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Volumn 277, Issue 5, 2002, Pages 3622-3631
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The N-terminal epidermal growth factor-like domain in factor IX and factor X represents an important recognition motif for binding to tissue factor
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Author keywords
[No Author keywords available]
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Indexed keywords
ACTIVATION ANALYSIS;
BIOASSAY;
BIOLOGICAL MEMBRANES;
BLOOD;
PHYSIOLOGY;
TISSUE;
ANTICOAGULANTS;
PROTEINS;
ANTITHROMBIN;
BLOOD CLOTTING FACTOR 10;
BLOOD CLOTTING FACTOR 7;
BLOOD CLOTTING FACTOR 9;
EPIDERMAL GROWTH FACTOR;
EPIDERMAL GROWTH FACTOR 1;
EPIDERMAL GROWTH FACTOR 2;
RECOMBINANT BLOOD CLOTTING FACTOR 7A;
RECOMBINANT BLOOD CLOTTING FACTOR 9;
SERINE PROTEINASE;
SIGNAL PEPTIDE;
THROMBOPLASTIN;
UNCLASSIFIED DRUG;
AMINO ACID SEQUENCE;
AMINO TERMINAL SEQUENCE;
ARTICLE;
CALCIUM BINDING;
CARBOXY TERMINAL SEQUENCE;
DNA SEQUENCE;
ENZYME ASSAY;
LIGAND BINDING;
MOLECULAR RECOGNITION;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PROTEIN FOLDING;
PROTEIN MOTIF;
PROTEIN PROTEIN INTERACTION;
STRUCTURE ACTIVITY RELATION;
AMINO ACID SEQUENCE;
BINDING SITES;
BINDING, COMPETITIVE;
DNA PRIMERS;
EPIDERMAL GROWTH FACTOR;
FACTOR IX;
FACTOR VII;
FACTOR VIIA;
FACTOR X;
HUMANS;
KINETICS;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
PEPTIDES;
PROTEIN CONFORMATION;
SERINE ENDOPEPTIDASES;
THROMBOPLASTIN;
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EID: 0036479111
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M111202200 Document Type: Article |
Times cited : (43)
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References (58)
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