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Volumn 54, Issue , 2010, Pages 57-68

Control of deneddylation by the cop9 signalosome

Author keywords

[No Author keywords available]

Indexed keywords

CULLIN; MULTIPROTEIN COMPLEX; PEPTIDE HYDROLASE; UBIQUITIN;

EID: 84875369954     PISSN: 03060225     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-1-4419-6676-6_5     Document Type: Article
Times cited : (23)

References (104)
  • 1
    • 0027165193 scopus 로고
    • Cloning of a cDNA which encodes a novel ubiquitin-like protein
    • Kumar, S., Yoshida, Y., Noda, M. (1993) Cloning of a cDNA which encodes a novel ubiquitin-like protein. Biochem Biophys Res Commun 195: pp. 393-399
    • (1993) Biochem Biophys Res Commun , vol.195 , pp. 393-399
    • Kumar, S.1    Yoshida, Y.2    Noda, M.3
  • 2
    • 0034256031 scopus 로고    scopus 로고
    • Ubiquitin and its kin: How close are the family ties?
    • Jentsch, S., Pyrowolakis, G. (2000) Ubiquitin and its kin: how close are the family ties?. Trends Cell Biol 10: pp. 335-342
    • (2000) Trends Cell Biol , vol.10 , pp. 335-342
    • Jentsch, S.1    Pyrowolakis, G.2
  • 3
    • 0032522382 scopus 로고    scopus 로고
    • A novel protein modification pathway related to the ubiquitin system
    • Liakopoulos, D., Doenges, G., Matuschewski, K. (1998) A novel protein modification pathway related to the ubiquitin system. EMBO J 17: pp. 2208-2214
    • (1998) EMBO J , vol.17 , pp. 2208-2214
    • Liakopoulos, D.1    Doenges, G.2    Matuschewski, K.3
  • 4
    • 0034192005 scopus 로고    scopus 로고
    • Unified nomenclature for the COP9 signalosome and its subunits: An essential regulator of development
    • Deng, X.W., Dubiel, W., Wei, N. (2000) Unified nomenclature for the COP9 signalosome and its subunits: an essential regulator of development. Trends Genet 16: pp. 202-203
    • (2000) Trends Genet , vol.16 , pp. 202-203
    • Deng, X.W.1    Dubiel, W.2    Wei, N.3
  • 5
    • 0027022309 scopus 로고
    • COP9: A new genetic locus involved in light-regulated development and gene expression in arabidopsis
    • Wei, N., Deng, X.W. (1992) COP9: a new genetic locus involved in light-regulated development and gene expression in arabidopsis. Plant Cell 4: pp. 1507-1518
    • (1992) Plant Cell , vol.4 , pp. 1507-1518
    • Wei, N.1    Deng, X.W.2
  • 6
    • 0030581153 scopus 로고    scopus 로고
    • The COP9 complex, a novel multisubunit nuclear regulator involved in light control of a plant developmental switch
    • Chamovitz, D.A., Wei, N., Osterlund, M.T. (1996) The COP9 complex, a novel multisubunit nuclear regulator involved in light control of a plant developmental switch. Cell 86: pp. 115-121
    • (1996) Cell , vol.86 , pp. 115-121
    • Chamovitz, D.A.1    Wei, N.2    Osterlund, M.T.3
  • 7
    • 0032133073 scopus 로고    scopus 로고
    • Characterization and purification of the mammalian COP9 complex, a conserved nuclear regulator initially identified as a repressor of photomorphogenesis in higher plants
    • Wei, N., Deng, X.W. (1998) Characterization and purification of the mammalian COP9 complex, a conserved nuclear regulator initially identified as a repressor of photomorphogenesis in higher plants. Photochem Photobiol 68: pp. 237-241
    • (1998) Photochem Photobiol , vol.68 , pp. 237-241
    • Wei, N.1    Deng, X.W.2
  • 8
    • 0031921216 scopus 로고    scopus 로고
    • A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits
    • Seeger, M., Kraft, R., Ferrell, K. (1998) A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits. FASEB J 12: pp. 469-478
    • (1998) FASEB J , vol.12 , pp. 469-478
    • Seeger, M.1    Kraft, R.2    Ferrell, K.3
  • 9
    • 25444464111 scopus 로고    scopus 로고
    • Prediction of a common structural scaffold for proteasome lid, COP9-signalosome and eIF3 complexes
    • Scheel, H., Hofmann, K. (2005) Prediction of a common structural scaffold for proteasome lid, COP9-signalosome and eIF3 complexes. BMC Bioinformatics 6: pp. 71
    • (2005) BMC Bioinformatics , vol.6
    • Scheel, H.1    Hofmann, K.2
  • 10
    • 0034725525 scopus 로고    scopus 로고
    • Electron microscopy and subunit-subunit interaction studies reveal a first architecture of COP9 signalosome
    • Kapelari, B., Bech-Otschir, D., Hegerl, R. (2000) Electron microscopy and subunit-subunit interaction studies reveal a first architecture of COP9 signalosome. J Mol Biol 300: pp. 1169-1178
    • (2000) J Mol Biol , vol.300 , pp. 1169-1178
    • Kapelari, B.1    Bech-Otschir, D.2    Hegerl, R.3
  • 11
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
    • Glickman, M.H., Rubin, D.M., Coux, O. (1998) A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell 94: pp. 615-623
