDate>Fri, 25 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488669</guid>        </item>
        <item>
            <title>Elaborate Nanoparticle-Based Traps for Catching Cytosolic Players in the Act.</title>
            <link>http://www.medworm.com/index.php?rid=5488668&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22121106%26dopt%3DAbstract</link>
            <description>Authors: Delehanty JB, Medintz IL
    Abstract
    Ferritin about: The Kim group has devised a nanoparticle-based system for monitoring intracellular bimolecular interactions in real time. The system uses the rapid, innate self-assembly of ferritin, expressing bait and prey molecules, into ordered nanoclusters whose morphology is tracked by using fluorescence microscopy.
    PMID: 22121106 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488668</comments>
            <pubDate>Fri, 25 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488668</guid>        </item>
        <item>
            <title>Substitution of a Conserved Disulfide in the Type IIa Bacteriocin, Leucocin A, with L-Leucine and L-Serine Residues: Effects on Activity and Three-Dimensional Structure.</title>
            <link>http://www.medworm.com/index.php?rid=5488667&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22121114%26dopt%3DAbstract</link>
            <description>Authors: Sit CS, Lohans CT, van Belkum MJ, Campbell CD, Miskolzie M, Vederas JC
    Abstract
    Bridge not required: The disulfide bridge in the antibacterial peptide leucocin A was replaced with two Ser or two Leu residues. The double leucine mutant was found to be active, and elucidation of its 3D structure showed that the two leucines interact to hold the N- and C-terminal domains together.
    PMID: 22121114 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488667</comments>
            <pubDate>Fri, 25 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488667</guid>        </item>
        <item>
            <title>Expansion of the Amino Acid Repertoire in Protein Biosynthesis in Silkworm Cells.</title>
            <link>http://www.medworm.com/index.php?rid=5488677&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22113829%26dopt%3DAbstract</link>
            <description>Authors: Teramoto H, Kojima K, Kajiwara H, Ishibashi J
    Abstract
    Toward silk production with UAAs: The strategy for residue-specific incorporation of unnatural amino acids (UAAs) into proteins was extended to silkworm cells. Here we report the incorporation of p-Cl-Phe into a reporter protein (EGFP) synthesized in silkworm cells that express an αA450G mutant of B. mori phenylalanyl-tRNA synthetase with relaxed substrate specificity.
    PMID: 22113829 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488677</comments>
            <pubDate>Thu, 24 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488677</guid>        </item>
        <item>
            <title>Shedding Light on Alzheimer's β-Amyloid Aggregation with Chemical Tools.</title>
            <link>http://www.medworm.com/index.php?rid=5488676&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22113851%26dopt%3DAbstract</link>
            <description>Authors: Kapurniotu A
    Abstract
    Early steps in self-assembly: Kelly and co-workers have presented a fluorescence-based assay system that differentially detects the early oligomers and fibrils formed by the Alzheimer's disease β-amyloid peptide, Aβ, and provided evidence that in vitro Aβ amyloidogenesis proceeds through a nucleated conformational conversion of nonfibrillar oligomers into amyloid fibrils.
    PMID: 22113851 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488676</comments>
            <pubDate>Thu, 24 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488676</guid>        </item>
        <item>
            <title>Solubilized Gramicidin A as Potential Systemic Antibiotics.</title>
            <link>http://www.medworm.com/index.php?rid=5488674&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22113881%26dopt%3DAbstract</link>
            <description>Authors: Wang F, Qin L, Pace CJ, Wong P, Malonis R, Gao J
    Abstract
    Makeover of an old antibiotic: The channel-forming toxin gramicidin A (gA) has been successfully converted into agents that selectively chase after bacterial cells. These novel D-Lys-containing gA mutants display potent antimicrobial activity and remarkable therapeutic indexes (&amp;gt;1000-fold).
    PMID: 22113881 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488674</comments>
            <pubDate>Thu, 24 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488674</guid>        </item>
        <item>
            <title>Discrimination between T/A and A/T Base Pairs of Pyrrole-Imidazole Polyamides Substituted with Chiral β-Hydroxy-γ-Aminobutyric Acid/β-Alanine Pairs.</title>
            <link>http://www.medworm.com/index.php?rid=5488673&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22113893%26dopt%3DAbstract</link>
            <description>Authors: Zhang W, Jiang SK, Wu YL, Guo CX, Zhang HF, Sugiyama H, Chen XL
    Abstract
    Base-T-specific recognition element: A chiral aliphatic amino acid, (S)-β-hydroxyl-γ-aminobutyric acid, when incorporated into polyamides, can act as a novel T-specific recognition element in DNA minor groove sequence-specific recognition event. Good flexibility of the novel T-reader implies that it could be incorporated into longer polyamides to regulate their curvature and thus allow discrimination of longer DNA sequences.
    PMID: 22113893 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488673</comments>
            <pubDate>Thu, 24 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488673</guid>        </item>
        <item>
            <title>Interaction of a Tat Substrate and a Tat Signal Peptide with Thylakoid Lipids at the Air-Water Interface.</title>
            <link>http://www.medworm.com/index.php?rid=5488671&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22114060%26dopt%3DAbstract</link>
            <description>In this study we investigated the initial states of this interaction with thylakoid lipid monolayers at the air-water interface by using monolayer techniques combined with infrared reflection-absorption spectroscopy (IRRAS). We used enhanced green fluorescent protein (EGFP) as a model substrate and the signal peptide SP16 from the 16 kDa protein of the spinach oxygen-evolving complex (OEC16). We found that the signal peptide is essential for the interaction of the model substrate with lipid monolayers. IRRA spectroscopy showed an increased amount of α-helical secondary structure elements for the chimeric model substrate i16/EGFP (SP16 fused to EGFP) compared with EGFP; this can be attributed to the signal peptide.
    PMID: 22114060 [PubMed - as supplied by publisher] (Source: Chembiochem...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488671</comments>
            <pubDate>Thu, 24 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488671</guid>        </item>
        <item>
            <title>Pericyclic Prenylation: Peptide Modification through a Claisen Rearrangement.</title>
            <link>http://www.medworm.com/index.php?rid=5488670&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22114066%26dopt%3DAbstract</link>
            <description>Authors: Majmudar JD, Gibbs RA
    Abstract
    LynF prenylates, but the prenyl migrates: Schmidt and co-workers have demonstrated that LynF from Lyngbya aestuarii is a reverse O-prenyl transferase. However, a forward C-prenylated product is obtained through a non-enzymatic Claisen rearrangement. The elucidation of this unprecedented two-step process is a significant contribution to our understanding of the biosynthesis of complex macrocyclic peptides.
