Mechanisms by which von willebrand disease mutations destabilize the A2 domain

Journal of Biological Chemistry

Volumn 288, Issue 9, 2013, Pages 6317-6324

  Xu, Amy J ^a   Springer, Timothy A ^a  

^a BOSTON CHILDREN S HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING; CALCIUM REMOVAL; FOLDED STATE; FORCE SENSING; FORCE SENSOR; HYDROPHOBIC CORE; METALLO-PROTEASE; REFOLDING; REFOLDING KINETICS; SHORT TIME SCALE; SINGLE MOLECULE; STRUCTURAL FEATURE; TEMPERATURE AND FORCE; THROMBOSPONDIN; TIME-SCALES; VASCULATURE; VON WILLEBRAND FACTOR;

CALCIUM; GLYCOPROTEINS; HYDROGEN BONDS; OPTICAL TWEEZERS;

DISEASES;

GLYCOPROTEIN; VON WILLEBRAND FACTOR; VON WILLEBRAND FACTOR CLEAVING PROTEINASE;

ARTICLE; CALCIUM BINDING; CIRCULAR DICHROISM; GENE MUTATION; HUMAN; HYDROGEN BOND; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PURIFICATION; SENSOR; THERMOSTABILITY; THROMBOGENICITY; VON WILLEBRAND DISEASE;

AMINO ACID SUBSTITUTION; CALCIUM; HOT TEMPERATURE; HUMANS; MUTATION, MISSENSE; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; VON WILLEBRAND DISEASES; VON WILLEBRAND FACTOR;

EID: 84874785770     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.422618     Document Type: Article

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