Activity of ADAM17 (a disintegrin and metalloprotease 17) is regulated by its noncatalytic domains and secondary structure of its substrates

Journal of Biological Chemistry

Volumn 288, Issue 31, 2013, Pages 22871-22879

  Stawikowska, Roma ^a   Cudic, Mare ^a   Giulianotti, Marc ^a   Houghten, Richard A ^a   Fields, Gregg B ^a   Minond, Dmitriy ^a  

^a TORREY PINES INSTITUTE FOR MOLECULAR STUDIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

METALLO-PROTEASE; NON-CATALYTIC; SECONDARY STRUCTURES; STRUCTURAL DETERMINANTS; STRUCTURAL ELEMENTS; SUBSTRATE SPECIFICITY;

BIOCHEMISTRY; BIOLOGY;

SUBSTRATES;

ADAM10 ENDOPEPTIDASE; CARBOHYDRATE BINDING PROTEIN; MEMBRANE PROTEIN; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME;

ALPHA HELIX; ARTICLE; CELL SURFACE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME GLYCOSYLATION; ENZYME REGULATION; ENZYME RELEASE; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN SECONDARY STRUCTURE; STRUCTURE ANALYSIS;

ADAM ADAMTS; CELL SURFACE ENZYMES; ENZYME INHIBITORS; ENZYME KINETICS; ENZYME MECHANISMS; EXOSITE INHIBITOR; EXOSITE SUBSTRATE; NONCATALYTIC DOMAINS; SUBSTRATE CONFORMATION;

ADAM PROTEINS; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CIRCULAR DICHROISM; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; SUBSTRATE SPECIFICITY;

EID: 84881253946     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.462267     Document Type: Article

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