메뉴 건너뛰기




Volumn 116, Issue 21, 2003, Pages 4283-4290

p97, a protein coping with multiple identities

Author keywords

AAA ATPase; Cdc48; Proteasome; SNARE; Ubiquitin

Indexed keywords

ADAPTOR PROTEIN; ADENOSINE TRIPHOSPHATASE; CELL PROTEIN; PROTEIN P47; PROTEIN P97; SNARE PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 0242635839     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00817     Document Type: Article
Times cited : (146)

References (88)
  • 1
    • 0037376172 scopus 로고    scopus 로고
    • Ubiquitin: Not just for proteasomes anymore
    • Aguilar, R. C. and Wendland, B. (2003). Ubiquitin: not just for proteasomes anymore. Curr. Opin. Cell Biol. 15, 184-190.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 184-190
    • Aguilar, R.C.1    Wendland, B.2
  • 2
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • Babst, M., Wendland, B., Estapa, E. J. and Emr, S. D. (1998). The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17, 2982-2993.
    • (1998) EMBO J. , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estapa, E.J.3    Emr, S.D.4
  • 3
    • 0036696804 scopus 로고    scopus 로고
    • ESCRT-III: An endosome-associated heterooligomeric protein complex required for MVB sorting
    • Babst, M., Katzmann, D. J., Estepa-Sabal, E. J., Meerloo, T. and Emr, S. D. (2002a). ESCRT-III: an endosome-associated heterooligomeric protein complex required for MVB sorting. Dev. Cell 3, 271-282.
    • (2002) Dev. Cell , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3    Meerloo, T.4    Emr, S.D.5
  • 4
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • Babst, M., Katzmann, D. J., Synder, W. B., Wendland, B. and Emr, S. D. (2002b). Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev. Cell 3, 283-289.
    • (2002) Dev. Cell , vol.3 , pp. 283-289
    • Babst, M.1    Katzmann, D.J.2    Synder, W.B.3    Wendland, B.4    Emr, S.D.5
  • 5
  • 7
    • 0344091553 scopus 로고    scopus 로고
    • Motions and negative cooperativity between p97 domains revealed by cryo-electron microscopy and quantised elastic deformational model
    • Beuron, F., Flynn, T. C., Ma, J., Kondo, H., Zhang, X. and Freemont, P. S. (2003). Motions and negative cooperativity between p97 domains revealed by cryo-electron microscopy and quantised elastic deformational model. J. Mol. Biol. 327, 619-629.
    • (2003) J. Mol. Biol. , vol.327 , pp. 619-629
    • Beuron, F.1    Flynn, T.C.2    Ma, J.3    Kondo, H.4    Zhang, X.5    Freemont, P.S.6
  • 8
    • 0036304360 scopus 로고    scopus 로고
    • The Vps27p-Hse1p complex binds ubiquitin and mediates endosomal protein sorting
    • Bilodeau, P. S., Urbanowski, J. L., Winistorfer, S. C. and Piper, R. C. (2002). The Vps27p-Hse1p complex binds ubiquitin and mediates endosomal protein sorting. Nat. Cell Biol. 4, 534-539.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 534-539
    • Bilodeau, P.S.1    Urbanowski, J.L.2    Winistorfer, S.C.3    Piper, R.C.4
  • 9
    • 0036544559 scopus 로고    scopus 로고
    • Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates
    • Bishop, N., Horman, A. and Woodman, P. (2002). Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates. J. Cell Biol. 157, 91-102.
    • (2002) J. Cell Biol. , vol.157 , pp. 91-102
    • Bishop, N.1    Horman, A.2    Woodman, P.3
  • 10
    • 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
  • 13
    • 0025359065 scopus 로고
    • SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast
    • Clary, D. O., Griff, I. C. and Rothman, J. E. (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
  • 14
    • 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
  • 15
    • 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
  • 16
    • 15444361471 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein, an ATPase co-purified with Ikappa Balpha and 26S Proteasome, in ubiquitin-proteasome-mediated degradation of Ikappa Balpha
    • 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 Ikappa Balpha and 26S Proteasome, in ubiquitin-proteasome-mediated degradation of Ikappa Balpha. 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
  • 17
    • 0035846895 scopus 로고    scopus 로고
    • Membrane traffic: What drives the AAA motor?
    • Dalal, S. and Hanson, P. I. (2001). Membrane traffic: what drives the AAA motor? Cell 104, 5-8.
    • (2001) Cell , vol.104 , pp. 5-8
    • Dalal, S.1    Hanson, P.I.2
  • 18
    • 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. (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.2
  • 19
    • 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
  • 20
    • 0035424237 scopus 로고    scopus 로고
    • ER quality control: Towards an understanding at the molecular level
    • Ellgaard, L. and Helenius, A. (2001). ER quality control: towards an understanding at the molecular level. Curr. Opin. Cell Biol. 13, 431-437.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 431-437
