ArticleBiochemistry2008
Photoinduced reactivity of the HIV-1 envelope glycoprotein with a membrane-embedded probe reveals insertion of portions of the HIV-1 Gp41 cytoplasmic tail into the viral membrane.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 34 citations in OpenAlex.
- HIV-1 envelope facilitates the development of protease inhibitor resistance through acquiring mutations associated with viral entry and immune escape.Frontiers in microbiology · 2024Article
- Cholesterol in the Viral Membrane is a Molecular Switch Governing HIV-1 Env Clustering.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- Review
- The lipid membrane of HIV-1 stabilizes the viral envelope glycoproteins and modulates their sensitivity to antibody neutralization.The Journal of biological chemistry · 2020Article
- Biochemical evidence of a role for matrix trimerization in HIV-1 envelope glycoprotein incorporation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The cytoplasmic tail of retroviral envelope glycoproteins.Progress in molecular biology and translational science · 2015Review
- The role of matrix in HIV-1 envelope glycoprotein incorporation.Trends in microbiology · 2014Review
- Understanding the process of envelope glycoprotein incorporation into virions in simian and feline immunodeficiency viruses.Viruses · 2014Review
- Second generation inactivated eastern equine encephalitis virus vaccine candidates protect mice against a lethal aerosol challenge.PloS one · 2014Article
- The frantic play of the concealed HIV envelope cytoplasmic tail.Retrovirology · 2013Review
- C-terminal tail of human immunodeficiency virus gp41: functionally rich and structurally enigmatic.The Journal of general virology · 2013Review
- The tale of the long tail: the cytoplasmic domain of HIV-1 gp41.Journal of virology · 2013Review
- Article
- HIV entry and envelope glycoprotein-mediated fusion.The Journal of biological chemistry · 2012Review
- Targeting HIV-1 gp41-induced fusion and pathogenesis for anti-viral therapy.Current topics in medicinal chemistry · 2011Review
- Highly conserved structural properties of the C-terminal tail of HIV-1 gp41 protein despite substantial sequence variation among diverse clades: implications for functions in viral replication.The Journal of biological chemistry · 2011Article
- Topology of the C-terminal tail of HIV-1 gp41: differential exposure of the Kennedy epitope on cell and viral membranes.PloS one · 2010Article
- Membrane topology analysis of HIV-1 envelope glycoprotein gp41.Retrovirology · 2010Article
- In-solution virus capture assay helps deconstruct heterogeneous antibody recognition of human immunodeficiency virus type 1.Journal of virology · 2010Article
- The cytoplasmic domain of human immunodeficiency virus type 1 transmembrane protein gp41 harbors lipid raft association determinants.Journal of virology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The interactions of HIV-1 Env (gp120-gp41) with CD4 and coreceptors trigger a barrage of conformational changes in Env that drive the membrane fusion process. Various regions of gp41 have profound effects on HIV entry and budding. However, the precise interactions between gp41 and the membrane have not been elucidated. To examine portions of membrane proteins that are embedded in membrane lipids, we have studied photoinduced chemical reactions in membranes using the lipid bilayer specific probe iodonaphthyl azide (INA). Here we show that in addition to the transmembrane anchor, amphipatic sequences in the cytoplasmic tail (CT) of HIV-1 gp41 are labeled by INA. INA labeling of the HIV-1 gp41 CT was similar whether wild-type or a mutant HIV-1 was used with uncleaved p55 Gag, which does not allow entry. These results shed light on the disposition of the HIV-1 gp41 CT with respect to the membrane. Moreover, our data have general implications for topology of membrane proteins and their in situ interactions with the lipid bilayer.
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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.