Effects of herpes simplex virus on structure and function of nectin-1/HveC. - Wikidata - awgldk - TriplyDB

Effects of herpes simplex virus on structure and function of nectin-1/HveC.

Effects of herpes simplex virus on structure and function of nectin-1/HveC.

http://www.wikidata.org/entity/Q34970789

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Cellular localization of nectin-1 and glycoprotein D during herpes simplex virus infection Mutations in the N-terminal domains of nectin-1 and nectin-2 reveal differences in requirements for entry of various alphaherpesviruses and for nectin-nectin interactions.Disruption of adherens junctions liberates nectin-1 to serve as receptor for herpes simplex virus and pseudorabies virus entry.Specific association of glycoprotein B with lipid rafts during herpes simplex virus entry Crystal Structure of the cis-Dimer of Nectin-1: IMPLICATIONS FOR THE ARCHITECTURE OF CELL-CELL JUNCTIONS Nectin ectodomain structures reveal a canonical adhesive interface Structure of Herpes Simplex Virus Glycoprotein D Bound to the Human Receptor Nectin-1 Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion Prominent role of the Ig-like V domain in trans-interactions of nectins. Nectin3 and nectin 4 bind to the predicted C-C'-C"-D beta-strands of the nectin1 V domain A key role for nectin-1 in the ventral hippocampus in contextual fear memory.Glycoprotein D actively induces rapid internalization of two nectin-1 isoforms during herpes simplex virus entry Deletion of the second immunoglobulin-like domain of nectin-1 alters its intracellular processing and localization and ability to mediate entry of herpes simplex virus Herpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entry The nectin-1alpha transmembrane domain, but not the cytoplasmic tail, influences cell fusion induced by HSV-1 glycoproteins.Amino acid substitutions in the V domain of nectin-1 (HveC) that impair entry activity for herpes simplex virus types 1 and 2 but not for Pseudorabies virus or bovine herpesvirus 1.HSV-1 Cgal+ infection promotes quaking RNA binding protein production and induces nuclear-cytoplasmic shuttling of quaking I-5 isoform in human hepatoma cells.αvβ6- and αvβ8-integrins serve as interchangeable receptors for HSV gH/gL to promote endocytosis and activation of membrane fusion.The herpesvirus glycoproteins B and H.L are sequentially recruited to the receptor-bound gD to effect membrane fusion at virus entry.Function of herpes simplex virus type 1 gD mutants with different receptor-binding affinities in virus entry and fusion Role of Proteolipid Protein in HSV-1 Entry in Oligodendrocytic Cells.Chlamydia persistence -- a tool to dissect chlamydia--host interactions.The herpes simplex virus receptor nectin-1 is down-regulated after trans-interaction with glycoprotein D.Induction of conformational changes at the N-terminus of herpes simplex virus glycoprotein D upon binding to HVEM and nectin-1 Herpesvirus Entry Mediator and Ocular Herpesvirus Infection: More than Meets the Eye.Herpes simplex virus glycoprotein D relocates nectin-1 from intercellular contacts.Generation of herpesvirus entry mediator (HVEM)-restricted herpes simplex virus type 1 mutant viruses: resistance of HVEM-expressing cells and identification of mutations that rescue nectin-1 recognition Characterization of soluble glycoprotein D-mediated herpes simplex virus type 1 infection.A double mutation in glycoprotein gB compensates for ineffective gD-dependent initiation of herpes simplex virus type 1 infection.Mutations in the cytoplasmic tail of herpes simplex virus 1 gH reduce the fusogenicity of gB in transfected cells.Ectodomain shedding of nectin-1 regulates the maintenance of dendritic spine density.

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Effects of herpes simplex virus on structure and function of nectin-1/HveC.

http://www.wikidata.org/entity/Q34970789

description

2002 nî lūn-bûn

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2002 թուականի Մարտին հրատարակուած գիտական յօդուած

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2002 թվականի մարտին հրատարակված գիտական հոդված

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2002年の論文

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年學術文章

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Effects of herpes simplex virus on structure and function of nectin-1/HveC.

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Effects of herpes simplex virus on structure and function of nectin-1/HveC.

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Effects of herpes simplex virus on structure and function of nectin-1/HveC.

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Effects of herpes simplex virus on structure and function of nectin-1/HveC.

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Effects of herpes simplex virus on structure and function of nectin-1/HveC.

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Effects of herpes simplex virus on structure and function of nectin-1/HveC.

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Effects of herpes simplex virus on structure and function of nectin-1/HveC.

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Effects of herpes simplex virus on structure and function of nectin-1/HveC.

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Effects of herpes simplex virus on structure and function of nectin-1/HveC.

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JVI.76.5.2424-2433.2002

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Journal of Virology

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Effects of herpes simplex virus on structure and function of nectin-1/HveC.

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P2093

Claude Krummenacher

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Gary H Cohen

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Isabelle Baribaud

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James F Sanzo

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P2860

Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein

Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily

A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection by mutants of herpes simplex virus type 1, herpes simplex virus type 2, and pseudorabies virus

Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor

The ectodomain of a novel member of the immunoglobulin subfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex virus types 1 and 2 in human cells

Nectin2alpha (PRR2alpha or HveB) and nectin2delta are low-efficiency mediators for entry of herpes simplex virus mutants carrying the Leu25Pro substitution in glycoprotein D

The V domain of herpesvirus Ig-like receptor (HIgR) contains a major functional region in herpes simplex virus-1 entry into cells and interacts physically with the viral glycoprotein D

Herpes simplex virus glycoprotein D bound to the human receptor HveA

Porcine HveC, a member of the highly conserved HveC/nectin 1 family, is a functional alphaherpesvirus receptor

Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities

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2424-2433

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scholarly article

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10.1128/JVI.76.5.2424-2433.2002

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5

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76

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Roselyn J. Eisenberg

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2002-03-01T00:00:00Z

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11525276

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11836420

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153823

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