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Volumn 14, Issue 1, 2003, Pages 262-273

SVIP is a novel VCP/p97-interacting protein whose expression causes cell vacuolation

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; POLYGLUTAMINE; PROTEIN P47; PROTEIN P97; PROTEIN SVIP; PROTEIN UFD1P; PROTEIN VCP; UNCLASSIFIED DRUG;

EID: 0037238393     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.02-07-0115     Document Type: Article
Times cited : (78)

References (61)
  • 1
    • 0029084786 scopus 로고
    • The formation of Golgi stacks from vesiculated Golgi membranes requires two distinct fusion events
    • Acharya, U., Jacobs, R., Peters, J.M., Watson, N., Farquhar, M.G., and Malhotra, V. (1995). The formation of Golgi stacks from vesiculated Golgi membranes requires two distinct fusion events. Cell 82, 895-904.
    • (1995) Cell , vol.82 , pp. 895-904
    • Acharya, U.1    Jacobs, R.2    Peters, J.M.3    Watson, N.4    Farquhar, M.G.5    Malhotra, V.6
  • 2
  • 3
    • 0034724727 scopus 로고    scopus 로고
    • Cloning and characterization of the murine glucosamine-6-phosphate acetyltransferase EMeg32. Differential expression and intracellular membrane association
    • Boehmelt, G., et al. (2000). Cloning and characterization of the murine glucosamine-6-phosphate acetyltransferase EMeg32. Differential expression and intracellular membrane association. J. Biol. Chem. 275, 12821-12832.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12821-12832
    • Boehmelt, G.1
  • 4
    • 0037084028 scopus 로고    scopus 로고
    • Role of the ubiquitin-selective CDC48UFD1/NPL4 chaperone (segregase) in ERAD of OLE1 and other substrates
    • Braun, S., Matuschewski, K., Rape, M., Thoms, S., and Jentsch, S. (2002). Role of the ubiquitin-selective CDC48UFD1/NPL4 chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J. 21, 615-621.
    • (2002) EMBO J. , vol.21 , pp. 615-621
    • Braun, S.1    Matuschewski, K.2    Rape, M.3    Thoms, S.4    Jentsch, S.5
  • 5
    • 0029328549 scopus 로고
    • A 200-amino acid ATPase module in search of a basic function
    • Confalonieri, F., and Duguet, M. (1995). A 200-amino acid ATPase module in search of a basic function. Bioessays 17, 639-650.
    • (1995) Bioessays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 7
    • 15444361471 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein, an ATPase co-purified with IκBα and 26 S proteasome, in ubiquitin-proteasome-iibiqui tin-protea some-mediated degradation of IκBα
    • Dai, R.M., Chen, E., Longo, D.L., Gorbea, C.M., and Li, C.-C.H. (1998). Involvement of valosin-containing protein, an ATPase co-purified with IκBα and 26 S proteasome, in ubiquitin-proteasome-iibiqui tin-protea some-mediated degradation of IκBα. J. Biol. Chem. 273, 3562-3573.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3562-3573
    • Dai, R.M.1    Chen, E.2    Longo, D.L.3    Gorbea, C.M.4    Li, C.-C.H.5
  • 8
    • 0034907973 scopus 로고    scopus 로고
    • Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation
    • Dai, R.M., and Li. C.-C.H. (2001). Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nat. Cell Biol. 3, 740-744.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 740-744
    • Dai, R.M.1    Li, C.-C.H.2
  • 9
    • 0032440124 scopus 로고    scopus 로고
    • Cell vacuolization induced by Helicobacter pylori VacA toxin: Cell line sensitivity and quantitative estimation
    • de Bernard, M., Moschioni, M., Papini, E., Telford, J., Rappuoli, R., and Montecucco, C. (1998). Cell vacuolization induced by Helicobacter pylori VacA toxin: cell line sensitivity and quantitative estimation. Toxicol. Lett. 99, 109-115.
    • (1998) Toxicol. Lett. , vol.99 , pp. 109-115
    • De Bernard, M.1    Moschioni, M.2    Papini, E.3    Telford, J.4    Rappuoli, R.5    Montecucco, C.6
  • 10
    • 0029904102 scopus 로고    scopus 로고
    • Nuclear transport defects and nuclear envelope alterations are associated with mutation of the Saccharomyces cerevisiae NPL4 gene
    • DeHoratius, C., and Silver, P.A. (1996). Nuclear transport defects and nuclear envelope alterations are associated with mutation of the Saccharomyces cerevisiae NPL4 gene. Mol. Biol. Cell 7, 1835-1855.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1835-1855
    • DeHoratius, C.1    Silver, P.A.2
  • 11
    • 0026660330 scopus 로고
    • VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation
    • Egerton, M., Ashe, O.R., Chen, D., Druker, B.J., Burgess, W.H., and Samelson, L.E. (1992). VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation. EMBO J. 11, 3533-3540.
