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148 related items for PubMed ID: 11178897

  • 1. A 2.1 A resolution structure of an uncleaved alpha(1)-antitrypsin shows variability of the reactive center and other loops.
    Kim S, Woo J, Seo EJ, Yu M, Ryu S.
    J Mol Biol; 2001 Feb 09; 306(1):109-19. PubMed ID: 11178897
    [Abstract] [Full Text] [Related]

  • 2. Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation.
    Nar H, Bauer M, Stassen JM, Lang D, Gils A, Declerck PJ.
    J Mol Biol; 2000 Mar 31; 297(3):683-95. PubMed ID: 10731421
    [Abstract] [Full Text] [Related]

  • 3. Wild-type alpha 1-antitrypsin is in the canonical inhibitory conformation.
    Elliott PR, Abrahams JP, Lomas DA.
    J Mol Biol; 1998 Jan 23; 275(3):419-25. PubMed ID: 9466920
    [Abstract] [Full Text] [Related]

  • 4. Modeling of serpin-protease complexes: antithrombin-thrombin, alpha 1-antitrypsin (358Met-->Arg)-thrombin, alpha 1-antitrypsin (358Met-->Arg)-trypsin, and antitrypsin-elastase.
    Whisstock J, Lesk AM, Carrell R.
    Proteins; 1996 Nov 23; 26(3):288-303. PubMed ID: 8953650
    [Abstract] [Full Text] [Related]

  • 5. Conformational changes in serpins: I. The native and cleaved conformations of alpha(1)-antitrypsin.
    Whisstock JC, Skinner R, Carrell RW, Lesk AM.
    J Mol Biol; 2000 Jan 21; 295(3):651-65. PubMed ID: 10623554
    [Abstract] [Full Text] [Related]

  • 6. The role of strand 1 of the C beta-sheet in the structure and function of alpha(1)-antitrypsin.
    Bottomley SP, Lawrenson ID, Tew D, Dai W, Whisstock JC, Pike RN.
    Protein Sci; 2001 Dec 21; 10(12):2518-24. PubMed ID: 11714919
    [Abstract] [Full Text] [Related]

  • 7. Conformational changes in serpins: I. The native and cleaved conformations of alpha(1)-antitrypsin.
    Whisstock JC, Skinner R, Carrell RW, Lesk AM.
    J Mol Biol; 2000 Feb 18; 296(2):685-99. PubMed ID: 10669617
    [Abstract] [Full Text] [Related]

  • 8. A 2.6 A structure of a serpin polymer and implications for conformational disease.
    Huntington JA, Pannu NS, Hazes B, Read RJ, Lomas DA, Carrell RW.
    J Mol Biol; 1999 Oct 29; 293(3):449-55. PubMed ID: 10543942
    [Abstract] [Full Text] [Related]

  • 9. Engineering an anion-binding cavity in antichymotrypsin modulates the "spring-loaded" serpin-protease interaction.
    Lukacs CM, Rubin H, Christianson DW.
    Biochemistry; 1998 Mar 10; 37(10):3297-304. PubMed ID: 9521649
    [Abstract] [Full Text] [Related]

  • 10. Probing the local conformational change of alpha1-antitrypsin.
    Baek JH, Im H, Kang UB, Seong KM, Lee C, Kim J, Yu MH.
    Protein Sci; 2007 Sep 10; 16(9):1842-50. PubMed ID: 17660256
    [Abstract] [Full Text] [Related]

  • 11. Structure of a serpin-protease complex shows inhibition by deformation.
    Huntington JA, Read RJ, Carrell RW.
    Nature; 2000 Oct 19; 407(6806):923-6. PubMed ID: 11057674
    [Abstract] [Full Text] [Related]

  • 12. Cleaved antitrypsin polymers at atomic resolution.
    Dunstone MA, Dai W, Whisstock JC, Rossjohn J, Pike RN, Feil SC, Le Bonniec BF, Parker MW, Bottomley SP.
    Protein Sci; 2000 Feb 19; 9(2):417-20. PubMed ID: 10716194
    [Abstract] [Full Text] [Related]

  • 13. The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: crystal structure of an uncleaved alpha1-antitrypsin at 2.7 A.
    Ryu SE, Choi HJ, Kwon KS, Lee KN, Yu MH.
    Structure; 1996 Oct 15; 4(10):1181-92. PubMed ID: 8939743
    [Abstract] [Full Text] [Related]

  • 14. Crystal structure of ovalbumin as a model for the reactive centre of serpins.
    Stein PE, Leslie AG, Finch JT, Turnell WG, McLaughlin PJ, Carrell RW.
    Nature; 1990 Sep 06; 347(6288):99-102. PubMed ID: 2395463
    [Abstract] [Full Text] [Related]

  • 15. Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop.
    Wei A, Rubin H, Cooperman BS, Christianson DW.
    Nat Struct Biol; 1994 Apr 06; 1(4):251-8. PubMed ID: 7656054
    [Abstract] [Full Text] [Related]

  • 16. Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function.
    Loebermann H, Tokuoka R, Deisenhofer J, Huber R.
    J Mol Biol; 1984 Aug 15; 177(3):531-57. PubMed ID: 6332197
    [Abstract] [Full Text] [Related]

  • 17.
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  • 18. Full or partial substitution of the reactive center loop of alpha-1-proteinase inhibitor by that of heparin cofactor II: P1 Arg is required for maximal thrombin inhibition.
    Filion ML, Bhakta V, Nguyen LH, Liaw PS, Sheffield WP.
    Biochemistry; 2004 Nov 23; 43(46):14864-72. PubMed ID: 15544357
    [Abstract] [Full Text] [Related]

  • 19. The structure of truncated recombinant human bile salt-stimulated lipase reveals bile salt-independent conformational flexibility at the active-site loop and provides insights into heparin binding.
    Moore SA, Kingston RL, Loomes KM, Hernell O, Bläckberg L, Baker HM, Baker EN.
    J Mol Biol; 2001 Sep 21; 312(3):511-23. PubMed ID: 11563913
    [Abstract] [Full Text] [Related]

  • 20. Cooperative unfolding of a metastable serpin to a molten globule suggests a link between functional and folding energy landscapes.
    Tsutsui Y, Wintrode PL.
    J Mol Biol; 2007 Aug 03; 371(1):245-55. PubMed ID: 17568610
    [Abstract] [Full Text] [Related]

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