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Volumn 273, Issue 21, 2006, Pages 4959-4971

The common phospholipid-binding activity of the N-terminal domains of PEX1 and VCP/p97

Author keywords

AAA ATPase; N terminal domain; PEX1; Phospholipid; Valosine containing protein

Indexed keywords

ADAPTOR PROTEIN; ADENOSINE TRIPHOSPHATASE; ARGININE; N ETHYLMALEIMIDE SENSITIVE FACTOR; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; PHOSPHATIDYLINOSITOL 4 PHOSPHATE; PHOSPHOLIPID; PROTEIN P47; PROTEIN PEX1; PROTEIN UFD1; PROTEIN VCP; UNCLASSIFIED DRUG;

EID: 33750085293     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2006.05494.x     Document Type: Article
Times cited : (24)

References (70)
  • 3
    • 14244267510 scopus 로고    scopus 로고
    • Peroxisomal disorders I: Biochemistry and genetics of peroxisome biogenesis disorders
    • Wanders RJ & Waterham HR (2005) Peroxisomal disorders I: biochemistry and genetics of peroxisome biogenesis disorders. Clin Genet 67, 107-133.
    • (2005) Clin Genet , vol.67 , pp. 107-133
    • Wanders, R.J.1    Waterham, H.R.2
  • 5
    • 0032555273 scopus 로고    scopus 로고
    • Disruption of a PEX1-PEX6 interaction is the most common cause of the neurologic disorders Zellweger syndrome, neonatal adrenoleukodystrophy, and infantile Refsum disease
    • Geisbrecht BV, Collins CS, Reuber BE & Gould SJ (1998) Disruption of a PEX1-PEX6 interaction is the most common cause of the neurologic disorders Zellweger syndrome, neonatal adrenoleukodystrophy, and infantile Refsum disease. Proc Natl Acad Sci USA 95, 8630-8635.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8630-8635
    • Geisbrecht, B.V.1    Collins, C.S.2    Reuber, B.E.3    Gould, S.J.4
  • 6
    • 0032515992 scopus 로고    scopus 로고
    • Human PEX1 cloned by functional complementation on a CHO cell mutant is responsible for peroxisome-deficient Zellweger syndrome of complementation group I
    • Tamura S, Okumoto K, Toyama R, Shimozawa N, Tsukamoto T, Suzuki Y, Osumi T, Kondo N & Fujiki Y (1998) Human PEX1 cloned by functional complementation on a CHO cell mutant is responsible for peroxisome-deficient Zellweger syndrome of complementation group I. Proc Natl Acad Sci USA 95, 4350-4355.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4350-4355
    • Tamura, S.1    Okumoto, K.2    Toyama, R.3    Shimozawa, N.4    Tsukamoto, T.5    Suzuki, Y.6    Osumi, T.7    Kondo, N.8    Fujiki, Y.9
  • 8
    • 0030459304 scopus 로고    scopus 로고
    • Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p, the PTS1 receptor: Evidence that PTS1 protein import is mediated by a cycling receptor
    • Dodt G & Gould SJ (1996) Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p, the PTS1 receptor: evidence that PTS1 protein import is mediated by a cycling receptor. J Cell Biol 135, 1763-1774.
    • (1996) J Cell Biol , vol.135 , pp. 1763-1774
    • Dodt, G.1    Gould, S.J.2
  • 9
    • 0029888487 scopus 로고    scopus 로고
    • The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a cytoplasmic ATPase required for stability of the PTS1 receptor
    • Yahraus T, Braverman N, Dodt G, Kalish JE, Morrell JC, Moser HW, Valle D & Gould SJ (1996) The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a cytoplasmic ATPase required for stability of the PTS1 receptor. EMBO J 15, 2914-2923.
    • (1996) EMBO J , vol.15 , pp. 2914-2923
    • Yahraus, T.1    Braverman, N.2    Dodt, G.3    Kalish, J.E.4    Morrell, J.C.5    Moser, H.W.6    Valle, D.7    Gould, S.J.8
  • 12
    • 11444254468 scopus 로고    scopus 로고
    • Structural and functional analysis of the interaction of the AAA-peroxins Pex1p and Pex6p
    • Birschmann I, Rosenkranz K, Erdmann R & Kunau WH (2005) Structural and functional analysis of the interaction of the AAA-peroxins Pex1p and Pex6p. FEBS J 272, 47-58.
