Identification of a region of β-amyloid precursor protein essential for its gelatinase A inhibitory activity

Journal of Biological Chemistry

Volumn 278, Issue 16, 2003, Pages 14020-14028

  Higashi, Shouichi ^a   Miyazaki, Kaoru ^b  

^a YOKOHAMA CITY UNIVERSITY   (Japan)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; ENZYMES; PROTEINS;

PRECURSORS;

ENZYME INHIBITION;

AMYLOID BETA PROTEIN; ASPARTIC ACID; GELATINASE A; GELATINASE B; GELATINASE INHIBITOR; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; HYDROXAMIC ACID; INTERSTITIAL COLLAGENASE; ISOLEUCINE; LEUCINE; MATRILYSIN; METHIONINE; PROLINE; PROTEIN PRECURSOR; STROMELYSIN; TYROSINE; AMINO ACID; ENZYME INHIBITOR; GELATIN; LYSYL ENDOPEPTIDASE; PEPTIDE; SERINE PROTEINASE; THROMBIN; TRYPSIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME INHIBITION; EXTRACELLULAR MATRIX; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN INTERACTION; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; CELL LINE; CHEMISTRY; DOSE RESPONSE; DRUG ANTAGONISM; GENETIC TRANSFECTION; HUMAN; IC 50; KINETICS; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; TEMPERATURE; TIME; WESTERN BLOTTING;

AMINO ACID SEQUENCE; AMINO ACIDS; AMYLOID BETA-PROTEIN; ANIMALS; ASPARTIC ACID; BINDING SITES; BLOTTING, WESTERN; CELL LINE; DOSE-RESPONSE RELATIONSHIP, DRUG; ENZYME INHIBITORS; GELATIN; GLUTATHIONE TRANSFERASE; HUMANS; INHIBITORY CONCENTRATION 50; KINETICS; MATRIX METALLOPROTEINASE 1; MATRIX METALLOPROTEINASE 2; MATRIX METALLOPROTEINASE 3; MATRIX METALLOPROTEINASE 7; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDES; PROTEIN BINDING; PROTEIN PRECURSORS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SERINE ENDOPEPTIDASES; TEMPERATURE; THROMBIN; TIME FACTORS; TRANSFECTION; TRYPSIN;

EID: 0037687306     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M212264200     Document Type: Article

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