Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs
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Targeting membrane-bound viral RNA synthesis reveals potent inhibition of diverse coronaviruses including the middle East respiratory syndrome virusMolecular advances in the cell biology of SARS-CoV and current disease prevention strategiesInhibition of SARS-CoV 3C-like Protease Activity by Theaflavin-3,3'-digallate (TF3)A genomic analysis of rat proteases and protease inhibitorsA model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidasesCoronavirus 3CLpro proteinase cleavage sites: possible relevance to SARS virus pathologyMolecular 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 designLocalization and Membrane Topology of Coronavirus Nonstructural Protein 4: Involvement of the Early Secretory Pathway in ReplicationFunctional Characterization of the Cleavage Specificity of the Sapovirus Chymotrypsin-Like ProteaseThe crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitorStructure-based design, synthesis, and biological evaluation of peptidomimetic SARS-CoV 3CLpro inhibitorsMutation of Gly-11 on the dimer interface results in the complete crystallographic dimer dissociation of severe acute respiratory syndrome coronavirus 3C-like protease: crystal structure with molecular dynamics simulationsStructures 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 DomainStructural Basis of Inhibition Specificities of 3C and 3C-like Proteases by Zinc-coordinating and Peptidomimetic CompoundsCrystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved propertyC-terminal domain of sars-CoV main protease can form a 3d domain-swapped dimerThe SARS-Unique Domain (SUD) of SARS Coronavirus Contains Two Macrodomains That Bind G-QuadruplexesStructure of the C-terminal domain of nsp4 from feline coronavirusThree-dimensional domain swapping as a mechanism to lock the active conformation in a super-active octamer of SARS-CoV main proteaseBroad-spectrum antivirals against 3C or 3C-like proteases of picornaviruses, noroviruses, and coronaviruses.Discovery, synthesis, and structure-based optimization of a series of N-(tert-butyl)-2-(N-arylamido)-2-(pyridin-3-yl) acetamides (ML188) as potent noncovalent small molecule inhibitors of the severe acute respiratory syndrome coronavirus (SARS-CoV)3C Protease of Enterovirus 68: Structure-Based Design of Michael Acceptor Inhibitors and Their Broad-Spectrum Antiviral Effects against PicornavirusesAutoproteolytic Activation of ThnT Results in Structural Reorganization Necessary for Substrate Binding and CatalysisMechanism for controlling the monomer-dimer conversion of SARS coronavirus main proteaseTargeting zoonotic viruses: Structure-based inhibition of the 3C-like protease from bat coronavirus HKU4--The likely reservoir host to the human coronavirus that causes Middle East Respiratory Syndrome (MERS)Characterization of an Immunodominant Epitope in the Endodomain of the Coronavirus Membrane ProteinSevere acute respiratory syndrome coronavirus as an agent of emerging and reemerging infectionGenome-wide analysis of protein-protein interactions and involvement of viral proteins in SARS-CoV replicationDynamically-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.Abelson Kinase Inhibitors Are Potent Inhibitors of Severe Acute Respiratory Syndrome Coronavirus and Middle East Respiratory Syndrome Coronavirus Fusion.
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P2860
Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs
description
2003 nî lūn-bûn
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2003 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
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name
Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs
@ast
Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs
@en
Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs
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type
label
Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs
@ast
Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs
@en
Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs
@nl
prefLabel
Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs
@ast
Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs
@en
Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs
@nl
P2093
P921
P3181
P356
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Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs
@en
P2093
Jeroen R Mesters
Kanchan Anand
Parvesh Wadhwani
P304
P3181
P356
10.1126/SCIENCE.1085658
P407
P577
2003-06-13T00:00:00Z