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Journal Abstract Search

223 related items for PubMed ID: 11242518

  • 1. Membrane-perturbing domains of HIV type 1 glycoprotein 41.
    Mobley PW, Pilpa R, Brown C, Waring AJ, Gordon LM.
    AIDS Res Hum Retroviruses; 2001 Mar 01; 17(4):311-27. PubMed ID: 11242518
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  • 3. The amino-terminal peptide of HIV-1 gp41 interacts with human serum albumin.
    Gordon LM, Curtain CC, McCloyn V, Kirkpatrick A, Mobley PW, Waring AJ.
    AIDS Res Hum Retroviruses; 1993 Nov 01; 9(11):1145-56. PubMed ID: 8312056
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  • 6. Inhibition of HIV-1 entry before gp41 folds into its fusion-active conformation.
    Kliger Y, Shai Y.
    J Mol Biol; 2000 Jan 14; 295(2):163-8. PubMed ID: 10623516
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  • 8. The amino-terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: peptide conformation, orientation and aggregation.
    Gordon LM, Curtain CC, Zhong YC, Kirkpatrick A, Mobley PW, Waring AJ.
    Biochim Biophys Acta; 1992 Aug 25; 1139(4):257-74. PubMed ID: 1355364
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  • 10. Design of a peptide inhibitor that blocks the cell fusion mediated by glycoprotein 41 of human immunodeficiency virus type 1.
    Jin BS, Ryu JR, Ahn K, Yu YG.
    AIDS Res Hum Retroviruses; 2000 Nov 20; 16(17):1797-804. PubMed ID: 11118065
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  • 11. Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex.
    Wild C, Dubay JW, Greenwell T, Baird T, Oas TG, McDanal C, Hunter E, Matthews T.
    Proc Natl Acad Sci U S A; 1994 Dec 20; 91(26):12676-80. PubMed ID: 7809100
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  • 12. A synthetic all D-amino acid peptide corresponding to the N-terminal sequence of HIV-1 gp41 recognizes the wild-type fusion peptide in the membrane and inhibits HIV-1 envelope glycoprotein-mediated cell fusion.
    Pritsker M, Jones P, Blumenthal R, Shai Y.
    Proc Natl Acad Sci U S A; 1998 Jun 23; 95(13):7287-92. PubMed ID: 9636141
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  • 13. Structural analysis and assembly of the HIV-1 Gp41 amino-terminal fusion peptide and the pretransmembrane amphipathic-at-interface sequence.
    Lorizate M, de la Arada I, Huarte N, Sánchez-Martínez S, de la Torre BG, Andreu D, Arrondo JL, Nieva JL.
    Biochemistry; 2006 Dec 05; 45(48):14337-46. PubMed ID: 17128972
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  • 14. Fatty acids can substitute the HIV fusion peptide in lipid merging and fusion: an analogy between viral and palmitoylated eukaryotic fusion proteins.
    Lev N, Shai Y.
    J Mol Biol; 2007 Nov 16; 374(1):220-30. PubMed ID: 17919659
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  • 15. Effect of nonpolar substitutions of the conserved Phe11 in the fusion peptide of HIV-1 gp41 on its function, structure, and organization in membranes.
    Pritsker M, Rucker J, Hoffman TL, Doms RW, Shai Y.
    Biochemistry; 1999 Aug 31; 38(35):11359-71. PubMed ID: 10471286
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  • 17. 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
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  • 18. Efficacy of fusion peptide homologs in blocking cell lysis and HIV-induced fusion.
    Silburn KA, McPhee DA, Maerz AL, Poumbourios P, Whittaker RG, Kirkpatrick A, Reilly WG, Manthey MK, Curtain CC.
    AIDS Res Hum Retroviruses; 1998 Mar 20; 14(5):385-92. PubMed ID: 9546797
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  • 19. Conserved Residue Asn-145 in the C-Terminal Heptad Repeat Region of HIV-1 gp41 is Critical for Viral Fusion and Regulates the Antiviral Activity of Fusion Inhibitors.
    Geng X, Liu Z, Yu D, Qin B, Zhu Y, Cui S, Chong H, He Y.
    Viruses; 2019 Jul 03; 11(7):. PubMed ID: 31277353
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