    • (1998) Cell , vol.94 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3
  • 12
    • 58149191374 scopus 로고    scopus 로고
    • Symmetrical modularity of the COP9 signalosome complex suggests its multifunctionality
    • Sharon, M., Mao, H., Boeri Erba, E. (2009) Symmetrical modularity of the COP9 signalosome complex suggests its multifunctionality. Structure 17: pp. 31-40
    • (2009) Structure , vol.17 , pp. 31-40
    • Sharon, M.1    Mao, H.2    Boeri Erba, E.3
  • 13
    • 46749125432 scopus 로고    scopus 로고
    • The Arabidopsis COP9 signalosome is essential for G2 phase progression and genomic stability
    • Dohmann, E.M., Levesque, M.P., Veylder, L. (2008) The Arabidopsis COP9 signalosome is essential for G2 phase progression and genomic stability. Development 135: pp. 2013-2022
    • (2008) Development , vol.135 , pp. 2013-2022
    • Dohmann, E.M.1    Levesque, M.P.2    Veylder, L.3
  • 14
    • 0038185375 scopus 로고    scopus 로고
    • Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and-independent mechanisms
    • Liu, C., Powell, K.A., Mundt, K. (2003) Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and-independent mechanisms. Genes Dev 17: pp. 1130-1140
    • (2003) Genes Dev , vol.17 , pp. 1130-1140
    • Liu, C.1    Powell, K.A.2    Mundt, K.3
  • 15
    • 0037509859 scopus 로고    scopus 로고
    • The ubiquitin ligase activity in the DD B2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage
    • Groisman, R., Polanowska, J., Kuraoka, I. (2003) The ubiquitin ligase activity in the DD B2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell 113: pp. 357-367
    • (2003) Cell , vol.113 , pp. 357-367
    • Groisman, R.1    Polanowska, J.2    Kuraoka, I.3
  • 16
    • 67650531886 scopus 로고    scopus 로고
    • Regulation of the anaphase-promoting complex by the COP9 signalosome
    • Kob, R., Kelm, J., Posorski, N. (2009) Regulation of the anaphase-promoting complex by the COP9 signalosome. Cell Cycle 8: pp. 2041-2049
    • (2009) Cell Cycle , vol.8 , pp. 2041-2049
    • Kob, R.1    Kelm, J.2    Posorski, N.3
  • 17
    • 64049106276 scopus 로고    scopus 로고
    • Revisiting the COP9 signalosome as a transcriptional regulator
    • Chamovitz, D.A. (2009) Revisiting the COP9 signalosome as a transcriptional regulator. EMBO Rep 10: pp. 352-358
    • (2009) EMBO Rep , vol.10 , pp. 352-358
    • Chamovitz, D.A.1
  • 18
    • 0036472506 scopus 로고    scopus 로고
    • The COP9 signalosome: At the interface between signal transduction and ubiquitin-dependent proteolysis
    • Bech-Otschir, D., Seeger, M., Dubiel, W. (2002) The COP9 signalosome: at the interface between signal transduction and ubiquitin-dependent proteolysis. J Cell Sci 115: pp. 467-473
    • (2002) J Cell Sci , vol.115 , pp. 467-473
    • Bech-Otschir, D.1    Seeger, M.2    Dubiel, W.3
  • 19
    • 33947606938 scopus 로고    scopus 로고
    • CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha
    • Schweitzer, K., Bozko, P.M., Dubiel, W. (2007) CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha. EMBO J 26: pp. 1532-1541
    • (2007) EMBO J , vol.26 , pp. 1532-1541
    • Schweitzer, K.1    Bozko, P.M.2    Dubiel, W.3
  • 20
    • 67349196860 scopus 로고    scopus 로고
    • COP9 signalosome controls the Carma1-Bcl10-Malt1 complex upon T-cell stimulation
    • Welteke, V., Eitelhuber, A., Duwel, M. (2009) COP9 signalosome controls the Carma1-Bcl10-Malt1 complex upon T-cell stimulation. EMBO Rep 10: pp. 642-648
    • (2009) EMBO Rep , vol.10 , pp. 642-648
    • Welteke, V.1    Eitelhuber, A.2    Duwel, M.3
  • 21
    • 39749142226 scopus 로고    scopus 로고
    • Cop9 signalosome subunit 8 (CSN8) is essential for Drosophila development
    • Oren-Giladi, P., Krieger, O., Edgar, B.A. (2008) Cop9 signalosome subunit 8 (CSN8) is essential for Drosophila development. Genes Cells 13: pp. 221-231
    • (2008) Genes Cells , vol.13 , pp. 221-231
    • Oren-Giladi, P.1    Krieger, O.2    Edgar, B.A.3
  • 22
    • 9644272422 scopus 로고    scopus 로고
    • The COP9 signalosome (CSN): An evolutionary conserved proteolysis regulator in eukaryotic development
    • Schwechheimer, C. (2004) The COP9 signalosome (CSN): an evolutionary conserved proteolysis regulator in eukaryotic development. Biochim Biophys Acta 1695: pp. 45-54
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 45-54
    • Schwechheimer, C.1
  • 23
    • 68149160205 scopus 로고    scopus 로고
    • The COP9 signalosome mediates beta-catenin degradation by deneddylation and blocks adenomatous polyposis coli destruction via USP15
    • Huang X, Langelotz C, Hetfeld-Pechoc BK et al. The COP9 signalosome mediates beta-catenin degradation by deneddylation and blocks adenomatous polyposis coli destruction via USP15. J Mol Biol 2009.
