(Q46954558)

26 December 2017

title

Molecular docking identifies the binding of 3-chloropyridine moieties specifically to the S1 pocket of SARS-CoV Mpro (English)

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John Christopher Vederas

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26 December 2017

author name string

Chunying Niu

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26 December 2017

Jiang Yin

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Jianmin Zhang

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Michael N G James

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language of work or name

English

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publication date

22 September 2007

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Bioorganic & Medicinal Chemistry

published in

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volume

16

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issue

1

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page(s)

293-302

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A novel coronavirus associated with severe acute respiratory syndrome

cites work

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12 December 2020

High-throughput screening identifies inhibitors of the SARS coronavirus main proteinase

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12 December 2020

A new lead for nonpeptidic active-site-directed inhibitors of the severe acute respiratory syndrome coronavirus main protease discovered by a combination of screening and docking methods

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12 December 2020

Discovery of a novel family of SARS-CoV protease inhibitors by virtual screening and 3D-QSAR studies

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12 December 2020

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12 December 2020

The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor

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12 December 2020

Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain

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12 December 2020

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12 December 2020

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12 December 2020

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12 December 2020

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12 December 2020

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12 December 2020

The Protein Data Bank

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12 December 2020

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12 December 2020

Small molecules targeting severe acute respiratory syndrome human coronavirus

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12 December 2020

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12 December 2020

Identification of novel inhibitors of the SARS coronavirus main protease 3CLpro.

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12 December 2020

Structure-based drug design and structural biology study of novel nonpeptide inhibitors of severe acute respiratory syndrome coronavirus main protease.

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The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain

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Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs

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Design and synthesis of dipeptidyl glutaminyl fluoromethyl ketones as potent severe acute respiratory syndrome coronovirus (SARS-CoV) inhibitors

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A mechanistic view of enzyme inhibition and peptide hydrolysis in the active site of the SARS-CoV 3C-like peptidase

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Virtual screening of novel noncovalent inhibitors for SARS-CoV 3C-like proteinase.

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Screening of electrophilic compounds yields an aziridinyl peptide as new active-site directed SARS-CoV main protease inhibitor

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Viral replicase gene products suffice for coronavirus discontinuous transcription

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Synthesis and evaluation of keto-glutamine analogues as potent inhibitors of severe acute respiratory syndrome 3CLpro

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Anti-SARS drug screening by molecular docking

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Design, synthesis, and evaluation of inhibitors for severe acute respiratory syndrome 3C-like protease based on phthalhydrazide ketones or heteroaromatic esters

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12 December 2020

10.1016/J.BMC.2007.09.034

Identifiers

DOI

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26 December 2017

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26 December 2017