Characterization of Determinants Important for Hepatitis C Virus p7 Function in Morphogenesis by Using trans-Complementation - Wikidata - awgldk - TriplyDB

Characterization of Determinants Important for Hepatitis C Virus p7 Function in Morphogenesis by Using trans-Complementation

Characterization of Determinants Important for Hepatitis C Virus p7 Function in Morphogenesis by Using trans-Complementation

http://www.wikidata.org/entity/Q27490303

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Structural and Functional Properties of the Hepatitis C Virus p7 Viroporin Viral Membrane Channels: Role and Function in the Virus Life Cycle Genetic Analysis of the Carboxy-Terminal Region of the Hepatitis C Virus Core Protein NMR Structure and Ion Channel Activity of the p7 Protein from Hepatitis C Virus Identification of New Functional Regions in Hepatitis C Virus Envelope Glycoprotein E2 Intracellular proton conductance of the hepatitis C virus p7 protein and its contribution to infectious virus production A concerted action of hepatitis C virus p7 and nonstructural protein 2 regulates core localization at the endoplasmic reticulum and virus assembly.Bile acids specifically increase hepatitis C virus RNA-replication.A single polar residue and distinct membrane topologies impact the function of the infectious bronchitis coronavirus E protein.Oligomerization state and supramolecular structure of the HIV-1 Vpu protein transmembrane segment in phospholipid bilayers The intraviral protein interaction network of hepatitis C virus.hepatitis c Virus p7 is critical for capsid assembly and envelopment Production of hepatitis C virus lacking the envelope-encoding genes for single-cycle infection by providing homologous envelope proteins or vesicular stomatitis virus glycoproteins in trans.Hepatitis B and C virus hepatocarcinogenesis: lessons learned and future challenges.The subcellular localization of the hepatitis C virus non-structural protein NS2 is regulated by an ion channel-independent function of the p7 protein Phosphatidylserine-specific phospholipase A1 involved in hepatitis C virus assembly through NS2 complex formation Last stop before exit - hepatitis C assembly and release as antiviral drug targets.Morphogenesis of infectious hepatitis C virus particles The N-terminal Helical Region of the Hepatitis C Virus p7 Ion Channel Protein Is Critical for Infectious Virus Production.A Coronavirus E Protein Is Present in Two Distinct Pools with Different Effects on Assembly and the Secretory Pathway.Subcellular localization and function of an epitope-tagged p7 viroporin in hepatitis C virus-producing cells Prevalence of HCV genotypes in district Mardan Ion Channel Function and Cross-Species Determinants in Viral Assembly of Nonprimate Hepacivirus p7 Efficiency of E2-p7 processing modulates production of infectious hepatitis C virus Hepatitis C virus: assembly and release of virus particles.Hepatitis C virus p7: molecular function and importance in hepatitis C virus life cycle and potential antiviral target.The coronavirus E protein: assembly and beyond.Are trans-complementation systems suitable for hepatitis C virus life cycle studies?Incorporation of hepatitis C virus E1 and E2 glycoproteins: the keystones on a peculiar virion.Hepatitis C virus p7-a viroporin crucial for virus assembly and an emerging target for antiviral therapy.Tricistronic hepatitis C virus subgenomic replicon expressing double transgenes.Incorporation of primary patient-derived glycoproteins into authentic infectious hepatitis C virus particles.Two methods of heterokaryon formation to discover HCV restriction factors.Role of JC virus agnoprotein in virion formation.Hepatitis C virus NS2 coordinates virus particle assembly through physical interactions with the E1-E2 glycoprotein and NS3-NS4A enzyme complexes.The Molecular Switch of Telomere Phages: High Binding Specificity of the PY54 Cro Lytic Repressor to a Single Operator Site.Classical swine fever virus nonstructural protein p7 modulates infectious virus production HCV enters the twenty-first century.Cell culture-adaptive mutations in hepatitis C virus promote viral production by enhancing viral replication and release.

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P2860

Characterization of Determinants Important for Hepatitis C Virus p7 Function in Morphogenesis by Using trans-Complementation

http://www.wikidata.org/entity/Q27490303

description

2009 nî lūn-bûn

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2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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Characterization of Determinan ...... by Using trans-Complementation

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Characterization of Determinan ...... by Using trans-Complementation

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Characterization of Determinan ...... by Using trans-Complementation

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Characterization of Determinan ...... by Using trans-Complementation

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Characterization of Determinan ...... by Using trans-Complementation

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Characterization of Determinan ...... by Using trans-Complementation

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Characterization of Determinan ...... by Using trans-Complementation

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Characterization of Determinan ...... by Using trans-Complementation

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Characterization of Determinan ...... by Using trans-Complementation

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Journal of Virology

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Characterization of Determinan ...... by Using trans-Complementation

@en

P2093

Arvind Patel

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Christiane Brohm

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Francois Penin

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Ivo C Lorenz

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Martina Friesland

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Thomas Pietschmann

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P2860

Broad-spectrum inhibition of retroviral and filoviral particle release by tetherin

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

Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system

Inhibition of Lassa and Marburg virus production by tetherin

Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction

Charged residues in the transmembrane domains of hepatitis C virus glycoproteins play a major role in the processing, subcellular localization, and assembly of these envelope proteins

Sequences in the 5' nontranslated region of hepatitis C virus required for RNA replication.

Robust hepatitis C virus infection in vitro.

Signal peptide cleavage and internal targeting signals direct the hepatitis C virus p7 protein to distinct intracellular membranes.

Subcellular Localization and Topology of the p7 Polypeptide of Hepatitis C Virus

P304

11682-93

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scholarly article

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10.1128/JVI.00691-09

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22

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P478

83

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Ralf Bartenschlager

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2009-11-01T00:00:00Z

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19726506

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P932

2772676

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