(Q45876288)

17 December 2017

title

Factors influencing the interaction of herpes simplex virus glycoprotein C with the third component of complement (English)

1 reference

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14 September 2022

author name string

H. P. Huemer

1

1 reference

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14 September 2022

C. Larcher

2

1 reference

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14 September 2022

M. P. Dierich

3

1 reference

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14 September 2022

D. Falke

4

1 reference

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14 September 2022

language of work or name

English

1 reference

National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=1333754

14 September 2022

publication date

1 January 1992

1 reference

17 December 2017

published in

Archives of Virology

1 reference

17 December 2017

volume

127

1 reference

17 December 2017

issue

1-4

1 reference

17 December 2017

page(s)

291-303

1 reference

17 December 2017

https://scigraph.springernature.com/pub.10.1007/bf01309591

exact match

0 references

cites work

Pathogenicity of glycoprotein C negative mutants of herpes simplex virus type 1 for the mouse central nervous system

1 reference

12 December 2020

Properdin binds to sulfatide [Gal(3-SO4)beta 1-1 Cer] and has a sequence homology with other proteins that bind sulfated glycoconjugates

1 reference

12 December 2020

Glycoprotein C-dependent attachment of herpes simplex virus to susceptible cells leading to productive infection

1 reference

12 December 2020

Inhibitory effect of heparin on herpes simplex virus

1 reference

12 December 2020

Evidence that neomycin inhibits binding of herpes simplex virus type 1 to the cellular receptor

1 reference

12 December 2020

Pathogenicity in mice of herpes simplex virus type 2 mutants unable to express glycoprotein C

1 reference

12 December 2020

Herpes simplex virus glycoproteins gC-1 and gC-2 bind to the third component of complement and provide protection against complement-mediated neutralization of viral infectivity

1 reference

12 December 2020

Complement component C3b binds directly to purified glycoprotein C of herpes simplex virus types 1 and 2.

1 reference

12 December 2020

Comparison of heparin-sensitive attachment of pseudorabies virus (PRV) and herpes simplex virus type 1 and identification of heparin-binding PRV glycoproteins

1 reference

12 December 2020

The interaction of small oligomers of complement 3B (C3B) with phagocytes. High affinity binding and phorbol ester-induced internalization by polymorphonuclear leukocytes

1 reference

12 December 2020

Localization on the herpes simplex virus type 1 genome of a region encoding proteins involved in adsorption to the cellular receptor

1 reference

12 December 2020

Glycoprotein C of herpes simplex virus 1 is an inhibitor of the complement cascade

1 reference

12 December 2020

Colonization of adrenal glands and ovaries of mice by HSV-2 variants. I. Virological studies

1 reference

12 December 2020

Identification of C3b-binding regions on herpes simplex virus type 2 glycoprotein C

1 reference

12 December 2020

Modulation of the formation of the amplification convertase of complement, C3b, Bb, by native and commercial heparin

1 reference

12 December 2020

Serological analysis of herpes simplex virus types 1 and 2 with monoclonal antibodies.

1 reference

12 December 2020

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

1 reference

12 December 2020

Herpes simplex virus type 1 glycoprotein C-negative mutants exhibit multiple phenotypes, including secretion of truncated glycoproteins

1 reference

12 December 2020

Recombinants between herpes simplex virus types 1 and 2: analyses of genome structures and expression of immediate early polypeptides

1 reference

12 December 2020

The leukocyte cell surface receptor(s) for the iC3b product of complement

1 reference

12 December 2020

Involvement of glycoprotein C (gC) in adsorption of herpes simplex virus type 1 (HSV-1) to the cell

1 reference

12 December 2020

Interaction of complement-solubilized immune complexes (IC) with CR1 receptors on human erythrocytes. Polysulfated compounds inhibit IC binding and induce IC-release from CR1

1 reference

12 December 2020

Genetic studies with herpes simplex virus type 1. The isolation of temperature-sensitive mutants, their arrangement into complementation groups and recombination analysis leading to a linkage map.

1 reference

12 December 2020

Glycoprotein C of herpes simplex virus type 1 prevents complement-mediated cell lysis and virus neutralization

1 reference

12 December 2020

Temperature-sensitive mutants of herpes simplex virus type 2.

1 reference

12 December 2020

Binding of complement component C3b to glycoprotein gC of herpes simplex virus type 1: mapping of gC-binding sites and demonstration of conserved C3b binding in low-passage clinical isolates

1 reference

12 December 2020

Protection of Mice by an Apathogenic Strain of HSV-1 Against Lethal Infection by a Pathogenic Strain of HSV-1

1 reference

12 December 2020

Glycoprotein C of herpes simplex virus 1 acts as a receptor for the C3b complement component on infected cells

1 reference

12 December 2020

1 reference

12 December 2020

Difference in the clustering of complement receptor type 1 (CR1) on polymorphonuclear leukocytes and erythrocytes: effect on immune adherence

1 reference

12 December 2020

Characterization of the human complement (c3b) receptor with a fluid phase C3b dimer

1 reference

12 December 2020

The difference in sensitivity to cicloxolone sodium between herpes simplex virus types 1 and 2 maps to the locations of genes UL22 (gH) and UL44 (gC)

1 reference

12 December 2020

Binding of complement component C3b to glycoprotein C is modulated by sialic acid on herpes simplex virus type 1-infected cells.

1 reference

12 December 2020

Replication of HSV-1 in murine peritoneal macrophages: Comparison of various virus strains with different properties

1 reference

12 December 2020

Large scale isolation of functionally active components of the human complement system

1 reference

12 December 2020

Cross-linking studies show that herpes simplex virus type 1 glycoprotein C molecules are clustered in the membrane of infected cells

1 reference

12 December 2020

Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivity

1 reference

12 December 2020

Physical mapping of herpes simplex virus-induced polypeptides

1 reference

12 December 2020

The central segment of herpes simplex virus type 1 glycoprotein C (gC) is not involved in C3b binding: demonstration by using monoclonal antibodies and recombinant gC expressed in Escherichia coli

1 reference

12 December 2020

Identifiers

DOI

10.1007/BF01309591

1 reference

17 December 2017

Dimensions Publication ID

1021024868

0 references

1 reference

17 December 2017