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Volumn 113, Issue 18, 2000, Pages 3289-3298

The lysosomal protease cathepsin D is efficiently sorted to and secreted from regulated secretory compartments in the rat basophilic/mast cell line RBL

Author keywords

Lysosomal protease; Mast cell; Secretory lysosome

Indexed keywords

2,4 DINITROPHENOL; AMMONIUM CHLORIDE; BIOLOGICAL MARKER; BOVINE SERUM ALBUMIN; CALCIUM; CATHEPSIN D; EGTAZIC ACID; HYDROLASE; IMMUNOGLOBULIN E; IMMUNOGLOBULIN E RECEPTOR; LYSOSOME ENZYME; MANNOSE 6 PHOSPHATE; MEMBRANE PROTEIN; MEMBRANE RECEPTOR; MONOCLONAL ANTIBODY; PROTEINASE; TOLONIUM CHLORIDE;

EID: 0033785510     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (54)

References (45)
  • 2
    • 0032526224 scopus 로고    scopus 로고
    • Sorting and storage during secretory granule biogenesis: Looking backward and looking forward
    • (1998) Biochem. J. , vol.332 , pp. 593-610
    • Arvan, P.1    Castle, D.2
  • 23
    • 0026584007 scopus 로고
    • The early and late processing of lysosomal enzymes: Proteolysis and compartmentation
    • (1992) Experientia , vol.48 , pp. 130-151
    • Hasilik, A.1
  • 34
    • 0020352681 scopus 로고
    • Weak bases and ionophores rapidly and reversibly raise the pH of endocytic vesicles in cultured mouse fibroblasts
    • (1982) J. Cell Biol. , vol.95 , pp. 676-681
    • Maxfield, F.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.