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Volumn 12, Issue 7, 2001, Pages 1957-1971

Topological and mutational analysis of Saccharomyces cerevisiae Ste14p, founding member of the isoprenylcysteine carboxyl methyltransferase family

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE DERIVATIVE; FUNGAL ENZYME; HYBRID PROTEIN; METHYLTRANSFERASE;

EID: 0035157562     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.12.7.1957     Document Type: Article
Times cited : (61)

References (36)
  • 9
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    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6024-6035
    • Deshaies, R.J.1    Schekman, R.2
  • 12
    • 0025051169 scopus 로고
    • Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in Saccharomyces cerevisiae
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5071-5076
    • Hrycyna, C.A.1    Clarke, S.2
  • 16
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes
    • (1994) Arch. Biochem. Biophys. , vol.310 , pp. 417-427
    • Kagan, R.M.1    Clarke, S.2
  • 36
    • 0025951859 scopus 로고
    • Study of membrane orientation and glycosylated extracellular loops of mouse P-glycoprotein by in vitro translation
    • (1991) J. Biol. Chem. , vol.266 , pp. 18224-18232
    • Zhang, J.-T.1    Ling, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.