    • Ellgaard, L.1    Helenius, A.2
  • 21
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer, D., Sutton, R. B., Brunger, A. T. and Jahn, R. (1998). Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc. Natl. Acad. Sci. USA 95, 15781-15786.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 22
    • 0025913947 scopus 로고
    • Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation, and gene expression
    • Fröhlich, K.-U., Fries, H.-W., Rüdiger, M., Erdmann, R., Botstein, D. and Mecke, D. (1991). Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation, and gene expression. J. Cell Biol. 114, 443-453.
    • (1991) J. Cell Biol. , vol.114 , pp. 443-453
    • Fröhlich, K.-U.1    Fries, H.-W.2    Rüdiger, M.3    Erdmann, R.4    Botstein, D.5    Mecke, D.6
  • 24
    • 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., Lévy, 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    Lévy, F.3    Varshavsky, A.4
  • 25
    • 0037125983 scopus 로고    scopus 로고
    • Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors
    • Haglund, K., Shimokawa, N., Szymkiewicz, I. and Dikic, I. (2002). Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors. Proc. Natl. Acad. Sci. USA 99, 12191-12196.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12191-12196
    • Haglund, K.1    Shimokawa, N.2    Szymkiewicz, I.3    Dikic, I.4
  • 26
    • 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, R., 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, 523-536.
    • (1997) Cell , vol.90 , pp. 523-536
    • Hanson, P.I.1    Roth, R.2    Morisaki, R.3    Jahn, R.4    Heuser, J.E.5
  • 28
    • 0037043340 scopus 로고    scopus 로고
    • An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport
    • Haynes, C. M., Caldwell, S. and Cooper, A. A. (2002). An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport. J. Cell Biol. 158, 91-102.
    • (2002) J. Cell Biol. , vol.158 , pp. 91-102
    • Haynes, C.M.1    Caldwell, S.2    Cooper, A.A.3
  • 31
    • 0030700220 scopus 로고    scopus 로고
    • Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins
    • Hicke, L. (1997). Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins. FASEB J. 11, 1215-1226.
    • (1997) FASEB J. , vol.11 , pp. 1215-1226
    • Hicke, L.1
  • 32
    • 0035293622 scopus 로고    scopus 로고
    • Ubiquitin and proteasomes. Protein regulation by monoubiquitin
    • Hicke, L. (2001). Ubiquitin and proteasomes. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell. Biol. 2, 195-201.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 34
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. (1996). Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30, 405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 35
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
    • Hoppe, T., Matuschewski, K., Rape, M., Schlenker, S., Ulrich, H. D. and Jentsch, S. (2000). Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102, 577-586.
    • (2000) Cell , vol.102 , pp. 577-586
    • Hoppe, T.1    Matuschewski, K.2    Rape, M.3    Schlenker, S.4    Ulrich, H.D.5    Jentsch, S.6
  • 37
    • 0030863058 scopus 로고    scopus 로고
    • An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal
    • Hui, N., Nakamura, N., Sönnichsen, B., Shima, D. T., Nilsson, T. and Warren, G. (1997). An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal. Mol. Biol. Cell 8, 1777-1787.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1777-1787
    • Hui, N.1    Nakamura, N.2    Sönnichsen, B.3    Shima, D.T.4    Nilsson, T.5    Warren, G.6
  • 39
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-1
    • Katzmann, D. J., Babst, M. and Emr, S. D. (2001). Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-1. Cell 106, 145-155.
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 40
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann, D. J., Odorizzi, G. and Emr, S. D. (2002). Receptor downregulation and multivesicular-body sorting. Nat. Rev. Cell Mol. Biol. 3, 893-905.
    • (2002) Nat. Rev. Cell Mol. Biol. , vol.3 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 41
    • 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
  • 43
    • 0029122698 scopus 로고
    • Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes
    • Latterich, M., Frölich, K.-U. and Schekman, R. (1995). Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes. Cell 82, 885-893.
    • (1995) Cell , vol.82 , pp. 885-893
    • Latterich, M.1    Frölich, K.-U.2    Schekman, R.3
  • 44
    • 0033006355 scopus 로고    scopus 로고
    • Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis
    • Lustgarten, V. and Gerst, J. E. (1999). Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis. Mol. Cell. Biol. 19, 4480-4494.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4480-4494
