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Journal Abstract Search

404 related items for PubMed ID: 10467100

  • 1. Autoprocessing of HIV-1 protease is tightly coupled to protein folding.
    Louis JM, Clore GM, Gronenborn AM.
    Nat Struct Biol; 1999 Sep; 6(9):868-75. PubMed ID: 10467100
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  • 2. Influence of flanking sequences on the dimer stability of human immunodeficiency virus type 1 protease.
    Wondrak EM, Louis JM.
    Biochemistry; 1996 Oct 01; 35(39):12957-62. PubMed ID: 8841142
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  • 3. Hydrophilic peptides derived from the transframe region of Gag-Pol inhibit the HIV-1 protease.
    Louis JM, Dyda F, Nashed NT, Kimmel AR, Davies DR.
    Biochemistry; 1998 Feb 24; 37(8):2105-10. PubMed ID: 9485357
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  • 5. Terminal interface conformations modulate dimer stability prior to amino terminal autoprocessing of HIV-1 protease.
    Agniswamy J, Sayer JM, Weber IT, Louis JM.
    Biochemistry; 2012 Feb 07; 51(5):1041-50. PubMed ID: 22242794
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  • 6. Disruption of the HIV-1 protease dimer with interface peptides: structural studies using NMR spectroscopy combined with [2-(13)C]-Trp selective labeling.
    Frutos S, Rodriguez-Mias RA, Madurga S, Collinet B, Reboud-Ravaux M, Ludevid D, Giralt E.
    Biopolymers; 2007 Feb 07; 88(2):164-73. PubMed ID: 17236209
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  • 7. Free energy calculations on dimer stability of the HIV protease using molecular dynamics and a continuum solvent model.
    Wang W, Kollman PA.
    J Mol Biol; 2000 Nov 03; 303(4):567-82. PubMed ID: 11054292
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  • 8. Contribution of the Gag-Pol transframe domain p6* and its coding sequence to morphogenesis and replication of human immunodeficiency virus type 1.
    Paulus C, Ludwig C, Wagner R.
    Virology; 2004 Dec 05; 330(1):271-83. PubMed ID: 15527852
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  • 10. Proteolytic processing of HIV-1 protease precursor, kinetics and mechanism.
    Louis JM, Wondrak EM, Kimmel AR, Wingfield PT, Nashed NT.
    J Biol Chem; 1999 Aug 13; 274(33):23437-42. PubMed ID: 10438521
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  • 12. Molecular analysis of the HIV-1 resistance development: enzymatic activities, crystal structures, and thermodynamics of nelfinavir-resistant HIV protease mutants.
    Kozísek M, Bray J, Rezácová P, Sasková K, Brynda J, Pokorná J, Mammano F, Rulísek L, Konvalinka J.
    J Mol Biol; 2007 Dec 07; 374(4):1005-16. PubMed ID: 17977555
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  • 13. The structural stability of the HIV-1 protease.
    Todd MJ, Semo N, Freire E.
    J Mol Biol; 1998 Oct 23; 283(2):475-88. PubMed ID: 9769219
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  • 14. Systematic mutational analysis of the active-site threonine of HIV-1 proteinase: rethinking the "fireman's grip" hypothesis.
    Strisovsky K, Tessmer U, Langner J, Konvalinka J, Kräusslich HG.
    Protein Sci; 2000 Sep 23; 9(9):1631-41. PubMed ID: 11045610
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  • 15. Illustration of HIV-1 protease folding through a molten-globule-like intermediate using an experimental model that implicates alpha-crystallin and calcium ions.
    Dash C, Sastry M, Rao M.
    Biochemistry; 2005 Mar 15; 44(10):3725-34. PubMed ID: 15751949
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  • 16. Naturally occurring amino acid polymorphisms in human immunodeficiency virus type 1 (HIV-1) Gag p7(NC) and the C-cleavage site impact Gag-Pol processing by HIV-1 protease.
    Goodenow MM, Bloom G, Rose SL, Pomeroy SM, O'Brien PO, Perez EE, Sleasman JW, Dunn BM.
    Virology; 2002 Jan 05; 292(1):137-49. PubMed ID: 11878916
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  • 20. The folding and dimerization of HIV-1 protease: evidence for a stable monomer from simulations.
    Levy Y, Caflisch A, Onuchic JN, Wolynes PG.
    J Mol Biol; 2004 Jun 25; 340(1):67-79. PubMed ID: 15184023
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