Herpes simplex virus glycoprotein D bound to the human receptor HveA (Q27634177)

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10 November 2019

title

Herpes simplex virus glycoprotein D bound to the human receptor HveA (English)

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host cell surface receptor binding

10 November 2019

main subject

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Gene Ontology release 2020-05-02

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4

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10 November 2019

author name string

A Carfí

1

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10 November 2019

S H Willis

2

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10 November 2019

J C Whitbeck

3

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10 November 2019

G H Cohen

5

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10 November 2019

R J Eisenberg

6

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10 November 2019

D C Wiley

7

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10 November 2019

language of work or name

English

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publication date

1 July 2001

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10 November 2019

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10 November 2019

volume

8

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10 November 2019

page(s)

169-179

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10 November 2019

issue

1

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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

10 November 2019

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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

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Localization of discontinuous epitopes of herpes simplex virus glycoprotein D: use of a nondenaturing ("native" gel) system of polyacrylamide gel electrophoresis coupled with Western blotting

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Glycoprotein D homologs in herpes simplex virus type 1, pseudorabies virus, and bovine herpes virus type 1 bind directly to human HveC(nectin-1) with different affinities.

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Deletions in herpes simplex virus glycoprotein D define nonessential and essential domains

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Anti-glycoprotein D antibodies that permit adsorption but block infection by herpes simplex virus 1 prevent virion-cell fusion at the cell surface

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

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Oligomeric structure of glycoproteins in herpes simplex virus type 1.

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7 January 2021

Glycoprotein C-independent binding of herpes simplex virus to cells requires cell surface heparan sulphate and glycoprotein B.

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7 January 2021

Neutralizing monoclonal antibodies specific for herpes simplex virus glycoprotein D inhibit virus penetration

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7 January 2021

Protein structure comparison by alignment of distance matrices

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Crystal structure of the CD2-binding domain of CD58 (lymphocyte function-associated antigen 3) at 1.8-A resolution

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Crystal structure at 2.8 A resolution of a soluble form of the cell adhesion molecule CD2

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7 January 2021

The first immunoglobulin-like domain of HveC is sufficient to bind herpes simplex virus gD with full affinity, while the third domain is involved in oligomerization of HveC.

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7 January 2021

Localization of a binding site for herpes simplex virus glycoprotein D on herpesvirus entry mediator C by using antireceptor monoclonal antibodies

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Characterization of cell-cell fusion mediated by herpes simplex virus 2 glycoproteins gB, gD, gH and gL in transfected cells

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7 January 2021

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Cell fusion induced by herpes simplex virus glycoproteins gB, gD, and gH-gL requires a gD receptor but not necessarily heparan sulfate

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7 January 2021

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Herpes Simplex Virus Type-1 Glycoprotein D Gene: Nucleotide Sequence and Expression inEscherichia coli

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Localization of the gD-binding region of the human herpes simplex virus receptor, HveA

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7 January 2021

Initial interaction of herpes simplex virus with cells is binding to heparan sulfate

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7 January 2021

10.1016/S1097-2765(01)00298-2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11511370%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

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