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Volumn 40, Issue 12, 2008, Pages 2927-2942

Ubxd1 is a novel co-factor of the human p97 ATPase

Author keywords

AAA ATPase; Degradation; p97; Proteasome; Ubiquitin

Indexed keywords

PROTEIN P47; PROTEIN P97; SMALL INTERFERING RNA; TYROSINE; UBIQUITIN; UBX DOMAIN CONTAINING 1; UNCLASSIFIED DRUG;

EID: 51249108640     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2008.06.008     Document Type: Article
Times cited : (39)

References (56)
  • 1
    • 33748752425 scopus 로고    scopus 로고
    • The PUB domain functions as a p97 binding module in human peptide N-glycanase
    • Allen M.D., Buchberger A., and Bycroft M. The PUB domain functions as a p97 binding module in human peptide N-glycanase. J Biol Chem 281 (2006) 25502-25508
    • (2006) J Biol Chem , vol.281 , pp. 25502-25508
    • Allen, M.D.1    Buchberger, A.2    Bycroft, M.3
  • 2
    • 33646582995 scopus 로고    scopus 로고
    • Conformational changes in the AAA ATPase p97-p47 adaptor complex
    • Beuron F., Dreveny I., Yuan X., Pye V.E., McKeown C., Briggs L.C., et al. Conformational changes in the AAA ATPase p97-p47 adaptor complex. EMBO J 25 (2006) 1967-1976
    • (2006) EMBO J , vol.25 , pp. 1967-1976
    • Beuron, F.1    Dreveny, I.2    Yuan, X.3    Pye, V.E.4    McKeown, C.5    Briggs, L.C.6
  • 4
    • 0035951636 scopus 로고    scopus 로고
    • Identification and characterization of UBXD1, a novel UBX domain-containing gene on human chromosome 19p13, and its mouse ortholog
    • Carim-Todd L., Escarceller M., Estivill X., and Sumoy L. Identification and characterization of UBXD1, a novel UBX domain-containing gene on human chromosome 19p13, and its mouse ortholog. Biochim Biophys Acta 1517 (2001) 298-301
    • (2001) Biochim Biophys Acta , vol.1517 , pp. 298-301
    • Carim-Todd, L.1    Escarceller, M.2    Estivill, X.3    Sumoy, L.4
  • 5
    • 0036143156 scopus 로고    scopus 로고
    • Systematic identification of novel protein domain families associated with nuclear functions
    • Doerks T., Copley R.R., Schultz J., Ponting C.P., and Bork P. Systematic identification of novel protein domain families associated with nuclear functions. Genome Res 12 (2002) 47-56
    • (2002) Genome Res , vol.12 , pp. 47-56
    • Doerks, T.1    Copley, R.R.2    Schultz, J.3    Ponting, C.P.4    Bork, P.5
  • 6
    • 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., and Freemont P.S. Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47. EMBO J 23 (2004) 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
  • 7
    • 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. VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in response to T cell antigen receptor activation. EMBO J 11 (1992) 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
  • 8
    • 0037501375 scopus 로고    scopus 로고
    • Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation
    • Ficarro S., Chertihin O., Westbrook V.A., White F., Jayes F., Kalab P., et al. Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation. J Biol Chem 278 (2003) 11579-11589
    • (2003) J Biol Chem , vol.278 , pp. 11579-11589
    • Ficarro, S.1    Chertihin, O.2    Westbrook, V.A.3    White, F.4    Jayes, F.5    Kalab, P.6
  • 9
    • 0036303981 scopus 로고    scopus 로고
    • Hassles with taking out the garbage: aggravating aggresomes
    • Garcia-Mata R., Gao Y.S., and Sztul E. Hassles with taking out the garbage: aggravating aggresomes. Traffic 3 (2002) 388-396
    • (2002) Traffic , vol.3 , pp. 388-396
    • Garcia-Mata, R.1    Gao, Y.S.2    Sztul, E.3
  • 10
    • 33745224935 scopus 로고    scopus 로고
    • p97: the cell's molecular purgatory?