    • Lustgarten, V.1    Gerst, J.E.2
  • 46
    • 0032561398 scopus 로고    scopus 로고
    • The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97
    • Meyer, H. H., Kondo, H. and Warren, G. (1998). The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97. FEBS Lett. 437, 255-257.
    • (1998) FEBS Lett. , vol.437 , pp. 255-257
    • Meyer, H.H.1    Kondo, H.2    Warren, G.3
  • 47
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian Ufd1 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 Ufd1 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
  • 48
    • 0036845476 scopus 로고    scopus 로고
    • Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4
    • Meyer, H. H., Wang, Y. and Warren, G. (2002). Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4. EMBO J. 21, 5645-5652.
    • (2002) EMBO J. , vol.21 , pp. 5645-5652
    • Meyer, H.H.1    Wang, Y.2    Warren, G.3
  • 49
    • 0028149757 scopus 로고
    • The ATPase activity of N-ethylmaleimide-sensitive fusion protein (NSF) is regulated by soluble NSF attachment proteins
    • Morgan, A., Dimaline, R. and Burgoyne, R. D. (1994). The ATPase activity of N-ethylmaleimide-sensitive fusion protein (NSF) is regulated by soluble NSF attachment proteins. J. Biol. Chem. 269, 29347-29350.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29347-29350
    • Morgan, A.1    Dimaline, R.2    Burgoyne, R.D.3
  • 51
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure-diverse function
    • Ogura, T. and Wilkinson, A. J. (2001). AAA+ 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
  • 52
    • 0030954439 scopus 로고    scopus 로고
    • Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of synaptic vesicles
    • Otto, H., Hanson, P. I. and Jahn, R. (1997). Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of synaptic vesicles. Proc. Natl. Acad. Sci. USA 94, 6120-6197.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6120-6197
    • Otto, H.1    Hanson, P.I.2    Jahn, R.3
  • 53
    • 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
  • 54
    • 0032489507 scopus 로고    scopus 로고
    • Organelle membrane fusion: A novel function for the syntaxin homolog Ufe1p in ER membrane fusion
    • Patel, S. K., Indig, F. E., Olivieri, N., Levine, N. D. and Latterich, M. (1998). Organelle membrane fusion: a novel function for the syntaxin homolog Ufe1p in ER membrane fusion. Cell 92, 611-620.
    • (1998) Cell , vol.92 , pp. 611-620
    • Patel, S.K.1    Indig, F.E.2    Olivieri, N.3    Levine, N.D.4    Latterich, M.5
  • 55
    • 0036284778 scopus 로고    scopus 로고
    • The anaphase-promoting complex: Proteolysis in mitosis and beyond
    • Peters, J. M. (2002). The anaphase-promoting complex: proteolysis in mitosis and beyond. Mol. Cell 9, 931-943.
    • (2002) Mol. Cell , vol.9 , pp. 931-943
    • Peters, J.M.1
  • 58
    • 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
  • 59
    • 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
  • 60
    • 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
  • 61
    • 0035977095 scopus 로고    scopus 로고
    • Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone
    • Rape, M., Hoppe, T., Gorr, I., Kalocay, M., Richly, H. and Jentsch, S. (2001). Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 107, 667-677.
    • (2001) Cell , vol.107 , pp. 667-677
    • Rape, M.1    Hoppe, T.2    Gorr, I.3    Kalocay, M.4    Richly, H.5    Jentsch, S.6
  • 62
    • 0036295232 scopus 로고    scopus 로고
    • Electron cryomicroscopy of VAT, the Archaeal p97/CDC48 homologue from Thermoplasma acidophilum
    • Rockel, B., Jakana, J., Chiu, W. and Baumeister, W. (2002). Electron cryomicroscopy of VAT, the Archaeal p97/CDC48 homologue from Thermoplasma acidophilum. J. Mol. Biol. 317, 673-681.
    • (2002) J. Mol. Biol. , vol.317 , pp. 673-681
    • Rockel, B.1    Jakana, J.2    Chiu, W.3    Baumeister, W.4
  • 63
    • 0028143698 scopus 로고
    • Mechanism of intracellular protein transport
    • Rothman, J. E. (1994). Mechanism of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 66
    • 0032579295 scopus 로고    scopus 로고
    • Role of vesicle-associated syntaxin 5 in the assembly of pre-Golgi intermediates
    • Rowe, A., Dascher, C., Bannykh, S., Plutner, H. and Balch, W. E. (1998). Role of vesicle-associated syntaxin 5 in the assembly of pre-Golgi intermediates. Science 279, 696-700.
    • (1998) Science , vol.279 , pp. 696-700
    • Rowe, A.1    Dascher, C.2    Bannykh, S.3    Plutner, H.4    Balch, W.E.5
  • 68
    • 0001417555 scopus 로고    scopus 로고
    • GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28
    • Sagiv, Y., Legesse-Miller, A., Porat, A. and Elazar, Z. (2000). GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28. EMBO J. 19, 1494-1504.
