ArticleBiochemistry2009
Hairpin folding of HIV gp41 abrogates lipid mixing function at physiologic pH and inhibits lipid mixing by exposed gp41 constructs.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 25 citations in OpenAlex.
- Article
- Biophysical studies of HIV-1 glycoprotein-41 interactions with peptides and small molecules - Effect of lipids and detergents.Biochimica et biophysica acta. General subjects · 2020Article
- HIV-1 gp41 transmembrane oligomerization monitored by FRET and FCS.FEBS letters · 2018Article
- Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers Containing the Fusion Peptide and Transmembrane Domains.Biochemistry · 2018Article
- Swapped-domain constructs of the glycoprotein-41 ectodomain are potent inhibitors of HIV infection.ACS chemical biology · 2015Article
- Magic angle spinning NMR of viruses.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid binding.Journal of biomolecular NMR · 2015Article
- REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Design and characterization of swapped-domain constructs of HIV-1 glycoprotein-41 as receptors for drug discovery.Protein engineering, design & selection : PEDS · 2015Article
- Conditional trimerization and lytic activity of HIV-1 gp41 variants containing the membrane-associated segments.Biochemistry · 2015Article
- pH-dependent vesicle fusion induced by the ectodomain of the human immunodeficiency virus membrane fusion protein gp41: Two kinetically distinct processes and fully-membrane-associated gp41 with predominant β sheet fusion peptide conformation.Biochimica et biophysica acta · 2015Article
- Article
- The three lives of viral fusion peptides.Chemistry and physics of lipids · 2014Review
- Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle state.Journal of molecular biology · 2014Article
- Quantitation of recombinant protein in whole cells and cell extracts via solid-state NMR spectroscopy.Biochemistry · 2013Article
- Biochemistry and biophysics of HIV-1 gp41 - membrane interactions and implications for HIV-1 envelope protein mediated viral-cell fusion and fusion inhibitor design.Current topics in medicinal chemistry · 2011Review
- Article
- HIV gp41 six-helix bundle constructs induce rapid vesicle fusion at pH 3.5 and little fusion at pH 7.0: understanding pH dependence of protein aggregation, membrane binding, and electrostatics, and implications for HIV-host cell fusion.European biophysics journal : EBJ · 2011Article
- Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.European biophysics journal : EBJ · 2011Article
- Comparative analysis of membrane-associated fusion peptide secondary structure and lipid mixing function of HIV gp41 constructs that model the early pre-hairpin intermediate and final hairpin conformations.Journal of molecular biology · 2010Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Conformational changes in the HIV gp41 protein are directly correlated with fusion between the HIV and target cell plasma membranes, which is the initial step of infection. Key gp41 fusion conformations include an early extended conformation termed prehairpin which contains exposed regions and a final low-energy conformation termed hairpin which has a compact six-helix bundle structure. Current fusion models debate the roles of hairpin and prehairpin conformations in the process of membrane merger. In the present work, gp41 constructs have been engineered which correspond to fusion relevant parts of both prehairpin and hairpin conformations and have been analyzed for their ability to induce lipid mixing between membrane vesicles. The data correlate membrane fusion function with the prehairpin conformation and suggest that one of the roles of the final hairpin conformation is sequestration of membrane-perturbing gp41 regions with consequent loss of the membrane disruption induced earlier by the prehairpin structure. To our knowledge, this is the first biophysical study to delineate the membrane fusion potential of gp41 constructs modeling key fusion conformations.
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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.