    PMID: 22114066 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488670</comments>
            <pubDate>Thu, 24 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488670</guid>        </item>
        <item>
            <title>Photochemical Modulation of DNA Conformation by Organic Dications.</title>
            <link>http://www.medworm.com/index.php?rid=5488680&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22109974%26dopt%3DAbstract</link>
            <description>Authors: Zinchenko AA, Tanahashi M, Murata S
    Abstract
    A group of azobenzene derivatives containing two quaternary ammonium groups with various intercharge distances between them was synthesised and used to control photochemically the conformation of genomic DNA by switching the distance between cationic ammonium groups in the dications. It was found that isomerisation of either dication from the trans form to cis resulted in an increase in the dication's efficiency for DNA compaction; this is associated with a decrease in intercharge distance between ammonium groups and leads to a better match of the binder's cationic groups to adjacent phosphate groups of DNA. Ammonium dications have several important advantages over the photosensitive surfactant type of diazobenzene reported earl...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488680</comments>
            <pubDate>Wed, 23 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488680</guid>        </item>
        <item>
            <title>Directed Evolution Strategies for Enantiocomplementary Haloalkane Dehalogenases: From Chemical Waste to Enantiopure Building Blocks.</title>
            <link>http://www.medworm.com/index.php?rid=5488679&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22109980%26dopt%3DAbstract</link>
            <description>Authors: van Leeuwen JG, Wijma HJ, Floor RJ, van der Laan JM, Janssen DB
    Abstract
    We used directed evolution to obtain enantiocomplementary haloalkane dehalogenase variants that convert the toxic waste compound 1,2,3-trichloropropane (TCP) into highly enantioenriched (R)- or (S)-2,3-dichloropropan-1-ol, which can easily be converted into optically active epichlorohydrins-attractive intermediates for the synthesis of enantiopure fine chemicals. A dehalogenase with improved catalytic activity but very low enantioselectivity was used as the starting point. A strategy that made optimal use of the limited capacity of the screening assay, which was based on chiral gas chromatography, was developed. We used pair-wise site-saturation mutagenesis (SSM) of all 16 noncatalytic active-site res...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488679</comments>
            <pubDate>Wed, 23 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488679</guid>        </item>
        <item>
            <title>Stable Analogues of OSB-AMP: Potent Inhibitors of MenE, the o-Succinylbenzoate-CoA Synthetase from Bacterial Menaquinone Biosynthesis.</title>
            <link>http://www.medworm.com/index.php?rid=5488678&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22109989%26dopt%3DAbstract</link>
            <description>Authors: Lu X, Zhou R, Sharma I, Li X, Kumar G, Swaminathan S, Tonge PJ, Tan DS
    Abstract
    MenE, the o-succinylbenzoate (OSB)-CoA synthetase from bacterial menaquinone biosynthesis, is a promising new antibacterial target. Sulfonyladenosine analogues of the cognate reaction intermediate, OSB-AMP, have been developed as inhibitors of the MenE enzymes from Mycobacterium tuberculosis (mtMenE), Staphylococcus aureus (saMenE) and Escherichia coli (ecMenE). Both a free carboxylate and a ketone moiety on the OSB side chain are required for potent inhibitory activity. OSB-AMS (4) is a competitive inhibitor of mtMenE with respect to ATP (K(i) =5.4±0.1 nM) and a noncompetitive inhibitor with respect to OSB (K(i) =11.2±0.9 nM). These data are consistent with a Bi Uni Uni Bi Ping-Pong kinetic ...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488678</comments>
            <pubDate>Wed, 23 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488678</guid>        </item>
        <item>
            <title>MBNL1-RNA Recognition: Contributions of MBNL1 Sequence and RNA Conformation.</title>
            <link>http://www.medworm.com/index.php?rid=5488681&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22106026%26dopt%3DAbstract</link>
            <description>Authors: Fu Y, Ramisetty SR, Hussain N, Baranger AM
    Abstract
    Muscleblind-like proteins (MBNL) are RNA-binding proteins that bind to the poly(CUG) and poly(CCUG) sequences that are the causative agents of myotonic dystrophy. It has been suggested that as a result of binding to the repeating RNA sequences, MBNL1 is abnormally expressed and translocated, which leads to many of the misregulated events in myotonic dystrophy. In this work, steady-state fluorescence quenching experiments suggest that MBNL1 alters the structure of helical RNA targets upon binding, which may explain the selectivity of MBNL1 for less structured RNA sites. The removal of one pair of zinc fingers greatly impairs the binding affinity of MBNL1, which indicates that the two pairs of zinc fingers might possibly in...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488681</comments>
            <pubDate>Tue, 22 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488681</guid>        </item>
        <item>
            <title>Bromomaleimide-Linked Bioconjugates Are Cleavable in Mammalian Cells.</title>
            <link>http://www.medworm.com/index.php?rid=5488684&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22095664%26dopt%3DAbstract</link>
            <description>Authors: Moody P, Smith ME, Ryan CP, Chudasama V, Baker JR, Molloy J, Caddick S
    Abstract
    Bromomaleimides are versatile scaffolds that allow facile conjugation of thiolated biomolecules. Here we demonstrate that bromomaleimide-linked GFP-rhodamine FRET pairs cleave in the cytoplasm of mammalian cells. We believe that bromomaleimide scaffolds provide a potential core structure for prodrugs designed to release bioactive cargo following cell internalisation.
    PMID: 22095664 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488684</comments>
            <pubDate>Fri, 18 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488684</guid>        </item>
        <item>
            <title>Fluorescence Detection of Single-Nucleotide Polymorphism with Single-Strand Triplex-Forming DNA Probes.</title>
            <link>http://www.medworm.com/index.php?rid=5488685&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22095630%26dopt%3DAbstract</link>
            <description>Authors: Li X, Wang Y, Guo J, Tang X
    Abstract
    Triple-helix-forming oligonucleotides (TFOs) are widespread in the genome and have been found in regulatory regions, especially in promoter zones and recombination hotspots of DNA. To specifically detect these polypurine sequences, we designed and synthesized two dual pyrene-labeled single-strand oligonucleotide probes (TFO-FPs) consisting of recognition, linker, and detection sequences. The hybridization processes of TFO-FPs with target polypurine oligonucleotides involve both Watson-Crick and Hoogsteen base-pairings. Through double sensing of oligonucleotide sequences, single mutations of target oligonucleotides are detected by monitoring changes in pyrene fluorescence. The high specificities of the probes are maintained over a wide t...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488685</comments>
            <pubDate>Thu, 17 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488685</guid>        </item>
        <item>
            <title>Intein-Mediated Construction of a Library of Fluorescent Rab GTPase Probes.</title>
            <link>http://www.medworm.com/index.php?rid=5488688&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22086656%26dopt%3DAbstract</link>
            <description>Authors: Wu YW, Goody RS, Alexandrov K
    Abstract
    Rab GTPases play a key role in the regulation of membrane trafficking. Post-translational geranylgeranylation is critical for their biological activity and is conferred by Rab geranylgeranyl transferease (RabGGTase), together with an accessory factor, Rab escort protein (REP). Mechanistic studies of Rab prenylation and identification of RabGGTase inhibitors require sensitive reporters of Rab prenylation. In the present work, a combination of protein engineering and expressed protein ligation was used to construct a library of semisynthetic Rab7 fluorescent conjugates. In order to avoid synthesis of a large number of fluorescently labeled peptides, we developed a strategy that combined thiol-reactive dye-labeling of cysteine with in vi...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488688</comments>
            <pubDate>Tue, 15 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488688</guid>        </item>
        <item>
            <title>Epoxyquinone Formation Catalyzed by a Two-Component Flavin-Dependent Monooxygenase Involved in Biosynthesis of the Antibiotic Actinorhodin.</title>
            <link>http://www.medworm.com/index.php?rid=5488687&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22086671%26dopt%3DAbstract</link>
            <description>Authors: Taguchi T, Okamoto S, Hasegawa K, Ichinose K
    Abstract
    The biosynthetic gene cluster of the aromatic polyketide antibiotic actinorhodin (ACT) in Streptomyces coelicolor A3(2) carries a pair of genes, actVA-ORF5 and actVB, that encode a two-component flavin-dependent monooxygenase (FMO). Our previous studies have demonstrated that the ActVA-ORF5/ActVB system functions as a quinone-forming C-6 oxygenase in ACT biosynthesis. Furthermore, we found that this enzyme system exhibits an additional oxygenation activity with dihydrokalafungin (DHK), a proposed intermediate in the ACT biosynthetic pathway, and generates two reaction products. These compounds were revealed to be monooxygenated derivatives of kalafungin, which is spontaneously formed through oxidative lactonization of D...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5488687</comments>
            <pubDate>Tue, 15 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5488687</guid>        </item>
        <item>
            <title>A New Fluorescent PET Probe for Hydrogen Peroxide and its Use in Enzymatic Assays for L-Lactate and D-Glucose.</title>
            <link>http://www.medworm.com/index.php?rid=5411418&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22076816%26dopt%3DAbstract</link>
            <description>We present a new probe for the determination of hydrogen peroxide (HP). It is based on the yellow fluorophore 4-amino-1,8-napththalimide, coupled to p-anisidine (as a redox-active group) to form a probe that is based on photoinduced electron transfer (PET). The preparation of the probe (which we refer to as &quot;HP Green&quot;) was accomplished in four steps with good yield. Its fluorescence is independent of pH in the physiological range and quenched by a PET process that occurs between the p-anisidine redox moiety and the naphthalimide luminophore. If the p-anisidine group is oxidized by HP, PET is suppressed and fluorescence intensity is strongly increased. Addition of horseradish peroxidase (HRP) enhances the oxidation of HP Green and further improves the detection limit of HP. The use of HRP a...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411418</comments>
