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Volumn 9, Issue 13, 2000, Pages 1919-1926

Mutations in the N-terminus of the X-linked retinitis pigmentosa protein RP2 interfere with the normal targeting of the protein to the plasma membrane

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CELL MEMBRANE PROTEIN; PROTEIN RP2; UNCLASSIFIED DRUG;

EID: 0034641595     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/9.13.1919     Document Type: Article
Times cited : (83)

References (25)
  • 10
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 11
    • 84866476582 scopus 로고    scopus 로고
    • Rapid plasma membrane anchoring of newly synthesized p59fyn: Selective requirement for NH2-terminal myristoylation and palmitoylation at cysteine-3
    • (1997) J. Cell Biol. , vol.136 , pp. 1023-1035
    • van't Hof, W.1    Resh, M.D.2
  • 18
    • 0030053810 scopus 로고    scopus 로고
    • Chemical inhibition of myristoylation of the G-protein G(il) alpha by 2-hydroxymyristate does not interfere with its palmitoylation or membrane association. Evidence that palmitoylation, but not myristoylation, attachment
    • (1996) Biochem. J. , vol.313 , pp. 717-720
    • Galbiati, F.1    Guzzi, F.2    Magee, A.I.3    Milligan, G.4    Parenti, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.