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250 related items for PubMed ID: 12927546

  • 1. Three dimensional structures of S189D chymotrypsin and D189S trypsin mutants: the effect of polarity at site 189 on a protease-specific stabilization of the substrate-binding site.
    Szabó E, Venekei I, Böcskei Z, Náray-Szabó G, Gráf L.
    J Mol Biol; 2003 Aug 29; 331(5):1121-30. PubMed ID: 12927546
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  • 2. Properties of the His57-Asp102 dyad of rat trypsin D189S in the zymogen, activated enzyme, and alpha1-proteinase inhibitor complexed forms.
    Kaslik G, Westler WM, Gráf L, Markley JL.
    Arch Biochem Biophys; 1999 Feb 15; 362(2):254-64. PubMed ID: 9989934
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  • 3. The crystal structure of a trypsin-like mutant chymotrypsin: the role of position 226 in the activity and specificity of S189D chymotrypsin.
    Jelinek B, Katona G, Fodor K, Venekei I, Gráf L.
    Protein J; 2008 Feb 15; 27(2):79-87. PubMed ID: 17805946
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  • 4. Ala226 to Gly and Ser189 to Asp mutations convert rat chymotrypsin B to a trypsin-like protease.
    Jelinek B, Antal J, Venekei I, Gráf L.
    Protein Eng Des Sel; 2004 Feb 15; 17(2):127-31. PubMed ID: 15047908
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  • 5. Attempts to convert chymotrypsin to trypsin.
    Venekei I, Szilágyi L, Gráf L, Rutter WJ.
    FEBS Lett; 1996 Mar 25; 383(1-2):143-7. PubMed ID: 8612781
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  • 6. Hydrophobic interactions control zymogen activation in the trypsin family of serine proteases.
    Hedstrom L, Lin TY, Fast W.
    Biochemistry; 1996 Apr 09; 35(14):4515-23. PubMed ID: 8605201
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  • 7. Attempts to convert chymotrypsin to trypsin.
    Venekei I, Szilágyi L, Gráf L, Rutter WJ.
    FEBS Lett; 1996 Jan 29; 379(2):143-7. PubMed ID: 8635580
    [Abstract] [Full Text] [Related]

  • 8. Converting trypsin to chymotrypsin: residue 172 is a substrate specificity determinant.
    Hedstrom L, Perona JJ, Rutter WJ.
    Biochemistry; 1994 Jul 26; 33(29):8757-63. PubMed ID: 8038165
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  • 9. Converting trypsin to chymotrypsin: structural determinants of S1' specificity.
    Kurth T, Ullmann D, Jakubke HD, Hedstrom L.
    Biochemistry; 1997 Aug 19; 36(33):10098-104. PubMed ID: 9254605
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  • 10. Structural consequences of accommodation of four non-cognate amino acid residues in the S1 pocket of bovine trypsin and chymotrypsin.
    Helland R, Czapinska H, Leiros I, Olufsen M, Otlewski J, Smalås AO.
    J Mol Biol; 2003 Oct 31; 333(4):845-61. PubMed ID: 14568540
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  • 12. New structural motifs on the chymotrypsin fold and their potential roles in complement factor B.
    Jing H, Xu Y, Carson M, Moore D, Macon KJ, Volanakis JE, Narayana SV.
    EMBO J; 2000 Jan 17; 19(2):164-73. PubMed ID: 10637221
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  • 14. The three-dimensional structure of Asp189Ser trypsin provides evidence for an inherent structural plasticity of the protease.
    Szabó E, Böcskei Z, Náray-Szabó G, Gráf L.
    Eur J Biochem; 1999 Jul 17; 263(1):20-6. PubMed ID: 10429182
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  • 17. Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid beta-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): engineering of inhibitors with altered specificities.
    Scheidig AJ, Hynes TR, Pelletier LA, Wells JA, Kossiakoff AA.
    Protein Sci; 1997 Sep 17; 6(9):1806-24. PubMed ID: 9300481
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