    • Halawani D., and Latterich M. p97: the cell's molecular purgatory?. Mol Cell 22 (2006) 713-717
    • (2006) Mol Cell , vol.22 , pp. 713-717
    • Halawani, D.1    Latterich, M.2
  • 11
    • 2342511583 scopus 로고    scopus 로고
    • The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and nonproteolytic ubiquitin-dependent processes
    • Hartmann-Petersen R., Wallace M., Hofmann K., Koch G., Johnsen A.H., Hendil K.B., et al. The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and nonproteolytic ubiquitin-dependent processes. Curr Biol 14 (2004) 824-828
    • (2004) Curr Biol , vol.14 , pp. 824-828
    • Hartmann-Petersen, R.1    Wallace, M.2    Hofmann, K.3    Koch, G.4    Johnsen, A.H.5    Hendil, K.B.6
  • 12
    • 27644438676 scopus 로고    scopus 로고
    • Development and use of antiproteasome monoclonal antibodies
    • Hendil K.B. Development and use of antiproteasome monoclonal antibodies. Methods Enzymol 398 (2005) 439-453
    • (2005) Methods Enzymol , vol.398 , pp. 439-453
    • Hendil, K.B.1
  • 14
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • Hofmann K., and Bucher P. The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem Sci 21 (1996) 172-173
    • (1996) Trends Biochem Sci , vol.21 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 15
    • 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. Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102 (2000) 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
  • 17
    • 0036173013 scopus 로고    scopus 로고
    • Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
    • Jarosch E., Taxis C., Volkwein C., Bordallo J., Finley D., Wolf D.H., et al. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 4 (2002) 134-139
    • (2002) Nat Cell Biol , vol.4 , pp. 134-139
    • Jarosch, E.1    Taxis, C.2    Volkwein, C.3    Bordallo, J.4    Finley, D.5    Wolf, D.H.6
  • 18
    • 33845939821 scopus 로고    scopus 로고
    • Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway?
    • Jentsch S., and Rumpf S. Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway?. Trends Biochem Sci 32 (2007) 6-11
    • (2007) Trends Biochem Sci , vol.32 , pp. 6-11
    • Jentsch, S.1    Rumpf, S.2
  • 19
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: a cellular response to misfolded proteins
    • Johnston J.A., Ward C.L., and Kopito R.R. Aggresomes: a cellular response to misfolded proteins. J Cell Biol 143 (1998) 1883-1898
    • (1998) J Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 20
  • 22
    • 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. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96 (1999) 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
  • 24
    • 0037566901 scopus 로고    scopus 로고
    • For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection
    • Kostova Z., and Wolf D.H. For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J 22 (2003) 2309-2317
    • (2003) EMBO J , vol.22 , pp. 2309-2317
    • Kostova, Z.1    Wolf, D.H.2
  • 25
    • 0029122698 scopus 로고
    • Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes
    • Latterich M., Fröhlich K.U., and Schekman R. Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes. Cell 82 (1995) 885-893
    • (1995) Cell , vol.82 , pp. 885-893
    • Latterich, M.1    Fröhlich, K.U.2    Schekman, R.3
  • 26
    • 0034610335 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of p97 regulates transitional endoplasmic reticulum assembly in vitro
    • Lavoie C., Chevet E., Roy L., Tonks N.K., Fazel A., Posner B.I., et al. Tyrosine phosphorylation of p97 regulates transitional endoplasmic reticulum assembly in vitro. Proc Natl Acad Sci USA 97 (2000) 13637-13642
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13637-13642
