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Volumn 8, Issue 5, 2009, Pages 1150-1164

Affinity purification strategy to capture human endogenous proteasome complexes diversity and to identify proteasome-interacting proteins

Author keywords

[No Author keywords available]

Indexed keywords

PROTEASOME; PROTEIN; PROTEIN MDM2; PROTEIN P53;

EID: 67449088488     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M800193-MCP200     Document Type: Article
Times cited : (53)

References (74)
  • 2
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M. H., and Ciechanover, A. (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82, 373-428 (Pubitemid 34654457)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 3
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: Biological regulation via destruction
    • DOI 10.1002/(SICI)1521-1878(200005)22:5<442::AID-BIES6>3.0.CO;2-Q
    • Ciechanover, A., Orian, A., and Schwartz, A. L. (2000) Ubiquitin-mediated proteolysis: biological regulation via destruction. BioEssays 22, 442-451 (Pubitemid 30308270)
    • (2000) BioEssays , vol.22 , Issue.5 , pp. 442-451
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 4
    • 34548780769 scopus 로고    scopus 로고
    • On prions, proteasomes, and mad cows
    • Goldberg, A. L. (2007) On prions, proteasomes, and mad cows. N. Engl. J. Med. 357, 1150-1152
    • (2007) N. Engl. J. Med. , vol.357 , pp. 1150-1152
    • Goldberg, A.L.1
  • 5
    • 23044506681 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and its role in cancer
    • DOI 10.1200/JCO.2005.05.081
    • Mani, A., and Gelmann, E. P. (2005) The ubiquitin-proteasome pathway and its role in cancer. J. Clin. Oncol. 23, 4776-4789 (Pubitemid 46224082)
    • (2005) Journal of Clinical Oncology , vol.23 , Issue.21 , pp. 4776-4789
    • Mani, A.1    Gelmann, E.P.2
  • 6
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • DOI 10.1016/S1535-6108(04)00120-5, PII S1535610804001205
    • Adams, J. (2004) The development of proteasome inhibitors as anticancer drugs. Cancer Cell 5, 417-421 (Pubitemid 38610244)
    • (2004) Cancer Cell , vol.5 , Issue.5 , pp. 417-421
    • Adams, J.1
  • 7
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and elF3
    • DOI 10.1016/S0092-8674(00)81603-7
    • Glickman, M. H., Rubin, D. M., Coux, O., Wefes, I., Pfeifer, G., Cjeka, Z., Baumeister, W., Fried, V. A., and Finley, D. (1998) A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and elF3. Cell 94, 615-623 (Pubitemid 28427580)
    • (1998) Cell , vol.94 , Issue.5 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3    Wefes, I.4    Pfeifer, G.5    Cjeka, Z.6    Baumeister, W.7    Fried, V.A.8    Finley, D.9
  • 8
    • 28844448619 scopus 로고    scopus 로고
    • Large- And small-scale purification of mammalian 26S proteasomes
    • DOI 10.1016/S0076-6879(05)99015-0, PII S0076687905990150, 15, Ubiquitin and Protein Degradation, Part B
    • Hirano, Y., Murata, S., and Tanaka, K. (2005) Large- and small-scale purification of mammalian 26S proteasomes. Methods Enzymol. 399, 227-240 (Pubitemid 41772732)
    • (2005) Methods in Enzymology , vol.399 , pp. 227-240
    • Hirano, Y.1    Murata, S.2    Tanaka, K.3
  • 9
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 Å resolution
    • DOI 10.1038/386463a0
    • Groll, M., Ditzel, L., Lowe, J., Stock, D., Bochtler, M., Bartunik, H. D., and Huber, R. (1997) Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 386, 463-471 (Pubitemid 27164066)
    • (1997) Nature , vol.386 , Issue.6624 , pp. 463-471
    • Groll, M.1    Ditzel, L.2    Lowe, J.3    Stock, D.4    Bochtler, M.5    Bartunik, H.D.6    Huber, R.7
  • 12
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
    • DOI 10.1038/416763a