    • (2009) J Mol Biol
    • Huang, X.1    Langelotz, C.2    Hetfeld-Pechoc, B.K.3
  • 24
    • 32644487282 scopus 로고    scopus 로고
    • The COP9 signalosome: Its possible role in the ubiquitin system
    • Mayer, J.R., Ciechanover, A., Rechsteiner, M. eds., WILEY-VCH Verlag GmbH and KGaA, Weinhei
    • Bech-Otschir, D., Kapelari, B., Dubiel, W. The COP9 signalosome: Its possible role in the ubiquitin system. In: Mayer, J.R., Ciechanover, A., Rechsteiner, M. eds. (2005) Ubiquitin and the Chemistry of Life. WILEY-VCH Verlag GmbH and KGaA, Weinheim, pp. 348-369
    • (2005) Ubiquitin and the Chemistry of Life , pp. 348-369
    • Bech-Otschir, D.1    Kapelari, B.2    Dubiel, W.3
  • 25
    • 34548030442 scopus 로고    scopus 로고
    • The ubiquitin-and proteasome-dependent degradation of COX-2 is regulated by the COP9 signalosome and differentially influenced by coxibs
    • Neuss, H., Huang, X., Hetfeld, B.K. (2007) The ubiquitin-and proteasome-dependent degradation of COX-2 is regulated by the COP9 signalosome and differentially influenced by coxibs. J Mol Med 85: pp. 961-970
    • (2007) J Mol Med , vol.85 , pp. 961-970
    • Neuss, H.1    Huang, X.2    Hetfeld, B.K.3
  • 26
    • 0035576892 scopus 로고    scopus 로고
    • The constitutive photomorphogenesis 9 signalosome directs vascular endothelial growth factor production in tumor cells
    • Pollmann, C., Huang, X., Mall, J. (2001) The constitutive photomorphogenesis 9 signalosome directs vascular endothelial growth factor production in tumor cells. Cancer Res 61: pp. 8416-8421
    • (2001) Cancer Res , vol.61 , pp. 8416-8421
    • Pollmann, C.1    Huang, X.2    Mall, J.3
  • 27
    • 21844464322 scopus 로고    scopus 로고
    • The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1
    • Hetfeld, B.K., Helfrich, A., Kapelari, B. (2005) The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1. Curr Biol 15: pp. 1217-1221
    • (2005) Curr Biol , vol.15 , pp. 1217-1221
    • Hetfeld, B.K.1    Helfrich, A.2    Kapelari, B.3
  • 28
    • 0037509945 scopus 로고    scopus 로고
    • Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzyme Ubp12p
    • Zhou, C., Wee, S., Rhee, E. (2003) Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzyme Ubp12p. Mol Cell 11: pp. 927-938
    • (2003) Mol Cell , vol.11 , pp. 927-938
    • Zhou, C.1    Wee, S.2    Rhee, E.3
  • 29
    • 0344837349 scopus 로고    scopus 로고
    • Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome
    • Uhle, S., Medalia, O., Waldron, R. (2003) Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome. EMBO J 22: pp. 1302-1312
    • (2003) EMBO J , vol.22 , pp. 1302-1312
    • Uhle, S.1    Medalia, O.2    Waldron, R.3
  • 30
    • 33845636937 scopus 로고    scopus 로고
    • Phosphorylation by COP9 signalosome-associated CK2 promotes degradation of p27 during the G1 cell cycle phase
    • Huang, X., Wagner, E., Dumdey, R. (2006) Phosphorylation by COP9 signalosome-associated CK2 promotes degradation of p27 during the G1 cell cycle phase. Isr J Chem 46: pp. 231-238
    • (2006) Isr J Chem , vol.46 , pp. 231-238
    • Huang, X.1    Wagner, E.2    Dumdey, R.3
  • 31
    • 0037195929 scopus 로고    scopus 로고
    • Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1
    • Sun, Y., Wilson, M.P., Majerus, P.W. (2002) Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1. J Biol Chem 277: pp. 45759-45764
    • (2002) J Biol Chem , vol.277 , pp. 45759-45764
    • Sun, Y.1    Wilson, M.P.2    Majerus, P.W.3
  • 32
    • 0037131242 scopus 로고    scopus 로고
    • Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1
    • Cope, G.A., Suh, G.S., Aravind, L. (2002) Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1. Science 298: pp. 608-611
    • (2002) Science , vol.298 , pp. 608-611
    • Cope, G.A.1    Suh, G.S.2    Aravind, L.3
  • 33
    • 0347416977 scopus 로고    scopus 로고
    • The structure of the APPBP1-UBA3-NED 8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1
    • Walden, H., Podgorski, M.S., Huang, D.T. (2003) The structure of the APPBP1-UBA3-NED 8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1. Mol Cell 12: pp. 1427-1437
    • (2003) Mol Cell , vol.12 , pp. 1427-1437
    • Walden, H.1    Podgorski, M.S.2    Huang, D.T.3
  • 34
    • 0037697382 scopus 로고    scopus 로고
    • Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimer
    • Bohnsack, R.N., Haas, A.L. (2003) Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimer. J Biol Chem 278: pp. 26823-26830
    • (2003) J Biol Chem , vol.278 , pp. 26823-26830
    • Bohnsack, R.N.1    Haas, A.L.2
  • 35
    • 0033597126 scopus 로고    scopus 로고
    • Identification of the activating and conjugating enzymes of the NED 8 conjugation pathway
    • Gong, L., Yeh, E.T. (1999) Identification of the activating and conjugating enzymes of the NED 8 conjugation pathway. J Biol Chem 274: pp. 12036-12042
    • (1999) J Biol Chem , vol.274 , pp. 12036-12042
    • Gong, L.1    Yeh, E.T.2
  • 36
    • 33846548206 scopus 로고    scopus 로고
    • Basis for a ubiquitin-like protein thioester switch toggling E1-E 2 affinity
    • Huang, D.T., Hunt, H.W., Zhuang, M. (2007) Basis for a ubiquitin-like protein thioester switch toggling E1-E 2 affinity. Nature 445: pp. 394-398
    • (2007) Nature , vol.445 , pp. 394-398
    • Huang, D.T.1    Hunt, H.W.2    Zhuang, M.3
  • 37
    • 61449164870 scopus 로고    scopus 로고
    • A second E2 for nedd8ylation expands substrate selection