    • (2005) FEBS J , vol.272 , pp. 47-58
    • Birschmann, I.1    Rosenkranz, K.2    Erdmann, R.3    Kunau, W.H.4
  • 13
    • 23144446970 scopus 로고    scopus 로고
    • Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol
    • Platta HW, Grunau S, Rosenkranz K, Girzalsky W & Erdmann R (2005) Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol. Nat Cell Biol 7, 817-822.
    • (2005) Nat Cell Biol , vol.7 , pp. 817-822
    • Platta, H.W.1    Grunau, S.2    Rosenkranz, K.3    Girzalsky, W.4    Erdmann, R.5
  • 14
    • 9444290733 scopus 로고    scopus 로고
    • Ubiquitination of the peroxisomal import receptor Pex5p
    • Platta HW, Girzalsky W & Erdmann R (2004) Ubiquitination of the peroxisomal import receptor Pex5p. Biochem J 384, 37-45.
    • (2004) Biochem J , vol.384 , pp. 37-45
    • Platta, H.W.1    Girzalsky, W.2    Erdmann, R.3
  • 15
    • 12544259938 scopus 로고    scopus 로고
    • Ubiquitination of the peroxisomal targeting signal type 1 receptor, Pex5p, suggests the presence of a quality control mechanism during peroxisomal matrix protein import
    • Kiel JA, Emmrich K, Meyer HE & Kunau WH (2005) Ubiquitination of the peroxisomal targeting signal type 1 receptor, Pex5p, suggests the presence of a quality control mechanism during peroxisomal matrix protein import. J Biol Chem 280, 1921-1930.
    • (2005) J Biol Chem , vol.280 , pp. 1921-1930
    • Kiel, J.A.1    Emmrich, K.2    Meyer, H.E.3    Kunau, W.H.4
  • 16
    • 14844311942 scopus 로고    scopus 로고
    • Endoplasmic reticulum-directed Pex3p routes to peroxisomes and restores peroxisome formation in Saccharomyces cerevisiae pex3 Delta strain
    • Kragt A, Voorn-Brouwer T, van den Berg M & Distel B (2005) Endoplasmic reticulum-directed Pex3p routes to peroxisomes and restores peroxisome formation in Saccharomyces cerevisiae pex3 Delta strain. J Biol Chem 280, 7867-7874.
    • (2005) J Biol Chem , vol.280 , pp. 7867-7874
    • Kragt, A.1    Voorn-Brouwer, T.2    Van Den Berg, M.3    Distel, B.4
  • 17
    • 24044485619 scopus 로고    scopus 로고
    • Obstruction of polyubiquitination affects PTS1 peroxisomal matrix protein
    • Kiel JA, Otzen M, Veenhuis M & van der Klei IJ (2005) Obstruction of polyubiquitination affects PTS1 peroxisomal matrix protein. Biochim Biophys Acta 1745, 176-186.
    • (2005) Biochim Biophys Acta , vol.1745 , pp. 176-186
    • Kiel, J.A.1    Otzen, M.2    Veenhuis, M.3    Van Der Klei, I.J.4
  • 19
    • 0030867609 scopus 로고    scopus 로고
    • Sequence analysis of the AAA protein family
    • Beyer A (1997) Sequence analysis of the AAA protein family. Protein Sci 6, 2043-2058.
    • (1997) Protein Sci , vol.6 , pp. 2043-2058
    • Beyer, A.1
  • 20
    • 0029089959 scopus 로고
    • An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments
    • Rabouille C, Levine TP, Peters JM & Warren G (1995) An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments. Cell 82, 905-914.
    • (1995) Cell , vol.82 , pp. 905-914
    • Rabouille, C.1    Levine, T.P.2    Peters, J.M.3    Warren, G.4
  • 21
    • 0025359065 scopus 로고
    • SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast
    • Clary DO, Griff IC & Rothman JE (1990) SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast. Cell 61, 709-721.