    • Lam, Y. A., Lawson, T. G., Velayutham, M., Zweier, J. L., and Pickart, C. M. (2002) A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal. Nature 416, 763-767 (Pubitemid 34429155)
    • (2002) Nature , vol.416 , Issue.6882 , pp. 763-767
    • Lam, Y.A.1    Lawson, T.G.2    Velayutham, M.3    Zweler, J.L.4    Pickart, C.M.5
  • 13
    • 20444384069 scopus 로고    scopus 로고
    • Analysis of polybiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets
    • DOI 10.1074/mcp.M400220-MCP200
    • Mayor, T., Lipford, J. R., Graumann, J., Smith, G. T., and Deshaies, R. J. (2005) Analysis of poiyubiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets. Mol. Cell. Proteomics 4, 741-751 (Pubitemid 40873003)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.6 , pp. 741-751
    • Mayor, T.1    Lipford, J.R.2    Graumann, J.3    Smith, G.T.4    Deshaies, R.J.5
  • 14
    • 0034964524 scopus 로고    scopus 로고
    • The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release
    • DOI 10.1016/S1097-2765(01)00274-X
    • Kolhler, A., Cascio, P., Leggett, D. S., Woo, K. M., Goldberg, A. L., and Finley, D. (2001) The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release. Mol. Cell 7, 1143-1152 (Pubitemid 32607349)
    • (2001) Molecular Cell , vol.7 , Issue.6 , pp. 1143-1152
    • Kohler, A.1    Cascio, P.2    Leggett, D.S.3    Woo, K.M.4    Goldberg, A.L.5    Finley, D.6
  • 15
    • 0037131243 scopus 로고    scopus 로고
    • Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
    • DOI 10.1126/science.1075898
    • Verma, R., Aravind, L., Oania, R., McDonald, W. H., Yates, J. R., III, Koonin, E. V., and Deshaies, R. J. (2002) Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 298, 611-615 (Pubitemid 35215317)
    • (2002) Science , vol.298 , Issue.5593 , pp. 611-615
    • Verma, R.1    Aravind, L.2    Oania, R.3    McDonald, W.H.4    Yates III, J.R.5    Koonin, E.V.6    Deshaies, R.J.7
  • 16
    • 0037126632 scopus 로고    scopus 로고
    • Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome
    • DOI 10.1093/emboj/20.24.7096
    • Fu, H., Reis, N., Lee, Y., Glickman, M. H., and Vierstra, R. D. (2001) Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome. EMBO J. 20, 7096-7107 (Pubitemid 34062301)
    • (2001) EMBO Journal , vol.20 , Issue.24 , pp. 7096-7107
    • Fu, H.1    Reis, N.2    Lee, Y.3    Glickman, M.H.4    Vierstra, R.D.5
  • 17
    • 33845416970 scopus 로고    scopus 로고
    • Global organization and function of mammalian cytosolic proteasome pools: Implications for PA28 and 19S regulatory complexes
    • DOI 10.1091/mbc.E06-04-0311
    • Shibatani, T., Carlson, E. J., Larabee, F., McCormack, A. L., Fruh, K., and Skach, W. R. (2006) Global organization and function of mammalian cytosolic proteasome pools: Implications for PA28 and 19S regulatory complexes. Mol. Biol. Cell 17, 4962-4971 (Pubitemid 44907342)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.12 , pp. 4962-4971
    • Shibatani, T.1    Carlson, E.J.2    Larabee, F.3    McCormack, A.L.4    Fruh, K.5    Skach, W.R.6
  • 18
    • 26844433577 scopus 로고    scopus 로고
    • Proteasome-associated proteins: Regulation of a proteolytic machine
    • DOI 10.1515/BC.2005.085
    • Schmidt, M., Hanna, J., Elsasser, S., and Finley, D. (2005) Proteasome-associated proteins: regulation of a proteolytic machine. Biol. Chem. 386, 725-737 (Pubitemid 41448153)
    • (2005) Biological Chemistry , vol.386 , Issue.8 , pp. 725-737
    • Schmidt, M.1    Hanna, J.2    Elsasser, S.3    Finley, D.4
  • 19
    • 34249085552 scopus 로고    scopus 로고
    • Proteasomes: Machines for All Reasons
    • DOI 10.1016/j.cell.2007.05.007, PII S0092867407005983
    • Demartino, G. N., and Gillette, T. G. (2007) Proteasomes: machines for all reasons. Cell 129, 659-662 (Pubitemid 46802388)
    • (2007) Cell , vol.129 , Issue.4 , pp. 659-662
    • Demartino, G.N.1    Gillette, T.G.2
  • 20