            <pubDate>Fri, 11 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411418</guid>        </item>
        <item>
            <title>Synthetic Virus-Like Particles and Conformationally Constrained Peptidomimetics in Vaccine Design.</title>
            <link>http://www.medworm.com/index.php?rid=5411417&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22076829%26dopt%3DAbstract</link>
            <description>Authors: Riedel T, Ghasparian A, Moehle K, Rusert P, Trkola A, Robinson JA
    Abstract
    Conformationally constrained peptidomimetics could be of great value in the design of vaccines targeting protective epitopes on viral and bacterial pathogens. But the poor immunogenicity of small synthetic molecules represents a serious obstacle for their use in vaccine development. Here, we show how a constrained epitope mimetic can be rendered highly immunogenic through multivalent display on the surface of synthetic virus-like nanoparticles. The target epitope is the V3 loop from the gp120 glycoprotein of HIV-1 bound to the neutralizing antibody F425-B4e8. The antibody-bound V3 loop adopts a β-hairpin conformation, which is effectively stabilized by transplantation onto a D-Pro-L-Pro template. T...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411417</comments>
            <pubDate>Fri, 11 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411417</guid>        </item>
        <item>
            <title>A Late-Stage Intermediate in Salinomycin Biosynthesis Is Revealed by Specific Mutation in the Biosynthetic Gene Cluster.</title>
            <link>http://www.medworm.com/index.php?rid=5411416&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22076845%26dopt%3DAbstract</link>
            <description>Authors: Yurkovich ME, Tyrakis PA, Hong H, Sun Y, Samborskyy M, Kamiya K, Leadlay PF
    PMID: 22076845 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411416</comments>
            <pubDate>Fri, 11 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411416</guid>        </item>
        <item>
            <title>A Two-Color, Self-Controlled Molecular Beacon.</title>
            <link>http://www.medworm.com/index.php?rid=5411415&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22076865%26dopt%3DAbstract</link>
            <description>Authors: Biner SM, Häner R
    PMID: 22076865 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411415</comments>
            <pubDate>Fri, 11 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411415</guid>        </item>
        <item>
            <title>Formation of Giant Protein Vesicles by a Lipid Cosolvent Method.</title>
            <link>http://www.medworm.com/index.php?rid=5411420&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22069223%26dopt%3DAbstract</link>
            <description>Authors: Hansen JS, Vararattanavech A, Vissing T, Torres J, Emnéus J, Hélix-Nielsen C
    Abstract
    This paper describes a method to create giant protein vesicles (GPVs) of ≥10 μm by solvent-driven fusion of large vesicles (0.1-0.2 μm) with reconstituted membrane proteins. We found that formation of GPVs proceeded from rotational mixing of protein-reconstituted large unilamellar vesicles (LUVs) with a lipid-containing solvent phase. We made GPVs by using n-decane and squalene as solvents, and applied generalized polarization (GP) imaging to monitor the polarity around the protein transmembrane region of aquaporins labeled with the polarity-sensitive probe Badan. Specifically, we created GPVs of spinach SoPIP2;1 and E. coli AqpZ aquaporins. Our findings show that hydrophobic intera...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411420</comments>
            <pubDate>Tue, 08 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411420</guid>        </item>
        <item>
            <title>(15) N Relaxation NMR Studies of Prolyl Oligopeptidase, an 80 kDa Enzyme, Reveal a Pre-existing Equilibrium between Different Conformational States.</title>
            <link>http://www.medworm.com/index.php?rid=5411419&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22069228%26dopt%3DAbstract</link>
            <description>Authors: Kichik N, Tarragó T, Claasen B, Gairí M, Millet O, Giralt E
    PMID: 22069228 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411419</comments>
            <pubDate>Tue, 08 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411419</guid>        </item>
        <item>
            <title>Tuning HP1α Chromodomain Selectivity for Di- and Trimethyllysine.</title>
            <link>http://www.medworm.com/index.php?rid=5411423&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22052799%26dopt%3DAbstract</link>
            <description>Authors: Eisert RJ, Waters ML
    Abstract
    Histone lysine methylation is a critical marker for controlling gene expression. The position and extent of methylation (mono-, di-, or tri-) controls the binding of effector proteins that determine whether the associated DNA is expressed or not. Dysregulation of histone protein methylation has been associated with a number of types of cancer, and development of inhibitors for the effector proteins is becoming an active area of research. For this reason, understanding the mechanism by which effector proteins obtain selectivity for the different methylation states of lysine is of great interest. To this end, we have performed mutation studies on the Drosophila HP1α chromodomain, which binds H3K9Me(2) and H3K9Me(3) with approximately equal affi...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411423</comments>
            <pubDate>Fri, 04 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411423</guid>        </item>
        <item>
            <title>Influence of Sugar Ring Conformation on the Transportability of Nucleosides by Human Nucleoside Transporters.</title>
            <link>http://www.medworm.com/index.php?rid=5411422&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22052809%26dopt%3DAbstract</link>
            <description>Authors: Damaraju VL, Mowles D, Smith KM, Yao SY, Young JD, Marquez VE, Cass CE
    Abstract
    The conformational preference of human nucleoside transporters (hNTs) with respect to sugar ring was examined using conformationally fixed purine and pyrimidine nucleosides built on a bicyclo[3.1.0]hexane template. These fixed-conformation nucleosides, methanocarba-deoxyadenosine or methanocarba-deoxycytidine in North (C3'-endo, N-MCdA and N-MCdC) or South (C2'-endo, S-MCdA and S-MCdC) conformations, were used to study inhibition of equilibrative (hENT1-4) and concentrative (hCNT1-3) nucleoside transport by individual recombinant hNTs produced in Saccharomyces cerevisiae cells or Xenopus laevis oocytes. Our results indicated that nucleosides in the North conformation were potent inhibitors of t...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411422</comments>
            <pubDate>Fri, 04 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411422</guid>        </item>
        <item>
            <title>Photoactivatable Caged Cyclic RGD Peptide for Triggering Integrin Binding and Cell Adhesion to Surfaces.</title>
            <link>http://www.medworm.com/index.php?rid=5411421&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22058073%26dopt%3DAbstract</link>
            <description>We report the synthesis and properties of a photoactivatable caged RGD peptide and its application for phototriggering integrin- and cell-binding to surfaces. We analysed in detail 1) the differences in the integrin-binding affinity of the caged and uncaged forms by quartz crystal microbalance (QCM) studies, 2) the efficiency and yield of the photolytic uncaging reaction, 3) the biocompatibility of the photolysis by-products and irradiation conditions, 4) the possibility of site, temporal and density control of integrin-binding and therefore human cell attachment, and 5) the possibility of in situ generation of cell patterns and cell gradients by controlling the UV exposure. These studies provide a clear picture of the potential and limitations of caged RGD for integrin-mediated cell adhes...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411421</comments>
            <pubDate>Fri, 04 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411421</guid>        </item>
        <item>
            <title>Abstracts.</title>
            <link>http://www.medworm.com/index.php?rid=5358233&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22031491%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22031491 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5358233</comments>
            <pubDate>Sat, 29 Oct 2011 05:35:27 +0100</pubDate>
            <guid isPermaLink="false">5358233</guid>        </item>
        <item>
            <title>Preview: ChemBioChem 17/2011.</title>
            <link>http://www.medworm.com/index.php?rid=5358232&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22031492%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22031492 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5358232</comments>
            <pubDate>Sat, 29 Oct 2011 05:35:15 +0100</pubDate>
            <guid isPermaLink="false">5358232</guid>        </item>
        <item>
            <title>Template-Directed RNA Polymerization: The Taming of the Milieu.</title>
            <link>http://www.medworm.com/index.php?rid=5358234&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22028272%26dopt%3DAbstract</link>
            <description>Authors: Lehman N, Hayden EJ
    PMID: 22028272 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5358234</comments>
            <pubDate>Wed, 26 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5358234</guid>        </item>
        <item>
            <title>Conformational Analysis of Bivalent Estrogen Receptor Ligands: From Intramolecular to Intermolecular Binding.</title>
            <link>http://www.medworm.com/index.php?rid=5358235&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22025425%26dopt%3DAbstract</link>
            <description>Authors: Shan M, Bujotzek A, Abendroth F, Wellner A, Gust R, Seitz O, Weber M, Haag R
    Abstract
    The estrogen receptor binding affinities of bivalent raloxifene ligands tethered by flexible spacers of different lengths have been evaluated in vitro. Two bivalent binding modes, intra- and intermolecular, were hypothesized to explain their different binding properties. The binding affinities of these bivalent ligands in an aqueous environment are influenced by their conformations, which can be determined by 2D NMR and UV spectral methods. Moreover, computer modeling and simulations were performed to explain the binding modes of these bivalent ligands and to estimate the conformational entropy difference between their unbound and bound states. It was found that bivalent ligands tethered ...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5358235</comments>
            <pubDate>Tue, 25 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5358235</guid>        </item>
        <item>
