The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site
about
Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunityNuclear localization of the NS3 protein of hepatitis C virus and factors affecting the localizationHepatitis C virus proteinsNS3 protease from hepatitis C virus: biophysical studies on an intrinsically disordered protein domainSelection of functional variants of the NS3-NS4A protease of hepatitis C virus by using chimeric sindbis virusesCharacterization of soluble hepatitis C virus RNA-dependent RNA polymerase expressed in Escherichia coli.Mutagenesis of the NS3 protease of dengue virus type 2.Hepatitis G virus encodes protease activities which can effect processing of the virus putative nonstructural proteins.Multiple enzymatic activities associated with recombinant NS3 protein of hepatitis C virusIn vivo selection of protease cleavage sites by using chimeric Sindbis virus librariesSubcellular localization, stability, and trans-cleavage competence of the hepatitis C virus NS3-NS4A complex expressed in tetracycline-regulated cell lines.Virus-specific cofactor requirement and chimeric hepatitis C virus/GB virus B nonstructural protein 3Isolation and characterization of monoclonal antibodies that inhibit hepatitis C virus NS3 proteaseMutations That Affect Dimer Formation and Helicase Activity of the Hepatitis C Virus HelicaseSpecific Interaction of Hepatitis C Virus Protease/Helicase NS3 with the 3'-Terminal Sequences of Viral Positive- and Negative-Strand RNAPurification and Characterization of West Nile Virus Nucleoside Triphosphatase (NTPase)/Helicase: Evidence for Dissociation of the NTPase and Helicase Activities of the EnzymeStimulation of hepatitis C virus (HCV) nonstructural protein 3 (NS3) helicase activity by the NS3 protease domain and by HCV RNA-dependent RNA polymeraseThe hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding.SCH 503034, a mechanism-based inhibitor of hepatitis C virus NS3 protease, suppresses polyprotein maturation and enhances the antiviral activity of alpha interferon in replicon cells.In Vitro Selection and Characterization of Hepatitis C Virus Serine Protease Variants Resistant to an Active-Site Peptide InhibitorIdentification of Hepatitis C Virus (HCV) Subtype 1b Strains That Are Highly, or Only Weakly, Associated with Hepatocellular Carcinoma on the Basis of the Secondary Structure of an Amino-Terminal Portion of the HCV NS3 ProteinThe NS3 proteinase domain of hepatitis C virus is a zinc-containing enzymeGB virus B and hepatitis C virus NS3 serine proteases share substrate specificityBovine viral diarrhea virus NS3 serine proteinase: polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replicationSerine protease of pestiviruses: determination of cleavage sitesProbing the substrate specificity of hepatitis C virus NS3 serine protease by using synthetic peptidesA point mutation abolishes the helicase but not the nucleoside triphosphatase activity of hepatitis C virus NS3 proteinIn vitro study of the NS2-3 protease of hepatitis C virusThe hepatitis C virus NS4A protein: interactions with the NS4B and NS5A proteinsCharacterization of engineered hepatitis C virus NS3 protease inhibitors affinity selected from human pancreatic secretory trypsin inhibitor and minibody repertoiresBiochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for enzymatic activityStudying Hepatitis C Virus: Making the Best of a Bad VirusConstruction, expression, and characterization of a novel fully activated recombinant single-chain hepatitis C virus proteaseComparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicasesConformational changes in the NS3 protease from hepatitis C virus strain Bk monitored by limited proteolysis and mass spectrometryStructural determinants for membrane association and dynamic organization of the hepatitis C virus NS3-4A complex.Hepatitis C virus NS2 is a protease stimulated by cofactor domains in NS3Hepatitis C Virus NS2 Protein Contributes to Virus Particle Assembly via Opposing Epistatic Interactions with the E1-E2 Glycoprotein and NS3-NS4A Enzyme ComplexesInhibition of the hepatitis C virus NS3/4A protease. The crystal structures of two protease-inhibitor complexesInhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain
P2860
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P2860
The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site
description
1996 nî lūn-bûn
@nan
1996 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
The crystal structure of hepat ...... a structural zinc binding site
@ast
The crystal structure of hepat ...... a structural zinc binding site
@en
The crystal structure of hepat ...... a structural zinc binding site
@nl
type
label
The crystal structure of hepat ...... a structural zinc binding site
@ast
The crystal structure of hepat ...... a structural zinc binding site
@en
The crystal structure of hepat ...... a structural zinc binding site
@nl
prefLabel
The crystal structure of hepat ...... a structural zinc binding site
@ast
The crystal structure of hepat ...... a structural zinc binding site
@en
The crystal structure of hepat ...... a structural zinc binding site
@nl
P2093
P3181
P1433
P1476
The crystal structure of hepat ...... a structural zinc binding site
@en
P2093
E W Moomaw
J A Wickersham
Z Hostomska
Z Hostomsky
P304
P3181
P356
10.1016/S0092-8674(00)81350-1
P407
P577
1996-10-18T00:00:00Z