Structure of the Yersinia pestis FabV Enoyl-ACP Reductase and Its Interaction with Two 2-Pyridone Inhibitors - Wikidata - wikimedia - TriplyDB

Structure of the Yersinia pestis FabV Enoyl-ACP Reductase and Its Interaction with Two 2-Pyridone Inhibitors

Structure of the Yersinia pestis FabV Enoyl-ACP Reductase and Its Interaction with Two 2-Pyridone Inhibitors

http://www.wikidata.org/entity/Q27676726

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Bacterial lipids: metabolism and membrane homeostasis Structures of trans-2-enoyl-CoA reductases from Clostridium acetobutylicum and Treponema denticola: insights into the substrate specificity and the catalytic mechanism Selectivity of Pyridone- and Diphenyl Ether-Based Inhibitors for the Yersinia pestis FabV Enoyl-ACP Reductase.Enoyl-Acyl Carrier Protein Reductase I (FabI) Is Essential for the Intracellular Growth of Listeria monocytogenes.Recent advances in inhibitors of bacterial fatty acid synthesis type II (FASII) system enzymes as potential antibacterial agents.Bacterial fatty acid metabolism in modern antibiotic discovery.

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Structure of the Yersinia pestis FabV Enoyl-ACP Reductase and Its Interaction with Two 2-Pyridone Inhibitors

http://www.wikidata.org/entity/Q27676726

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2012 nî lūn-bûn

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2012 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2012 թվականի հունվարին հրատարակված գիտական հոդված

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2012年の論文

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Structure of the Yersinia pest ...... with Two 2-Pyridone Inhibitors

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Structure of the Yersinia pest ...... with Two 2-Pyridone Inhibitors

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Structure of the Yersinia pest ...... with Two 2-Pyridone Inhibitors

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Structure of the Yersinia pest ...... with Two 2-Pyridone Inhibitors

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Structure of the Yersinia pest ...... with Two 2-Pyridone Inhibitors

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Structure of the Yersinia pest ...... with Two 2-Pyridone Inhibitors

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Structure of the Yersinia pest ...... with Two 2-Pyridone Inhibitors

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Structure of the Yersinia pest ...... with Two 2-Pyridone Inhibitors

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Structure of the Yersinia pest ...... with Two 2-Pyridone Inhibitors

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Structure of the Yersinia pest ...... with Two 2-Pyridone Inhibitors

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Carla Neckles

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Christoph A Sotriffer

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Maria W Hirschbeck

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Sonam Shah

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Steffen Wagner

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P2860

Medium- and short-chain dehydrogenase/reductase gene and protein families : the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes

PHENIX: a comprehensive Python-based system for macromolecular structure solution

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Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites

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Yersinia pestis

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