            <title>Aptamers can Discriminate Alkaline Proteins with High Specificity.</title>
            <link>http://www.medworm.com/index.php?rid=5358238&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22021204%26dopt%3DAbstract</link>
            <description>Authors: Yu H, Jiang B, Chaput JC
    Abstract
    Aptamers are single-stranded nucleic acids that fold into stable three-dimensional structures with ligand binding sites that are complementary in shape and charge to a desired target. Aptamers are generated by an iterative process known as in vitro selection, which permits their isolation from pools of random sequences. While aptamers have been selected to bind a wide range of targets, it is generally thought that these molecules are incapable of discriminating strongly alkaline proteins due to the attractive forces that govern oppositely charged polymers (e.g., polyelectrolyte effect). Histones, eukaryotic proteins that make up the core structure of nucleosomes are attractive targets for exploring the binding properties of aptamers becaus...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5358238</comments>
            <pubDate>Fri, 21 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5358238</guid>        </item>
        <item>
            <title>Mechanistic Basis for RNA Aptamer-Based Induction of TetR.</title>
            <link>http://www.medworm.com/index.php?rid=5358237&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22021209%26dopt%3DAbstract</link>
            <description>Authors: Steber M, Arora A, Hofmann J, Brutschy B, Suess B
    Abstract
    The TetR aptamer induces TetR controlled gene expression, and represents an interesting tool for application in synthetic biology. We have analysed the mechanistic basis for RNA aptamer-based induction of TetR. The aptamer binds TetR with a high affinity in the order of 10(7)  M(-1) , which is similar to operator DNA binding under the used ionic conditions. We identified the binding epitope of the aptamer on TetR, which consists of amino acids T27, N47 and K48 of both monomers, using loss-of-function analysis and electrophoretic mobility shift assays. Tetracycline-induced conformational changes of TetR led to reorientation of the DNA reading head. This movement destroys the composite binding epitope for the aptam...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5358237</comments>
            <pubDate>Fri, 21 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5358237</guid>        </item>
        <item>
            <title>Rational Design of Fluorescent Biosensor for Cyclic di-GMP.</title>
            <link>http://www.medworm.com/index.php?rid=5358236&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22021215%26dopt%3DAbstract</link>
            <description>Authors: Ho CL, Koh SL, Chuah ML, Luo Z, Tan WJ, Low DK, Liang ZX
    PMID: 22021215 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5358236</comments>
            <pubDate>Fri, 21 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5358236</guid>        </item>
        <item>
            <title>NMR Spectroscopic Investigations of the Activated p38α Mitogen-Activated Protein Kinase.</title>
            <link>http://www.medworm.com/index.php?rid=5358241&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22012687%26dopt%3DAbstract</link>
            <description>Authors: Nielsen G, Schwalbe H
    Abstract
    Phosphorylation of protein kinases is a central mechanism involved in numerous cellular regulatory circuits, both in prokaryotic and eukaryotic cells. An understanding of the structural and functional consequences of protein phosphorylation is of considerable importance for the design of selective, small-molecule kinase inhibitors. NMR spectroscopy is a central method to support structure-based drug design. Here, we present the NMR assignment of the activated p38α kinase and compare it to the NMR assignment of unphosphorylated p38α. Conformational changes in solution induced by activation can be located to the activation loop, an adjacent loop, and an insert part of the polypeptide chain that is specific for the family of mitogen-activated ...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5358241</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5358241</guid>        </item>
        <item>
            <title>Identification of a Catalytic Base for Sugar Oxidation in the Pyranose 2-Oxidase Reaction.</title>
            <link>http://www.medworm.com/index.php?rid=5358240&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22012709%26dopt%3DAbstract</link>
            <description>In this study, the mechanistic role of the conserved residues His548 and Asn593 in P2O was investigated by using site-directed mutagenesis, transient kinetics, and pH-dependence studies. As single mutants of H548 resulted in mixed populations of noncovalently bound and covalently linked FAD, double mutants containing H167A were constructed, in which the covalent histidyl-FAD linkage was removed in addition to having the H548 mutation. Single mutants H548A, H548N, H548S, H548D and double mutants (with H167A) could not be reduced by D-glucose. For the H167A/H548R mutant, the flavin could be reduced by D-glucose with the reduction rate constant about 220 times lower than that of the H167A mutant. The pH-dependence studies of H167A/H548R indicated that the rate constant of flavin reduction inc...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5358240</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5358240</guid>        </item>
        <item>
            <title>Kinetic Capillary Electrophoresis with Mass-Spectrometry Detection (KCE-MS) Facilitates Label-Free Solution-Based Kinetic Analysis of Protein-Small Molecule Binding.</title>
            <link>http://www.medworm.com/index.php?rid=5358239&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22012742%26dopt%3DAbstract</link>
            <description>Authors: Bao J, Krylova SM, Wilson DJ, Reinstein O, Johnson PE, Krylov SN
    PMID: 22012742 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5358239</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5358239</guid>        </item>
        <item>
            <title>DNA Nanotechnology for Nucleic Acid Analysis: DX Motif-Based Sensor.</title>
            <link>http://www.medworm.com/index.php?rid=5358242&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22006680%26dopt%3DAbstract</link>
            <description>Authors: Kolpashchikov DM, Gerasimova YV, Khan MS
    PMID: 22006680 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5358242</comments>
            <pubDate>Tue, 18 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5358242</guid>        </item>
        <item>
            <title>Smallest Genetically Encoded Phosphorylation Status Sensor.</title>
            <link>http://www.medworm.com/index.php?rid=5358243&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22002880%26dopt%3DAbstract</link>
            <description>Authors: Li S
    PMID: 22002880 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5358243</comments>
            <pubDate>Fri, 14 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5358243</guid>        </item>
        <item>
            <title>Creation of Aggregation-Defective α-Synuclein Variants by Engineering the Sequence Connecting β-Strand-Forming Domains.</title>
            <link>http://www.medworm.com/index.php?rid=5323923&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21998035%26dopt%3DAbstract</link>
            <description>Authors: Hernandez M, Golbert S, Zhang LG, Kim JR
    Abstract
    The aggregation of α-synuclein (αS), which is implicated in the pathology of Parkinson's disease, produces fibrils in which layers of parallel, in-register β-sheet-loop-β-sheets are formed. The effects of sequence variation in the loop-forming region (referred to as the linker region) on αS aggregation have yet to be systematically studied. In the study described here, we created and characterized αS variants containing mutations in the linker regions. Our results indicate that although the physicochemical properties of the linker region, evaluated based on an intrinsic property of a single amino acid, still play a significant role in aggregation, additional factors can also determine aggregation of αS linker mutants...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5323923</comments>
            <pubDate>Thu, 13 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5323923</guid>        </item>
        <item>
            <title>Evaluation of a Fluorescent Derivative of AMD3100 and its Interaction with the CXCR4 Chemokine Receptor.</title>
            <link>http://www.medworm.com/index.php?rid=5323922&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21998043%26dopt%3DAbstract</link>
            <description>Authors: Knight JC, Hallett AJ, Brancale A, Paisey SJ, Clarkson RW, Edwards PG
    Abstract
    AMD3100 is a potent and selective antagonist of the CXCR4 receptor; it has been shown to block the route of entry of HIV into host T-cells. This compound and its analogues have since been found to act as haematopoietic stem cell mobilisation agents and, more recently, as anti-cancer agents. Here, we have examined a fluorescent derivative of AMD3100, L(1) , which offered the potential to assess the behaviour of AMD3100 at the cell surface by using optical imaging modalities. The binuclear Zn(II) , Cu(II) and Ni(II) complexes of L(1) have also been investigated as these metals have been previously shown to enhance the binding properties of AMD3100. Furthermore, Zn(II) and Cu(II) are known to enhan...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5323922</comments>
            <pubDate>Thu, 13 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5323922</guid>        </item>
        <item>
            <title>Burning off DNA Methylation: New Evidence for Oxygen-Dependent DNA Demethylation.</title>
            <link>http://www.medworm.com/index.php?rid=5323921&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21998074%26dopt%3DAbstract</link>
            <description>Authors: Jurkowski TP, Jeltsch A
    PMID: 21998074 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5323921</comments>
            <pubDate>Thu, 13 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5323921</guid>        </item>
        <item>
            <title>Photoswitchable Click Amino Acids: Light Control of Conformation and Bioactivity.</title>
            <link>http://www.medworm.com/index.php?rid=5323920&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21998087%26dopt%3DAbstract</link>
            <description>Authors: Hoppmann C, Schmieder P, Heinrich N, Beyermann M
    PMID: 21998087 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5323920</comments>
            <pubDate>Thu, 13 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5323920</guid>        </item>
        <item>
            <title>P450(BM3)  on Steroids: The Swiss Army Knife P450 Enzyme Just Gets Better.</title>
            <link>http://www.medworm.com/index.php?rid=5323919&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21998091%26dopt%3DAbstract</link>
            <description>P450(BM3) on Steroids: The Swiss Army Knife P450 Enzyme Just Gets Better.
