Allosteric Site Inhibitor Disrupting Auto-Processing of Malarial Cysteine Proteases - Test2 - elhamkhani - TriplyDB

Allosteric Site Inhibitor Disrupting Auto-Processing of Malarial Cysteine Proteases

Allosteric Site Inhibitor Disrupting Auto-Processing of Malarial Cysteine Proteases

http://www.wikidata.org/entity/Q58577506

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Allosteric Site Inhibitor Disrupting Auto-Processing of Malarial Cysteine Proteases

http://www.wikidata.org/entity/Q58577506

description

article publié dans la revue scientifique Scientific Reports

@fr

im November 2018 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published in Scientific Reports

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в листопаді 2018

@uk

name

Allosteric Site Inhibitor Disrupting Auto-Processing of Malarial Cysteine Proteases

@en

Allosteric Site Inhibitor Disrupting Auto-Processing of Malarial Cysteine Proteases

@nl

type

label

Allosteric Site Inhibitor Disrupting Auto-Processing of Malarial Cysteine Proteases

@en

Allosteric Site Inhibitor Disrupting Auto-Processing of Malarial Cysteine Proteases

@nl

prefLabel

Allosteric Site Inhibitor Disrupting Auto-Processing of Malarial Cysteine Proteases

@en

Allosteric Site Inhibitor Disrupting Auto-Processing of Malarial Cysteine Proteases

@nl

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S41598-018-34564-8

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Scientific Reports

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Allosteric Site Inhibitor Disrupting Auto-Processing of Malarial Cysteine Proteases

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A K Saxena

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A Pant

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K C Pandey

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N A Wani

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R Rai

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R Sharma

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S Verma

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V Pande

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P2860

Falstatin, a cysteine protease inhibitor of Plasmodium falciparum, facilitates erythrocyte invasion

Identification of specific histidines as pH sensors in flavivirus membrane fusion

Vinyl Sulfones as Antiparasitic Agents and a Structural Basis for Drug Design

Structures of Falcipain-2 and Falcipain-3 Bound to Small Molecule Inhibitors: Implications for Substrate Specificity ‡

Pseudilins: halogenated, allosteric inhibitors of the non-mevalonate pathway enzyme IspD

Evidence that a point mutation in dihydrofolate reductase-thymidylate synthase confers resistance to pyrimethamine in falciparum malaria.

Expression and characterization of the Plasmodium falciparum haemoglobinase falcipain-3

Biochemical and Structural Characterization of Selective Allosteric Inhibitors of the Plasmodium falciparum Drug Target, Prolyl-tRNA-synthetase

The Ionic and hydrophobic interactions are required for the auto activation of cysteine proteases of Plasmodium falciparum

Structural basis for unique mechanisms of folding and hemoglobin binding by a malarial protease

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scholarly article

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10.1038/S41598-018-34564-8

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1

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Rajnikant Dixit

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2018-11-01T00:00:00Z

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30385827

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allosteric inhibitor

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