    • (1990) Cell , vol.61 , pp. 709-721
    • Clary, D.O.1    Griff, I.C.2    Rothman, J.E.3
  • 22
    • 0742323006 scopus 로고    scopus 로고
    • Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway
    • Dalal S, Rosser MF, Cyr DM & Hanson PI (2004) Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway. Mol Biol Cell 15, 637-648.
    • (2004) Mol Biol Cell , vol.15 , pp. 637-648
    • Dalal, S.1    Rosser, M.F.2    Cyr, D.M.3    Hanson, P.I.4
  • 23
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich E, Kerem A, Frohlich KU, Diamant N & Bar-Nun S (2002) AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol Cell Biol 22, 626-634.
    • (2002) Mol Cell Biol , vol.22 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Frohlich, K.U.3    Diamant, N.4    Bar-Nun, S.5
  • 24
    • 0028835784 scopus 로고
    • SNAPs and NSF: General members of the fusion apparatus
    • Whiteheart SW & Kubalek EW (1995) SNAPs and NSF: general members of the fusion apparatus. Trends Cell Biol 5, 64-68.
    • (1995) Trends Cell Biol , vol.5 , pp. 64-68
    • Whiteheart, S.W.1    Kubalek, E.W.2
  • 25
    • 0030796026 scopus 로고    scopus 로고
    • SNAREs and NSF in targeted membrane fusion
    • Hay JC & Scheller RH (1997) SNAREs and NSF in targeted membrane fusion. Curr Opin Cell Biol 9, 505-512.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 505-512
    • Hay, J.C.1    Scheller, R.H.2
  • 26
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye Y, Meyer HH & Rapoport TA (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162, 71-84.
    • (2003) J Cell Biol , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 27
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer HH, Shorter JG, Seemann J, Pappin D & Warren G (2000) A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J 19, 2181-2192.
    • (2000) EMBO J , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 30
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retrotranslocation from the ER lumen into the cytosol
    • Ye Y, Shibata Y, Yun C, Ron D & Rapoport TA (2004) A membrane protein complex mediates retrotranslocation from the ER lumen into the cytosol. Nature 429, 841-847.
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 31
    • 26444621357 scopus 로고    scopus 로고
    • Inaugural article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane
    • Ye Y, Shibata Y, Kikkert M, van Voorden S, Wiertz E & Rapoport TA (2004) Inaugural article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. Proc Natl Acad Sci USA 102, 14132-14138.
    • (2004) Proc Natl Acad Sci USA , vol.102 , pp. 14132-14138
    • Ye, Y.1    Shibata, Y.2    Kikkert, M.3    Van Voorden, S.4    Wiertz, E.5    Rapoport, T.A.6
  • 34
    • 0033165864 scopus 로고    scopus 로고
    • NSF N-terminal domain crystal structure: Models of NSF function
    • Yu RC, Jahn R & Brunger AT (1999) NSF N-terminal domain crystal structure: models of NSF function. Mol Cell 4, 97-107.
    • (1999) Mol Cell , vol.4 , pp. 97-107
    • Yu, R.C.1    Jahn, R.2    Brunger, A.T.3
  • 35
    • 0033163807 scopus 로고    scopus 로고
    • Crystal structure of the amino-terminal domain of N-ethylmaleimide- sensitive fusion protein
    • May AP, Misura KM, Whiteheart SW & Weis WI (1999) Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein. Nat Cell Biol 1, 175-182.
    • (1999) Nat Cell Biol , vol.1 , pp. 175-182
    • May, A.P.1    Misura, K.M.2    Whiteheart, S.W.3    Weis, W.I.4
  • 37
    • 0842268045 scopus 로고    scopus 로고
    • Supra-domains: Evolutionary units larger than single protein domains
    • Vogel C, Berzuini C, Bashton M, Gough J & Teichmann SA (2004) Supra-domains: evolutionary units larger than single protein domains. J Mol Biol 336, 809-823.
    • (2004) J Mol Biol , vol.336 , pp. 809-823
    • Vogel, C.1    Berzuini, C.2    Bashton, M.3    Gough, J.4    Teichmann, S.A.5
  • 38
    • 1842576796 scopus 로고    scopus 로고
    • Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47
    • Dreveny I, Kondo H, Uchiyama K, Shaw A, Zhang X & Freemont PS (2004) Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47. EMBO J 23, 1030-1039.
