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224 related items for PubMed ID: 1606144

  • 1. Crystallographic analysis of transition-state mimics bound to penicillopepsin: phosphorus-containing peptide analogues.
    Fraser ME, Strynadka NC, Bartlett PA, Hanson JE, James MN.
    Biochemistry; 1992 Jun 09; 31(22):5201-14. PubMed ID: 1606144
    [Abstract] [Full Text] [Related]

  • 2. Crystallographic analysis of transition state mimics bound to penicillopepsin: difluorostatine- and difluorostatone-containing peptides.
    James MN, Sielecki AR, Hayakawa K, Gelb MH.
    Biochemistry; 1992 Apr 21; 31(15):3872-86. PubMed ID: 1567842
    [Abstract] [Full Text] [Related]

  • 3. Structural study of the complex between human pepsin and a phosphorus-containing peptidic -transition-state analog.
    Fujinaga M, Cherney MM, Tarasova NI, Bartlett PA, Hanson JE, James MN.
    Acta Crystallogr D Biol Crystallogr; 2000 Mar 21; 56(Pt 3):272-9. PubMed ID: 10713513
    [Abstract] [Full Text] [Related]

  • 4. Inhibition of human immunodeficiency virus-1 protease by a C2-symmetric phosphinate. Synthesis and crystallographic analysis.
    Abdel-Meguid SS, Zhao B, Murthy KH, Winborne E, Choi JK, DesJarlais RL, Minnich MD, Culp JS, Debouck C, Tomaszek TA.
    Biochemistry; 1993 Aug 10; 32(31):7972-80. PubMed ID: 8347601
    [Abstract] [Full Text] [Related]

  • 5. Conformational flexibility in the active sites of aspartyl proteinases revealed by a pepstatin fragment binding to penicillopepsin.
    James MN, Sielecki A, Salituro F, Rich DH, Hofmann T.
    Proc Natl Acad Sci U S A; 1982 Oct 10; 79(20):6137-41. PubMed ID: 6755464
    [Abstract] [Full Text] [Related]

  • 6. Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues.
    Holden HM, Tronrud DE, Monzingo AF, Weaver LH, Matthews BW.
    Biochemistry; 1987 Dec 29; 26(26):8542-53. PubMed ID: 3442675
    [Abstract] [Full Text] [Related]

  • 7. Comparison of the structures of three carboxypeptidase A-phosphonate complexes determined by X-ray crystallography.
    Kim H, Lipscomb WN.
    Biochemistry; 1991 Aug 20; 30(33):8171-80. PubMed ID: 1868092
    [Abstract] [Full Text] [Related]

  • 8. Crystal structure of the complex of carboxypeptidase A with a strongly bound phosphonate in a new crystalline form: comparison with structures of other complexes.
    Kim H, Lipscomb WN.
    Biochemistry; 1990 Jun 12; 29(23):5546-55. PubMed ID: 2386784
    [Abstract] [Full Text] [Related]

  • 9. Crystal structures of alpha-lytic protease complexes with irreversibly bound phosphonate esters.
    Bone R, Sampson NS, Bartlett PA, Agard DA.
    Biochemistry; 1991 Feb 26; 30(8):2263-72. PubMed ID: 1998685
    [Abstract] [Full Text] [Related]

  • 10. Possible role for water dissociation in the slow binding of phosphorus-containing transition-state-analogue inhibitors of thermolysin.
    Bartlett PA, Marlowe CK.
    Biochemistry; 1987 Dec 29; 26(26):8553-61. PubMed ID: 3442676
    [Abstract] [Full Text] [Related]

  • 11. Phosphonate analogues of carboxypeptidase A substrates are potent transition-state analogue inhibitors.
    Hanson JE, Kaplan AP, Bartlett PA.
    Biochemistry; 1989 Jul 25; 28(15):6294-305. PubMed ID: 2790000
    [Abstract] [Full Text] [Related]

  • 12. X-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin.
    Bailey D, Cooper JB, Veerapandian B, Blundell TL, Atrash B, Jones DM, Szelke M.
    Biochem J; 1993 Jan 15; 289 ( Pt 2)(Pt 2):363-71. PubMed ID: 8424781
    [Abstract] [Full Text] [Related]

  • 13. X-ray analyses of aspartic proteinases. III Three-dimensional structure of endothiapepsin complexed with a transition-state isostere inhibitor of renin at 1.6 A resolution.
    Veerapandian B, Cooper JB, Sali A, Blundell TL.
    J Mol Biol; 1990 Dec 20; 216(4):1017-29. PubMed ID: 2266553
    [Abstract] [Full Text] [Related]

  • 14. Effect of pH on the activities of penicillopepsin and Rhizopus pepsin and a proposal for the productive substrate binding mode in penicillopepsin.
    Hofmann T, Hodges RS, James MN.
    Biochemistry; 1984 Feb 14; 23(4):635-43. PubMed ID: 6424704
    [Abstract] [Full Text] [Related]

  • 15. Inhibition of thermolysin by phosphonamidate transition-state analogues: measurement of 31P-15N bond lengths and chemical shifts in two enzyme-inhibitor complexes by solid-state nuclear magnetic resonance.
    Copié V, Kolbert AC, Drewry DH, Bartlett PA, Oas TG, Griffin RG.
    Biochemistry; 1990 Oct 02; 29(39):9176-84. PubMed ID: 2271586
    [Abstract] [Full Text] [Related]

  • 16. Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin.
    Tronrud DE, Monzingo AF, Matthews BW.
    Eur J Biochem; 1986 Jun 02; 157(2):261-8. PubMed ID: 3709536
    [Abstract] [Full Text] [Related]

  • 17. Penicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to k(cat).
    Cao QN, Stubbs M, Ngo KQ, Ward M, Cunningham A, Pai EF, Tu GC, Hofmann T.
    Protein Sci; 2000 May 02; 9(5):991-1001. PubMed ID: 10850809
    [Abstract] [Full Text] [Related]

  • 18. Synthesis of the novel pi-(benzyloxymethyl)-protected histidine analogue of statine. Inhibition of penicillopepsin by pepstatin-derived peptides containing different statine side-chain derivatives.
    Maibaum J, Rich DH.
    J Med Chem; 1989 Jul 02; 32(7):1571-6. PubMed ID: 2661819
    [Abstract] [Full Text] [Related]

  • 19. Direct observation by X-ray analysis of the tetrahedral "intermediate" of aspartic proteinases.
    Veerapandian B, Cooper JB, Sali A, Blundell TL, Rosati RL, Dominy BW, Damon DB, Hoover DJ.
    Protein Sci; 1992 Mar 02; 1(3):322-8. PubMed ID: 1304340
    [Abstract] [Full Text] [Related]

  • 20. Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: a novel class of transition-state analogues for zinc peptidases.
    Monzingo AF, Matthews BW.
    Biochemistry; 1984 Nov 20; 23(24):5724-9. PubMed ID: 6395881
    [Abstract] [Full Text] [Related]

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