Structure of the catalytic domain of the hepatitis C virus NS2-3 protease. - Wikidata - wikimedia - TriplyDB

Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.

Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.

http://www.wikidata.org/entity/Q34550380

about

Hepatitis C virus NS2 protease inhibits host cell antiviral response by inhibiting IKKε and TBK1 functions Signal peptidase complex subunit 1 participates in the assembly of hepatitis C virus through an interaction with E2 and NS2 Hepatitis C virus proteins Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad Emerging therapies for the treatment of hepatitis C Compensatory Mutations in E1, p7, NS2, and NS3 Enhance Yields of Cell Culture-Infectious Intergenotypic Chimeric Hepatitis C Virus Hepatitis C Virus p7 and NS2 Proteins Are Essential for Production of Infectious Virus Studying Hepatitis C Virus: Making the Best of a Bad Virus Hepatitis C Virus Diversity and Evolution in the Full Open-Reading Frame during Antiviral Therapy Advantages of a single-cycle production assay to study cell culture-adaptive mutations of hepatitis C virus NS3 Helicase Domains Involved in Infectious Intracellular Hepatitis C Virus Particle Assembly Hepatitis C virus JFH-1 strain infection in chimpanzees is associated with low pathogenicity and emergence of an adaptive mutation High-Resolution Functional Profiling of Hepatitis C Virus Genome Structural and Functional Characterization of Nonstructural Protein 2 for Its Role in Hepatitis C Virus Assembly Hepatitis C virus NS2 is a protease stimulated by cofactor domains in NS3 trans-Complementation of an NS2 Defect in a Late Step in Hepatitis C Virus (HCV) Particle Assembly and Maturation Hepatitis C Virus NS2 Protein Contributes to Virus Particle Assembly via Opposing Epistatic Interactions with the E1-E2 Glycoprotein and NS3-NS4A Enzyme Complexes Architects of assembly: roles of Flaviviridae non-structural proteins in virion morphogenesis Hepatitis C: recent successes and continuing challenges in the development of improved treatment modalities Determinants of the Hepatitis C Virus Nonstructural Protein 2 Protease Domain Required for Production of Infectious Virus A comparative analysis of the fluorescence properties of the wild-type and active site mutants of the hepatitis C virus autoprotease NS2-3 Structural and Functional Studies of Nonstructural Protein 2 of the Hepatitis C Virus Reveal Its Key Role as Organizer of Virion Assembly NS2 Proteins of GB Virus B and Hepatitis C Virus Share Common Protease Activities and Membrane Topologies Structure of the NS2B-NS3 protease from Zika virus after self-cleavage Identification and characterization of the host protein DNAJC14 as a broadly active flavivirus replication modulator Determinants for membrane association of the hepatitis C virus NS2 protease domain.Novel nucleotide and amino acid covariation between the 5'UTR and the NS2/NS3 proteins of hepatitis C virus: bioinformatic and functional analyses.Maturation mechanism of severe acute respiratory syndrome (SARS) coronavirus 3C-like proteinase.Structure of the autocatalytic cysteine protease domain of potyvirus helper-component proteinase Amphipathic alpha-helix AH2 is a major determinant for the oligomerization of hepatitis C virus nonstructural protein 4B The intraviral protein interaction network of hepatitis C virus.Hepatitis C virus NS2 protein serves as a scaffold for virus assembly by interacting with both structural and nonstructural proteins Targeting the non-structural proteins of hepatitis C virus: beyond hepatitis C virus protease and polymerase.An overview of HCV molecular biology, replication and immune responses.Identification of two internal signal peptide sequences: critical for classical swine fever virus non-structural protein 2 to trans-localize to the endoplasmic reticulum.Inhibition of hepatitis C virus infection by DNA aptamer against NS2 protein.Epoxide based inhibitors of the hepatitis C virus non-structural 2 autoprotease A conserved NS3 surface patch orchestrates NS2 protease stimulation, NS5A hyperphosphorylation and HCV genome replication.CleavPredict: A Platform for Reasoning about Matrix Metalloproteinases Proteolytic Events.Identification of a lead like inhibitor of the hepatitis C virus non-structural NS2 autoprotease.