    • (2004) EMBO J , vol.23 , pp. 1030-1039
    • Dreveny, I.1    Kondo, H.2    Uchiyama, K.3    Shaw, A.4    Zhang, X.5    Freemont, P.S.6
  • 39
    • 21744460209 scopus 로고    scopus 로고
    • Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites
    • Park S, Isaacson R, Kim HT, Silver PA & Wagner G (2005) Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Structure 13, 995-1005.
    • (2005) Structure , vol.13 , pp. 995-1005
    • Park, S.1    Isaacson, R.2    Kim, H.T.3    Silver, P.A.4    Wagner, G.5
  • 40
    • 0033592895 scopus 로고    scopus 로고
    • Crystal structure of the Sec18p N-terminal domain
    • Babor SM & Fass D (1999) Crystal structure of the Sec18p N-terminal domain. Proc Natl Acad Sci USA 96, 14759-14764.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14759-14764
    • Babor, S.M.1    Fass, D.2
  • 41
    • 0039969327 scopus 로고    scopus 로고
    • Putative fusogenic activity of NSF is restricted to a lipid mixture whose coalescence is also triggered by other factors
    • Brugger B, Nickel W, Weber T, Parlati F, McNew JA, Rothman JE & Sollner T (2000) Putative fusogenic activity of NSF is restricted to a lipid mixture whose coalescence is also triggered by other factors. EMBO J 19, 1272-1278.
    • (2000) EMBO J , vol.19 , pp. 1272-1278
    • Brugger, B.1    Nickel, W.2    Weber, T.3    Parlati, F.4    McNew, J.A.5    Rothman, J.E.6    Sollner, T.7
  • 42
    • 0033560750 scopus 로고    scopus 로고
    • Cytosolic ATPases, p97 and NSF, are sufficient to mediate rapid membrane fusion
    • Otter-Nilsson M, Hendriks R, Pecheur-Huet EI, Hoekstra D & Nilsson T (1999) Cytosolic ATPases, p97 and NSF, are sufficient to mediate rapid membrane fusion. EMBO J 18, 2074-2083.
    • (1999) EMBO J , vol.18 , pp. 2074-2083
    • Otter-Nilsson, M.1    Hendriks, R.2    Pecheur-Huet, E.I.3    Hoekstra, D.4    Nilsson, T.5
  • 43
    • 0034019904 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate regulates two steps of homotypic vacuole fusion
    • Mayer A, Scheglmann D, Dove S, Glatz A, Wickner W & Haas A (2000) Phosphatidylinositol 4,5-bisphosphate regulates two steps of homotypic vacuole fusion. Mol Biol Cell 11, 807-817.
    • (2000) Mol Biol Cell , vol.11 , pp. 807-817
    • Mayer, A.1    Scheglmann, D.2    Dove, S.3    Glatz, A.4    Wickner, W.5    Haas, A.6
  • 44
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge O, Bourne HR & Cohen FE (1996) An evolutionary trace method defines binding surfaces common to protein families. J Mol Biol 257, 342-358.
    • (1996) J Mol Biol , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 45
    • 0034459679 scopus 로고    scopus 로고
    • Evolutionary trace analysis of TGF-beta and related growth factors: Implications for site-directed mutagenesis
    • Innis CA, Shi J & Blundell TL (2000) Evolutionary trace analysis of TGF-beta and related growth factors: implications for site-directed mutagenesis. Protein Eng 13, 839-847.
    • (2000) Protein Eng , vol.13 , pp. 839-847
    • Innis, C.A.1    Shi, J.2    Blundell, T.L.3
  • 46
    • 10844235653 scopus 로고    scopus 로고
    • Optimal docking area: A new method for predicting protein-protein interaction sites
    • Fernandez-Recio J, Totrov M, Skorodurnov C & Abagyan R (2005) Optimal docking area: a new method for predicting protein-protein interaction sites. Proteins 58, 134-143.
