Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain - Wikidata - wikimedia - TriplyDB

Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain

Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain

http://www.wikidata.org/entity/Q27621765

about

Combined X-ray, NMR, and Kinetic Analyses Reveal Uncommon Binding Characteristics of the Hepatitis C Virus NS3-NS4A Protease Inhibitor BI 201335 Inhibiting viral proteases: challenges and opportunities.Serpin mechanism of hepatitis C virus nonstructural 3 (NS3) protease inhibition: induced fit as a mechanism for narrow specificity.Mechanistic and kinetic characterization of hepatitis C virus NS3 protein interactions with NS4A and protease inhibitors.Structure and dynamics of coxsackievirus B4 2A proteinase, an enyzme involved in the etiology of heart disease Structure-based design of hepatitis C virus inhibitors.The NS4A Cofactor Dependent Enhancement of HCV NS3 Protease Activity Correlates with a 4D Geometrical Measure of the Catalytic Triad Region.Identification of residues in the dengue virus type 2 NS2B cofactor that are critical for NS3 protease activation.The effect of prime-site occupancy on the hepatitis C virus NS3 protease structure.Molecular biology of liver disorders:the hepatitis C virus and molecular targets for drug development.Mimicry between the hepatitis C virus polyprotein and antigenic targets of nuclear and smooth muscle antibodies in chronic hepatitis C virus infection.Inhibition of hepatitis C virus NS3 protease by peptides derived from complementarity-determining regions (CDRs) of the monoclonal antibody 8D4: tolerance of a CDR peptide to conformational changes of a target.

P2860

Q27666747-2ED20262-38D2-4B58-A1FA-CA21F8028C6A Q31112139-4EC8288D-0F3C-46AE-A6F0-047ABA525D0F Q33196330-8A7CD76E-2B9F-40D3-A788-EEB1F4BF2C7D Q33782666-3E70A593-0AE4-4BE6-A40A-89D3622A37B8 Q34302090-31CE086E-3407-4553-B089-665C235BF654 Q35591283-9141F87B-B136-45D7-8B24-4C375A986C73 Q36218266-B63C539A-0A5C-444F-96F4-6291EA5721BD Q37682862-A44C2A46-D8DF-4ACC-AEB5-4CB9AAB1CD17 Q38269787-1B7598AA-F81E-455A-97A2-0EEA0D07D849 Q42264259-5D621FA7-1BFC-41AB-8A5A-02A1CD18BF34 Q45722151-123EB31C-AC08-4A6F-9AA2-06D989D3F3EF Q45731473-BD41259D-B2AF-4B7F-B43B-CB050A1BE187

P2860

Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain

http://www.wikidata.org/entity/Q27621765

description

2000 nî lūn-bûn

@nan

2000 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի մարտին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

