The proximal carboxyl-terminal domains of ADAMTS13 determine substrate specificity and are all required for cleavage of von Willebrand factor

Journal of Biological Chemistry

Volumn 280, Issue 33, 2005, Pages 29428-29434

  Ai, Jihui ^a   Smith, Paula ^a   Wang, Shuwei ^a   Zhang, Ping ^a   Zheng, X Long ^a,b,c  

^a CHILDREN S HOSPITAL OF PHILADELPHIA   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLATION; CHEMICAL BONDS; DISINTEGRATION; ENERGY TRANSFER; FLUORESCENCE; RESONANCE;

CARBOXYL-TERMINAL DOMAINS; FLUORESCENCE RESONANCE ENERGY TRANSFER (FRETS); PROTEOLYSIS; VOL WILLEBRAND FACTOR;

ENZYMES;

ARGININE; ASPARTIC ACID; CYSTEINE; GLUTATHIONE TRANSFERASE; METALLOPROTEINASE; METHIONINE; TYROSINE; VON WILLEBRAND FACTOR; VON WILLEBRAND FACTOR CLEAVING PROTEINASE;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONCENTRATION RESPONSE; CONTROLLED STUDY; ENZYME SPECIFICITY; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; HUMAN CELL; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; THROMBOSIS;

ADAM PROTEINS; AMINO ACID SEQUENCE; HUMANS; METALLOENDOPEPTIDASES; MOLECULAR SEQUENCE DATA; SUBSTRATE SPECIFICITY; VON WILLEBRAND FACTOR;

EID: 23844465898     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M505513200     Document Type: Article

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