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Volumn 113, Issue 11, 2000, Pages 2075-2083

Colocalization of chaperone Cpn60, proinsulin and convertase PC1 within immature secretory granules of insulin-secreting cells suggests a role for Cpn60 in insulin processing

Author keywords

Chaperonin; Immunocytochemistry; Insulin; Pancreas; Proinsulin; Secretion

Indexed keywords

CHAPERONE; CONVERTASE; ENZYME; HEAT SHOCK PROTEIN; INSULIN; PROINSULIN; UNCLASSIFIED DRUG;

EID: 0343729333     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (16)

References (12)
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  • 5
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    • A member of the eukaryotic subtilisin family (PC3) has the enzymic properties of the type 1 proinsulin-converting endopeptidase
    • Bailyes, E. M., Shennan, K. I., Seal, A. J., Smeekens, S. P., Steiner, D. F. Hutton, J. C. and Docherry, K. (1992). A member of the eukaryotic subtilisin family (PC3) has the enzymic properties of the type 1 proinsulin-converting endopeptidase. Biochem. J. 285, 391-394.
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    • Proprotein conversion is determined by a multiplicity of factors including convertase processing, substrate specificity and intracellular environment
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.