Tissue factor mutated at the allosteric Cys186-Cys209 disulfide bond is severely impaired in decrypted procoagulant activity

Blood

Volumn 116, Issue 3, 2010, Pages 500-501

  Ruf, Wolfram ^a   Versteeg, Henri H ^b  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b LEIDEN UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 7A; CYSTEINE; ENZYME PRECURSOR; PROTEINASE ACTIVATED RECEPTOR 2; THROMBOPLASTIN; CYSTINE; DISULFIDE; MUTANT PROTEIN; RECOMBINANT PROTEIN;

ALLOSTERISM; BLOOD LEVEL; CELL SURFACE; CONTROLLED STUDY; CYTOLYSIS; DISULFIDE BOND; HUMAN; HUMAN CELL; LETTER; PRIORITY JOURNAL; PROTEIN EXPRESSION; AMINO ACID SUBSTITUTION; BINDING SITE; CHEMISTRY; ENDOTHELIUM CELL; GENETIC TRANSDUCTION; GENETICS; IN VITRO STUDY; METABOLISM; NOTE; SITE DIRECTED MUTAGENESIS;

ALLOSTERIC SITE; AMINO ACID SUBSTITUTION; CYSTINE; DISULFIDES; ENDOTHELIAL CELLS; FACTOR VIIA; HUMANS; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; RECOMBINANT PROTEINS; THROMBOPLASTIN; TRANSDUCTION, GENETIC;

EID: 77955907854     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2010-04-281287     Document Type: Letter

References (10)

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