ArticleJournal of virology1990
In vitro synthesis and processing of herpes simplex virus type 2 gG-2, using cell-free transcription and translation systems.
Article in Journal of virology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 12 citations in OpenAlex.
- Identification of the Cleavage Domain within Glycoprotein G of Herpes Simplex Virus Type 2.Viruses · 2020Article
- Herpes simplex virus type 2 glycoprotein G-negative clinical isolates are generated by single frameshift mutations.Journal of virology · 1999Article
- Development of a high-throughput quantitative assay for detecting herpes simplex virus DNA in clinical samples.Journal of clinical microbiology · 1999Article
- Herpesvirus papio 2, an SA8-like alpha-herpesvirus of baboons.Archives of virology · 1995Article
- Orientation of the cleavage site of the herpes simplex virus glycoprotein G-2.Journal of virology · 1993Article
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
Translation of in vitro-synthesized herpes simplex virus type 2 (HSV-2) gG-2 mRNA in a reticulocyte lysate system was used to study the processing of HSV-2 gG-2. In the presence of canine pancreatic microsomal membranes, a single species that is protected from trypsin digestion was detected. This product comigrates with the 104,000-Mr (104K) high mannose intermediate seen in HSV-2-infected-cell lysates. Endo-beta-N-acetylglucosaminidase H treatment of the in vitro-synthesized 104K protein yielded a single product migrating at 100 K. The 72K and 31K cleavage products of gG-2 were not observed in the in vitro system. These data show that the molecular weight of the nonglycosylated form of the gG-2 protein is 100,000 and that the cotranslational processing of this protein in the endoplasmic reticulum yields the 104K high-mannose intermediate.
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Registered trials
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