    • Lavoie, C.1    Chevet, E.2    Roy, L.3    Tonks, N.K.4    Fazel, A.5    Posner, B.I.6
  • 27
    • 27644581602 scopus 로고    scopus 로고
    • Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome
    • Li G., Zhou X., Zhao G., Schindelin H., and Lennarz W.J. Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome. Proc Natl Acad Sci USA 102 (2005) 15809-15814
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15809-15814
    • Li, G.1    Zhou, X.2    Zhao, G.3    Schindelin, H.4    Lennarz, W.J.5
  • 28
    • 33744817103 scopus 로고    scopus 로고
    • The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor
    • Li G., Zhao G., Zhou X., Schindelin H., and Lennarz W.J. The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor. Proc Natl Acad Sci USA 103 (2006) 8348-8353
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8348-8353
    • Li, G.1    Zhao, G.2    Zhou, X.3    Schindelin, H.4    Lennarz, W.J.5
  • 29
    • 33750472289 scopus 로고    scopus 로고
    • Characterization of erasin (UBXD2): a new ER protein that promotes ER-associated protein degradation
    • Liang J., Yin C., Doong H., Fang S., Peterhoff C., Nixon R.A., et al. Characterization of erasin (UBXD2): a new ER protein that promotes ER-associated protein degradation. J Cell Sci 119 (2006) 4011-4024
    • (2006) J Cell Sci , vol.119 , pp. 4011-4024
    • Liang, J.1    Yin, C.2    Doong, H.3    Fang, S.4    Peterhoff, C.5    Nixon, R.A.6
  • 30
    • 20044383388 scopus 로고    scopus 로고
    • p25alpha stimulates alpha-synuclein aggregation and is co-localized with aggregated alpha-synuclein in alpha-synucleinopathies
    • Lindersson E., Lundvig D., Petersen C., Madsen P., Nyengaard J.R., Højrup P., et al. p25alpha stimulates alpha-synuclein aggregation and is co-localized with aggregated alpha-synuclein in alpha-synucleinopathies. J Biol Chem 280 (2005) 5703-5715
    • (2005) J Biol Chem , vol.280 , pp. 5703-5715
    • Lindersson, E.1    Lundvig, D.2    Petersen, C.3    Madsen, P.4    Nyengaard, J.R.5    Højrup, P.6
  • 31
    • 24744434431 scopus 로고    scopus 로고
    • Valosin-containing protein phosphorylation at Ser784 in response to DNA damage
    • Livingstone M., Ruan H., Weiner J., Clauser K.R., Strack P., Jin S., et al. Valosin-containing protein phosphorylation at Ser784 in response to DNA damage. Cancer Res 65 (2005) 7533-7540
    • (2005) Cancer Res , vol.65 , pp. 7533-7540
    • Livingstone, M.1    Ruan, H.2    Weiner, J.3    Clauser, K.R.4    Strack, P.5    Jin, S.6
  • 32
    • 0031932987 scopus 로고    scopus 로고
    • Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of Cdc48p
    • Madeo F., Schlauer J., Zischka H., Mecke D., and Fröhlich K.U. Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of Cdc48p. Mol Biol Cell 9 (1998) 131-141
    • (1998) Mol Biol Cell , vol.9 , pp. 131-141
    • Madeo, F.1    Schlauer, J.2    Zischka, H.3    Mecke, D.4    Fröhlich, K.U.5
  • 33
    • 10644266779 scopus 로고    scopus 로고
    • A novel UBA and UBX domain protein that binds polyubiquitin and VCP and is a substrate for SAPKs
    • McNeill H., Knebel A., Arthur J.S., Cuenda A., and Cohen P. A novel UBA and UBX domain protein that binds polyubiquitin and VCP and is a substrate for SAPKs. Biochem J 384 (2004) 391-400
    • (2004) Biochem J , vol.384 , pp. 391-400
    • McNeill, H.1    Knebel, A.2    Arthur, J.S.3    Cuenda, A.4    Cohen, P.5
  • 34
    • 26444494585 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress compromises the ubiquitin-proteasome system
    • Menendez-Benito V., Verhoef L.G., Masucci M.G., and Dantuma N.P. Endoplasmic reticulum stress compromises the ubiquitin-proteasome system. Hum Mol Genet 14 (2005) 2787-2799
    • (2005) Hum Mol Genet , vol.14 , pp. 2787-2799