    • (1992) EMBO J. , vol.11 , pp. 3533-3540
    • Egerton, M.1    Ashe, O.R.2    Chen, D.3    Druker, B.J.4    Burgess, W.H.5    Samelson, L.E.6
  • 12
    • 0029814693 scopus 로고    scopus 로고
    • Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae
    • Ghislain, M., Dohmen, R.J., Levy, F., and Varshavsky, A. (1996). Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae. EMBO J. 15, 4884-4899.
    • (1996) EMBO J. , vol.15 , pp. 4884-4899
    • Ghislain, M.1    Dohmen, R.J.2    Levy, F.3    Varshavsky, A.4
  • 13
    • 0032825282 scopus 로고    scopus 로고
    • The Janus face of the archaeal Cdc48/p97 homologue VAT: Protein folding versus unfolding
    • Golbik, R., Lupas, A.N., Koretke, K.K., Baumeister, W., and Peters, J. (1999). The Janus face of the archaeal Cdc48/p97 homologue VAT: protein folding versus unfolding. J. Biol. Chem. 380, 1049-1062.
    • (1999) J. Biol. Chem. , vol.380 , pp. 1049-1062
    • Golbik, R.1    Lupas, A.N.2    Koretke, K.K.3    Baumeister, W.4    Peters, J.5
  • 14
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P.I., Roth, R., Morisaki, H., Jahn, R., and Heuser, J.E. (1997). Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90, 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 15
    • 0034607967 scopus 로고    scopus 로고
    • Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking
    • Hatsuzawa, K., Hirose, H., Tani, K., Yamamoto, A., Scheller, R.H., and Tagaya, M. (2000). Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking. J. Biol. Chem. 275, 13713-13720.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13713-13720
    • Hatsuzawa, K.1    Hirose, H.2    Tani, K.3    Yamamoto, A.4    Scheller, R.H.5    Tagaya, M.6
  • 17
    • 0034772572 scopus 로고    scopus 로고
    • VCP/p97 in abnormal protein aggregates, cytoplasmic vacuoles, and cell death, phenotypes relevant to neurodegeneration
    • Hirabayashi, M., et al. (2001). VCP/p97 in abnormal protein aggregates, cytoplasmic vacuoles, and cell death, phenotypes relevant to neurodegeneration. Cell Death Diff. 8, 977-984.
    • (2001) Cell Death Diff. , vol.8 , pp. 977-984
    • Hirabayashi, M.1
  • 18
    • 0034746779 scopus 로고    scopus 로고
    • The conserved Np14 protein complex mediates proteasome-dependent membrane-bound transcription factor activation
    • Hitchcock, A.L., Krebber, H., Frietze, S., Lin, A., Latterich, M., and Silver, P.A. (2001). The conserved Np14 protein complex mediates proteasome-dependent membrane-bound transcription factor activation. Mol. Biol. Cell 12, 3226-3241.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3226-3241
    • Hitchcock, A.L.1    Krebber, H.2    Frietze, S.3    Lin, A.4    Latterich, M.5    Silver, P.A.6
  • 20
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E.S., Ma, P.C., Ota, I.M., and Varshavsky, A. (1995). A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270, 17442-17456.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 21
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H.D., Mayer, T.U., and Jentsch, S. (1999). A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96, 635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 22
    • 0023111691 scopus 로고
    • Use of a cDNA clone to identify a supposed precursor protein containing valosin
    • Koller, K.J., and Brownstein, M.J. (1987). Use of a cDNA clone to identify a supposed precursor protein containing valosin. Nature 325, 542-545.
    • (1987) Nature , vol.325 , pp. 542-545
    • Koller, K.J.1    Brownstein, M.J.2
  • 24
    • 0029122698 scopus 로고
    • Membrane fusion and the cell cylce: Cdc48p participates in the fusion of ER membranes
    • Latterich, M., Frohlich, K.-U., and Schekman, R. (1995). Membrane fusion and the cell cylce: Cdc48p participates in the fusion of ER membranes. Cell 82, 885-893.