    • Pichler, A. (2009) A second E2 for nedd8ylation expands substrate selection. Structure 17: pp. 321-322
    • (2009) Structure , vol.17 , pp. 321-322
    • Pichler, A.1
  • 38
    • 0032727343 scopus 로고    scopus 로고
    • The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2
    • Kamura, T., Conrad, M.N., Yan, Q. (1999) The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2. Genes Dev 13: pp. 2928-2933
    • (1999) Genes Dev , vol.13 , pp. 2928-2933
    • Kamura, T.1    Conrad, M.N.2    Yan, Q.3
  • 39
    • 0037423760 scopus 로고    scopus 로고
    • Nedd8-modification of Cul1 is promoted by Roc1 as a Nedd8-E 3 ligase and regulates its stability
    • Morimoto, M., Nishida, T., Nagayama, Y. (2003) Nedd8-modification of Cul1 is promoted by Roc1 as a Nedd8-E 3 ligase and regulates its stability. Biochem Biophys Res Commun 301: pp. 392-398
    • (2003) Biochem Biophys Res Commun , vol.301 , pp. 392-398
    • Morimoto, M.1    Nishida, T.2    Nagayama, Y.3
  • 40
    • 21744455599 scopus 로고    scopus 로고
    • The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. Elegans and S. cerevisiae
    • Kurz, T., Ozlu, N., Rudolf, F. (2005) The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae. Nature 435: pp. 1257-1261
    • (2005) Nature , vol.435 , pp. 1257-1261
    • Kurz, T.1    Ozlu, N.2    Rudolf, F.3
  • 41
    • 3142570737 scopus 로고    scopus 로고
    • Mdm2-mediated NED 8 conjugation of p53 inhibits its transcriptional activity
    • Xirodimas, D.P., Saville, M.K., Bourdon, J.C. (2004) Mdm2-mediated NED 8 conjugation of p53 inhibits its transcriptional activity. Cell 118: pp. 83-97
    • (2004) Cell , vol.118 , pp. 83-97
    • Xirodimas, D.P.1    Saville, M.K.2    Bourdon, J.C.3
  • 42
    • 33746797288 scopus 로고    scopus 로고
    • Conjugation to Nedd8 instigates ubiquitylation and down-regulation of activated receptor tyrosine kinases
    • Oved, S., Mosesson, Y., Zwang, Y. (2006) Conjugation to Nedd8 instigates ubiquitylation and down-regulation of activated receptor tyrosine kinases. J Biol Chem 281: pp. 21640-21651
    • (2006) J Biol Chem , vol.281 , pp. 21640-21651
    • Oved, S.1    Mosesson, Y.2    Zwang, Y.3
  • 43
    • 44449129585 scopus 로고    scopus 로고
    • A targeted proteomic analysis of the ubiquitin-like modifier nedd8 and associated proteins
    • Jones, J., Wu, K., Yang, Y. (2008) A targeted proteomic analysis of the ubiquitin-like modifier nedd8 and associated proteins. J Proteome Res 7: pp. 1274-1287
    • (2008) J Proteome Res , vol.7 , pp. 1274-1287
    • Jones, J.1    Wu, K.2    Yang, Y.3
  • 44
    • 40249111681 scopus 로고    scopus 로고
    • Ribosomal proteins are targets for the NED 8 pathway
    • Xirodimas, D.P., Sundqvist, A., Nakamura, A. (2008) Ribosomal proteins are targets for the NED 8 pathway. EMBO Rep 9: pp. 280-286
    • (2008) EMBO Rep , vol.9 , pp. 280-286
    • Xirodimas, D.P.1    Sundqvist, A.2    Nakamura, A.3
  • 45
    • 62049086263 scopus 로고    scopus 로고
    • The mechanism of poly-NED 8 chain formation in vitro
    • Ohki, Y., Funatsu, N., Konishi, N. (2009) The mechanism of poly-NED 8 chain formation in vitro. Biochem Biophys Res Commun 381: pp. 443-447
    • (2009) Biochem Biophys Res Commun , vol.381 , pp. 443-447
    • Ohki, Y.1    Funatsu, N.2    Konishi, N.3
  • 46
    • 0032146145 scopus 로고    scopus 로고
    • A new NED 8-ligating system for cullin-4A
    • Osaka, F., Kawasaki, H., Aida, N. (1998) A new NED 8-ligating system for cullin-4A. Genes and Development 12: pp. 2263-2268
    • (1998) Genes and Development , vol.12 , pp. 2263-2268
    • Osaka, F.1    Kawasaki, H.2    Aida, N.3
  • 47
    • 3142570737 scopus 로고    scopus 로고
    • Mdm2-Mediated NED 8 Conjugation of p53 Inhibits Its Transcriptional Activity
    • Xirodimas, D. (2004) Mdm2-Mediated NED 8 Conjugation of p53 Inhibits Its Transcriptional Activity. Cell 118: pp. 83-97
    • (2004) Cell , vol.118 , pp. 83-97
    • Xirodimas, D.1
  • 48
    • 53249154203 scopus 로고    scopus 로고
    • Function and regulation of protein neddylation. ‘Protein modifications: Beyond the usual suspects’ review series
    • Rabut, G., Peter, M. (2008) Function and regulation of protein neddylation. ‘Protein modifications: beyond the usual suspects’ review series. EMBO Rep 9: pp. 969-976
    • (2008) EMBO Rep , vol.9 , pp. 969-976
    • Rabut, G.1    Peter, M.2
  • 49
    • 0033581899 scopus 로고    scopus 로고
    • Covalent modification of all members of human cullin family proteins by NED 8
    • Hori, T., Osaka, F., Chiba, T. (1999) Covalent modification of all members of human cullin family proteins by NED 8. Oncogene 18: pp. 6829-6834
    • (1999) Oncogene , vol.18 , pp. 6829-6834
    • Hori, T.1    Osaka, F.2    Chiba, T.3
  • 50
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski, M.D., Deshaies, R.J. (2005) Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol 6: pp. 9-20
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 51
    • 17844411190 scopus 로고    scopus 로고
    • NED 8 recruits E2-ubiquitin to SCF E3 ligase
    • Kawakami, T., Chiba, T., Suzuki, T. (2001) NED 8 recruits E2-ubiquitin to SCF E3 ligase. EMBO J 20: pp. 4003-4012
    • (2001) EMBO J , vol.20 , pp. 4003-4012
    • Kawakami, T.1    Chiba, T.2    Suzuki, T.3
  • 52
    • 0036929129 scopus 로고    scopus 로고
    • NED 8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases
    • Liu, J., Furukawa, M., Matsumoto, T. (2002) NED 8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases. Molecular Cell 10: pp. 1511-1518
