ReviewEuropean biophysics journal : EBJ2011
Insights into the mechanism of HIV-1 envelope induced membrane fusion as revealed by its inhibitory peptides.
Review in European biophysics journal : EBJ, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Research strategies of the N-peptide fusion inhibitor: a promising direction for discovering novel antivirals.Journal of virology · 2025Review
- Structural and Mechanistic Evidence for Calcium Interacting Sites in the HIV Transmembrane Protein gp41 Involved in Membrane Fusion.Biochemistry · 2022Article
- Six-helix bundle completion in the distal C-terminal heptad repeat region of gp41 is required for efficient human immunodeficiency virus type 1 infection.Retrovirology · 2018Article
- Customizable de novo design strategies for DOCK: Application to HIVgp41 and other therapeutic targets.Journal of computational chemistry · 2017Article
- Structure-based identification of inhibitors targeting obstruction of the HIVgp41 N-heptad repeat trimer.Bioorganic & medicinal chemistry letters · 2017Article
- Small molecule inhibitors of HIVgp41 N-heptad repeat trimer formation.Bioorganic & medicinal chemistry letters · 2015Article
- Recombinant expression, purification, and biophysical characterization of the transmembrane and membrane proximal domains of HIV-1 gp41.Protein science : a publication of the Protein Society · 2014Article
- The Type VI secretion system spike protein VgrG5 mediates membrane fusion during intercellular spread by pseudomallei group Burkholderia species.Infection and immunity · 2014Article
- Dissociation of the trimeric gp41 ectodomain at the lipid-water interface suggests an active role in HIV-1 Env-mediated membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structure of an HIV-1-neutralizing antibody target, the lipid-bound gp41 envelope membrane proximal region trimer.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Biological and biochemical characterization of HIV-1 Gag/dgp41 virus-like particles expressed in Nicotiana benthamiana.Plant biotechnology journal · 2013Article
- A fusion-inhibiting peptide against Rift Valley fever virus inhibits multiple, diverse viruses.PLoS neglected tropical diseases · 2013Article
- A GxxxG-like motif within HIV-1 fusion peptide is critical to its immunosuppressant activity, structure, and interaction with the transmembrane domain of the T-cell receptor.The Journal of biological chemistry · 2012Article
- Computer-Aided Approaches for Targeting HIVgp41.Biology · 2012Article
- Structural basis of potent and broad HIV-1 fusion inhibitor CP32M.The Journal of biological chemistry · 2012Article
- HIV-1 gp41 transmembrane domain interacts with the fusion peptide: implication in lipid mixing and inhibition of virus-cell fusion.Biochemistry · 2012Article
- Intercellular adhesion molecule 1 promotes HIV-1 attachment but not fusion to target cells.PloS one · 2012Article
- A novel chimeric protein-based HIV-1 fusion inhibitor targeting gp41 glycoprotein with high potency and stability.The Journal of biological chemistry · 2011Article
- Viral envelope protein folding and membrane hemifusion are enhanced by the conserved loop region of HIV-1 gp41.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HIV-1 fusion with its target cells is mediated by the glycoprotein 41 (gp41) transmembrane subunit of the viral envelope glycoprotein (ENV). The current models propose that gp41 undergoes several conformational changes between the apposing viral and cell membranes to facilitate fusion. In this review we focus on the progress that has been made in revealing the dynamic role of the N-terminal heptad repeat (NHR) and the C-terminal heptad repeat (CHR) regions within gp41 to the fusion process. The involvement of these regions in the formation of the gp41 pre-hairpin and hairpin conformations during an ongoing fusion event was mainly discovered by their derived inhibitory peptides. For example, the core structure within the hairpin conformation in a dynamic fusion event is suggested to be larger than its high resolution structure and its minimal boundaries were determined in situ. Also, inhibitory peptides helped reveal the dual contribution of the NHR to the fusion process. Finally, we will also discuss several developments in peptide design that has led to a deeper understanding of the mechanism of viral membrane fusion.
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Registered trials
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