    • 1342346597 scopus 로고    scopus 로고
    • Purification of the Arabidopsis 26 S proteasome: Biochemical and molecular analyses revealed the presence of multiple isoforms
    • DOI 10.1074/jbc.M311977200
    • Yang, P., Fu, H., Walker, J., Papa, C. M., Smalle, J., Ju, Y. M., and Vierstra, R. D. (2004) Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms. J. Biol. Chem. 279, 6401-6413 (Pubitemid 38248774)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.8 , pp. 6401-6413
    • Yang, P.1    Fu, H.2    Walker, J.3    Papa, C.M.4    Smalle, J.5    Ju, Y.-M.6    Vierstra, R.D.7
  • 21
    • 33748418308 scopus 로고    scopus 로고
    • Comparative proteome analysis of changes in the 26S proteasome during oocyte maturation in goldfish
    • Horiguchi, R., Dohra, H., and Tokumoto, T. (2006) Comparative proteome analysis of changes in the 26S proteasome during oocyte maturation in goldfish. Proteomics 6, 4195-4202
    • (2006) Proteomics , vol.6 , pp. 4195-4202
    • Horiguchi, R.1    Dohra, H.2    Tokumoto, T.3
  • 22
    • 0031815994 scopus 로고    scopus 로고
    • The regulatory particle of the Saccharomyces cerevisiae proteasome
    • Glickman, M. H., Rubin, D. M., Fried, V. A., and Finley, D. (1998) The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol. Cell. Biol. 18, 3149-3162 (Pubitemid 28240488)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.6 , pp. 3149-3162
    • Glickman, M.H.1    Rubin, D.M.2    Fried, V.A.3    Finley, D.4
  • 23
    • 0032912818 scopus 로고    scopus 로고
    • Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome
    • Papa, F. R., Amerik, A. Y., and Hochstrasser, M. (1999) Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome. Mol. Biol. Cell 10, 741-756 (Pubitemid 29144635)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.3 , pp. 741-756
    • Papa, F.R.1    Amerik, A.Y.2    Hochstrasser, M.3
  • 24
    • 0026539795 scopus 로고
    • Multiple forms of the 20 S multicatalytic and the 26 S ubiquitin/ATP-dependent proteases from rabbit reticulocyte lysate
    • Hoffman, L., Pratt, G., and Rechsteiner, M. (1992) Multiple forms of the 20 S multicatalytic and the 26 S ubiquitin/ATP-dependent proteases from rabbit reticulocyte lysate. J. Biol. Chem. 267, 22362-22368
    • (1992) J. Biol. Chem. , vol.267 , pp. 22362-22368
    • Hoffman, L.1    Pratt, G.2    Rechsteiner, M.3
  • 25
    • 0033791447 scopus 로고    scopus 로고
    • Proteasomal proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
    • Verma, R., Chen, S., Feldman, R., Schiefe, D., Yates, J., Dohmen, J., and Deshaies, R. J. (2000) Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol. Biol. Cell 11, 3425-3439 (Pubitemid 30781942)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.10 , pp. 3425-3439
    • Verma, R.1    Chen, S.2    Feldman, R.3    Schieltz, D.4    Yates, J.5    Dohmen, J.6    Deshaies, R.J.7
  • 28
    • 33644670152 scopus 로고    scopus 로고
    • An integrated mass spectrometry-based proteomic approach: Quantitave analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network
    • DOI 10.1074/mcp.M500303-MCP200
    • Guerrero, C., Tagwerker, C., Kaiser, P., and Huang, L. (2006) An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network. Mol. Cell. Proteomics 5, 366-378 (Pubitemid 43329314)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.2 , pp. 366-378
    • Guerrero, C.1    Tagwerker, C.2    Kaiser, P.3    Huang, L.4
  • 29
    • 0035841193 scopus 로고    scopus 로고
    • Two-hybrid analysis of the Saccharomyces cerevisiae 26S proteasome
    • Cagney, G., Uetz, P., and Fields, S. (2001) Two-hybrid analysis of the Saccharomyces cerevisiae 26S proteasome. Physiol. Genomics 7, 27-34
    • (2001) Physiol. Genomics , vol.7 , pp. 27-34
    • Cagney, G.1    Uetz, P.2    Fields, S.3
  • 30
    • 33749348820 scopus 로고    scopus 로고
    • A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes
