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449 related items for PubMed ID: 15882063

  • 1. Induced fit in HIV-neutralizing antibody complexes: evidence for alternative conformations of the gp120 V3 loop and the molecular basis for broad neutralization.
    Rosen O, Chill J, Sharon M, Kessler N, Mester B, Zolla-Pazner S, Anglister J.
    Biochemistry; 2005 May 17; 44(19):7250-8. PubMed ID: 15882063
    [Abstract] [Full Text] [Related]

  • 2. HIV-1 peptide vaccine candidates: selecting constrained V3 peptides with highest affinity to antibody 447-52D.
    Mester B, Manor R, Mor A, Arshava B, Rosen O, Ding FX, Naider F, Anglister J.
    Biochemistry; 2009 Aug 25; 48(33):7867-77. PubMed ID: 19552398
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  • 3. Design of immunogens that present the crown of the HIV-1 V3 loop in a conformation competent to generate 447-52D-like antibodies.
    Chakraborty K, Durani V, Miranda ER, Citron M, Liang X, Schleif W, Joyce JG, Varadarajan R.
    Biochem J; 2006 Nov 01; 399(3):483-91. PubMed ID: 16827663
    [Abstract] [Full Text] [Related]

  • 4. Conformation of the principal neutralizing determinant of human immunodeficiency virus type 1 in complex with an anti-gp120 virus neutralizing antibody studied by two-dimensional nuclear magnetic resonance difference spectroscopy.
    Zvi A, Feigelson DJ, Hayek Y, Anglister J.
    Biochemistry; 1997 Jul 15; 36(28):8619-27. PubMed ID: 9214308
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  • 5. Structural studies of human HIV-1 V3 antibodies.
    Stanfield RL, Wilson IA.
    Hum Antibodies; 2005 Jul 15; 14(3-4):73-80. PubMed ID: 16720977
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  • 9. Solid-state NMR yields structural constraints on the V3 loop from HIV-1 Gp120 bound to the 447-52D antibody Fv fragment.
    Sharpe S, Kessler N, Anglister JA, Yau WM, Tycko R.
    J Am Chem Soc; 2004 Apr 21; 126(15):4979-90. PubMed ID: 15080704
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  • 10. Conformational preferences of a chimeric peptide HIV-1 immunogen from the C4-V3 domains of gp120 envelope protein of HIV-1 CAN0A based on solution NMR: comparison to a related immunogenic peptide from HIV-1 RF.
    Vu HM, de Lorimier R, Moody MA, Haynes BF, Spicer LD.
    Biochemistry; 1996 Apr 23; 35(16):5158-65. PubMed ID: 8611499
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  • 11. Alternative conformations of HIV-1 V3 loops mimic beta hairpins in chemokines, suggesting a mechanism for coreceptor selectivity.
    Sharon M, Kessler N, Levy R, Zolla-Pazner S, Görlach M, Anglister J.
    Structure; 2003 Feb 23; 11(2):225-36. PubMed ID: 12575942
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  • 12. NMR structure of an anti-gp120 antibody complex with a V3 peptide reveals a surface important for co-receptor binding.
    Tugarinov V, Zvi A, Levy R, Hayek Y, Matsushita S, Anglister J.
    Structure; 2000 Apr 15; 8(4):385-95. PubMed ID: 10801487
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  • 13. Expression, purification, and isotope labeling of a gp120 V3 peptide and production of a Fab from a HIV-1 neutralizing antibody for NMR studies.
    Sharon M, Görlach M, Levy R, Hayek Y, Anglister J.
    Protein Expr Purif; 2002 Apr 15; 24(3):374-83. PubMed ID: 11922753
    [Abstract] [Full Text] [Related]

  • 14. Glycosylation affects both the three-dimensional structure and antibody binding properties of the HIV-1IIIB GP120 peptide RP135.
    Huang X, Barchi JJ, Lung FD, Roller PP, Nara PL, Muschik J, Garrity RR.
    Biochemistry; 1997 Sep 09; 36(36):10846-56. PubMed ID: 9312273
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  • 15. The effect of low-profile serine substitutions in the V3 loop of HIV-1 gp120 IIIB/LAI on the immunogenicity of the envelope protein.
    Peet NM, McKeating JA, de Souza JB, Roitt IM, Delves PJ, Lund T.
    Virology; 1998 Nov 10; 251(1):59-70. PubMed ID: 9813203
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  • 16. Permissive residues within the minimal epitopes of neutralizing monoclonal antibodies to the V3 loop of HIV-1.
    Laisney IL, Benjamin H, Gefter M, Strosberg AD.
    Eur J Immunol; 1996 Jul 10; 26(7):1634-40. PubMed ID: 8766572
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  • 17. Mimicking the structure of the V3 epitope bound to HIV-1 neutralizing antibodies.
    Mor A, Segal E, Mester B, Arshava B, Rosen O, Ding FX, Russo J, Dafni A, Schvartzman F, Scherf T, Naider F, Anglister J.
    Biochemistry; 2009 Apr 21; 48(15):3288-303. PubMed ID: 19281264
    [Abstract] [Full Text] [Related]

  • 18. Structure-based design of a constrained peptide mimic of the HIV-1 V3 loop neutralization site.
    Ghiara JB, Ferguson DC, Satterthwait AC, Dyson HJ, Wilson IA.
    J Mol Biol; 1997 Feb 14; 266(1):31-9. PubMed ID: 9054968
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  • 19. Affinity maturation of a high-affinity human monoclonal antibody against the third hypervariable loop of human immunodeficiency virus: use of phage display to improve affinity and broaden strain reactivity.
    Thompson J, Pope T, Tung JS, Chan C, Hollis G, Mark G, Johnson KS.
    J Mol Biol; 1996 Feb 16; 256(1):77-88. PubMed ID: 8609615
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  • 20. Comparative studies on neutralisation of primary HIV-1 isolates by human sera and rabbit anti-V3 peptide sera.
    Lawoko AL, Johansson B, Hjalmarsson S, Christensson B, Ljungberg B, Al-Khalili L, Sjölund M, Pipkorn R, Fenyö EM, Blomberg J.
    J Med Virol; 1999 Oct 16; 59(2):169-79. PubMed ID: 10459152
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