    • (1995) Cell , vol.82 , pp. 885-893
    • Latterich, M.1    Frohlich, K.-U.2    Schekman, R.3
  • 26
    • 0344614600 scopus 로고    scopus 로고
    • Identification of TER94, an AAA ATPase protein, as a Bam-dependent component of the Drosophila fusome
    • Leon, A., and McKearin, D. (1999). Identification of TER94, an AAA ATPase protein, as a Bam-dependent component of the Drosophila fusome. Mol. Biol. Cell 10, 3825-3834.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3825-3834
    • Leon, A.1    McKearin, D.2
  • 27
    • 0033602381 scopus 로고    scopus 로고
    • Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease
    • Leonhard, K., Stiegler, A., Neupert, W., and Langer, T. (1999). Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease. Nature 398, 348-351.
    • (1999) Nature , vol.398 , pp. 348-351
    • Leonhard, K.1    Stiegler, A.2    Neupert, W.3    Langer, T.4
  • 28
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas, A., Van Dyke, M., and Stock, J. (1991). Predicting coiled coils from protein sequences. Science 252, 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 29
    • 0023202836 scopus 로고
    • Cytochrome P-450 and NADPH-cytochrome P450 reductase are degraded in the autolysosomes in rat liver
    • Masaki, R., Yamamoto, A., and Tashiro, Y. (1987). Cytochrome P-450 and NADPH-cytochrome P450 reductase are degraded in the autolysosomes in rat liver. J. Cell Biol. 104, 1207-1215.
    • (1987) J. Cell Biol. , vol.104 , pp. 1207-1215
    • Masaki, R.1    Yamamoto, A.2    Tashiro, Y.3
  • 30
    • 0033163807 scopus 로고    scopus 로고
    • Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein
    • May, A.P., Misura, K.M., Whiteheart, S.W., and Weis, W.I. (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
  • 31
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian Ufdl and Np14 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer, H.H., Shorter, J.G., Seemann, J., Pappin, D., and Warren, G. (2000). A complex of mammalian Ufdl and Np14 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
  • 33
    • 0028802295 scopus 로고
    • Each domain of the N-ethylmaleimide-sensitive fusion protein contributes to its transport activity
    • Nagiec, E.E., Bernstein, A., and Whiteheart, S.W. (1995). Each domain of the N-ethylmaleimide-sensitive fusion protein contributes to its transport activity. J. Biol. Chem. 270, 29182-29188.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29182-29188
    • Nagiec, E.E.1    Bernstein, A.2    Whiteheart, S.W.3
  • 34
    • 0034097137 scopus 로고    scopus 로고
    • Syntaxin 7 mediates endocytic trafficking to late endosomes
    • Nakamura, N., Yamamoto, A., Wada, Y., and Futai, M. (2000). Syntaxin 7 mediates endocytic trafficking to late endosomes. J. Biol. Chem. 275, 6523-6529.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6523-6529
    • Nakamura, N.1    Yamamoto, A.2    Wada, Y.3    Futai, M.4
  • 35
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A.F., Aravind, L., Spouge, J.L., and Koonin, E.V. (1999). AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 36
    • 0034885052 scopus 로고    scopus 로고
    • + superfamily ATPases: Common structure-diverse function
    • + superfamily ATPases: common structure-diverse function. Genes Cells 6, 575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 37
    • 0031973716 scopus 로고    scopus 로고
    • The AAA team: Related ATPases with diverse functions
    • Patel, S., and Latterich, M. (1998). The AAA team: related ATPases with diverse functions. Trends Cell Biol. 8, 65-71.
    • (1998) Trends Cell Biol. , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 38
    • 0027493180 scopus 로고
    • Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein
    • Pleasure, I.T., Black, M.M., and Keen, J.H. (1993). Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein. Nature 365, 459-462.
    • (1993) Nature , vol.365 , pp. 459-462
    • Pleasure, I.T.1    Black, M.M.2    Keen, J.H.3
  • 39
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich, E., Kerem, A., Frohlich, K.U., Diamant, N., and 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
  • 40
    • 0032489499 scopus 로고    scopus 로고
    • Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro
    • Rabouille, C., Kondo, H., Newman, R., Hui, N., Freemont, P., and Warren, G. (1998). Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro. Cell 92, 603-610.