    • (2005) Proteins , vol.58 , pp. 134-143
    • Fernandez-Recio, J.1    Totrov, M.2    Skorodurnov, C.3    Abagyan, R.4
  • 47
    • 0031577297 scopus 로고    scopus 로고
    • Characterization of the pleckstrin homology domain of Btk as an inositol polyphosphate and phosphoinositide binding domain
    • Kojima T, Fukuda M, Watanabe Y, Hamazato F & Mikoshiba K (1997) Characterization of the pleckstrin homology domain of Btk as an inositol polyphosphate and phosphoinositide binding domain. Biochem Biophys Res Commun 236, 333-339.
    • (1997) Biochem Biophys Res Commun , vol.236 , pp. 333-339
    • Kojima, T.1    Fukuda, M.2    Watanabe, Y.3    Hamazato, F.4    Mikoshiba, K.5
  • 48
    • 0031930956 scopus 로고    scopus 로고
    • Two AAA family peroxins, PpPex1p and PpPex6p, interact with each other in an ATP-dependent manner and are associated with different subcellular membranous structures distinct from peroxisomes
    • Faber KN, Heyman JA & Subramani S (1998) Two AAA family peroxins, PpPex1p and PpPex6p, interact with each other in an ATP-dependent manner and are associated with different subcellular membranous structures distinct from peroxisomes. Mol Cell Biol 18, 936-943.
    • (1998) Mol Cell Biol , vol.18 , pp. 936-943
    • Faber, K.N.1    Heyman, J.A.2    Subramani, S.3
  • 49
    • 0034627808 scopus 로고    scopus 로고
    • Fusion of small peroxisomal vesicles in vitro reconstructs an early step in the in vivo multistep peroxisome assembly pathway of Yarrowia lipolytica
    • Titorenko VI, Chan H & Rachubinski RA (2000) Fusion of small peroxisomal vesicles in vitro reconstructs an early step in the in vivo multistep peroxisome assembly pathway of Yarrowia lipolytica. J Cell Biol 148, 29-44.
    • (2000) J Cell Biol , vol.148 , pp. 29-44
    • Titorenko, V.I.1    Chan, H.2    Rachubinski, R.A.3
  • 50
    • 0037161267 scopus 로고    scopus 로고
    • Analysis of NSF mutants reveals residues involved in SNAP binding and ATPase stimulation
    • Horsnell WG, Steel GJ & Morgan A (2002) Analysis of NSF mutants reveals residues involved in SNAP binding and ATPase stimulation. Biochemistry 41, 5230-5235.
    • (2002) Biochemistry , vol.41 , pp. 5230-5235
    • Horsnell, W.G.1    Steel, G.J.2    Morgan, A.3
  • 54
    • 0033618147 scopus 로고    scopus 로고
    • The Hansenula polymorpha PDD1 gene product, essential for the selective degradation of peroxisomes, is a homologue of Saccharomyces cerevisiae Vps34p
    • Kiel JA, Rechinger KB, van der Klei IJ, Salomons FA, Titorenko VI & Veenhuis M (1999) The Hansenula polymorpha PDD1 gene product, essential for the selective degradation of peroxisomes, is a homologue of Saccharomyces cerevisiae Vps34p. Yeast 15, 741-754.
    • (1999) Yeast , vol.15 , pp. 741-754
    • Kiel, J.A.1    Rechinger, K.B.2    Van Der Klei, I.J.3    Salomons, F.A.4    Titorenko, V.I.5    Veenhuis, M.6
  • 55
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T (1995) Protein modules and signalling networks. Nature 373, 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 56
    • 0038394714 scopus 로고    scopus 로고
    • The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes
    • Matsumoto N, Tamura S & Fujiki Y (2003) The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA ATPase complexes to peroxisomes. Nat Cell Biol 5, 454-460.
    • (2003) Nat Cell Biol , vol.5 , pp. 454-460
    • Matsumoto, N.1    Tamura, S.2    Fujiki, Y.3
  • 57
    • 0037632981 scopus 로고    scopus 로고
    • Pex15p of Saccharomyces cerevisiae provides a molecular basis for recruitment of the AAA peroxin Pex6p to peroxisomal membranes
    • Birschmann I, Stroobants AK, van den Berg M, Schafer A, Rosenkranz K, Kunau WH & Tabak HF (2003) Pex15p of Saccharomyces cerevisiae provides a molecular basis for recruitment of the AAA peroxin Pex6p to peroxisomal membranes. Mol Biol Cell 14, 2226-2236.