    Chembiochem. 2011 Oct 13;
    Authors: Wong LL
    PMID: 21998091 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5323919</comments>
            <pubDate>Thu, 13 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5323919</guid>        </item>
        <item>
            <title>Mechanisms of Glycosyltransferases: The In and the Out.</title>
            <link>http://www.medworm.com/index.php?rid=5323924&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21994148%26dopt%3DAbstract</link>
            <description>Authors: Jakeman DL
    PMID: 21994148 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5323924</comments>
            <pubDate>Wed, 12 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5323924</guid>        </item>
        <item>
            <title>Long-Chain Lipids Are Required for the Innate Immune Recognition of Trehalose Diesters by Macrophages.</title>
            <link>http://www.medworm.com/index.php?rid=5323927&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21990105%26dopt%3DAbstract</link>
            <description>Authors: Khan AA, Chee SH, McLaughlin RJ, Harper JL, Kamena F, Timmer MS, Stocker BL
    PMID: 21990105 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5323927</comments>
            <pubDate>Tue, 11 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5323927</guid>        </item>
        <item>
            <title>SEM Observation of Wet Biological Specimens Pretreated with Room-Temperature Ionic Liquid.</title>
            <link>http://www.medworm.com/index.php?rid=5323926&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21990115%26dopt%3DAbstract</link>
            <description>Authors: Tsuda T, Nemoto N, Kawakami K, Mochizuki E, Kishida S, Tajiri T, Kushibiki T, Kuwabata S
    PMID: 21990115 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5323926</comments>
            <pubDate>Tue, 11 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5323926</guid>        </item>
        <item>
            <title>Biosynthesis of Sesqui- and Diterpenes by the Gibberellin Producer Fusarium fujikuroi.</title>
            <link>http://www.medworm.com/index.php?rid=5323925&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21990128%26dopt%3DAbstract</link>
            <description>Authors: Brock NL, Tudzynski B, Dickschat JS
    Abstract
    The fungus Fusarium fujikuroi IMI58289 emits a complex pattern of volatile terpenoids including two major compounds, the sesquiterpene alcohol α-acorenol and the diterpene ent-kaurene. ent-Kaurene is the precursor for the phytohormone gibberellic acid (GA(3) ) and is produced from geranylgeranyl diphosphate (GGPP) via ent-copalyl diphosphate by the bifunctional ent-copalyl diphosphate/ent-kaurene synthase (CPS/KS). Several structurally related diterpenes were identified as side products of the CPS/KS. Deletion of the cps/ks gene or the whole GA(3) biosynthetic gene cluster resulted in completely abolished diterpene production. Mutants with deletions of the cytochrome P450 monooxygenase gene P450-4, which is responsible for the ...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5323925</comments>
            <pubDate>Tue, 11 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5323925</guid>        </item>
        <item>
            <title>A Triple Spin-Labeling Strategy Coupled with DEER Analysis to Detect DNA Modifications and Enzymatic Repair.</title>
            <link>http://www.medworm.com/index.php?rid=5308826&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21984076%26dopt%3DAbstract</link>
            <description>Authors: Flaender M, Sicoli G, Aci-Seche S, Reignier T, Maurel V, Saint-Pierre C, Boulard Y, Gambarelli S, Gasparutto D
    PMID: 21984076 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5308826</comments>
            <pubDate>Fri, 07 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5308826</guid>        </item>
        <item>
            <title>Cell Targeting with Hybrid Qβ Virus-Like Particles Displaying Epidermal Growth Factor.</title>
            <link>http://www.medworm.com/index.php?rid=5272667&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21956837%26dopt%3DAbstract</link>
            <description>Authors: Pokorski JK, Hovlid ML, Finn MG
    Abstract
    Structurally uniform protein nanoparticles derived from the self-assembly of viral capsid proteins are attractive platforms for the multivalent display of cell-targeting motifs for use in nanomedicine. Virus-based nanoparticles are of particular interest because the scaffold can be manipulated both genetically and chemically to simultaneously display targeting groups and carry a functional payload. Here, we displayed the human epidermal growth factor (EGF) on the exterior surface of bacteriophage Qβ as a C-terminal genetic fusion to the Qβ capsid protein. The co-assembly of wild-type Qβ and EGF-modified subunits resulted in structurally homogeneous nanoparticles displaying between 5 and 12 copies of EGF on their exterior surface....</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272667</comments>
            <pubDate>Thu, 29 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272667</guid>        </item>
        <item>
            <title>Heteromeric Assembled Polypeptidic Artificial Hydrolases with a Six-Helical Bundle Scaffold.</title>
            <link>http://www.medworm.com/index.php?rid=5272666&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21957084%26dopt%3DAbstract</link>
            <description>Authors: Bai Y, Ling Y, Shi W, Cai L, Jia Q, Jiang S, Liu K
    Abstract
    Enzyme efficiency results from the cooperation of functional groups in the catalytic site. In order to mimic a natural enzyme, a definite 3D scaffold must be carefully designed so that the functional groups can work cooperatively. During the HIV-1 fusion process, the gp41 N- and C-terminal heptad repeat regions form a coiled-coil six-helical bundle (6HB) that brings the viral and target cell membranes into close proximity for fusion. We used 6HB as the molecular model for a novel scaffold for the design of an artificial enzyme, in which the modified C34 and N36 peptides formed a unique 6HB structure through specific molecular recognition, and the position and orientation of the side-chain groups on this scaffold w...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272666</comments>
            <pubDate>Thu, 29 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272666</guid>        </item>
        <item>
            <title>Semisynthesis of Prenylated Rab GTPases by Click Ligation.</title>
            <link>http://www.medworm.com/index.php?rid=5272665&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21960422%26dopt%3DAbstract</link>
            <description>Authors: Yi L, Abootorabi M, Wu YW
    PMID: 21960422 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272665</comments>
            <pubDate>Thu, 29 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272665</guid>        </item>
        <item>
            <title>Investigating Mithramycin Deoxysugar Biosynthesis: Enzymatic Total Synthesis of TDP-D-Olivose.</title>
            <link>http://www.medworm.com/index.php?rid=5272664&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21960454%26dopt%3DAbstract</link>
            <description>Authors: Wang G, Kharel MK, Pahari P, Rohr J
    PMID: 21960454 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272664</comments>
            <pubDate>Thu, 29 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272664</guid>        </item>
        <item>
            <title>The Chemistry and Biology of Trypanosomal trans-Sialidases: Virulence Factors in Chagas Disease and Sleeping Sickness.</title>
            <link>http://www.medworm.com/index.php?rid=5272668&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21956798%26dopt%3DAbstract</link>
            <description>Authors: Schauer R, Kamerling JP
    Abstract
    trans-Sialidases constitute a special group of the sialidase family. They occur in some trypanosome species and, in a unique reversible reaction, transfer sialic acids from one glycosidic linkage with galactose (donor) to another galactose (acceptor), to form (α2-3)-sialyl linkages. Trypanosomes cause such devastating human diseases as Chagas disease in South America (Trypanosoma cruzi) or sleeping sickness in Africa (Trypanosoma brucei). The trans-sialidases strongly contribute to the pathogenicity of the trypanosomes by scavenging sialic acids from the host or blood meal to coat the parasite surface; this aids their survival strategy in the insect's intestine, and in the blood circulation or cells of the host, and serves to compromise th...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272668</comments>
            <pubDate>Wed, 28 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272668</guid>        </item>
        <item>
            <title>Fluorescence of 1,2-Diaminoanthraquinone and its Nitric Oxide Reaction Product within Macrophage Cells.</title>
            <link>http://www.medworm.com/index.php?rid=5272677&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21953703%26dopt%3DAbstract</link>
            <description>Authors: Marín MJ, Thomas P, Fabregat V, Luis SV, Russell DA, Galindo F
    Abstract
    Nitric oxide (NO) is involved in many biological processes. Aromatic ortho-diamine derivatives are commonly used in the fluorescence imaging of NO in living cells. ortho-diamino (o-diamino) compounds are believed to react with NO in an oxygenated medium leading to the formation of a triazole derivative. One such o-diamino compound, 1,2-diaminoanthraquinone (DAA), is a nontoxic probe for the detection of NO in living tissues and cells. The formation of the DAA triazole derivative (DAA-TZ) upon reaction of DAA with NO/O(2) within cells has not been demonstrated previously. The aim of this study was to confirm that DAA-TZ is the species formed intracellularly when DAA reacts with NO in the presence of ox...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272677</comments>
            <pubDate>Tue, 27 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272677</guid>        </item>
        <item>
            <title>An Additional Dehydratase-like Activity is Required for Lankacidin Antibiotic Biosynthesis.</title>
            <link>http://www.medworm.com/index.php?rid=5272676&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21953738%26dopt%3DAbstract</link>
            <description>Authors: Dickschat JS, Vergnolle O, Hong H, Garner S, Bidgood SR, Dooley HC, Deng Z, Leadlay PF, Sun Y
    PMID: 21953738 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272676</comments>
            <pubDate>Tue, 27 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272676</guid>        </item>
        <item>
            <title>The Binding Mode of Cladocoran A to the Human Group IIA Phospholipase A(2).</title>
            <link>http://www.medworm.com/index.php?rid=5272675&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21953776%26dopt%3DAbstract</link>
            <description>Authors: Monti MC, Chini MG, Margarucci L, Riccio R, Bifulco G, Casapullo A
    Abstract
    The molecular basis for human group IIA phospholipase A(2) inactivation by the marine natural product cladocoran A (CLD A) has been studied in order to elucidate its relevant anti-inflammatory properties. Indeed, secretory phospholipases A(2) are well-known to be implicated in the pathogenesis of inflammation, such as rheumatoid arthritis, septic shock, psoriasis and asthma, thus the understanding of their inactivation mechanism could be useful for the development of new chemical classes of selective inhibitors. Our results, collected by a combination of biochemical approaches, advanced mass spectrometry and molecular modeling, suggest a competitive inhibition mechanism guided by a noncovalent mole...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272675</comments>
            <pubDate>Tue, 27 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272675</guid>        </item>
        <item>
            <title>Peptide-Controlled Access to the Interior Surface of Empty Virus Nanoparticles.</title>
            <link>http://www.medworm.com/index.php?rid=5272674&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21953809%26dopt%3DAbstract</link>
            <description>Authors: Sainsbury F, Saunders K, Aljabali AA, Evans DJ, Lomonossoff GP
    Abstract
    The structure of Cowpea mosaic virus (CPMV) is known to high resolution, thereby enabling the rational use of the particles in diverse applications, from vaccine design to nanotechnology. A recently devised method for the production of empty virus-like particles (eVLPs) has opened up new possibilities for CPMV capsid-based technologies, such as internal mineralisation of the particle. We have investigated the role of the carboxyl (C) terminus of the small coat (S) protein in controlling access to the interior of CPMV eVLPs by determining the efficiency of internal mineralisation. The presence of the C-terminal 24-amino acid peptide of the S protein was found to inhibit internal mineralisation, an effec...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272674</comments>
            <pubDate>Tue, 27 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272674</guid>        </item>
        <item>
            <title>Two Pathways for Pyrrole Formation in Coumermycin A(1)  Biosynthesis: The Central Pyrrole Moiety is Formed From L-Threonine.</title>
            <link>http://www.medworm.com/index.php?rid=5272672&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21953874%26dopt%3DAbstract</link>
            <description>Two Pathways for Pyrrole Formation in Coumermycin A(1) Biosynthesis: The Central Pyrrole Moiety is Formed From L-Threonine.