@yue

2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

name

Inhibitor binding induces acti ...... protein serine protease domain

@ast

Inhibitor binding induces acti ...... protein serine protease domain

@en

Inhibitor binding induces acti ...... protein serine protease domain

@nl

type

label

Inhibitor binding induces acti ...... protein serine protease domain

@ast

Inhibitor binding induces acti ...... protein serine protease domain

@en

Inhibitor binding induces acti ...... protein serine protease domain

@nl

prefLabel

Inhibitor binding induces acti ...... protein serine protease domain

@ast

Inhibitor binding induces acti ...... protein serine protease domain

@en

Inhibitor binding induces acti ...... protein serine protease domain

@nl

P1433

Q27621765-B0D8B7A0-B166-4381-95FF-C3D93D12E755

P1476

Q27621765-58B700FE-99DE-4C7D-B9BD-0308C0230DAD

P2093

Q27621765-0EF672B2-6123-41C9-86A9-BDEA75B91910

Q27621765-1CB6C736-454D-4EE3-88BB-BADEC593C868

Q27621765-4D15FB45-BFDE-41A2-B7DF-852FD6DC4E44

Q27621765-6542BC0E-3A3F-4180-AA2B-B679ACFFCFCB

Q27621765-70248006-E3E4-403A-8F83-B58290C273AD

Q27621765-9C51F6BC-DC37-491C-8BA6-5A548373FDDF

Q27621765-C4A65CBF-E444-4194-AAD1-49FC1D2CA2E6

Q27621765-E31BD88D-5F56-4307-853A-A3F5628F230E

Q27621765-EE860CEB-61AA-4B3E-876D-3ADE167F6A85

P2860

Q27621765-001EAA4A-7B52-4AF3-B6E6-D645C1B5C4AE

Q27621765-02138C56-8035-4B4B-B4F7-E8B067B88C66

Q27621765-04D5B0BC-057D-49DD-BC69-AEE27A74F962

Q27621765-06B63B03-1466-441F-9684-56566CFD6D71

Q27621765-09C248AA-13B8-456F-ACF6-3A58CB2A6CB6

Q27621765-0DBB9AA9-1A4A-4620-907E-12EFB6DBB11F

Q27621765-0FE9FC98-66A9-4CDE-BBAE-CC73391B097C

Q27621765-18081376-F045-4436-AEC1-ED7A8E12CCC3

Q27621765-1B6BBAAA-5A84-48D2-8AC7-27BB62DBE150

Q27621765-23F0DCB4-B273-4840-9C4B-0DC55AEDEAE2

P304

Q27621765-FC589F3C-7426-4E82-989C-801DAEC4889A

P31

Q27621765-8B9308FC-FB67-4BB6-BF79-3F712F67B4E8

P356

Q27621765-B504413F-F043-4FA4-8311-E5D27DE29C0A

P407

Q27621765-E6ED38EE-FDCC-45DC-8238-283FF3136F95

P433

Q27621765-C158583F-F064-42D1-B1A9-6948449F753D

P478

Q27621765-E3A0157A-6730-4404-9AA6-B1739CDC220B

P50

Q27621765-87F5F822-6991-40C8-B6CC-25F3F4F3900F

P577

Q27621765-B92AEA60-4698-4E8D-B853-73AFF43E5E19

P5875

Q27621765-8898F0ED-6002-46C9-B114-3B179CCD0083

P698

Q27621765-23D6ED4D-B312-4B33-A41D-A697D28A391D

P932

Q27621765-9B1E9879-635E-4A0C-B9C7-B14C600ABB53

P356

P1433

The EMBO Journal

P1476

Inhibitor binding induces acti ...... protein serine protease domain

@en

P2093

B Gerlach

http://www.w3.org/2001/XMLSchema#string

D O Cicero

http://www.w3.org/2001/XMLSchema#string

F Cordier

http://www.w3.org/2001/XMLSchema#string

F Narjes

http://www.w3.org/2001/XMLSchema#string

G Barbato

http://www.w3.org/2001/XMLSchema#string

R Bazzo

http://www.w3.org/2001/XMLSchema#string

R De Francesco

http://www.w3.org/2001/XMLSchema#string

S Sambucini

http://www.w3.org/2001/XMLSchema#string

V G Matassa

http://www.w3.org/2001/XMLSchema#string

P2860

Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy

Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications

Complex of NS3 protease and NS4A peptide of BK strain hepatitis C virus: A 2.2 Å resolution structure in a hexagonal crystal form

Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of hepatitis C virus

The solution structure of the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein provides new insights into its activation and catalytic mechanism

Three-dimensional structure of the complexes between bovine chymotrypsinogen A and two recombinant variants of human pancreatic secretory trypsin inhibitor (Kazal-type)

Geometry of binding of the benzamidine- and arginine-based inhibitors N alpha-(2-naphthyl-sulphonyl-glycyl)-DL-p-amidinophenylalanyl-pipe ridine (NAPAP) and (2R,4R)-4-methyl-1-[N alpha-(3-methyl-1,2,3,4-tetrahydro-8- quinolinesulphonyl)-L-arginyl]-2

Structure of human neutrophil elastase in complex with a peptide chloromethyl ketone inhibitor at 1.84-A resolution

The 1.8 A structure of the complex between chymostatin and Streptomyces griseus protease A. A model for serine protease catalytic tetrahedral intermediates

The refined 2.2-A (0.22-nm) X-ray crystal structure of the ternary complex formed by bovine trypsinogen, valine-valine and the Arg15 analogue of bovine pancreatic trypsin inhibitor

P304

1195-206

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1093/EMBOJ/19.6.1195

http://www.w3.org/2001/XMLSchema#string

P407

P433

6

http://www.w3.org/2001/XMLSchema#string

P478

19

http://www.w3.org/2001/XMLSchema#string

P50

Stephan Grzesiek

P577

2000-03-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

12598797

http://www.w3.org/2001/XMLSchema#string

P698

10716920

http://www.w3.org/2001/XMLSchema#string

P932

305661

http://www.w3.org/2001/XMLSchema#string