    • (2002) Molecular Cell , vol.10 , pp. 1511-1518
    • Liu, J.1    Furukawa, M.2    Matsumoto, T.3
  • 53
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NED 8 activation of cullin-RING ligases: Conformational control of conjugation
    • Duda, D.M., Borg, L.A., Scott, D.C. (2008) Structural insights into NED 8 activation of cullin-RING ligases: conformational control of conjugation. Cell 134: pp. 995-1006
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3
  • 54
    • 67649964217 scopus 로고    scopus 로고
    • RING domain E3 ubiquitin ligases
    • Deshaies, R.J., Joazeiro, C.A. (2009) RING domain E3 ubiquitin ligases. Annu Rev Biochem 78: pp. 399-434
    • (2009) Annu Rev Biochem , vol.78 , pp. 399-434
    • Deshaies, R.J.1    Joazeiro, C.A.2
  • 55
    • 53349121021 scopus 로고    scopus 로고
    • Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation
    • Saha, A., Deshaies, R.J. (2008) Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation. Mol Cell 32: pp. 21-31
    • (2008) Mol Cell , vol.32 , pp. 21-31
    • Saha, A.1    Deshaies, R.J.2
  • 56
    • 0037423760 scopus 로고    scopus 로고
    • Nedd8-modification of Cul1 is promoted by Roc1 as a Nedd8-E 3 ligase and regulates its stability
    • Morimoto, M. (2003) Nedd8-modification of Cul1 is promoted by Roc1 as a Nedd8-E 3 ligase and regulates its stability. Biochem Biophys Res Comm 301: pp. 392-398
    • (2003) Biochem Biophys Res Comm , vol.301 , pp. 392-398
    • Morimoto, M.1
  • 57
    • 44449129585 scopus 로고    scopus 로고
    • A targeted proteomic analysis of the ubiquitin-like modifier nedd8 and associated proteins
    • Jones, J., Wu, K., Yang, Y. (2008) A targeted proteomic analysis of the ubiquitin-like modifier nedd8 and associated proteins. J Proteome Res 7: pp. 1274-1287
    • (2008) J Proteome Res , vol.7 , pp. 1274-1287
    • Jones, J.1    Wu, K.2    Yang, Y.3
  • 58
    • 33749346301 scopus 로고    scopus 로고
    • Modification of Proteins by Ubiquitin and Ubiquitin-Like Proteins
    • Kerscher, O., Felberbaum, R., Hochstrasser, M. (2006) Modification of Proteins by Ubiquitin and Ubiquitin-Like Proteins. Annu Rev Cell Dev Biol 22: pp. 159-180
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 159-180
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 59
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • Amerik, A.Y., Hochstrasser, M. (2004) Mechanism and function of deubiquitinating enzymes. In Biochim Biophys Acta 1695: pp. 189-207
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 60
    • 22544441125 scopus 로고    scopus 로고
    • Nep1, a Schizosaccharomyces pombe deneddylating enzyme
    • Zhou, L., Watts, F.Z. (2005) Nep1, a Schizosaccharomyces pombe deneddylating enzyme. Biochem J 389: pp. 307-314
    • (2005) Biochem J , vol.389 , pp. 307-314
    • Zhou, L.1    Watts, F.Z.2
  • 61
    • 17844379780 scopus 로고    scopus 로고
    • Structural basis of NED 8 ubiquitin discrimination by the deNED ylating enzyme NED P1
    • Shen, L.N., Liu, H., Dong, C. (2005) Structural basis of NED 8 ubiquitin discrimination by the deNED ylating enzyme NED P1. EMBO J 24: pp. 1341-1351
    • (2005) EMBO J , vol.24 , pp. 1341-1351
    • Shen, L.N.1    Liu, H.2    Dong, C.3
  • 62
    • 0041853732 scopus 로고    scopus 로고
    • Identification and Characterization of DE N1, a Deneddylase of the ULP Family
    • Gan-Erdene, T. (2003) Identification and Characterization of DE N1, a Deneddylase of the ULP Family. Journal of Biological Chemistry 278: pp. 28892-28900
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 28892-28900
    • Gan-Erdene, T.1
  • 63
    • 0043208977 scopus 로고    scopus 로고
    • DE N1 is a dual function protease capable of processing the C terminus of Nedd8 and deconjugating hyper-neddylated CUL1
    • Wu, K., Yamoah, K., Dolios, G. (2003) DE N1 is a dual function protease capable of processing the C terminus of Nedd8 and deconjugating hyper-neddylated CUL1. J Biol Chem 278: pp. 28882-28891
    • (2003) J Biol Chem , vol.278 , pp. 28882-28891
    • Wu, K.1    Yamoah, K.2    Dolios, G.3
  • 64
    • 55449124589 scopus 로고    scopus 로고
    • DE N1 deneddylates noncullin proteins in vivo
    • Chan, Y., Yoon, J., Wu, J. (2008) DE N1 deneddylates noncullin proteins in vivo. J Cell Sci 121: pp. 3218-3223
    • (2008) J Cell Sci , vol.121 , pp. 3218-3223
    • Chan, Y.1    Yoon, J.2    Wu, J.3
  • 65
    • 0034640373 scopus 로고    scopus 로고
    • Identification of a novel isopeptidase with dual specificity for ubiquitinand NED 8-conjugated proteins
    • Gong, L., Kamitani, T., Millas, S. (2000) Identification of a novel isopeptidase with dual specificity for ubiquitinand NED 8-conjugated proteins. J Biol Chem 275: pp. 14212-14216
    • (2000) J Biol Chem , vol.275 , pp. 14212-14216
    • Gong, L.1    Kamitani, T.2    Millas, S.3
  • 66
    • 34547535639 scopus 로고    scopus 로고
    • The functions of UCH-L1 and its relation to neurodegenerative diseases
    • Setsuie, R., Wada, K. (2007) The functions of UCH-L1 and its relation to neurodegenerative diseases. Neurochem Int 51: pp. 105-111
    • (2007) Neurochem Int , vol.51 , pp. 105-111
    • Setsuie, R.1    Wada, K.2
  • 67
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson’s and Alzheimer’s diseases
    • Choi, J., Levey, A.I., Weintraub, S.T. (2004) Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson’s and Alzheimer’s diseases. J Biol Chem 279: pp. 13256-13264