    Chembiochem. 2011 Sep 27;
    Authors: Siebenberg S, Burkard N, Knuplesch A, Gust B, Grond S, Heide L
    Abstract
    Coumermycin A(1) is an aminocoumarin antibiotic produced by Streptomyces rishiriensis. It contains three pyrrole rings, that is, two terminal 5-methyl-pyrrole-2-carboxyl moieties and a central 3-methylpyrrole-2,4-dicarboxylic acid moiety. The biosynthesis of the terminal pyrrole moieties has been elucidated previously. However, the biosynthetic precursors of the central pyrrole moiety have remained unknown, and none of the genes or enzymes involved in its formation has been identified. We now show that five genes, contained in a contiguous 4.7 kb ...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272672</comments>
            <pubDate>Tue, 27 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272672</guid>        </item>
        <item>
            <title>Making Proteins with Unnatural Amino Acids: The First Engineered Aminoacyl-tRNA Synthetase Revisited.</title>
            <link>http://www.medworm.com/index.php?rid=5272670&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21953917%26dopt%3DAbstract</link>
            <description>Authors: Kast P
    PMID: 21953917 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272670</comments>
            <pubDate>Mon, 26 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272670</guid>        </item>
        <item>
            <title>In Situ RBL Receptor Visualization and Its Mediated Anticancer Activity for Solasodine Rhamnosides.</title>
            <link>http://www.medworm.com/index.php?rid=5272669&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21953983%26dopt%3DAbstract</link>
            <description>Authors: Wang Y, Gao J, Gu G, Li G, Cui C, Sun B, Lou H
    PMID: 21953983 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272669</comments>
            <pubDate>Mon, 26 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272669</guid>        </item>
        <item>
            <title>Direct Investigation of the Aspergillus GDP-Mannose Transporter by STD NMR Spectroscopy.</title>
            <link>http://www.medworm.com/index.php?rid=5272673&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21953835%26dopt%3DAbstract</link>
            <description>Authors: Maggioni A, Meier J, Routier F, Haselhorst T, Tiralongo J
    PMID: 21953835 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272673</comments>
            <pubDate>Fri, 23 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272673</guid>        </item>
        <item>
            <title>Condensin Engages Chromatin.</title>
            <link>http://www.medworm.com/index.php?rid=5272671&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21953888%26dopt%3DAbstract</link>
            <description>Authors: Petrova B, Haering CH
    PMID: 21953888 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5272671</comments>
            <pubDate>Fri, 23 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5272671</guid>        </item>
        <item>
            <title>Identification and Characterisation of a Calcium Carbonate-Binding Protein, Blue Mussel Shell Protein (BMSP), from the Nacreous Layer.</title>
            <link>http://www.medworm.com/index.php?rid=5240244&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21932217%26dopt%3DAbstract</link>
            <description>Authors: Suzuki M, Iwashima A, Tsutsui N, Ohira T, Kogure T, Nagasawa H
    Abstract
    The nacreous layer of molluscan shells consists of a highly organised, layered structure comprising calcium carbonate aragonite crystals, each surrounded by an organic matrix. In the Japanese pearl oyster Pinctada fucata, the Pif protein from the nacreous layer functions in aragonite binding, and plays a key role in nacre formation. Here, we investigated whether the blue mussel Mytilus galloprovincialis also has a protein with similar functions in the nacreous layer. By using a calcium carbonate-binding assay, we identified the novel protein blue mussel shell protein (BMSP) 100 that can bind calcium carbonate crystals of both aragonite and calcite. When the entire sequence of a cDNA encoding BMSP 100 w...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5240244</comments>
            <pubDate>Tue, 20 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5240244</guid>        </item>
        <item>
            <title>Abstracts.</title>
            <link>http://www.medworm.com/index.php?rid=5225497&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21913297%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 21913297 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5225497</comments>
            <pubDate>Sat, 17 Sep 2011 23:45:08 +0100</pubDate>
            <guid isPermaLink="false">5225497</guid>        </item>
        <item>
            <title>Definition of the Common and Divergent Steps in Carbapenem β-Lactam Antibiotic Biosynthesis.</title>
            <link>http://www.medworm.com/index.php?rid=5225496&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21913298%26dopt%3DAbstract</link>
            <description>Authors: Bodner MJ, Li R, Phelan RM, Freeman MF, Moshos KA, Lloyd EP, Townsend CA
    Abstract
    Approximately 50 naturally occurring carbapenem β-lactam antibiotics are known. All but one of these have been isolated from Streptomyces species and are disubstituted structural variants of a simple core that is synthesized by Pectobacterium carotovorum (Erwinia carotovora), a phylogenetically distant plant pathogen. While the biosynthesis of the simple carbapenem, (5R)-carbapen-2-em-3-carboxylic acid, is impressively efficient requiring only three enzymes, CarA, CarB and CarC, the formation of thienamycin, one of the former group of metabolites from Streptomyces, is markedly more complex. Despite their phylogenetic separation, bioinformatic analysis of the encoding gene clusters suggests t...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5225496</comments>
            <pubDate>Sat, 17 Sep 2011 23:44:55 +0100</pubDate>
            <guid isPermaLink="false">5225496</guid>        </item>
        <item>
            <title>Preview: ChemBioChem 15/2011.</title>
            <link>http://www.medworm.com/index.php?rid=5225495&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21913299%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 21913299 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5225495</comments>
            <pubDate>Sat, 17 Sep 2011 23:44:42 +0100</pubDate>
            <guid isPermaLink="false">5225495</guid>        </item>
        <item>
            <title>Correlated Optical and Electrical Single-Molecule Measurements Reveal Conformational Diffusion from Ligand Binding to Channel Gating in the Nicotinic Acetylcholine Receptor.</title>
            <link>http://www.medworm.com/index.php?rid=5225493&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21915985%26dopt%3DAbstract</link>
            <description>Authors: Schmauder R, Kosanic D, Hovius R, Vogel H
    PMID: 21915985 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5225493</comments>
            <pubDate>Wed, 14 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5225493</guid>        </item>
        <item>
            <title>Enhancing the Thermal Robustness of an Enzyme by Directed Evolution: Least Favorable Starting Points and Inferior Mutants Can Map Superior Evolutionary Pathways.</title>
            <link>http://www.medworm.com/index.php?rid=5225494&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21913300%26dopt%3DAbstract</link>
            <description>Authors: Gumulya Y, Reetz MT
    Abstract
    In a previous directed evolution study, the B-FIT approach to increasing the thermal robustness of proteins was introduced and applied to the lipase from Bacillus subtilis. It is based on the general concept of iterative saturation mutagenesis (ISM), according to which sites in an enzyme are subjected to saturation mutagenesis, the best hit of a given library is then used as a template for randomization at other sites, and the process is continued until the desired catalyst improvement has been achieved. The appropriate choice of the ISM sites is crucial; in the B-FIT method the criterion is residues characterized by highest B factors available from X-ray crystallography data. In the present study, B-FIT was employed in order to increase the th...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5225494</comments>
            <pubDate>Tue, 13 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5225494</guid>        </item>
        <item>
            <title>Simultaneous &quot;One Pot&quot; Expressed Protein Ligation and Cu(I) -Catalyzed Azide/Alkyne Cycloaddition for Protein Immobilization.</title>
            <link>http://www.medworm.com/index.php?rid=5215445&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21901810%26dopt%3DAbstract</link>
            <description>Simultaneous &quot;One Pot&quot; Expressed Protein Ligation and Cu(I) -Catalyzed Azide/Alkyne Cycloaddition for Protein Immobilization.
