ArticleJournal of virology1997
The role of eukaryotic subtilisin-like endoproteases for the activation of human immunodeficiency virus glycoproteins in natural host cells.
Article in Journal of virology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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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.
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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
36 citing papers in PubMed, 79 citations in OpenAlex.
- Design, Synthesis, and Characterization of Dichlorobiphenyl-Derived Inhibitors of the Proprotein Convertase Furin.Journal of medicinal chemistry · 2025Article
- Beyond Processing: Furin as a Central Hub in Viral Pathogenesis and Genetic Susceptibility.Biomolecules · 2025Review
- Article
- The Emergence of the Spike Furin Cleavage Site in SARS-CoV-2.Molecular biology and evolution · 2022Review
- The Proteolytic Regulation of Virus Cell Entry by Furin and Other Proprotein Convertases.Viruses · 2019Review
- PC7 and the related proteases Furin and Pace4 regulate E-cadherin function during blastocyst formation.The Journal of cell biology · 2015Article
- Article
- A novel minigene scaffold for therapeutic cancer vaccines.Oncoimmunology · 2014Article
- The tale of the long tail: the cytoplasmic domain of HIV-1 gp41.Journal of virology · 2013Review
- Initiation of duck hepatitis B virus infection requires cleavage by a furin-like protease.Journal of virology · 2010Article
- Proteolytic activation of the spike protein at a novel RRRR/S motif is implicated in furin-dependent entry, syncytium formation, and infectivity of coronavirus infectious bronchitis virus in cultured cells.Journal of virology · 2009Article
- Cell-surface processing of extracellular human immunodeficiency virus type 1 Vpr by proprotein convertases.Virology · 2008Article
- Efficient trapping of HIV-1 envelope protein by hetero-oligomerization with an N-helix chimera.Retrovirology · 2005Article
- Alterations of pr-M cleavage and virus export in pr-M junction chimeric dengue viruses.Journal of virology · 2004Article
- Glycine decarboxylase mediates a postbinding step in duck hepatitis B virus infection.Journal of virology · 2004Article
- Conditional expression of alpha1-antitrypsin delivered by recombinant SV40 vectors protects lymphocytes against HIV.Gene therapy · 2003Article
- Cleavage of the ADAMTS13 propeptide is not required for protease activity.The Journal of biological chemistry · 2003Article
- Crimean-Congo hemorrhagic fever virus glycoprotein proteolytic processing by subtilase SKI-1.Journal of virology · 2003Article
- HIV-1 proprotein processing as a target for gene therapy.Gene therapy · 2003Article
- The virulence of mouse hepatitis virus strain A59 is not dependent on efficient spike protein cleavage and cell-to-cell fusion.Journal of neurovirology · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteolytic activation of the precursor envelope glycoproteins gp160 of human immunodeficiency virus type 1 (HIV-1) and gp140 of HIV-2, a prerequisite for viral infection, results in the formation of gp120/gp41 and gp125/gp36, respectively. Cleavage is mediated by cellular proteases. Furin, a member of the eukaryotic subtilisin family, has been shown to be an activating protease for HIV. Here, we compared the presence of furin and other mammalian subtilisins in lymphatic cells and tissues. Northern blot analyses revealed that furin and the recently discovered protease LPC/PC7 were the only subtilisin-like enzymes transcribed in such cells. Furin was identified as an enzymatically active endoprotease present in different lymphocytic, as well as monocytic, cell lines. When expressed from vaccinia virus vectors, the proprotein convertases were correctly processed, transported, and secreted into the media and enzymatically active. Coexpression of different subtilisins with the HIV envelope precursors revealed that furin and LPC/PC7 are able to cleave HIV-1 gp160. Moreover, both enzymes proteolytically processed the envelope precursor of HIV-2. gp140 was also cleaved to some extent by PC1, which is not, however, present in lymphatic cells. Furin- and LPC/PC7-catalyzed cleavage of HIV-1 gp160 resulted in biologically active envelope protein. In conclusion, among the known members of the subtilisin family, only furin and LPC/PC7 fulfill the requirements of a protease responsible for in vivo activation of HIV envelope glycoproteins.
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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.