Protein disulfide isomerase-mediated disulfide bonds regulate the gelatinolytic activity and secretion of matrix metalloproteinase-9

Experimental Cell Research

Volumn 318, Issue 8, 2012, Pages 904-914

  Khan, Maola M G ^a,b   Simizu, Siro ^a,c   Suzuki, Takehiro ^a   Masuda, Akiko ^a   Kawatani, Makoto ^a   Muroi, Makoto ^a   Dohmae, Naoshi ^a,b   Osada, Hiroyuki ^a,b  

^a RIKEN   (Japan)

^b SAITAMA UNIVERSITY   (Japan)

^c KEIO UNIVERSITY   (Japan)

Author keywords

Cysteine switch; Disulfide bond; Matrix metalloproteinase 9; Protein disulfide isomerase

Indexed keywords

CYSTEINE; GELATINASE B; HEMOPEXIN; MUTANT PROTEIN; PROTEIN DISULFIDE ISOMERASE;

ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME RELEASE; GENE OVEREXPRESSION; HUMAN; HUMAN CELL; INTRACELLULAR TRANSPORT; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROCESSING; PROTEIN TARGETING; WILD TYPE;

EID: 84862783592     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2012.02.021     Document Type: Article

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