    Chembiochem. 2011 Sep 8;
    Authors: Steinhagen M, Holland-Nell K, Meldal M, Beck-Sickinger AG
    PMID: 21901810 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215445</comments>
            <pubDate>Thu, 08 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215445</guid>        </item>
        <item>
            <title>Delineation of the Core Aggregation Sequences of TDP-43 C-Terminal Fragment.</title>
            <link>http://www.medworm.com/index.php?rid=5215444&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21905193%26dopt%3DAbstract</link>
            <description>Authors: Saini A, Chauhan VS
    Abstract
    Ubiquitinated cytoplasmic inclusions of TDP-43 and its C-terminal cleavage products are the pathological hallmarks of amyotrophic lateral sclerosis and frontotemporal lobar degeneration with ubiquitinated inclusions. The C-terminal fragments (CTFs) of TDP-43 are increasingly considered to play an important role in its aggregation and in disease. Here, we employed a set of synthetic peptides spanning the length of the TDP-43 CTF (220-414) in order to find out its core aggregation domains. Two regions, one in the RRM-2 domain (246-255) and the other in the C-terminal domain (311-320) of TDP-43, stand out as highly aggregation prone. Studies done on recombinant purified TDP-43 CTF and its three mutants, in which these sequences were deleted indivi...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215444</comments>
            <pubDate>Thu, 08 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215444</guid>        </item>
        <item>
            <title>Identification of Anchor Points for Chemical Modification of a Small Cysteine-Rich Protein by Using a Cysteine Scan.</title>
            <link>http://www.medworm.com/index.php?rid=5215443&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21905194%26dopt%3DAbstract</link>
            <description>Authors: Vinther TN, Ribel U, Askov Pedersen T, Kjeldsen TB, Jensen KJ, Hubálek F
    Abstract
    Chemical modifications of proteins are increasingly important in the development of protein drugs with fine-tuned properties. Regioselective modification, such as the chemoselective alkylation of an unpaired cysteine residue, is a prerequisite for obtaining homogenous protein products. The introduction of an unpaired Cys into the Cys-rich protein, insulin, was investigated by using a Cys scan. This was challenging as the introduced Cys could interfere with insulin's three existing disulfide bonds. However, eight insulin precursors were expressed in Saccharomyces cerevisiae with good yields. Although extensive post-translational modifications of the unpaired Cys were observed, the majority co...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5215443</comments>
            <pubDate>Thu, 08 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5215443</guid>        </item>
        <item>
            <title>An Acyloxymethyl Ketone-Based Probe to Monitor the Activity of Glutathionylspermidine Amidase in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5186796&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21887840%26dopt%3DAbstract</link>
            <description>Authors: Chong CM, Gao S, Chiang BY, Hsu WH, Lin TC, Chen TC, Lin CH
    PMID: 21887840 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5186796</comments>
            <pubDate>Thu, 01 Sep 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5186796</guid>        </item>
        <item>
            <title>Highly Fluorescent 5-(5,6-Dimethoxybenzothiazol-2-yl)-2'-Deoxyuridine 5'-Triphosphate as an Efficient Substrate for DNA Polymerases.</title>
            <link>http://www.medworm.com/index.php?rid=5186795&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21887841%26dopt%3DAbstract</link>
            <description>Authors: Sato K, Sasaki A, Matsuda A
    Abstract
    We herein describe the synthesis of fluorescent 5-(5,6-dimethoxybenzothiazol-2-yl)-2'-deoxyuridine 5'-triphosphate (d(bt) UTP) and primer extension reactions using d(bt) UTP. We also carried out primer extension reactions using the (bt) U template. B family DNA polymerases, such as KOD, Deep Vent (exo-), and 9°N(m) DNA polymerases, were effective for elongation with d(bt) UTP. Deep Vent (exo-) and KOD DNA polymerases have excellent fidelity for incorporating d(bt) UTP only at the site opposite the adenine template and only dATP when using the (bt) U template. Therefore, d(bt) UTP is an excellent fluorescent nucleotide that can be incorporated into DNA by DNA polymerases.
    PMID: 21887841 [PubMed - as supplied by publisher] (Source: C...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5186795</comments>
            <pubDate>Thu, 01 Sep 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5186795</guid>        </item>
        <item>
            <title>New Insight into Marine Alkaloid Metabolic Pathways: Revisiting Oroidin Biosynthesis.</title>
            <link>http://www.medworm.com/index.php?rid=5186797&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21882331%26dopt%3DAbstract</link>
            <description>Authors: Genta-Jouve G, Cachet N, Holderith S, Oberhänsli F, Teyssié JL, Jeffree R, Al Mourabit A, Thomas OP
    PMID: 21882331 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5186797</comments>
            <pubDate>Tue, 30 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5186797</guid>        </item>
        <item>
            <title>Sponge Biosilica Formation Involves Syneresis Following Polycondensation in vivo.</title>
            <link>http://www.medworm.com/index.php?rid=5170932&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21858907%26dopt%3DAbstract</link>
            <description>Authors: Wang X, Schröder HC, Brandt D, Wiens M, Lieberwirth I, Glasser G, Schloßmacher U, Wang S, Müller WE
    Abstract
    Syneresis is a process observed during the maturation/aging of silica gels obtained by sol-gel synthesis that results in shrinkage and expulsion of water due to a rearrangement and increase in the number of bridging siloxane bonds. Here we describe how the process of biosilica deposition during spicule (&quot;biosilica&quot; skeleton of the siliceous sponges) formation involves a phase of syneresis that occurs after the enzyme-mediated polycondensation reaction. Primmorphs from the demosponge Suberites domuncula were used to study syneresis and the inhibition of this mechanism. We showed by scanning electron microscopy that spicules added to primmorphs that have been incub...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5170932</comments>
            <pubDate>Thu, 18 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5170932</guid>        </item>
        <item>
            <title>Investigations of the Uptake of Dimethylsulfoniopropionate by Phytoplankton.</title>
            <link>http://www.medworm.com/index.php?rid=5170934&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21853511%26dopt%3DAbstract</link>
            <description>Authors: Spielmeyer A, Gebser B, Pohnert G
    PMID: 21853511 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5170934</comments>
            <pubDate>Wed, 17 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5170934</guid>        </item>
        <item>
            <title>A Rapid Assay for miRNA Maturation by Using Unmodified pre-miRNA.</title>
            <link>http://www.medworm.com/index.php?rid=5170933&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21853512%26dopt%3DAbstract</link>
            <description>Authors: Neubacher S, Dojahn CM, Arenz C
    PMID: 21853512 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5170933</comments>
            <pubDate>Wed, 17 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5170933</guid>        </item>
        <item>
            <title>Crystal Structures of Novel Allosteric Peptide Inhibitors of HIV Integrase Identify New Interactions at the LEDGF Binding Site.</title>
            <link>http://www.medworm.com/index.php?rid=5170936&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21850718%26dopt%3DAbstract</link>
            <description>Authors: Rhodes DI, Peat TS, Vandegraaff N, Jeevarajah D, Newman J, Martyn J, Coates JA, Ede NJ, Rea P, Deadman JJ
    Abstract
    An optimised method of solution cyclisation gave us access to a series of peptides including SLKIDNLD (2). We investigated the crystallographic complexes of the HIV integrase (HIV-IN) catalytic core domain with 13 of the peptides and identified multiple interactions at the binding site, including hydrogen bonds with residues Thr125 and Gln95, that have not previously been described as being accessible within the binding site. We show that the peptides inhibit the interaction of lens epithelium-derived growth factor (LEDGF) with HIV-IN in a proximity AlphaScreen assay and in an assay for the LEDGF enhancement of HIV-IN strand transfer. The interactions identifi...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5170936</comments>
            <pubDate>Tue, 16 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5170936</guid>        </item>
        <item>
            <title>A Comprehensive Panel of Turn-On Caspase Biosensors for Investigating Caspase Specificity and Caspase Activation Pathways.</title>
            <link>http://www.medworm.com/index.php?rid=5170935&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21850719%26dopt%3DAbstract</link>
            <description>Authors: Shekhawat SS, Campbell ST, Ghosh I
    Abstract
    Caspases play a central role in apoptosis, differentiation, and proliferation, and represent important therapeutic targets for treating cancer and inflammatory disorders. Toward the goal of developing new tools to probe caspase substrate cleavage specificity as well as to systematically interrogate caspase activation pathways, we have constructed and investigated a comprehensive panel of caspase biosensors with a split-luciferase enabled bioluminescent read out. We first interrogated the panel of caspase biosensors for substrate cleavage specificity of caspase 1-10 in widely utilized in vitro translation systems, namely, rabbit reticulocyte lysate (RRL) and wheat germ extract (WGE). Commercial RRL was found to be unsuitable for i...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5170935</comments>
            <pubDate>Tue, 16 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5170935</guid>        </item>
        <item>
            <title>Abstracts.</title>
            <link>http://www.medworm.com/index.php?rid=5138713&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21818834%26dopt%3DAbstract</link>
            <description>Authors: 
    
    PMID: 21818834 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5138713</comments>
            <pubDate>Mon, 15 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5138713</guid>        </item>
        <item>
            <title>Preview: ChemBioChem 13/2011.</title>
            <link>http://www.medworm.com/index.php?rid=5138702&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21818835%26dopt%3DAbstract</link>
            <description>Authors: 
    
    PMID: 21818835 [PubMed - in process] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5138702</comments>
            <pubDate>Mon, 15 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5138702</guid>        </item>
        <item>
            <title>A BODIPY-Cyclooctyne for Protein Imaging in Live Cells.</title>
            <link>http://www.medworm.com/index.php?rid=5138606&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21830285%26dopt%3DAbstract</link>
            <description>Authors: Beatty KE, Szychowski J, Fisk JD, Tirrell DA
    
    PMID: 21830285 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5138606</comments>