    • (2004) J Biol Chem , vol.279 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3
  • 69
    • 33747032806 scopus 로고    scopus 로고
    • Identification by functional proteomics of a deubiquitinating/deNeddylating enzyme in Plasmodium falciparum
    • Artavanis-Tsakonas, K., Misaghi, S., Comeaux, C.A. (2006) Identification by functional proteomics of a deubiquitinating/deNeddylating enzyme in Plasmodium falciparum. Mol Microbiol 61: pp. 1187-1195
    • (2006) Mol Microbiol , vol.61 , pp. 1187-1195
    • Artavanis-Tsakonas, K.1    Misaghi, S.2    Comeaux, C.A.3
  • 70
    • 0035907047 scopus 로고    scopus 로고
    • Interactions of the COP9 signalosome with the E3 ubiquitin ligase SCFTIRI in mediating auxin response
    • Schwechheimer, C., Serino, G., Callis, J. (2001) Interactions of the COP9 signalosome with the E3 ubiquitin ligase SCFTIRI in mediating auxin response. Science 292: pp. 1379-1382
    • (2001) Science , vol.292 , pp. 1379-1382
    • Schwechheimer, C.1    Serino, G.2    Callis, J.3
  • 71
    • 0035906430 scopus 로고    scopus 로고
    • Promotion of NED-CUL1 conjugate cleavage by COP9 signalosome
    • Lyapina, S., Cope, G., Shevchenko, A. (2001) Promotion of NED-CUL1 conjugate cleavage by COP9 signalosome. Science 292: pp. 1382-1385
    • (2001) Science , vol.292 , pp. 1382-1385
    • Lyapina, S.1    Cope, G.2    Shevchenko, A.3
  • 72
    • 39549120409 scopus 로고    scopus 로고
    • Targeted inactivation of the COP9 signalosome impairs multiple stages of T-cell development
    • Panattoni, M., Sanvito, F., Basso, V. (2008) Targeted inactivation of the COP9 signalosome impairs multiple stages of T-cell development. J Exp Med 205: pp. 465-477
    • (2008) J Exp Med , vol.205 , pp. 465-477
    • Panattoni, M.1    Sanvito, F.2    Basso, V.3
  • 73
    • 56449094567 scopus 로고    scopus 로고
    • The COP9 signalosome: More than a protease
    • Wei, N., Serino, G., Deng, X.W. (2008) The COP9 signalosome: more than a protease. Trends Biochem Sci 33: pp. 592-600
    • (2008) Trends Biochem Sci , vol.33 , pp. 592-600
    • Wei, N.1    Serino, G.2    Deng, X.W.3
  • 74
    • 0345099331 scopus 로고    scopus 로고
    • The COP9 signalosome: An assembly and maintenance platform for cullin ubiquitin ligases?
    • Wolf, D.A., Zhou, C., Wee, S. (2003) The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases?. Nat Cell Biol 5: pp. 1029-1033
    • (2003) Nat Cell Biol , vol.5 , pp. 1029-1033
    • Wolf, D.A.1    Zhou, C.2    Wee, S.3
  • 75
    • 32044442093 scopus 로고    scopus 로고
    • Targeted silencing of Jab1/Csn5 in human cells downregulates SCF activity through reduction of F-box protein levels
    • Cope, G.A., Deshaies, R.J. (2006) Targeted silencing of Jab1/Csn5 in human cells downregulates SCF activity through reduction of F-box protein levels. BMC Biochem 7: pp. 1
    • (2006) BMC Biochem , vol.7
    • Cope, G.A.1    Deshaies, R.J.2
  • 76
    • 47749097571 scopus 로고    scopus 로고
    • The COP9/signalosome increases the efficiency of von Hippel-Lindau protein ubiquitin ligase-mediated hypoxia-inducible factor-alpha ubiquitination
    • Miyauchi, Y., Kato, M., Tokunaga, F. (2008) The COP9/signalosome increases the efficiency of von Hippel-Lindau protein ubiquitin ligase-mediated hypoxia-inducible factor-alpha ubiquitination. J Biol Chem 283: pp. 16622-16631
    • (2008) J Biol Chem , vol.283 , pp. 16622-16631
    • Miyauchi, Y.1    Kato, M.2    Tokunaga, F.3
  • 77
    • 66849097663 scopus 로고    scopus 로고
    • An interaction network of the mammalian COP9 signalosome identifies Dda1 as a core subunit of multiple Cul4-based E3 ligases
    • Olma, M.H., Roy, M., Bihan, T. (2009) An interaction network of the mammalian COP9 signalosome identifies Dda1 as a core subunit of multiple Cul4-based E3 ligases. J Cell Sci 122: pp. 1035-1044
    • (2009) J Cell Sci , vol.122 , pp. 1035-1044
    • Olma, M.H.1    Roy, M.2    Bihan, T.3
  • 78
    • 3042727952 scopus 로고    scopus 로고
    • The fission yeast COP9/signalosome is involved in cullin modification by ubiquitin-related Ned8p
    • Zhou, C., Seibert, V., Geyer, R. (2001) The fission yeast COP9/signalosome is involved in cullin modification by ubiquitin-related Ned8p. BMC Biochem 2: pp. 7
    • (2001) BMC Biochem , vol.2
    • Zhou, C.1    Seibert, V.2    Geyer, R.3
  • 79
    • 23644447173 scopus 로고    scopus 로고
    • Consequences of COP9 signalosome and 26S proteasome interaction
    • Huang, X., Hetfeld, B.K., Seifert, U. (2005) Consequences of COP9 signalosome and 26S proteasome interaction. Febs J 272: pp. 3909-3917
    • (2005) Febs J , vol.272 , pp. 3909-3917
    • Huang, X.1    Hetfeld, B.K.2    Seifert, U.3
  • 80
    • 0038686677 scopus 로고    scopus 로고
    • Evidence for a physical association of the COP9 signalosome, the proteasome and specific SCF E3 ligases in vivo
    • Peng, Z., Shen, Y., Feng, S. (2003) Evidence for a physical association of the COP9 signalosome, the proteasome and specific SCF E3 ligases in vivo. Curr Biol 13: pp. R504-R505
    • (2003) Curr Biol , vol.13 , pp. 504-505
    • Peng, Z.1    Shen, Y.2    Feng, S.3
  • 81
    • 34248350363 scopus 로고    scopus 로고
    • MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function
    • Maytal-Kivity, V., Reis, N., Hofmann, K. (2002) MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function. BMC Biochem 3: pp. 28
    • (2002) BMC Biochem , vol.3
