ArticleJournal of virology2006
Identification of functional domains in herpes simplex virus 2 glycoprotein B.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Engineering HSV-1 for oncolytic therapy: From molecular entry mechanisms to retargeting strategies.Genes & diseases · 2026Review
- Functional fluorescent protein insertions in herpes simplex virus gB report on gB conformation before and after execution of membrane fusion.PLoS pathogens · 2014Article
- Residues within the C-terminal arm of the herpes simplex virus 1 glycoprotein B ectodomain contribute to its refolding during the fusion step of virus entry.Journal of virology · 2012Article
- Impact of valency of a glycoprotein B-specific monoclonal antibody on neutralization of herpes simplex virus.Journal of virology · 2011Article
- Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infection.Antimicrobial agents and chemotherapy · 2009Article
- Analysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesis.Journal of virology · 2009Article
- Random linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein B.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Mutational evidence of internal fusion loops in herpes simplex virus glycoprotein B.Journal of virology · 2007Article
- Antigenic and mutational analyses of herpes simplex virus glycoprotein B reveal four functional regions.Journal of virology · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Glycoprotein B (gB) is one of four membrane proteins that are essential for the entry of herpes simplex viruses (HSV) into cells, and coexpression of the same combination of proteins in transfected cells results in cell fusion. The latter effect is reminiscent of the ability of virus infection to cause cell fusion, particularly since the degree of fusion is greatly increased by syncytial mutations in gB. Despite intensive efforts with the gB homologs of HSV and some other herpesviruses, information about functionally important regions in the 700-amino-acid ectodomain of this protein is very limited at present. This is largely due to the misfolding of the majority of the mutants examined. It was shown previously that the percentage of correctly folded mutants could be increased by targeting only predicted loop regions (i.e., not alpha-helix or beta-strand), and by using this approach new functional domains in HSV-2 gB have now been identified.
Indexed as
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.