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Journal Abstract Search


280 related items for PubMed ID: 31409642

  • 1. Fully hydrophobic HIV gp41 adopts a hemifusion-like conformation in phospholipid bilayers.
    Lee M, Morgan CA, Hong M.
    J Biol Chem; 2019 Oct 04; 294(40):14732-14744. PubMed ID: 31409642
    [Abstract] [Full Text] [Related]

  • 2. Oligomeric Structure and Three-Dimensional Fold of the HIV gp41 Membrane-Proximal External Region and Transmembrane Domain in Phospholipid Bilayers.
    Kwon B, Lee M, Waring AJ, Hong M.
    J Am Chem Soc; 2018 Jul 05; 140(26):8246-8259. PubMed ID: 29888593
    [Abstract] [Full Text] [Related]

  • 3. Cholesterol-Mediated Clustering of the HIV Fusion Protein gp41 in Lipid Bilayers.
    Tran N, Oh Y, Sutherland M, Cui Q, Hong M.
    J Mol Biol; 2022 Jan 30; 434(2):167345. PubMed ID: 34762895
    [Abstract] [Full Text] [Related]

  • 4. Cholesterol Interaction with the Trimeric HIV Fusion Protein gp41 in Lipid Bilayers Investigated by Solid-State NMR Spectroscopy and Molecular Dynamics Simulations.
    Kwon B, Mandal T, Elkins MR, Oh Y, Cui Q, Hong M.
    J Mol Biol; 2020 Jul 24; 432(16):4705-4721. PubMed ID: 32592698
    [Abstract] [Full Text] [Related]

  • 5. Topological analysis of the gp41 MPER on lipid bilayers relevant to the metastable HIV-1 envelope prefusion state.
    Wang Y, Kaur P, Sun ZJ, Elbahnasawy MA, Hayati Z, Qiao ZS, Bui NN, Chile C, Nasr ML, Wagner G, Wang JH, Song L, Reinherz EL, Kim M.
    Proc Natl Acad Sci U S A; 2019 Nov 05; 116(45):22556-22566. PubMed ID: 31624123
    [Abstract] [Full Text] [Related]

  • 6. Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions.
    Buzon V, Natrajan G, Schibli D, Campelo F, Kozlov MM, Weissenhorn W.
    PLoS Pathog; 2010 May 06; 6(5):e1000880. PubMed ID: 20463810
    [Abstract] [Full Text] [Related]

  • 7. Solid-state nuclear magnetic resonance measurements of HIV fusion peptide 13CO to lipid 31P proximities support similar partially inserted membrane locations of the α helical and β sheet peptide structures.
    Gabrys CM, Qiang W, Sun Y, Xie L, Schmick SD, Weliky DP.
    J Phys Chem A; 2013 Oct 03; 117(39):9848-59. PubMed ID: 23418890
    [Abstract] [Full Text] [Related]

  • 8. Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers Containing the Fusion Peptide and Transmembrane Domains.
    Liang S, Ratnayake PU, Keinath C, Jia L, Wolfe R, Ranaweera A, Weliky DP.
    Biochemistry; 2018 Feb 20; 57(7):1219-1235. PubMed ID: 29345922
    [Abstract] [Full Text] [Related]

  • 9. Insights into the Conformation of the Membrane Proximal Regions Critical to the Trimerization of the HIV-1 gp41 Ectodomain Bound to Dodecyl Phosphocholine Micelles.
    Louis JM, Baber JL, Ghirlando R, Aniana A, Bax A, Roche J.
    PLoS One; 2016 Feb 20; 11(8):e0160597. PubMed ID: 27513582
    [Abstract] [Full Text] [Related]

  • 10. Folded monomers and hexamers of the ectodomain of the HIV gp41 membrane fusion protein: potential roles in fusion and synergy between the fusion peptide, hairpin, and membrane-proximal external region.
    Banerjee K, Weliky DP.
    Biochemistry; 2014 Nov 25; 53(46):7184-98. PubMed ID: 25372604
    [Abstract] [Full Text] [Related]

