The factor V CI domain is involved in membrane binding: Identification of functionally important amino acid residues within the CI domain of factor V using alanine scanning mutagenesis

Thrombosis and Haemostasis

Volumn 91, Issue 1, 2004, Pages 16-27

  Saleh, Mahasen ^a,b   Peng, Weimin ^a   Quinn Allen, Mary Ann ^a   Macedo Ribeiro, Sandra ^c,d   Fuentes Prior, Pablo ^c   Bode, Wolfram ^c   Kane, William H ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

^b KING FAISAL SPECIALIST HOSPITAL AND RESEARCH CENTER   (Saudi Arabia)

^c MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^d UNIVERSITY OF COIMBRA   (Portugal)

Author keywords

Factor V; Factor VIII; Phospholipids procoagulant; Site directed mutagenesis

Indexed keywords

AMINO ACID; BLOOD CLOTTING FACTOR 5; BLOOD CLOTTING FACTOR 5 C1; BLOOD CLOTTING FACTOR 5 C2; PHOSPHOLIPID; PROTHROMBIN; UNCLASSIFIED DRUG; ALANINE; COMPLEMENTARY DNA; PHOSPHATIDYLSERINE; THROMBOPLASTIN;

ARTICLE; BINDING SITE; ENZYME ACTIVITY; ENZYME ASSAY; FLUORESCENCE RESONANCE ENERGY TRANSFER; HYDROPHOBICITY; MOLECULAR MODEL; MOUSE; MUTANT; MUTATION; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN IMMOBILIZATION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; ANIMAL; CELL MEMBRANE; CELL STRAIN COS1; CHEMICAL STRUCTURE; CHEMISTRY; CULTURE MEDIUM; DOSE RESPONSE; ENZYME LINKED IMMUNOSORBENT ASSAY; HUMAN; KINETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE;

ALANINE; AMINO ACID SEQUENCE; ANIMALS; CELL MEMBRANE; COS CELLS; CULTURE MEDIA, CONDITIONED; DNA, COMPLEMENTARY; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME-LINKED IMMUNOSORBENT ASSAY; FACTOR V; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMANS; KINETICS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHOSPHATIDYLSERINES; PHOSPHOLIPIDS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; THROMBOPLASTIN;

EID: 1642556716     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/th03-04-0222     Document Type: Article

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