Capturing the Herpes Simplex Virus Core Fusion Complex (gB-gH/gL) in an Acidic Environment
Author:
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
Reference59 articles.
1. Cascade of events governing cell-cell fusion induced by herpes simplex virus glycoproteins gD, gH/gL, and gB;Atanasiu;J. Virol.,2010
2. Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion;Atanasiu;Proc. Natl. Acad. Sci. U. S. A.,2007
3. Bimolecular complementation defines functional regions of herpes simplex virus gB that are involved with gH/gL as a necessary step leading to cell fusion;Atanasiu;J. Virol.,2010
4. Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein;Avitabile;J. Virol.,2007
5. Cross talk among the glycoproteins involved in herpes simplex virus entry and fusion: the interaction between gB and gH/gL does not necessarily require gD;Avitabile;J. Virol.,2009
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2. Growth defect of domain III glycoprotein B mutants of human cytomegalovirus reverted by compensatory mutations co-localizing in post-fusion conformation;2023-03-30
3. Multiple Sites on Glycoprotein H (gH) Functionally Interact with the gB Fusion Protein to Promote Fusion during Herpes Simplex Virus (HSV) Entry;mBio;2023-02-28
4. Multiple sites on glycoprotein H (gH) functionally interact with the gB fusion protein to promote fusion during herpes simplex virus (HSV) entry;2022-12-08
5. Conformational Changes in Herpes Simplex Virus Glycoprotein C;Journal of Virology;2022-08-24
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