  • 11. A large HIV gp41 construct with trimer-of-hairpins structure exhibits V2E mutation-dominant attenuation of vesicle fusion and helicity very similar to V2E attenuation of HIV fusion and infection and supports: (1) hairpin stabilization of membrane apposition with larger distance for V2E; and (2) V2E dominance by an antiparallel β sheet with interleaved fusion peptide strands from two gp41 trimers.
    Rokonujjaman M, Sahyouni A, Wolfe R, Jia L, Ghosh U, Weliky DP.
    Biophys Chem; 2023 Feb 25; 293():106933. PubMed ID: 36508984
    [Abstract] [Full Text] [Related]

  • 12. Viral fusion protein transmembrane domain adopts β-strand structure to facilitate membrane topological changes for virus-cell fusion.
    Yao H, Lee MW, Waring AJ, Wong GC, Hong M.
    Proc Natl Acad Sci U S A; 2015 Sep 01; 112(35):10926-31. PubMed ID: 26283363
    [Abstract] [Full Text] [Related]

  • 13. The Atomic Structure of the HIV-1 gp41 Transmembrane Domain and Its Connection to the Immunogenic Membrane-proximal External Region.
    Apellániz B, Rujas E, Serrano S, Morante K, Tsumoto K, Caaveiro JM, Jiménez MÁ, Nieva JL.
    J Biol Chem; 2015 May 22; 290(21):12999-3015. PubMed ID: 25787074
    [Abstract] [Full Text] [Related]

  • 14. Conformation and Trimer Association of the Transmembrane Domain of the Parainfluenza Virus Fusion Protein in Lipid Bilayers from Solid-State NMR: Insights into the Sequence Determinants of Trimer Structure and Fusion Activity.
    Lee M, Yao H, Kwon B, Waring AJ, Ruchala P, Singh C, Hong M.
    J Mol Biol; 2018 Mar 02; 430(5):695-709. PubMed ID: 29330069
    [Abstract] [Full Text] [Related]

  • 15. 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.
    Sackett K, Nethercott MJ, Zheng Z, Weliky DP.
    J Mol Biol; 2014 Mar 06; 426(5):1077-94. PubMed ID: 24246500
    [Abstract] [Full Text] [Related]

  • 16. Conformational partitioning of the fusion peptide of HIV-1 gp41 and its structural analogs in bilayer membranes.
    Maddox MW, Longo ML.
    Biophys J; 2002 Dec 06; 83(6):3088-96. PubMed ID: 12496080
    [Abstract] [Full Text] [Related]

  • 17. Distinct functions for the membrane-proximal ectodomain region (MPER) of HIV-1 gp41 in cell-free and cell-cell viral transmission and cell-cell fusion.
    Narasimhulu VGS, Bellamy-McIntyre AK, Laumaea AE, Lay CS, Harrison DN, King HAD, Drummer HE, Poumbourios P.
    J Biol Chem; 2018 Apr 20; 293(16):6099-6120. PubMed ID: 29496992
    [Abstract] [Full Text] [Related]

  • 18. Conditional trimerization and lytic activity of HIV-1 gp41 variants containing the membrane-associated segments.
    Dai Z, Tao Y, Liu N, Brenowitz MD, Girvin ME, Lai JR.
    Biochemistry; 2015 Mar 03; 54(8):1589-99. PubMed ID: 25658332
    [Abstract] [Full Text] [Related]

  • 19. Fusion-competent state induced by a C-terminal HIV-1 fusion peptide in cholesterol-rich membranes.
    Apellániz B, Nieva JL.
    Biochim Biophys Acta; 2015 Apr 03; 1848(4):1014-22. PubMed ID: 25617671
    [Abstract] [Full Text] [Related]

  • 20. Exposure of the HIV-1 broadly neutralizing antibody 10E8 MPER epitope on the membrane surface by gp41 transmembrane domain scaffolds.
    Oakes V, Torralba J, Rujas E, Nieva JL, Domene C, Apellaniz B.
    Biochim Biophys Acta Biomembr; 2018 Jun 03; 1860(6):1259-1271. PubMed ID: 29477358
    [Abstract] [Full Text] [Related]


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