    • (1998) Cell , vol.92 , pp. 603-610
    • Rabouille, C.1    Kondo, H.2    Newman, R.3    Hui, N.4    Freemont, P.5    Warren, G.6
  • 41
    • 0029089959 scopus 로고
    • An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments
    • Rabouille, C., Levine, T.P., Peters, J.M., and 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
  • 45
    • 0034651727 scopus 로고    scopus 로고
    • Membrane fusion proteins are required for oskar mRNA localization in the Drosophila egg chamber
    • Ruden, D.M., Sollars, V., Wang, X., Mori, D., Alterman, M., and Lu, X. (2000). Membrane fusion proteins are required for oskar mRNA localization in the Drosophila egg chamber. Dev. Biol. 218, 314-325.
    • (2000) Dev. Biol. , vol.218 , pp. 314-325
    • Ruden, D.M.1    Sollars, V.2    Wang, X.3    Mori, D.4    Alterman, M.5    Lu, X.6
  • 46
    • 0027943759 scopus 로고
    • Tyrosine phosphorylation of VCP, the mammalian homologue of the Saccharomyces cerevisiae CDC48 protein, is unusually sensitive to stimulation by sodium vanadate and hydrogen peroxide
    • Schulte, R.J., Campbell, M.A., Fischer, W.H., and Sefton, B.M. (1994). Tyrosine phosphorylation of VCP, the mammalian homologue of the Saccharomyces cerevisiae CDC48 protein, is unusually sensitive to stimulation by sodium vanadate and hydrogen peroxide. J. Immunol. 153, 5465-5472.
    • (1994) J. Immunol. , vol.153 , pp. 5465-5472
    • Schulte, R.J.1    Campbell, M.A.2    Fischer, W.H.3    Sefton, B.M.4
  • 47
    • 0033451992 scopus 로고    scopus 로고
    • Synergistic roles for Pim-1, and c-Myc in STAT3-mediated cell cycle progression, and antiapoptosis
    • Shirogane, T., Fukada, T., Muller, J.M., Shima, D.T., Hibi, M., and Hirano, T. (1999). Synergistic roles for Pim-1, and c-Myc in STAT3-mediated cell cycle progression, and antiapoptosis. Immunity 11, 709-719.
    • (1999) Immunity , vol.11 , pp. 709-719
    • Shirogane, T.1    Fukada, T.2    Muller, J.M.3    Shima, D.T.4    Hibi, M.5    Hirano, T.6
  • 49
    • 0029671426 scopus 로고    scopus 로고
    • 2+-ATP-induced release of N-ethylmaleimide-sensitive factor from the Golgi apparatus in digitonin-permeabilized PC12 cells
    • 2+-ATP-induced release of N-ethylmaleimide-sensitive factor from the Golgi apparatus in digitonin-permeabilized PC12 cells. J. Biol. Chem. 271, 466-470.
    • (1996) J. Biol. Chem. , vol.271 , pp. 466-470
    • Tagaya, M.1    Furuno, A.2    Mizushima, S.3
  • 50
    • 0027474007 scopus 로고
    • Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport
    • Tagaya, M., Wilson, D.W., Brunner, M., Arango, N., and Rothman, J.E. (1993). Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport. J. Biol. Chem. 268, 2662-2666.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2662-2666
    • Tagaya, M.1    Wilson, D.W.2    Brunner, M.3    Arango, N.4    Rothman, J.E.5
  • 51
    • 0028789982 scopus 로고
    • Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins
    • Tanaka, M., Gupta, R., and Mayer, B.J. (1995). Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins. Mol. Cell. Biol. 15, 6829-6837.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6829-6837
    • Tanaka, M.1    Gupta, R.2    Mayer, B.J.3
  • 52
    • 0034632063 scopus 로고    scopus 로고
    • AAA proteins: Lords of the ring
    • Vale, R.D. (2000). AAA proteins: lords of the ring. J. Cell Biol. 150, F13-F20.
    • (2000) J. Cell Biol. , vol.150
    • Vale, R.D.1
  • 53
    • 0033621043 scopus 로고    scopus 로고
    • Protein-protein interaction between the testis brain RNA-binding protein and the transitional endoplasmic reticulum ATPase, a cytoskeletal γ actin and Trax in male germ cells and the brain
    • Wu, X.-Q., Lefrancois, S., Morales, C., and Hecht, N.B. (1999). Protein-protein interaction between the testis brain RNA-binding protein and the transitional endoplasmic reticulum ATPase, a cytoskeletal γ actin and Trax in male germ cells and the brain. Biochemistry 38, 11261-11270.
