Regulation of fibrinolysis by C-terminal lysines operates through plasminogen and plasmin but not tissue-type plasminogen activator

Journal of Thrombosis and Haemostasis

Volumn 10, Issue 11, 2012, Pages 2354-2360

  Silva, M M C G ^a   Thelwell, C ^a   Williams, S C ^a   Longstaff, C ^a  

^a NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS AND CONTROL   (United Kingdom)

Author keywords

Antifibrinolytics; Fibrinolysis; Kringles; TAFI

Indexed keywords

BLOOD CLOTTING FACTOR 13A; CARBOXYPEPTIDASE B; FIBRIN; LYSINE; PLASMIN; PLASMINOGEN; TISSUE PLASMINOGEN ACTIVATOR; TRANEXAMIC ACID;

ARTICLE; BLOOD CLOT LYSIS; CONTROLLED STUDY; DRUG BINDING; FIBRINOLYSIS; GENE SWITCHING; GENETIC ENGINEERING; KRINGLE DOMAIN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN INTERACTION;

ANTIFIBRINOLYTICS; FIBRINOLYSIS; KRINGLES; TAFI;

BINDING SITES; CARBOXYPEPTIDASE B; FIBRIN; FIBRINOLYSIN; FIBRINOLYSIS; HUMANS; KINETICS; KRINGLES; LYSINE; PLASMINOGEN; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; TISSUE PLASMINOGEN ACTIVATOR; TRANEXAMIC ACID; UROKINASE-TYPE PLASMINOGEN ACTIVATOR;

EID: 84868149988     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2012.04925.x     Document Type: Article

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