    • (2000) EMBO J. , vol.19 , pp. 1494-1504
    • Sagiv, Y.1    Legesse-Miller, A.2    Porat, A.3    Elazar, Z.4
  • 69
    • 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., Müller, 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    Müller, J.M.3    Shima, D.T.4    Hibi, M.5    Hirano, T.6
  • 70
  • 71
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Söllner, T., Bennett, M. K., Whiteheart, S. W., Scheller, R. H. and Rothman, J. E. (1993a). A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75, 409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 73
    • 0027058051 scopus 로고
    • Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum
    • Stirling, C., Rothblatt, J., Hosobuchi, M., Deshaies, R. and Schekman, R. (1992). Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. Biol. Cell 3, 129-142.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 129-142
    • Stirling, C.1    Rothblatt, J.2    Hosobuchi, M.3    Deshaies, R.4    Schekman, R.5
  • 74
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4Å resolution
    • Sutton, R. B., Fasshauer, D., Jahn, R. and Brünger, A. T. (1998). Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4Å resolution. Nature 395, 347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brünger, A.T.4
  • 75
    • 0031847684 scopus 로고    scopus 로고
    • Formation and turnover of NSF- and SNAP-containing "fusion" complexes occur on undocked, clathrin-coated vesicle-derived membranes
    • Swanton, E., Sheehan, J., Bishop, N., High, S. and Woodman, P. (1998). Formation and turnover of NSF- and SNAP-containing "fusion" complexes occur on undocked, clathrin-coated vesicle-derived membranes. Mol. Biol. Cell 9, 1633-1647.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1633-1647
    • Swanton, E.1    Sheehan, J.2    Bishop, N.3    High, S.4    Woodman, P.5
  • 76
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai, B., Ye, Y. and Rapoport, T. A. (2002). Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat. Rev. Mol. Cell Biol. 3, 246-255.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 78
    • 0037815483 scopus 로고    scopus 로고
    • The localization and phosphorylation of p47 are important for Golgi disassembly-assembly during the cell cycle
    • Uchiyama, K., Jokitalo, E., Lindman, M., Jackman, M., Kano, F., Murata, M., Zhang, X. and Kondo, H. (2003). The localization and phosphorylation of p47 are important for Golgi disassembly-assembly during the cell cycle. J. Cell Biol. 161, 1067-1079.
    • (2003) J. Cell Biol. , vol.161 , pp. 1067-1079
    • Uchiyama, K.1    Jokitalo, E.2    Lindman, M.3    Jackman, M.4    Kano, F.5    Murata, M.6    Zhang, X.7    Kondo, H.8
  • 81
    • 0035292759 scopus 로고    scopus 로고
    • Ubiquitin and proteasomes: Themes and variations on ubiquitylation
    • Weissman, A. M. (2001). Ubiquitin and proteasomes: themes and variations on ubiquitylation. Nat. Rev. Mol. Cell. Biol. 2, 169-178.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 82
    • 0028132782 scopus 로고
    • N-ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • Whiteheart, S. W., Rossnagel, K., Buhrow, S. A., Brunner, M., Jaenicke, R. and Rothman, J. E. (1994). N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J. Cell Biol. 126, 945-954.
    • (1994) J. Cell Biol. , vol.126 , pp. 945-954
    • Whiteheart, S.W.1    Rossnagel, K.2    Buhrow, S.A.3    Brunner, M.4    Jaenicke, R.5    Rothman, J.E.6
  • 83
    • 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
  • 84
    • 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
  • 85
    • 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, H. H. and Rapoport, T. A. (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
  • 86
    • 0035839113 scopus 로고    scopus 로고
    • Solution structure and interaction surface of the C-terminal domain from p47: A major p97-cofactor involved in SNARE disassembly
    • Yuan, X., Shaw, A., Zhang, X., Kondo, H., Lally, J., Freemont, P. S. and Matthews, S. (2001). Solution structure and interaction surface of the C-terminal domain from p47: a major p97-cofactor involved in SNARE disassembly. J. Mol. Biol. 311, 255-263.
    • (2001) J. Mol. Biol. , vol.311 , pp. 255-263
    • Yuan, X.1    Shaw, A.2    Zhang, X.3    Kondo, H.4    Lally, J.5    Freemont, P.S.6    Matthews, S.7
  • 87
    • 0028587687 scopus 로고
    • Isolation and characterisation of the principal ATPase associated with transitional endoplasmic reticulum of rat liver
    • Zhang, L., Ashendel, C. L., Becker, G. W. and Morré, D. J. (1994). Isolation and characterisation of the principal ATPase associated with transitional endoplasmic reticulum of rat liver. 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    Morré, D.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.