    • Menendez-Benito, V.1    Verhoef, L.G.2    Masucci, M.G.3    Dantuma, N.P.4
  • 36
    • 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. The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97. FEBS Lett 437 (1998) 255-257
    • (1998) FEBS Lett , vol.437 , pp. 255-257
    • Meyer, H.H.1    Kondo, H.2    Warren, G.3
  • 37
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer H.H., Shorter J.G., Seemann J., Pappin D., and Warren G. A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J 19 (2000) 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
  • 38
    • 34247106724 scopus 로고    scopus 로고
    • Protein domain-domain interactions and requirements for the negative regulation of Arabidopsis CDC48/p97 by the plant ubiquitin regulatory × (UBX) domain-containing protein, PUX1
    • Park S., Rancour D.M., and Bednarek S.Y. Protein domain-domain interactions and requirements for the negative regulation of Arabidopsis CDC48/p97 by the plant ubiquitin regulatory × (UBX) domain-containing protein, PUX1. J Biol Chem 282 (2007) 5217-5224
    • (2007) J Biol Chem , vol.282 , pp. 5217-5224
    • Park, S.1    Rancour, D.M.2    Bednarek, S.Y.3
  • 41
    • 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. Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 107 (2001) 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
  • 42
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly H., Rape M., Braun S., Rumpf S., Hoege C., and Jentsch S. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120 (2005) 73-84
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 43
    • 4444284299 scopus 로고    scopus 로고
    • Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation
    • Schuberth C., Richly H., Rumpf S., and Buchberger A. Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation. EMBO Rep 5 (2004) 818-824
    • (2004) EMBO Rep , vol.5 , pp. 818-824
    • Schuberth, C.1    Richly, H.2    Rumpf, S.3    Buchberger, A.4
  • 44
    • 27144539523 scopus 로고    scopus 로고
    • Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation
    • Schuberth C., and Buchberger A. Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation. Nat Cell Biol 7 (2005) 999-1006
    • (2005) Nat Cell Biol , vol.7 , pp. 999-1006
    • Schuberth, C.1    Buchberger, A.2
  • 45
    • 28144436887 scopus 로고    scopus 로고
    • The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway
    • Schulze A., Standera S., Buerger E., Kikkert M., van Voorden S., Wiertz E., et al. The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway. J Mol Biol 354 (2005) 1021-1027
    • (2005) J Mol Biol , vol.354 , pp. 1021-1027
    • Schulze, A.1    Standera, S.2    Buerger, E.3    Kikkert, M.4    van Voorden, S.5    Wiertz, E.6
  • 46
    • 0023736896 scopus 로고
    • Alpha 2-macroglobulin used to isolate intracellular endopeptidases from mammalian cells in culture
    • Slot L.A., and Hendil K.B. Alpha 2-macroglobulin used to isolate intracellular endopeptidases from mammalian cells in culture. Biochem J 255 (1988) 437-443
    • (1988) Biochem J , vol.255 , pp. 437-443
    • Slot, L.A.1    Hendil, K.B.2
  • 47
    • 14844340788 scopus 로고    scopus 로고
    • Human Fas-associated factor 1, interacting with ubiquitinated proteins and valosin-containing protein, is involved in the ubiquitin-proteasome pathway
    • Song E.J., Yim S.H., Kim E., Kim N.S., and Lee K.J. Human Fas-associated factor 1, interacting with ubiquitinated proteins and valosin-containing protein, is involved in the ubiquitin-proteasome pathway. Mol Cell Biol 25 (2005) 2511-2524
    • (2005) Mol Cell Biol , vol.25 , pp. 2511-2524
    • Song, E.J.1    Yim, S.H.2    Kim, E.3    Kim, N.S.4    Lee, K.J.5
  • 48
    • 0035850770 scopus 로고    scopus 로고
