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Volumn 40, Issue 37, 2001, Pages 11261-11269
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The distinct roles that Gln-192 and Glu-217 of factor IX play in selectivity for macromolecular substrates and inhibitors
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b
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a,d
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Author keywords
[No Author keywords available]
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Indexed keywords
CLOTTING;
BLOOD;
CATALYST SELECTIVITY;
COAGULATION;
COMPLEXATION;
MACROMOLECULES;
PHYSIOLOGY;
PROTEINS;
SUBSTRATES;
ENZYME INHIBITION;
ANTITHROMBIN III;
BLOOD CLOTTING FACTOR 8A;
BLOOD CLOTTING FACTOR 9;
GLUTAMIC ACID;
GLUTAMINE;
HEPARIN;
RECOMBINANT BLOOD CLOTTING FACTOR 9;
ARTICLE;
BLOOD CLOTTING;
CATALYSIS;
COMPLEX FORMATION;
DISSOCIATION CONSTANT;
HYDROLYSIS;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN PROTEIN INTERACTION;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
ANTITHROMBIN III;
BLOOD COAGULATION;
CYSTEINE ENDOPEPTIDASES;
FACTOR IX;
FACTOR IXA;
FACTOR VIIIA;
FACTOR X;
GLUTAMIC ACID;
GLUTAMINE;
HYDROLYSIS;
MODELS, CHEMICAL;
MUTAGENESIS;
MUTATION;
NEOPLASM PROTEINS;
PEPTIDES;
PLANT PROTEINS;
SERINE ENDOPEPTIDASES;
SERINE PROTEINASE INHIBITORS;
SERPINS;
SUBSTRATE SPECIFICITY;
TRYPSIN INHIBITORS;
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EID: 0035909082
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi010262t Document Type: Article |
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Times cited : (11)
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References (40)
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