Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain.
about
Discovery of the first insect nidovirus, a missing evolutionary link in the emergence of the largest RNA virus genomesTargeting membrane-bound viral RNA synthesis reveals potent inhibition of diverse coronaviruses including the middle East respiratory syndrome virusThe footprint of genome architecture in the largest genome expansion in RNA virusesMolecular mechanisms of severe acute respiratory syndrome (SARS)Functional and genetic analysis of coronavirus replicase-transcriptase proteinsDesign of wide-spectrum inhibitors targeting coronavirus main proteasesFrom SARS to MERS: crystallographic studies on coronaviral proteases enable antiviral drug designFunctional Characterization of the Cleavage Specificity of the Sapovirus Chymotrypsin-Like ProteaseStructure of arterivirus nsp4. The smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion holeThe crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitorStructures of Two Coronavirus Main Proteases: Implications for Substrate Binding and Antiviral Drug DesignMechanism for Controlling the Dimer-Monomer Switch and Coupling Dimerization to Catalysis of the Severe Acute Respiratory Syndrome Coronavirus 3C-Like ProteaseStructure of the Main Protease from a Global Infectious Human Coronavirus, HCoV-HKU1Development of Broad-Spectrum Halomethyl Ketone Inhibitors Against Coronavirus Main Protease 3CLproCrystal Structures of Two Coronavirus ADP-Ribose-1''-Monophosphatases and Their Complexes with ADP-Ribose: a Systematic Structural Analysis of the Viral ADRP DomainC-terminal domain of sars-CoV main protease can form a 3d domain-swapped dimerThree-dimensional domain swapping as a mechanism to lock the active conformation in a super-active octamer of SARS-CoV main proteaseEnterovirus 71 and Coxsackievirus A16 3C Proteases: Binding to Rupintrivir and Their Substrates and Anti-Hand, Foot, and Mouth Disease Virus Drug DesignBroad-spectrum antivirals against 3C or 3C-like proteases of picornaviruses, noroviruses, and coronaviruses.Structural Basis for Antiviral Inhibition of the Main Protease, 3C, from Human Enterovirus 93Mechanism for controlling the monomer-dimer conversion of SARS coronavirus main proteaseDynamically-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.Characterization of a torovirus main proteinaseMutagenesis analysis of the nsp4 main proteinase reveals determinants of arterivirus replicase polyprotein autoprocessing.Automated protein structure homology modeling: a progress report.Overview of protein structural and functional folds.Evaluation of metal-conjugated compounds as inhibitors of 3CL protease of SARS-CoV.Analysis of murine hepatitis virus strain A59 temperature-sensitive mutant TS-LA6 suggests that nsp10 plays a critical role in polyprotein processingMutation of Glu-166 blocks the substrate-induced dimerization of SARS coronavirus main protease.Dynamically-driven enhancement of the catalytic machinery of the SARS 3C-like protease by the S284-T285-I286/A mutations on the extra domain.A norovirus protease structure provides insights into active and substrate binding site integrityMaturation mechanism of severe acute respiratory syndrome (SARS) coronavirus 3C-like proteinase.Coronaviruses resistant to a 3C-like protease inhibitor are attenuated for replication and pathogenesis, revealing a low genetic barrier but high fitness cost of resistanceBiosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase.Crystallization and diffraction analysis of the SARS coronavirus nsp10-nsp16 complex.Crystallization and preliminary crystallographic study of Porcine epidemic diarrhea virus main protease in complex with an inhibitorCrystallization and preliminary crystallographic study of Feline infectious peritonitis virus main protease in complex with an inhibitorStructures of the Middle East respiratory syndrome coronavirus 3C-like protease reveal insights into substrate specificity.Reversible unfolding of the severe acute respiratory syndrome coronavirus main protease in guanidinium chloride
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P2860
Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain.
description
2002 nî lūn-bûn
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2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Structure of coronavirus main ...... an extra alpha-helical domain
@nl
Structure of coronavirus main ...... an extra alpha-helical domain.
@ast
Structure of coronavirus main ...... an extra alpha-helical domain.
@en
type
label
Structure of coronavirus main ...... an extra alpha-helical domain
@nl
Structure of coronavirus main ...... an extra alpha-helical domain.
@ast
Structure of coronavirus main ...... an extra alpha-helical domain.
@en
prefLabel
Structure of coronavirus main ...... an extra alpha-helical domain
@nl
Structure of coronavirus main ...... an extra alpha-helical domain.
@ast
Structure of coronavirus main ...... an extra alpha-helical domain.
@en
P2093
P2860
P3181
P356
P1433
P1476
Structure of coronavirus main ...... an extra alpha-helical domain.
@en
P2093
Gottfried J Palm
Jeroen R Mesters
Kanchan Anand
Stuart G Siddell
P2860
P304
P3181
P356
10.1093/EMBOJ/CDF327
P407
P577
2002-07-01T00:00:00Z