    • The PUB domain: a putative protein-protein interaction domain implicated in the ubiquitin-proteasome pathway
    • Suzuki T., Park H., Till E.A., and Lennarz W.J. The PUB domain: a putative protein-protein interaction domain implicated in the ubiquitin-proteasome pathway. Biochem Biophys Res Commun 287 (2001) 1083-1087
    • (2001) Biochem Biophys Res Commun , vol.287 , pp. 1083-1087
    • Suzuki, T.1    Park, H.2    Till, E.A.3    Lennarz, W.J.4
  • 49
    • 0037049466 scopus 로고    scopus 로고
    • VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo
    • Uchiyama K., Jokitalo E., Kano F., Murata M., Zhang X., Canas B., et al. VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo. J Cell Biol 159 (2002) 855-866
    • (2002) J Cell Biol , vol.159 , pp. 855-866
    • Uchiyama, K.1    Jokitalo, E.2    Kano, F.3    Murata, M.4    Zhang, X.5    Canas, B.6
  • 51
    • 0029909097 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis centers in HeLa cells: indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome
    • Wójcik C., Schroeter D., Wilk S., Lamprecht J., and Paweletz N. Ubiquitin-mediated proteolysis centers in HeLa cells: indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome. Eur J Cell Biol 71 (1996) 311-318
    • (1996) Eur J Cell Biol , vol.71 , pp. 311-318
    • Wójcik, C.1    Schroeter, D.2    Wilk, S.3    Lamprecht, J.4    Paweletz, N.5
  • 52
    • 18544394748 scopus 로고    scopus 로고
    • RNA interference of valosin-containing protein (VCP/p97) reveals multiple cellular roles linked to ubiquitin/proteasome-dependent proteolysis
    • Wójcik C., Yano M., and DeMartino G.N. RNA interference of valosin-containing protein (VCP/p97) reveals multiple cellular roles linked to ubiquitin/proteasome-dependent proteolysis. J Cell Sci 117 (2004) 281-292
    • (2004) J Cell Sci , vol.117 , pp. 281-292
    • Wójcik, C.1    Yano, M.2    DeMartino, G.N.3
  • 53
    • 33750528166 scopus 로고    scopus 로고
    • Valosin-containing protein (p97) is a regulator of endoplasmic reticulum stress and of the degradation of N-end rule and ubiquitin-fusion degradation pathway substrates in mammalian cells
    • Wójcik C., Rowicka M., Kudlicki A., Nowis D., McConnell E., Kujawa M., et al. Valosin-containing protein (p97) is a regulator of endoplasmic reticulum stress and of the degradation of N-end rule and ubiquitin-fusion degradation pathway substrates in mammalian cells. Mol Biol Cell 17 (2006) 4606-4618
    • (2006) Mol Biol Cell , vol.17 , pp. 4606-4618
    • Wójcik, C.1    Rowicka, M.2    Kudlicki, A.3    Nowis, D.4    McConnell, E.5    Kujawa, M.6
  • 54
    • 33749236210 scopus 로고    scopus 로고
    • Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase
    • Ye Y. Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase. J Struct Biol 156 (2006) 29-40
    • (2006) J Struct Biol , vol.156 , pp. 29-40
    • Ye, Y.1
  • 55
    • 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. VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells. DNA Cell Biol 19 (2000) 253-263
    • (2000) DNA Cell Biol , vol.19 , pp. 253-263
    • Zhang, H.1    Wang, Q.2    Kajino, K.3    Greene, M.I.4
  • 56
    • 34547419767 scopus 로고    scopus 로고
    • Studies on peptide:N-glycanse-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation
    • Zhao G., Zhou X., Wang L., Li G., Schindelin H., and Lennarz W.J. Studies on peptide:N-glycanse-p97 interaction suggest that p97 phosphorylation modulates endoplasmic reticulum-associated degradation. Proc Natl Acad Sci USA 104 (2007) 8785-8790
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8785-8790
    • Zhao, G.1    Zhou, X.2    Wang, L.3    Li, G.4    Schindelin, H.5    Lennarz, W.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.