메뉴 건너뛰기




Volumn 3, Issue 7, 2001, Pages 613-618

Phox domain interaction with Ptdlns(3)P targets the Vam7 t-SNARE to vacuole membranes

Author keywords

[No Author keywords available]

Indexed keywords

LIPID; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3 KINASE; SNARE PROTEIN;

EID: 0034947026     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/35083000     Document Type: Article
Times cited : (321)

References (39)
  • 1
    • 0029850711 scopus 로고    scopus 로고
    • Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: Binding partners of SH3 domains?
    • (1996) Protein Sci. , vol.5 , pp. 2353-2357
    • Ponting, C.P.1
  • 2
    • 0035161467 scopus 로고    scopus 로고
    • Autosomal recessive chronic granulomatous disease caused by defects in NCF-1, the gene encoding the phagocyte p47-phox: Mutations not arising in the NCF-1 pseudogenes
    • (2001) Blood , vol.97 , pp. 305-311
    • Noack, D.1
  • 4
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting
    • (1993) Science , vol.260 , pp. 88-91
    • Schu, P.V.1
  • 6
    • 0032488032 scopus 로고    scopus 로고
    • The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae
    • (1998) Curr. Biol. , vol.8 , pp. 1219-1222
    • Cooke, F.T.1
  • 8
  • 12
    • 0032111444 scopus 로고    scopus 로고
    • Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains
    • (1998) Mol. Cell , vol.2 , pp. 157-162
    • Burd, C.G.1    Emr, S.D.2
  • 15
    • 0034282751 scopus 로고    scopus 로고
    • Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells
    • (2000) EMBO J. , vol.19 , pp. 4577-4588
    • Gillooly, D.J.1
  • 20
    • 0035017670 scopus 로고    scopus 로고
    • Self-assembly and binding of a sorting nexin to sorting endosomes
    • (2001) J. Cell. Sci. , vol.114 , pp. 1743-1756
    • Kurten, R.C.1
  • 24
    • 0342350252 scopus 로고    scopus 로고
    • Influence of phosphatidylinositol 4,5-bisphosphate on human phospholipase D1 wild-type and deletion mutants: Is there evidence for an interaction of phosphatidylinositol 4,5-bisphosphate with the putative pleckstrin homology domain?
    • (2000) Biochim. Biophys. Acta , vol.1481 , pp. 189-201
    • Hoer, A.1    Cetindag, C.2    Oberdisse, E.3
  • 25
    • 0033985026 scopus 로고    scopus 로고
    • Phospholipase D regulation and localisation is dependent upon a phosphatidylinositol 4,5-bisphosphate-specific PH domain
    • (2000) Curr. Biol. , vol.10 , pp. 43-46
    • Hodgkin, M.N.1
  • 26
    • 0040737600 scopus 로고    scopus 로고
    • Phosphorylation and activation of phospholipase D1 by protein kinase C in vivo: Determination of multiple phosphorylation sites
    • (1999) Biochemistry , vol.38 , pp. 10344-10351
    • Kim, Y.1
  • 29
    • 0033635275 scopus 로고    scopus 로고
    • Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains
    • (2000) Mol. Cell , vol.6 , pp. 373-384
    • Ferguson, K.M.1
  • 31
    • 0035134328 scopus 로고    scopus 로고
    • Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis
    • (2001) Science , vol.291 , pp. 1047-1051
    • Itoh, T.1
  • 32
    • 0035135419 scopus 로고    scopus 로고
    • 2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes
    • (2001) Science , vol.291 , pp. 1051-1055
    • Ford, M.G.1
  • 33
    • 0029437296 scopus 로고
    • Pulsed field gradient multi-dimensional NMR methods for the study of protein structure and dynamics in solution
    • (1995) Prog. Biophys. Mol. Biol. , vol.63 , pp. 277-299
    • Kay, L.E.1
  • 36
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 39
    • 0029881450 scopus 로고    scopus 로고
    • The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase
    • (1996) Nature Struct. Biol. , vol.3 , pp. 340-345
    • Grzesiek, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.