The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity - Wikidata - awgldk - TriplyDB

The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity

The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity

http://www.wikidata.org/entity/Q27658866

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Cofactor mobility determines reaction outcome in the IMPDH and GMPR (β-α)8 barrel enzymes Identification of novel Mt-Guab2 inhibitor series active against M. tuberculosis Bacillus anthracis Inosine 5′-Monophosphate Dehydrogenase in Action: The First Bacterial Series of Structures of Phosphate Ion-, Substrate-, and Product-Bound Complexes Structure ofPseudomonas aeruginosainosine 5′-monophosphate dehydrogenase Optimization of Benzoxazole-Based Inhibitors of Cryptosporidium parvum Inosine 5′-Monophosphate Dehydrogenase The Inosine Monophosphate Dehydrogenase, GuaB2, Is a Vulnerable New Bactericidal Drug Target for Tuberculosis.A screening pipeline for antiparasitic agents targeting cryptosporidium inosine monophosphate dehydrogenase Triazole-linked inhibitors of inosine monophosphate dehydrogenase from human and Mycobacterium tuberculosis Mycobacterium tuberculosis IMPDH in Complexes with Substrates, Products and Antitubercular Compounds Cryptosporidium in humans and animals-a one health approach to prophylaxis.The antibiotic potential of prokaryotic IMP dehydrogenase inhibitors Repurposing cryptosporidium inosine 5'-monophosphate dehydrogenase inhibitors as potential antibacterial agents.Structural determinants of inhibitor selectivity in prokaryotic IMP dehydrogenases.Synthesis, in vitro evaluation and cocrystal structure of 4-oxo-[1]benzopyrano[4,3-c]pyrazole Cryptosporidium parvum inosine 5'-monophosphate dehydrogenase (CpIMPDH) inhibitors.A novel cofactor-binding mode in bacterial IMP dehydrogenases explains inhibitor selectivity.Kinetically controlled drug resistance: how Penicillium brevicompactum survives mycophenolic acid Structure of Cryptosporidium IMP dehydrogenase bound to an inhibitor with in vivo antiparasitic activity.Structure-activity relationship study of selective benzimidazole-based inhibitors of Cryptosporidium parvum IMPDH.Adaptive evolution of drug targets in producer and non-producer organisms.Does changing the predicted dynamics of a phospholipase C alter activity and membrane binding?Phthalazinone inhibitors of inosine-5'-monophosphate dehydrogenase from Cryptosporidium parvum.2-(Quinolin-4-yloxy)acetamides Are Active against Drug-Susceptible and Drug-Resistant Mycobacterium tuberculosis Strains.Selective and potent urea inhibitors of cryptosporidium parvum inosine 5'-monophosphate dehydrogenase.Validation of IMP dehydrogenase inhibitors in a mouse model of cryptosporidiosis.The dynamic determinants of reaction specificity in the IMPDH/GMPR family of (β/α)(8) barrel enzymes.Inosine 5'-monophosphate dehydrogenase inhibitors as antimicrobial agents: recent progress and future perspectives.Allosteric activation via kinetic control: potassium accelerates a conformational change in IMP dehydrogenase.Inosine-5'-monophosphate dehydrogenase (IMPDH) inhibitors: a patent and scientific literature review (2002-2016).Benzoxazoles, phthalazinones, and arylurea-based compounds with IMPDH-independent antibacterial activity against Francisella tularensis.Inhibition of Inosine-5'-monophosphate Dehydrogenase from Bacillus anthracis: Mechanism Revealed by Pre-Steady-State Kinetics.Binding mode of inhibitors and Cryptosporidium parvum IMP dehydrogenase: A combined ligand- and receptor-based study.Expanding benzoxazole based inosine 5'-monophosphate dehydrogenase (IMPDH) inhibitor structure-activity as potential anti-tuberculosis agents.

P2860

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P2860

The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity

http://www.wikidata.org/entity/Q27658866

description

2010 nî lūn-bûn

@nan

2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի փետրվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity

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The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity

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The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity

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The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity

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The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity

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The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity

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The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity

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The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity

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The Structural Basis of Cryptosporidium-Specific IMP Dehydrogenase Inhibitor Selectivity

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Journal of the American Chemical Society

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The structural basis of Cryptosporidium -specific IMP dehydrogenase inhibitor selectivity

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Gregory D Cuny

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Iain S Macpherson

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J Alejandro D'Aquino

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Lizbeth Hedstrom

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Minjia Zhang

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Sivapriya Kirubakaran

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Suresh Kumar Gorla

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P2860

Complete Genome Sequence of the Apicomplexan, Cryptosporidium parvum

The genome of Cryptosporidium hominis

IMP dehydrogenase: structure, mechanism, and inhibition.

Crystal structure at 2.4 A resolution of Borrelia burgdorferi inosine 5'-monophosphate dehydrogenase: evidence of a substrate-induced hinged-lid motion by loop 6

Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid

Genetic complementation in apicomplexan parasites

The structure of inosine 5'-monophosphate dehydrogenase and the design of novel inhibitors.

Triazole inhibitors of Cryptosporidium parvum inosine 5'-monophosphate dehydrogenase

Cryptosporidium: a water-borne zoonotic parasite.

An updated review on Cryptosporidium and Giardia.

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