Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature
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Moonlighting O-acetylserine sulfhydrylase: New functions for an old proteinStructure ofLeishmania majorcysteine synthaseThe narrow active-site cleft of O-acetylserine sulfhydrylase from Leishmania donovani allows complex formation with serine acetyltransferases with a range of C-terminal sequencesFrom protein structure to function via single crystal optical spectroscopyIdentification of natural inhibitors of Entamoeba histolytica cysteine synthase from microbial secondary metabolitesComparative thermodynamic studies on substrate and product binding of O-acetylserine sulfhydrylase reveals two different ligand recognition modesIsozyme-specific ligands for O-acetylserine sulfhydrylase, a novel antibiotic targetTargeting cystalysin, a virulence factor of treponema denticola-supported periodontitis.Three-stage assembly of the cysteine synthase complex from Escherichia coliIdentification of a target cell permissive factor required for contact-dependent growth inhibition (CDI).Structural insight into the interaction of O-acetylserine sulfhydrylase with competitive, peptidic inhibitors by saturation transfer difference-NMR.Unraveling the essential role of CysK in CDI toxin activation.Computational Insights into the Mechanism of Inhibition of OASS-A by a Small Molecule Inhibitor.Chemogenomics of pyridoxal 5'-phosphate dependent enzymes.Activation of an anti-bacterial toxin by the biosynthetic enzyme CysK: mechanism of binding, interaction specificity and competition with cysteine synthase.Ergot alkaloids: From witchcraft till in silico analysis. Multi-receptor analysis of ergotamine metabolites.ATP binding to human serine racemase is cooperative and modulated by glycine.Modulation of Escherichia coli serine acetyltransferase catalytic activity in the cysteine synthase complex.Cyclopropane-1,2-dicarboxylic acids as new tools for the biophysical investigation of O-acetylserine sulfhydrylases by fluorimetric methods and saturation transfer difference (STD) NMR.Regulation of human serine racemase activity and dynamics by halides, ATP and malonateDesign and synthesis of trans-2-substituted-cyclopropane-1-carboxylic acids as the first non-natural small molecule inhibitors of O-acetylserine sulfhydrylaseRefining the structure-activity relationships of 2-phenylcyclopropane carboxylic acids as inhibitors of O-acetylserine sulfhydrylase isoformsInhibition of O-acetylserine sulfhydrylase by fluoroalanine derivativesDiscovery of novel fragments inhibiting O-acetylserine sulphhydrylase by combining scaffold hopping and ligand-based drug design
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P2860
Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature
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2010 nî lūn-bûn
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2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
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2010 թվականի հունվարին հրատարակված գիտական հոդված
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2010年の論文
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2010年論文
@yue
2010年論文
@zh-hant
2010年論文
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2010年論文
@zh-mo
2010年論文
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2010年论文
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name
Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature
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Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature
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Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature
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Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature
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Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature
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Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature
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Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature
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Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature
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Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature
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P2093
P2860
P50
P356
P1476
Design of O -Acetylserine Sulfhydrylase Inhibitors by Mimicking Nature
@en
P2093
Alessio Amadasi
Alexander S Bayden
Barbara Campanini
Enea Salsi
Paul F Cook
Pietro Cozzini
Steven L Roderick
Tetyana Dodatko
P2860
P304
P356
10.1021/JM901325E
P407
P577
2010-01-14T00:00:00Z