    • Maytal-Kivity, V.1    Reis, N.2    Hofmann, K.3
  • 82
    • 0036899860 scopus 로고    scopus 로고
    • Ubiquitin system: JAMMing in the name of the lid
    • Berndt, C., Bech-Otschir, D., Dubiel, W. (2002) Ubiquitin system: JAMMing in the name of the lid. Curr Biol 12: pp. R815-7
    • (2002) Curr Biol , vol.12 , pp. 815-817
    • Berndt, C.1    Bech-Otschir, D.2    Dubiel, W.3
  • 83
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao, T., Cohen, R.E. (2002) A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 419: pp. 403-407
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 84
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley, D. (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78: pp. 477-513
    • (2009) Annu Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 85
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • Verma, R., Aravind, L., Oania, R. (2002) Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298: pp. 611-615
    • (2002) Science , vol.298 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3
  • 86
    • 62649104153 scopus 로고    scopus 로고
    • K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1
    • Cooper, E.M., Cutcliffe, C., Kristiansen, T.Z. (2009) K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1. EMBO J 28: pp. 621-631
    • (2009) EMBO J , vol.28 , pp. 621-631
    • Cooper, E.M.1    Cutcliffe, C.2    Kristiansen, T.Z.3
  • 87
    • 52149103164 scopus 로고    scopus 로고
    • Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains
    • Sato, Y., Yoshikawa, A., Yamagata, A. (2008) Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains. Nature 455: pp. 358-362
    • (2008) Nature , vol.455 , pp. 358-362
    • Sato, Y.1    Yoshikawa, A.2    Yamagata, A.3
  • 88
    • 38649109469 scopus 로고    scopus 로고
    • The COP9 signalosome-mediated deneddylation is stimulated by caspases during apoptosis
    • Hetfeld, B.K., Peth, A., Sun, X.M. (2008) The COP9 signalosome-mediated deneddylation is stimulated by caspases during apoptosis. Apoptosis 13: pp. 187-195
    • (2008) Apoptosis , vol.13 , pp. 187-195
    • Hetfeld, B.K.1    Peth, A.2    Sun, X.M.3
  • 89
    • 1842472483 scopus 로고    scopus 로고
    • Caspase activation inhibits proteasome function during apoptosis
    • Sun, X.M., Butterworth, M., MacFarlane, M. (2004) Caspase activation inhibits proteasome function during apoptosis. Mol Cell 14: pp. 81-93
    • (2004) Mol Cell , vol.14 , pp. 81-93
    • Sun, X.M.1    Butterworth, M.2    Macfarlane, M.3
  • 90
    • 33746830878 scopus 로고    scopus 로고
    • Regulation of neddylation and deneddylation of cullin1 in SCFSkp2 ubiquitin ligase by F-box protein and substrate
    • Bornstein, G., Ganoth, D., Hershko, A. (2006) Regulation of neddylation and deneddylation of cullin1 in SCFSkp2 ubiquitin ligase by F-box protein and substrate. Proc Natl Acad Sci USA 103: pp. 11515-11520
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11515-11520
    • Bornstein, G.1    Ganoth, D.2    Hershko, A.3
  • 91
    • 34447135496 scopus 로고    scopus 로고
    • Substrate-mediated regulation of cullin neddylation
    • Chew, E.H., Hagen, T. (2007) Substrate-mediated regulation of cullin neddylation. J Biol Chem 282: pp. 17032-17040
    • (2007) J Biol Chem , vol.282 , pp. 17032-17040
    • Chew, E.H.1    Hagen, T.2
  • 92
    • 0037127256 scopus 로고    scopus 로고
    • The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1/CSN5 and the COP9 signalosome complex
    • Tomoda, K., Kubota, Y., Arata, Y. (2002) The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1/CSN5 and the COP9 signalosome complex. J Biol Chem 277: pp. 2302-2310
    • (2002) J Biol Chem , vol.277 , pp. 2302-2310
    • Tomoda, K.1    Kubota, Y.2    Arata, Y.3
  • 93
    • 0035794541 scopus 로고    scopus 로고
    • COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system
    • Bech-Otschir, D., Kraft, R., Huang, X. (2001) COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system. EMBO J 20: pp. 1630-1639
    • (2001) EMBO J , vol.20 , pp. 1630-1639
    • Bech-Otschir, D.1    Kraft, R.2    Huang, X.3
  • 94
    • 29944435762 scopus 로고    scopus 로고
    • The emerging role of the COP9 signalosome in cancer
    • Richardson, K.S., Zundel, W. (2005) The emerging role of the COP9 signalosome in cancer. Mol Cancer Res 3: pp. 645-653
    • (2005) Mol Cancer Res , vol.3 , pp. 645-653
    • Richardson, K.S.1    Zundel, W.2
  • 95
    • 0031048236 scopus 로고    scopus 로고
    • Increased proteasome-dependent degradation of the cyclin-dependent kinase inhibitor p27 in aggressive colorectal carcinomas
    • Loda, M., Cukor, B., Tam, S.W. (1997) Increased proteasome-dependent degradation of the cyclin-dependent kinase inhibitor p27 in aggressive colorectal carcinomas. Nat Med 3: pp. 231-234
    • (1997) Nat Med , vol.3 , pp. 231-234
    • Loda, M.1    Cukor, B.2    Tam, S.W.3
  • 96
    • 26844485466 scopus 로고    scopus 로고
    • Novel curcumin-and emodin-related compounds identified by in silico 2D/3D conformer screening induce apoptosis in tumor cells
    • Fullbeck, M., Huang, X., Dumdey, R. (2005) Novel curcumin-and emodin-related compounds identified by in silico 2D/3D conformer screening induce apoptosis in tumor cells. BMC Cancer 5: pp. 97
    • (2005) BMC Cancer , vol.5
    • Fullbeck, M.1    Huang, X.2    Dumdey, R.3
  • 97
    • 54949145754 scopus 로고    scopus 로고
    • Multi-targeted therapy by curcumin: How spicy is it?
