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Volumn 11, Issue 13, 2001, Pages 1074-1078

A yeast homolog of the mammalian mannose 6-phosphate receptors contributes to the sorting of vacuolar hydrolases

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYPEPTIDASE; CELL MEMBRANE TRANSPORT; CELL VACUOLE; ENDOSOME; FUNGAL ENZYME; GENE DELETION; GOLGI COMPLEX; HYDROLASE; MOLECULAR RECOGNITION; PROTEIN CONFORMATION; SACCHAROMYCES CEREVISIAE; SOMATOMEDIN B RECEPTOR;

EID: 0035838461     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(01)00273-1     Document Type: Article
Times cited : (43)

References (22)
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    • Structure and function of the mannose 6-phosphate/insulinlike growth factor II receptors
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    • Kornfeld, S.1
  • 4
    • 0035838410 scopus 로고    scopus 로고
    • The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan recognizing proteins
    • (2001) Curr Biol , vol.11
    • Munro, S.1
  • 5
    • 0029905298 scopus 로고    scopus 로고
    • Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases
    • (1996) J Cell Biol , vol.133 , pp. 529-541
    • Cooper, A.A.1    Stevens, T.H.2
  • 6
  • 13
    • 0027186301 scopus 로고
    • Vps1p, a member of the dynamin GTPase family, is necessary for Golgi membrane protein retention in Saccharomyces cerevisiae
    • (1993) EMBO J , vol.12 , pp. 3049-3059
    • Wilsbach, K.1    Payne, G.S.2
  • 14
    • 0022898326 scopus 로고
    • Protein sorting in yeast: Mutants defective in vacuole biogenesis mislocalize vacuolar proteins into the late secretory pathway
    • (1986) Cell , vol.47 , pp. 1041-1051
    • Rothman, J.H.1    Stevens, T.H.2
  • 21
    • 15144361572 scopus 로고    scopus 로고
    • Mannose 6-phosphate/insulin-like growth factor-II receptor targets the urokinase receptor to lysosomes via a novel binding interaction
    • (1998) J Cell Biol , vol.141 , pp. 815-828
    • Nykjaer, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.