    • (2003) Mol Biol Cell , vol.14 , pp. 2226-2236
    • Birschmann, I.1    Stroobants, A.K.2    Van Den Berg, M.3    Schafer, A.4    Rosenkranz, K.5    Kunau, W.H.6    Tabak, H.F.7
  • 59
    • 1342331863 scopus 로고    scopus 로고
    • The PRESAT-vector: Asymmetric T-vector for high-throughput screening of soluble protein domains for structural proteomics
    • Goda N, Tenno T, Takasu H, Hiroaki H & Shirakawa M (2004) The PRESAT-vector: asymmetric T-vector for high-throughput screening of soluble protein domains for structural proteomics. Protein Sci 13, 652-658.
    • (2004) Protein Sci , vol.13 , pp. 652-658
    • Goda, N.1    Tenno, T.2    Takasu, H.3    Hiroaki, H.4    Shirakawa, M.5
  • 60
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F & Higgins DG (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 24, 4876-4882.
    • (1997) Nucleic Acids Res , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 63
    • 25844454807 scopus 로고    scopus 로고
    • Coincidence detection in phosphoinositide signaling
    • Carlton JG & Cullen PJ (2005) Coincidence detection in phosphoinositide signaling. Trends Cell Biol 15, 540-547.
    • (2005) Trends Cell Biol , vol.15 , pp. 540-547
    • Carlton, J.G.1    Cullen, P.J.2
  • 65
    • 0037195810 scopus 로고    scopus 로고
    • PIKfyve kinase and SKD1 AAA ATPase define distinct endocytic compartments. Only PIKfyve expression inhibits the cell-vacuolating activity of Helicobacter pylori VacA toxin
    • Ikonomov OC, Sbrissa D, Yoshimori T, Cover TL & Shisheva A (2002) PIKfyve kinase and SKD1 AAA ATPase define distinct endocytic compartments. Only PIKfyve expression inhibits the cell-vacuolating activity of Helicobacter pylori VacA toxin. J Biol Chem 277, 46785-46790.
    • (2002) J Biol Chem , vol.277 , pp. 46785-46790
    • Ikonomov, O.C.1    Sbrissa, D.2    Yoshimori, T.3    Cover, T.L.4    Shisheva, A.5
  • 66
    • 0038343926 scopus 로고    scopus 로고
    • Localization of a highly active pool of type II phosphatidylinositol 4-kinase in a p97/valosin-containing-protein-rich fraction of the endoplasmic reticulum
    • Waugh MG, Minogue S, Anderson JS, Balinger A, Blumenkrantz D, Calnan DP, Cramer R & Hsuan JJ (2003) Localization of a highly active pool of type II phosphatidylinositol 4-kinase in a p97/valosin-containing-protein-rich fraction of the endoplasmic reticulum. Biochem J 373, 57-63.
    • (2003) Biochem J , vol.373 , pp. 57-63
    • Waugh, M.G.1    Minogue, S.2    Anderson, J.S.3    Balinger, A.4    Blumenkrantz, D.5    Calnan, D.P.6    Cramer, R.7    Hsuan, J.J.8
  • 67
    • 0035937773 scopus 로고    scopus 로고
    • Differential binding of traffic-related proteins to phosphatidic acid- or phosphatidylinositol (4,5)-bisphosphate-coupled affinity reagents
    • Manifava M, Thuring JW, Lim ZY, Packman L, Holmes AB & Ktistakis NT (2001) Differential binding of traffic-related proteins to phosphatidic acid- or phosphatidylinositol (4,5)-bisphosphate-coupled affinity reagents. J Biol Chem 276, 8987-8994.
    • (2001) J Biol Chem , vol.276 , pp. 8987-8994
    • Manifava, M.1    Thuring, J.W.2    Lim, Z.Y.3    Packman, L.4    Holmes, A.B.5    Ktistakis, N.T.6


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