Identification of basic amino acids at the N-terminal end of the core protein that are crucial for hepatitis C virus infectivity. - Wikidata - awgldk - TriplyDB

Identification of basic amino acids at the N-terminal end of the core protein that are crucial for hepatitis C virus infectivity.

Identification of basic amino acids at the N-terminal end of the core protein that are crucial for hepatitis C virus infectivity.

http://www.wikidata.org/entity/Q34416559

about

Hepatitis C virus replication and Golgi function in brefeldin a-resistant hepatoma-derived cells HCV core residues critical for infectivity are also involved in core-NS5A complex formation Coordination of Hepatitis C Virus Assembly by Distinct Regulatory Regions in Nonstructural Protein 5A Aminoacylase 3 binds to and cleaves the N-terminus of the hepatitis C virus core protein.Conserved glycine 33 residue in flexible domain I of hepatitis C virus core protein is critical for virus infectivity.Hepatitis C virus capsid protein and intracellular lipids interplay and its association with hepatic steatosis Bidirectional lipid droplet velocities are controlled by differential binding strengths of HCV core DII protein.A genetic interaction between the core and NS3 proteins of hepatitis C virus is essential for production of infectious virus Strong correlation between liver and serum levels of hepatitis C virus core antigen and RNA in chronically infected patients Morphogenesis of infectious hepatitis C virus particles Hepatitis C Virus Envelope Glycoprotein E1 Forms Trimers at the Surface of the Virion.Inhibition of hepatitis C virus in chimeric mice by short synthetic hairpin RNAs: sequence analysis of surviving virus shows added selective pressure of combination therapy.HCV core protein and virus assembly: what we know without structures.Incorporation of hepatitis C virus E1 and E2 glycoproteins: the keystones on a peculiar virion.Identification of Novel Functions for Hepatitis C Virus Envelope Glycoprotein E1 in Virus Entry and Assembly Polyphenols Inhibit Hepatitis C Virus Entry by a New Mechanism of Action.The antimalarial ferroquine is an inhibitor of hepatitis C virus.(-)-Epigallocatechin-3-gallate is a new inhibitor of hepatitis C virus entry.The role of PTEN - HCV core interaction in hepatitis C virus replication.HCV replication and assembly: a play in one act Functional Study of the C-Terminal Part of the Hepatitis C Virus E1 Ectodomain

P2860

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P2860

Identification of basic amino acids at the N-terminal end of the core protein that are crucial for hepatitis C virus infectivity.

http://www.wikidata.org/entity/Q34416559

description

2010 nî lūn-bûn

@nan

2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Identification of basic amino ...... hepatitis C virus infectivity.

@ast

Identification of basic amino ...... hepatitis C virus infectivity.

@en

Identification of basic amino ...... hepatitis C virus infectivity.

@nl

type

label

Identification of basic amino ...... hepatitis C virus infectivity.

@ast

Identification of basic amino ...... hepatitis C virus infectivity.

@en

Identification of basic amino ...... hepatitis C virus infectivity.

@nl

prefLabel

Identification of basic amino ...... hepatitis C virus infectivity.

@ast

Identification of basic amino ...... hepatitis C virus infectivity.

@en

Identification of basic amino ...... hepatitis C virus infectivity.

@nl

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P1433

Journal of Virology

P1476

Identification of basic amino ...... hepatitis C virus infectivity.

@en

P2093

André Pillez

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

Czeslaw Wychowski

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

Gilles Duverlie

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

Khaled Alsaleh

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

Pierre-Yves Delavalle

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

Véronique Descamps

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

P2860

Characterization of hepatitis C virus E2 glycoprotein interaction with a putative cellular receptor, CD81.

Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets

A cellular RNA-binding protein enhances internal ribosomal entry site-dependent translation through an interaction downstream of the hepatitis C virus polyprotein initiation codon

Sequence analysis of the core gene of 14 hepatitis C virus genotypes

Evidence for a functional RNA element in the hepatitis C virus core gene

Hepatitis C virus structural proteins assemble into viruslike particles in insect cells.

Identification of Residues in the Hepatitis C Virus Core Protein That Are Critical for Capsid Assembly in a Cell-Free System

Interaction of hepatitis C virus core protein with viral sense RNA and suppression of its translation

Core protein-coding sequence, but not core protein, modulates the efficiency of cap-independent translation directed by the internal ribosome entry site of hepatitis C virus

Robust hepatitis C virus infection in vitro.

P304

12515-12528

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scholarly article

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10.1128/JVI.01393-10

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P433

24

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84

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2010-10-13T00:00:00Z

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20943968

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P932

3004332

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