Crystal structure of the conserved herpesvirus fusion regulator complex gH–gL (Q27663096)

4

object named as

Gary H Cohen

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author name string

Tirumala K Chowdary

1

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Tina M Cairns

2

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Doina Atanasiu

3

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Ekaterina E Heldwein

Nature Structural & Molecular Biology

6

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publication date

July 2010

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published in

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volume

17

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issue

7

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page(s)

882-8

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cites work

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Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion

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Characterization of the human cytomegalovirus gH/gL/UL128-131 complex that mediates entry into epithelial and endothelial cells.

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Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane

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Evidence for a role of the membrane-proximal region of herpes simplex virus type 1 glycoprotein H in membrane fusion and virus inhibition

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N-terminal mutants of herpes simplex virus type 2 gH are transported without gL but require gL for function

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Crystal structure of glycoprotein B from herpes simplex virus 1.

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Heptad repeat 2 in herpes simplex virus 1 gH interacts with heptad repeat 1 and is critical for virus entry and fusion

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A heptad repeat in herpes simplex virus 1 gH, located downstream of the alpha-helix with attributes of a fusion peptide, is critical for virus entry and fusion

29 September 2017

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The ectodomain of herpes simplex virus glycoprotein H contains a membrane alpha-helix with attributes of an internal fusion peptide, positionally conserved in the herpesviridae family

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Host range of human T-cell leukemia virus type I analyzed by a cell fusion-dependent reporter gene activation assay

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Structural and antigenic analysis of a truncated form of the herpes simplex virus glycoprotein gH-gL complex.

29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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Three-dimensional structure of herpes simplex virus from cryo-electron tomography

2 June 2018

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

2 June 2018

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The properties and sequence of glycoprotein H of herpes simplex virus type 1.

2 June 2018

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Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B.

27 November 2018

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Herpes simplex virus type 1 glycoprotein L mutants that fail to promote trafficking of glycoprotein H and fail to function in fusion can induce binding of glycoprotein L-dependent anti-glycoprotein H antibodies

27 November 2018

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27 November 2018

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27 November 2018

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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

27 November 2018

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Characterisation and physical mapping of an HSV-1 glycoprotein of approximately 115 X 10(3) molecular weight

27 November 2018

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27 November 2018

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Processing of X-ray diffraction data collected in oscillation mode

31 March 2020

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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.

31 March 2020

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Identifiers

DOI

10.1038/NSMB.1837

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Dimensions Publication ID

2294982

1036632395

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Fatcat ID

release_wbrdsahvvjd6lktv5rgid27ryy

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Fatcat

https://api.fatcat.wiki/v0/release/wbrdsahvvjd6lktv5rgid27ryy

mapped directly with Wikidata item

24 November 2022

based on heuristic

2294982

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1 reference

1 reference