Characterization of the envelope glycoproteins associated with infectious hepatitis C virus - Test2 - elhamkhani - TriplyDB

Characterization of the envelope glycoproteins associated with infectious hepatitis C virus

Characterization of the envelope glycoproteins associated with infectious hepatitis C virus

http://www.wikidata.org/entity/Q34120689

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The HIV glycan shield as a target for broadly neutralizing antibodies Hepatitis C virus comes for dinner: How the hepatitis C virus interferes with autophagy Genetic Diversity Underlying the Envelope Glycoproteins of Hepatitis C Virus: Structural and Functional Consequences and the Implications for Vaccine Design The hepatitis C virus glycan shield and evasion of the humoral immune response Identification of a novel drug lead that inhibits HCV infection and cell-to-cell transmission by targeting the HCV E2 glycoprotein Identification of New Functional Regions in Hepatitis C Virus Envelope Glycoprotein E2 Crystal structure of glycoprotein E2 from bovine viral diarrhea virus Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design Comparative Proteomics Reveals Important Viral-Host Interactions in HCV-Infected Human Liver Cells Cell culture replication of a genotype 1b hepatitis C virus isolate cloned from a patient who underwent liver transplantation Antiviral lectins from red and blue-green algae show potent in vitro and in vivo activity against hepatitis C virus Coordination of Hepatitis C Virus Assembly by Distinct Regulatory Regions in Nonstructural Protein 5A Fusogenic properties of the ectodomains of hepatitis C virus envelope proteins.Conserved glycine 33 residue in flexible domain I of hepatitis C virus core protein is critical for virus infectivity.Hepatitis C Virus Is Released via a Noncanonical Secretory Route.The missing pieces of the HCV entry puzzle.Conformational Flexibility in the Immunoglobulin-Like Domain of the Hepatitis C Virus Glycoprotein E2.Regulated Entry of Hepatitis C Virus into Hepatocytes.Characterization of the ectodomain of the envelope protein of dengue virus type 4: expression, membrane association, secretion and particle formation in the absence of precursor membrane protein.NS2 protein of hepatitis C virus interacts with structural and non-structural proteins towards virus assembly.Modulation of triglyceride and cholesterol ester synthesis impairs assembly of infectious hepatitis C virus.Hepatitis C virus in the new era: perspectives in epidemiology, prevention, diagnostics and predictors of response to therapy.Identification of conserved residues in hepatitis C virus envelope glycoprotein E2 that modulate virus dependence on CD81 and SRB1 entry factors.Role of N-linked glycans in the functions of hepatitis C virus envelope proteins incorporated into infectious virions.Innate immune cell networking in hepatitis C virus infection Biochemical and morphological properties of hepatitis C virus particles and determination of their lipidome.C-terminal helical domains of dengue virus type 4 E protein affect the expression/stability of prM protein and conformation of prM and E proteins.Interplay between basic residues of hepatitis C virus glycoprotein E2 with viral receptors, neutralizing antibodies and lipoproteins.Mean protein evolutionary distance: a method for comparative protein evolution and its application.hepatitis c Virus p7 is critical for capsid assembly and envelopment Hepatitis C virus life cycle and lipid metabolism Hepatitis C virus (HCV) envelope glycoproteins E1 and E2 contain reduced cysteine residues essential for virus entry.Last stop before exit - hepatitis C assembly and release as antiviral drug targets.Vaccine-induced cross-genotype reactive neutralizing antibodies against hepatitis C virus.Characterization of hepatitis C virus interaction with heparan sulfate proteoglycans.Morphogenesis of infectious hepatitis C virus particles Hepatitis C Virus E1 and E2 Proteins Used as Separate Immunogens Induce Neutralizing Antibodies with Additive Properties Identification of a Potent and Broad-Spectrum Hepatitis C Virus Fusion Inhibitory Peptide from the E2 Stem Domain Hepatitis C Virus Envelope Glycoprotein E1 Forms Trimers at the Surface of the Virion.Hepatitis C Virus Sensing by Human Trophoblasts Induces Innate Immune Responses and Recruitment of Maternal NK Cells: Potential Implications for Limiting Vertical Transmission.

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P2860

Characterization of the envelope glycoproteins associated with infectious hepatitis C virus

http://www.wikidata.org/entity/Q34120689

description

2010 nî lūn-bûn

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2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2010 թվականի հուլիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Characterization of the envelo ...... h infectious hepatitis C virus

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Characterization of the envelo ...... h infectious hepatitis C virus

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Characterization of the envelo ...... h infectious hepatitis C virus

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Characterization of the envelo ...... h infectious hepatitis C virus

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Characterization of the envelo ...... h infectious hepatitis C virus

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Characterization of the envelo ...... h infectious hepatitis C virus

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Characterization of the envelo ...... h infectious hepatitis C virus

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Characterization of the envelo ...... h infectious hepatitis C virus

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Journal of Virology

P1476

Characterization of the envelo ...... h infectious hepatitis C virus

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P2093

Arvind H Patel

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Gabrielle Vieyres

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Gilles Duverlie

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Véronique Descamps

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Xavier Thomas

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P2860

Binding of hepatitis C virus to CD81

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

Identification of amino acid residues in CD81 critical for interaction with hepatitis C virus envelope glycoprotein E2.

Hepatitis B virus morphogenesis

Infectious hepatitis C virus pseudo-particles containing functional E1-E2 envelope protein complexes

The transmembrane domain of hepatitis C virus glycoprotein E1 is a signal for static retention in the endoplasmic reticulum.

Acid-resistant bovine pestivirus requires activation for pH-triggered fusion during entry.

A retention signal necessary and sufficient for endoplasmic reticulum localization maps to the transmembrane domain of hepatitis C virus glycoprotein E2.

Human monoclonal antibodies that inhibit binding of hepatitis C virus E2 protein to CD81 and recognize conserved conformational epitopes

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

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10159-10168

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scholarly article

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10.1128/JVI.01180-10

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19

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84

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2010-07-28T00:00:00Z

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20668082

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2937754

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