            <pubDate>Mon, 08 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5138606</guid>        </item>
        <item>
            <title>Using Modularly Assembled Ligands To Bind RNA Internal Loops Separated by Different Distances.</title>
            <link>http://www.medworm.com/index.php?rid=5138597&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21830289%26dopt%3DAbstract</link>
            <description>Authors: Childs-Disney JL, Tsitovich PB, Disney MD
    
    PMID: 21830289 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5138597</comments>
            <pubDate>Mon, 08 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5138597</guid>        </item>
        <item>
            <title>Spontaneous Crowding of Ribosomes and Proteins inside Vesicles: A Possible Mechanism for the Origin of Cell Metabolism.</title>
            <link>http://www.medworm.com/index.php?rid=5138551&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21830290%26dopt%3DAbstract</link>
            <description>Authors: Pereira de Souza T, Steiniger F, Stano P, Fahr A, Luisi PL
    One of the open questions in the origin of life is the spontaneous formation of primitive cell-like compartments from free molecules in solution and membranes. &quot;Metabolism-first&quot; and &quot;replicator-first&quot; theories claim that early catalytic cycles first evolved in solution, and became encapsulated inside lipid vesicles later on. &quot;Compartment-first&quot; theories suggest that metabolism progressively occurred inside compartments. Both views have some weaknesses: the low probability of co-entrapment of several compounds inside the same compartment, and the need to control nutrient uptake and waste release, respectively. By using lipid vesicles as early-cell models, we show that ribosomes, proteins and lipids spontaneously self-o...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5138551</comments>
            <pubDate>Mon, 08 Aug 2011 23:00:00 +0100</pubDate>
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        <item>
            <title>Isolation, Amino Acid Sequence and Biological Activities of Novel Long-Chain Polyamine-Associated Peptide Toxins from the Sponge Axinyssa aculeata.</title>
            <link>http://www.medworm.com/index.php?rid=5138540&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21830292%26dopt%3DAbstract</link>
            <description>Authors: Matsunaga S, Jimbo M, Gill MB, Lash-Van Wyhe LL, Murata M, Nonomura K, Swanson GT, Sakai R
    A novel family of functionalized peptide toxins, aculeines (ACUs), was isolated from the marine sponge Axinyssa aculeate. ACUs are polypeptides with N-terminal residues that are modified by the addition of long-chain polyamines (LCPA). Aculeines were present in the sponge extract as a complex mixture with differing polyamine chain lengths and peptide structures. ACU-A and B, which were purified in this study, share a common polypeptide chain but differ in their N-terminal residue modifications. The amino acid sequence of the polypeptide portion of ACU-A and B was deduced from 3' and 5' RACE, and supported by Edman degradation and mass spectral analysis of peptide fragments. ACU induced c...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5138540</comments>
            <pubDate>Mon, 08 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5138540</guid>        </item>
        <item>
            <title>Papain-Catalyzed Peptide Bond Formation: Enzyme-Specific Activation with Guanidinophenyl Esters.</title>
            <link>http://www.medworm.com/index.php?rid=5138618&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21826775%26dopt%3DAbstract</link>
            <description>Authors: de Beer RJ, Zarzycka B, Amatdjais-Groenen HI, Jans SC, Nuijens T, Quaedflieg PJ, van Delft FL, Nabuurs SB, Rutjes FP
    The substrate mimetics approach is a versatile method for small-scale enzymatic peptide-bond synthesis in aqueous systems. The protease-recognized amino acid side chain is incorporated in an ester leaving group, the substrate mimetic. This shift of the specific moiety enables the acceptance of amino acids and peptide sequences that are normally not recognized by the enzyme. The guanidinophenyl group (OGp), a known substrate mimetic for the serine proteases trypsin and chymotrypsin, has now been applied for the first time in combination with papain, a cheap and commercially available cysteine protease. To provide insight in the binding mode of various Z-X(AA) -OG...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5138618</comments>
            <pubDate>Sun, 07 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5138618</guid>        </item>
        <item>
            <title>Fatty Acyl-AMP Ligase Involvement in the Production of Alkylresorcylic Acid by a Myxococcus xanthus Type III Polyketide Synthase.</title>
            <link>http://www.medworm.com/index.php?rid=5138735&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21815236%26dopt%3DAbstract</link>
            <description>Authors: Hayashi T, Kitamura Y, Funa N, Ohnishi Y, Horinouchi S
    Fatty acyl-AMP ligases (FAALs) activate fatty acids as acyladenylates, and subsequently catalyze their transfer onto the acyl carrier proteins (ACPs) of polyketide synthases (PKSs) or nonribosomal peptide synthetases to produce lipidic metabolites. Myxococcus xanthus contains a polyketide biosynthesis gene cluster in which putative FAAL (FtpD) and ACP (FtpC) genes are located close to a type III PKS (FtpA) gene. Here we describe the characterization of these three proteins in vitro. FtpD adenylated stearic acid and produced stearoyl-FtpC. The stearoyl moiety was then transferred to FtpA. When extender substrates (malonyl-CoA and methylmalonyl-CoA) were added to the reaction, the alkylresorcinol 5-heptadecyl-4-methyl-benzen...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5138735</comments>
            <pubDate>Wed, 03 Aug 2011 23:00:00 +0100</pubDate>
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        <item>
            <title>Intracellular Detection of Cytosine Incorporation in Genomic DNA by Using 5-Ethynyl-2'-Deoxycytidine.</title>
            <link>http://www.medworm.com/index.php?rid=5087740&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21805552%26dopt%3DAbstract</link>
            <description>Authors: Guan L, van der Heijden GW, Bortvin A, Greenberg MM
    5-Ethynyl-2'-deoxycytidine triphosphate (EdCTP) was synthesized as a probe to be used in conjunction with fluorescent labeling to facilitate the analysis of the in vivo dynamics of DNA-centered processes (DNA replication, repair and cytosine demethylation). Kinetic analysis showed that EdCTP is accepted as a substrate by Klenow exo(-) and DNA polymerase β. Incorporation of 5-ethynyl-2'-deoxycytidine (EdC) into DNA by these enzymes is, at most, modestly less efficient than native dC. EdC-containing DNA was visualized by using a click reaction with a fluorescent azide, following polymerase incorporation and T4 DNA ligase mediated ligation. Subsequent experiments in mouse male germ cells and zygotes demonstrated that EdC is a s...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5087740</comments>
            <pubDate>Sun, 31 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5087740</guid>        </item>
        <item>
            <title>Synthesis of Cyclic Peptides through an Intramolecular Amide Bond Rearrangement.</title>
            <link>http://www.medworm.com/index.php?rid=5087739&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21805553%26dopt%3DAbstract</link>
            <description>Authors: Macmillan D, De Cecco M, Reynolds NL, Santos LF, Barran PE, Dorin JR
    
    PMID: 21805553 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5087739</comments>
            <pubDate>Sun, 31 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5087739</guid>        </item>
        <item>
            <title>DNA Recognition by Synthetic Constructs.</title>
            <link>http://www.medworm.com/index.php?rid=5087742&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21805550%26dopt%3DAbstract</link>
            <description>Authors: Pazos E, Mosquera J, Vázquez ME, Mascareñas JL
    The interaction of transcription factors with specific DNA sites is key for the regulation of gene expression. Despite the availability of a large body of structural data on protein-DNA complexes, we are still far from fully understanding the molecular and biophysical bases underlying such interactions. Therefore, the development of non-natural agents that can reproduce the DNA-recognition properties of natural transcription factors remains a major and challenging goal in chemical biology. In this review we summarize the basics of double-stranded DNA recognition by transcription factors, and describe recent developments in the design and preparation of synthetic DNA binders. We mainly focus on synthetic peptides that have been d...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5087742</comments>
            <pubDate>Thu, 28 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5087742</guid>        </item>
        <item>
            <title>Structural Framework for the Modulation of the Activity of the Hybrid Antibiotic Peptide Cecropin A-Melittin [CA(1-7)M(2-9)] by N(ε) -Lysine Trimethylation.</title>
            <link>http://www.medworm.com/index.php?rid=5087741&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21805551%26dopt%3DAbstract</link>
            <description>Authors: Díaz MD, de la Torre BG, Fernández-Reyes M, Rivas L, Andreu D, Jiménez-Barbero J
    The 3D structures of six linear pentadecapeptides derived from the cecropin A-melittin antimicrobial peptide CA(1-7)M(2-9) [KWKLFKKIGAVLKVL-NH(2) ] have been studied. These analogues are modified by ε-NH(2) trimethylation of one or more lysine residues and showed variation in both antimicrobial and cytotoxic activities, depending on the number and position of modified lysines. Since it is expected that these peptides will display a strong conformational ordering when in contact with membranes, we have investigated their structure on the basis of the data extracted from NMR experiments performed in membrane-mimetic environments. We show that inclusion of N(ε) -trimethylated lysine residues ind...</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5087741</comments>
            <pubDate>Thu, 28 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5087741</guid>        </item>
        <item>
            <title>Molecular Recognition of Watson-Crick-Like Purine-Purine Base Pairs.</title>
            <link>http://www.medworm.com/index.php?rid=5087738&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21805554%26dopt%3DAbstract</link>
            <description>Authors: Buckley R, Enekwa CD, Williams LD, Hud NV
    
    PMID: 21805554 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5087738</comments>
            <pubDate>Thu, 28 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5087738</guid>        </item>
        <item>
            <title>Identifying Protein Variants with Cross-Reactive Aptamer Arrays.</title>
            <link>http://www.medworm.com/index.php?rid=5087746&amp;cid=s_37781_60_f&amp;fid=37781&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21796750%26dopt%3DAbstract</link>
            <description>Authors: Stewart S, Syrett A, Pothukuchy A, Bhadra S, Ellington A, Anslyn E
    
    PMID: 21796750 [PubMed - as supplied by publisher] (Source: Chembiochem)</description>
            <author>Chembiochem</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5087746</comments>
            <pubDate>Tue, 26 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5087746</guid>        </item>
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