    • Goel, A., Jhurani, S., Aggarwal, B.B. (2008) Multi-targeted therapy by curcumin: how spicy is it?. Mol Nutr Food Res 52: pp. 1010-1030
    • (2008) Mol Nutr Food Res , vol.52 , pp. 1010-1030
    • Goel, A.1    Jhurani, S.2    Aggarwal, B.B.3
  • 98
    • 45549097323 scopus 로고    scopus 로고
    • Novel anti-angiogenic compounds for application in tumor therapy-COP9 signalosome-associated kinases as possible targets
    • Braumann, C., Tangermann, J., Jacobi, C.A. (2008) Novel anti-angiogenic compounds for application in tumor therapy-COP9 signalosome-associated kinases as possible targets. Mini Rev Med Chem 8: pp. 421-428
    • (2008) Mini Rev Med Chem , vol.8 , pp. 421-428
    • Braumann, C.1    Tangermann, J.2    Jacobi, C.A.3
  • 99
    • 39049134967 scopus 로고    scopus 로고
    • CSN5 isopeptidase activity links COP9 signalosome activation to breast cancer progression
    • Adler, A.S., Littlepage, L.E., Lin, M. (2008) CSN5 isopeptidase activity links COP9 signalosome activation to breast cancer progression. Cancer Res 68: pp. 506-515
    • (2008) Cancer Res , vol.68 , pp. 506-515
    • Adler, A.S.1    Littlepage, L.E.2    Lin, M.3
  • 100
    • 48249136165 scopus 로고    scopus 로고
    • Overexpression of Jab1 in hepatocellular carcinoma and its inhibition by peroxisome proliferator-activated receptor(Gamma) ligands in vitro and in vivo
    • Hsu, M.C., Huang, C.C., Chang, H.C. (2008) Overexpression of Jab1 in hepatocellular carcinoma and its inhibition by peroxisome proliferator-activated receptor(gamma) ligands in vitro and in vivo. Clin Cancer Res 14: pp. 4045-4052
    • (2008) Clin Cancer Res , vol.14 , pp. 4045-4052
    • Hsu, M.C.1    Huang, C.C.2    Chang, H.C.3
  • 101
    • 3242806804 scopus 로고    scopus 로고
    • Prognostic significance of localized p27Kip1 and potential role of Jab1/CSN5 in pancreatic cancer
    • Fukumoto, A., Ikeda, N., Sho, M. (2004) Prognostic significance of localized p27Kip1 and potential role of Jab1/CSN5 in pancreatic cancer. Oncol Rep 11: pp. 277-284
    • (2004) Oncol Rep , vol.11 , pp. 277-284
    • Fukumoto, A.1    Ikeda, N.2    Sho, M.3
  • 102
    • 67650657199 scopus 로고    scopus 로고
    • Ubiquitin-mediated control of oncogene and tumor suppressor gene products
    • Kitagawa K, Kotake Y, Kitagawa M. Ubiquitin-mediated control of oncogene and tumor suppressor gene products. Cancer Sci 2009.
    • (2009) Cancer Sci
    • Kitagawa, K.1    Kotake, Y.2    Kitagawa, M.3
  • 103
    • 27644440307 scopus 로고    scopus 로고
    • Purification Method of the COP9 Signalosome from Human Erythrocytes
    • Hetfeld, B.K.J., Bechotschir, D., Dubiel, W. (2005) Purification Method of the COP9 Signalosome from Human Erythrocytes. Meth Enzymol 398: pp. 481-491
    • (2005) Meth Enzymol , vol.398 , pp. 481-491
    • Hetfeld, B.1    Bechotschir, D.2    Dubiel, W.3
  • 104
    • 33947605240 scopus 로고    scopus 로고
    • Ubiquitin-dependent Proteolysis of the Microtubule End-binding Protein 1, EB1, Is Controlled by the COP9 Signalosome: Possible Consequences for Microtubule Filament Stability
    • Peth, A., Boettcher, J.P., Dubiel, W. (2007) Ubiquitin-dependent Proteolysis of the Microtubule End-binding Protein 1, EB1, Is Controlled by the COP9 Signalosome: Possible Consequences for Microtubule Filament Stability. J Mol Biol 368: pp. 550-563
    • (2007) J Mol Biol , vol.368 , pp. 550-563
    • Peth, A.1    Boettcher, J.P.2    Dubiel, W.3


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