P2860

Q24301741-BE7BDACF-E0E6-4CCD-A981-B425BD616363 Q24322876-A4EC61AE-4A8A-45F6-BCEC-3871EE8359D9 Q24563969-C0CB666F-94EE-44CA-8369-2340C2AAD01E Q26781998-EB3691C0-FFE5-45B4-B97E-920CDDC0A4D4 Q27003319-2FC4C1CE-7869-42CA-BBEC-B5DE5F54CC32 Q27478033-25618701-2FE6-4DA5-BC61-8AFAE110E584 Q27481018-D9C72B28-C80B-4DB8-B793-FB15266A2426 Q27481034-7243E9A3-EFD6-4AF9-A088-CA2CE9188D9B Q27486013-A5C56E63-A24A-4D8C-B7F9-830B8FC447D9 Q27486103-78051D35-65E9-4C0D-848B-297A387684A5 Q27486581-290C2887-72FE-4DEF-874C-F4BD0B257418 Q27486836-C2EA6879-656F-44D3-9FC0-78B083ED1F82 Q27487019-F6B4126C-6B4E-4D88-A80A-F505AF28D393 Q27488261-0B25CAA9-2DF1-4447-A260-8F02D421F3DF Q27488282-60275D51-90AC-4EF8-BB50-57D55A34CE3A Q27488316-126C747B-1BA4-48DC-AA2E-424D016CD6BB Q27489514-138D8AAA-6C85-44B0-A9C6-4FA7D3B6FAA8 Q27490193-3DBB3640-32D7-43BB-98F8-EFFC0189EA0F Q27490426-85518922-5071-4A4E-A0C7-D6124E205F78 Q27490479-12D53128-52B4-4201-A6E7-37BA76B562A9 Q27490941-CEADEF63-2639-4F53-9EE5-B3BF6E28AA4B Q27666400-F76EED31-077F-4B11-AFC4-A682AB1E7A7A Q27683450-A00D288D-8A44-4933-8BA5-D196DD6694F7 Q27869770-472CC2B8-61EB-42CE-8A05-F592E563BD81 Q28476726-BA591971-5D36-4107-BDEA-0A3D2A52823B Q33887730-D9C92BD0-BA07-4A9B-87BE-0E4D203FEAEE Q34043316-408B3C79-F1B0-4339-ADFD-21269E3FEEB4 Q34107407-E48620DF-7ED7-4351-A58F-79FBC946EF1D Q34182659-E8CDB4AB-2D77-4D43-888F-9BC6DB49308A Q34416649-85541C35-6575-4F1E-AACA-4E29A505E7A6 Q34418887-B85054B3-71D5-4669-BE0E-15DF594DC98E Q34457862-BA9584F0-1CCF-4FB7-B51F-910383C02A54 Q34620091-B28976AC-482B-498F-9629-A95871948779 Q34916120-FC2D1D9B-73B9-477C-A2EF-49B6827F3A8D Q35040106-154FC8A2-32C7-4E76-A845-FC51F8B9630D Q35108971-265BC73C-7A94-46AE-815E-578C420E3597 Q35431032-2FFEC947-1A54-43AF-841B-B35D9373C86C Q35578182-26104AA0-FE2A-43FC-9AA1-B2B35E8213AB Q35638306-4295530A-F2CB-4D55-BA54-7C67ED108E73 Q35827684-63059772-95C8-4463-B3B9-25CACD8E413D

P2860

Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.

http://www.wikidata.org/entity/Q34550380

description

2006 nî lūn-bûn

@nan

2006 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.

@ast

Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.

@en

Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.

@nl

type

label

Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.

@ast

Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.

@en

Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.

@nl

prefLabel

Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.

@ast

Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.

@en

Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.

@nl

P1433

Q34550380-DC12B8BF-9D47-416D-8C06-50262AA581A8

P1476

Q34550380-21D2DC18-CD2C-4E50-ADCC-11CF30BE4961

P2093

Q34550380-3075F9E6-5645-4D25-9968-879B42729DE8

Q34550380-3BF12426-8B86-4600-8DEF-382478FFA038

Q34550380-6B074BE8-0F82-4F9E-96FE-659381229429

Q34550380-7B9B5395-6B46-4304-B756-A1651A81BEAF

P2860

Q34550380-0976334A-B03C-4B6D-8134-08475EF05A0E

Q34550380-137AC597-71EC-4DF0-BF16-2924F4DCBB4E

Q34550380-28188A66-BA24-4D26-80CE-AAFC90CC0B0E

Q34550380-36CA8E68-C8D1-40C5-831B-17D3E96ADF80

Q34550380-4150C771-87D0-4CEA-9D63-6AE119B569C9

Q34550380-4C757F21-A14B-4B6D-AF2C-A9ACC84E3705

Q34550380-633ECFCD-3AED-4965-9E1E-A6DA8089C768

Q34550380-65FD6BE2-248A-4387-AABF-281950F2FFB2

Q34550380-6CEE774B-9D93-4F3D-B556-C3286B8C42A8

Q34550380-6E1F96C6-4A83-46CC-A759-5722647D5C42

P2888

Q34550380-89744BD0-99E6-401C-ADC3-88F266446706

P304

Q34550380-01D59226-B73C-4F75-B007-069631560580

P31

Q34550380-8000343D-E6FE-4D9B-BA8E-747759440BB3

P356

Q34550380-4CCC258B-1B55-4ECF-93A4-31EA3D6F3D6F

P407

Q34550380-D40C1E75-2CDC-4215-B744-F8F9397EB867

P433

Q34550380-35F8506A-6B9A-41EB-9A46-5A78C2933CF7

P478

Q34550380-DBF05CA0-48F3-43AD-9A7B-2F9FF3D6848C

P577

Q34550380-C8894B23-DCCD-4BD5-A6C6-6BB106D9CB97

P5875

Q34550380-1923D053-5531-4446-AF7F-C55BA4A27413

P6179

Q34550380-3B0354EE-1154-4F7A-A46C-E791DA434960

P698

Q34550380-3031ACD2-9086-4349-B695-5A32DFDF5D02

P356

P1433

P1476

Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.

@en

P2093

Charles M Rice

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

Ivo C Lorenz

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

Joseph Marcotrigiano

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

Thomas G Dentzer

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

P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Characterization of the hepatitis C virus NS2/3 processing reaction by using a purified precursor protein

Construction and characterization of infectious intragenotypic and intergenotypic hepatitis C virus chimeras

Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo

Refined structure of Sindbis virus core protein and comparison with other chymotrypsin-like serine proteinase structures

The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site

Crystal structure of the hepatitis C virus NS3 protease domain complexed with a synthetic NS4A cofactor peptide

Refined X-ray crystallographic structure of the poliovirus 3C gene product

Protein structure comparison by alignment of distance matrices

P2888

P304

831-835

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

P31

scholarly article

P356

10.1038/NATURE04975

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

P407

P433

7104

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

P478

442

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

P577

2006-07-23T00:00:00Z

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

P5875

6924227

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

P6179

1039688397

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

P698

16862121

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