A structural view of the inactivation of the SARS coronavirus main proteinase by benzotriazole esters
about
From SARS to MERS: crystallographic studies on coronaviral proteases enable antiviral drug designThree-dimensional domain swapping as a mechanism to lock the active conformation in a super-active octamer of SARS-CoV main protease3C Protease of Enterovirus 68: Structure-Based Design of Michael Acceptor Inhibitors and Their Broad-Spectrum Antiviral Effects against PicornavirusesDynamically-driven inactivation of the catalytic machinery of the SARS 3C-like protease by the N214A mutation on the extra domainCharacterization of Bafinivirus main protease autoprocessing activities.Dynamically-driven enhancement of the catalytic machinery of the SARS 3C-like protease by the S284-T285-I286/A mutations on the extra domain.Coronaviruses resistant to a 3C-like protease inhibitor are attenuated for replication and pathogenesis, revealing a low genetic barrier but high fitness cost of resistanceCrystallization and preliminary crystallographic study of Porcine epidemic diarrhea virus main protease in complex with an inhibitorMild and General Access to Diverse 1H-Benzotriazoles via Diboron-Mediated N-OH Deoxygenation and Palladium-Catalyzed C-C and C-N Bond FormationAssessing activity and inhibition of Middle East respiratory syndrome coronavirus papain-like and 3C-like proteases using luciferase-based biosensors.Design, synthesis and antiviral efficacy of a series of potent chloropyridyl ester-derived SARS-CoV 3CLpro inhibitors.Inhibitors of SARS-3CLpro: virtual screening, biological evaluation, and molecular dynamics simulation studies.Structure-based antivirals for emerging and neglected RNA viruses: an emerging field for medicinal chemistry in academia.Liberation of SARS-CoV main protease from the viral polyprotein: N-terminal autocleavage does not depend on the mature dimerization mode.Autoprocessing mechanism of severe acute respiratory syndrome coronavirus 3C-like protease (SARS-CoV 3CLpro) from its polyproteins.
P2860
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P2860
A structural view of the inactivation of the SARS coronavirus main proteinase by benzotriazole esters
description
2008 nî lūn-bûn
@nan
2008 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
A structural view of the inact ...... einase by benzotriazole esters
@ast
A structural view of the inact ...... einase by benzotriazole esters
@en
A structural view of the inact ...... einase by benzotriazole esters
@nl
type
label
A structural view of the inact ...... einase by benzotriazole esters
@ast
A structural view of the inact ...... einase by benzotriazole esters
@en
A structural view of the inact ...... einase by benzotriazole esters
@nl
prefLabel
A structural view of the inact ...... einase by benzotriazole esters
@ast
A structural view of the inact ...... einase by benzotriazole esters
@en
A structural view of the inact ...... einase by benzotriazole esters
@nl
P2093
P1476
A structural view of the inact ...... einase by benzotriazole esters
@en
P2093
Jeroen R Mesters
Koen H G Verschueren
Ksenia Pumpor
Shuai Chen
Stefan Anemüller
P304
P356
10.1016/J.CHEMBIOL.2008.04.011
P577
2008-06-01T00:00:00Z