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Volumn 54, Issue 11, 2001, Pages 874-881

Isolation and structural determination of phepropeptins A, B, C, and D, new proteasome inhibitors, produced by Streptomyces sp.

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; CHEMICAL COMPOUND; CHYMOTRYPSIN; CHYMOTRYPSIN A; EPOXOMICIN; HEXAPEPTIDE; LACTACYSTIN; PEPTIDE; PHEPROPEPTIN A; PHEPROPEPTIN B; PHEPROPEPTIN C; PHEPROPEPTIN D; PROTEASOME INHIBITOR; UNCLASSIFIED DRUG;

EID: 0035211024     PISSN: 00218820     EISSN: None     Source Type: Journal    
DOI: 10.7164/antibiotics.54.874     Document Type: Article
Times cited : (18)

References (13)
  • 2
    • 0027410433 scopus 로고
    • Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids
    • (1993) Biochemistry , vol.32 , pp. 1563-1572
    • Orlowski, M.1    Cardozo, C.2    Michaud, C.3
  • 13
    • 0030294381 scopus 로고    scopus 로고
    • Specific inhibition of the chymotrypsin-like activity of the proteasome induces a bipolar morphology in neuroblastoma cells
    • (1996) Chem. Biol. , vol.3 , pp. 905-912
    • Fenteany, G.1    Schreiber, S.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.