    • (1999) Biochemistry , vol.38 , pp. 11261-11270
    • Wu, X.-Q.1    Lefrancois, S.2    Morales, C.3    Hecht, N.B.4
  • 54
    • 0033959478 scopus 로고    scopus 로고
    • p97 ATPase, an ATPase involved in membrane fusion, interacts with DNA unwinding factor (DUF) that functions in DNA replication
    • Yamada, T., Okuhara, K., Iwamatsu, A., Seo, H., Ohta, K., Shibata, T., and Murofushi, H. (2000). p97 ATPase, an ATPase involved in membrane fusion, interacts with DNA unwinding factor (DUF) that functions in DNA replication. FEBS Lett. 466, 287-291.
    • (2000) FEBS Lett. , vol.466 , pp. 287-291
    • Yamada, T.1    Okuhara, K.2    Iwamatsu, A.3    Seo, H.4    Ohta, K.5    Shibata, T.6    Murofushi, H.7
  • 55
    • 0030754817 scopus 로고    scopus 로고
    • Possible involvement of heterotrimeric G proteins in the organization of the Golgi apparatus
    • Yamaguchi, T., Yamamoto, A., Furuno, A., Hatsuzawa, K., Tani, K., Himeno, M., and Tagaya, M. (1997). Possible involvement of heterotrimeric G proteins in the organization of the Golgi apparatus. J. Biol. Chem. 272, 25260-25266.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25260-25266
    • Yamaguchi, T.1    Yamamoto, A.2    Furuno, A.3    Hatsuzawa, K.4    Tani, K.5    Himeno, M.6    Tagaya, M.7
  • 56
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., Meyer, H.H., and Rapoport, T.A. (2001). The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414, 652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 57
    • 0034548716 scopus 로고    scopus 로고
    • Involvement of the ubiquitin-proteasome pathway in the degradation of nontyrosine kinase-type cytokine receptors of IL-9, IL-2, and erythropoietin
    • Yen, C.H., Yang, Y.C., Ruscetti, S.K., Kirken, R.A., Dai, R.M., and Li, C.-C.H. (2000). Involvement of the ubiquitin-proteasome pathway in the degradation of nontyrosine kinase-type cytokine receptors of IL-9, IL-2, and erythropoietin. J. Immunol. 165, 6372-6380.
    • (2000) J. Immunol. , vol.165 , pp. 6372-6380
    • Yen, C.H.1    Yang, Y.C.2    Ruscetti, S.K.3    Kirken, R.A.4    Dai, R.M.5    Li, C.-C.H.6
  • 58
    • 0033165864 scopus 로고    scopus 로고
    • NSF N-terminal domain crystal structure: Models of NSF fusion
    • Yu, R.C., Jahn, R., and Brunger, A.T. (1999). NSF N-terminal domain crystal structure: models of NSF fusion. Mol. Cell 4, 97-107.
    • (1999) Mol. Cell , vol.4 , pp. 97-107
    • Yu, R.C.1    Jahn, R.2    Brunger, A.T.3
  • 59
    • 0028587687 scopus 로고
    • Isolation and characterization of the principal ATPase associated with transitional endoplasmic reticulum
    • Zhang, L., Ashendel, C.L., Becker, G.W., and Morre, J. (1994). Isolation and characterization of the principal ATPase associated with transitional endoplasmic reticulum. J. Cell Biol. 127, 1871-1883.
    • (1994) J. Cell Biol. , vol.127 , pp. 1871-1883
    • Zhang, L.1    Ashendel, C.L.2    Becker, G.W.3    Morre, J.4
  • 60
    • 0034502514 scopus 로고    scopus 로고
    • Structure of the AAA ATPase p97
    • Zhang, X., et al. (2000a). Structure of the AAA ATPase p97. Mol. Cell 6, 1473-1484.
    • (2000) Mol. Cell , vol.6 , pp. 1473-1484
    • Zhang, X.1
  • 61
    • 0033855808 scopus 로고    scopus 로고
    • VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells
    • Zhang, H., Wang, Q., Kajino, K., and Greene, M.I. (2000b). VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells. DNA Cell Biol. 19, 253-263.
    • (2000) DNA Cell Biol. , vol.19 , pp. 253-263
    • Zhang, H.1    Wang, Q.2    Kajino, K.3    Greene, M.I.4


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