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465 related items for PubMed ID: 3064813

  • 1. Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo.
    McPhalen CA, James MN.
    Biochemistry; 1988 Aug 23; 27(17):6582-98. PubMed ID: 3064813
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  • 2. Effects of eglin-c binding to thermitase: three-dimensional structure comparison of native thermitase and thermitase eglin-c complexes.
    Gros P, Teplyakov AV, Hol WG.
    Proteins; 1992 Jan 23; 12(1):63-74. PubMed ID: 1553381
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  • 3. The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry.
    Bode W, Papamokos E, Musil D.
    Eur J Biochem; 1987 Aug 03; 166(3):673-92. PubMed ID: 3301348
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  • 4. Refined crystal structure of the complex of subtilisin BPN' and Streptomyces subtilisin inhibitor at 1.8 A resolution.
    Takeuchi Y, Satow Y, Nakamura KT, Mitsui Y.
    J Mol Biol; 1991 Sep 05; 221(1):309-25. PubMed ID: 1920411
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  • 5. Refined 1.2 A crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin and its detailed interaction with subtilisin.
    Bode W, Papamokos E, Musil D, Seemueller U, Fritz H.
    EMBO J; 1986 Apr 05; 5(4):813-8. PubMed ID: 3519213
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  • 6. Crystal and molecular structure of the inhibitor eglin from leeches in complex with subtilisin Carlsberg.
    McPhalen CA, Schnebli HP, James MN.
    FEBS Lett; 1985 Aug 19; 188(1):55-8. PubMed ID: 3926539
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  • 7. Differences in binding modes of enantiomers of 1-acetamido boronic acid based protease inhibitors: crystal structures of gamma-chymotrypsin and subtilisin Carlsberg complexes.
    Stoll VS, Eger BT, Hynes RC, Martichonok V, Jones JB, Pai EF.
    Biochemistry; 1998 Jan 13; 37(2):451-62. PubMed ID: 9425066
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  • 8. Binding of the recombinant proteinase inhibitor eglin c from leech Hirudo medicinalis to serine (pro)enzymes: a comparative thermodynamic study.
    Ascenzi P, Aducci P, Amiconi G, Ballio A, Guaragna A, Menegatti E, Schnebli HP, Bolognesi M.
    J Mol Recognit; 1991 Jan 13; 4(4):113-9. PubMed ID: 1799460
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  • 9. Variability of the canonical loop conformations in serine proteinases inhibitors and other proteins.
    Apostoluk W, Otlewski J.
    Proteins; 1998 Sep 01; 32(4):459-74. PubMed ID: 9726416
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  • 13. Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98 A resolution and comparison of two crystal forms that differ in calcium content.
    Gros P, Betzel C, Dauter Z, Wilson KS, Hol WG.
    J Mol Biol; 1989 Nov 20; 210(2):347-67. PubMed ID: 2689655
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  • 14. A novel serine protease inhibition motif involving a multi-centered short hydrogen bonding network at the active site.
    Katz BA, Elrod K, Luong C, Rice MJ, Mackman RL, Sprengeler PA, Spencer J, Hataye J, Janc J, Link J, Litvak J, Rai R, Rice K, Sideris S, Verner E, Young W.
    J Mol Biol; 2001 Apr 13; 307(5):1451-86. PubMed ID: 11292354
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  • 15. Affinity and specificity of serine endopeptidase-protein inhibitor interactions. Empirical free energy calculations based on X-ray crystallographic structures.
    Krystek S, Stouch T, Novotny J.
    J Mol Biol; 1993 Dec 05; 234(3):661-79. PubMed ID: 8254666
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  • 16. Refined crystal structures of subtilisin novo in complex with wild-type and two mutant eglins. Comparison with other serine proteinase inhibitor complexes.
    Heinz DW, Priestle JP, Rahuel J, Wilson KS, Grütter MG.
    J Mol Biol; 1991 Jan 20; 217(2):353-71. PubMed ID: 1992167
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  • 18. Modeling the 3D structure of wheat subtilisin/chymotrypsin inhibitor (WSCI). Probing the reactive site with two susceptible proteinases by time-course analysis and molecular dynamics simulations.
    Facchiano AM, Costantini S, Di Maro A, Panichi D, Chambery A, Parente A, Di Gennaro S, Poerio E.
    Biol Chem; 2006 Jul 20; 387(7):931-40. PubMed ID: 16913843
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