    • DOI 10.1038/sj.emboj.7601338, PII 7601338
    • Hamazaki, J., Iemura, S., Natsume, T., Yashiroda, H., Tanaka, K., and Murata, S. (2006) A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes. EMBO J. 25, 4524-4536 (Pubitemid 44498126)
    • (2006) EMBO Journal , vol.25 , Issue.19 , pp. 4524-4536
    • Hamazaki, J.1    Iemura, S.-I.2    Natsume, T.3    Yashiroda, H.4    Tanaka, K.5    Murata, S.6
  • 31
    • 33845713194 scopus 로고    scopus 로고
    • HRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37
    • DOI 10.1038/sj.emboj.7601450, PII 7601450
    • Qiu, X. B., Ouyang, S. Y., Li, C. J., Miao, S., Wang, L., and Goldberg, A. L. (2006) hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37. EMBO J. 25, 5742-5753 (Pubitemid 44967758)
    • (2006) EMBO Journal , vol.25 , Issue.24 , pp. 5742-5753
    • Qiu, X.-B.1    Ouyang, S.-Y.2    Li, C.-J.3    Miao, S.4    Wang, L.5    Goldberg, A.L.6
  • 32
    • 39049117451 scopus 로고    scopus 로고
    • Identifying dynamic interactors of protein complexes by quantitative mass spectrometry
    • DOI 10.1074/mcp.M700261-MCP200
    • Wang, X., and Huang, L. (2008) Identifying dynamic interactors of protein complexes by quantitative mass spectrometry. Mol. Cell. Proteomics 7, 46-57 (Pubitemid 351248233)
    • (2008) Molecular and Cellular Proteomics , vol.7 , Issue.1 , pp. 46-57
    • Wang, X.1    Huang, L.2
  • 34
    • 10644254712 scopus 로고    scopus 로고
    • Identification of protein-protein interactions using in vivo cross-linking and mass spectrometry
    • DOI 10.1002/pmic.200400856
    • Vasilescu, J., Guo, X., and Kast, J. (2004) Identification of protein-protein interactions using in vivo cross-linking and mass spectrometry. Proteomics 4, 3845-3854 (Pubitemid 39657461)
    • (2004) Proteomics , vol.4 , Issue.12 , pp. 3845-3854
    • Vasilescu, J.1    Guo, X.2    Kast, J.3
  • 35
    • 0035242489 scopus 로고    scopus 로고
    • Quaternary structure of the ATPase complex of human 26s proteasomes determined by chemical cross-linking
    • DOI 10.1006/abbi.2000.2178
    • Hartmann-Petersen, R., Tanaka, K., and Hendil, K. B. (2001) Quaternary structure of the ATPase complex of human 26S proteasomes determined by chemical cross-linking. Arch. Biochem. Biophys. 386, 89-94 (Pubitemid 32980180)
    • (2001) Archives of Biochemistry and Biophysics , vol.386 , Issue.1 , pp. 89-94
    • Hartmann-Petersen, R.1    Tanaka, K.2    Hendil, K.B.3
  • 37
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide by nano-electrospray mass spectromtry
    • DOI 10.1038/379466a0
    • Wilm, M., Shevchenko, A., Houthaeve, T., Breit, S., Schweigerer, L., Fotsis, T., and Mann, M. (1996) Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Mature 379, 466-469 (Pubitemid 26039530)
    • (1996) Nature , vol.379 , Issue.6564 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 38
    • 34848925460 scopus 로고    scopus 로고
    • Mascot file parsing and quantification (MFPaQ), a new software to parse, validate, and quantify proteomics data generated by ICAT and SILAC mass spectrometric analyses: Application to the proteomics study of membrane proteins from primary human endothelial cells
    • DOI 10.1074/mcp.T600069-MCP200
    • Bouyssie, D., de Peredo, A. G., Mouton, E., Albigot, R., Roussel, L., Ortega, N., Cayrol, C., Burlet-Schiltz, O., Girard, J. P., and Monsarrat, B. (2007) Mascot file parsing and quantification (MFPaQ), a new software to parse, validate, and quantify proteomics data generated by ICAT and SILAC mass spectrometric analyses: application to the proteomics study of membrane proteins from primary human endothelial cells. Mol. Cell. Proteomics 6, 1621-1637 (Pubitemid 47506172)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.9 , pp. 1621-1637
    • Bouyssie, D.1    Gonzalez De Peredo, A.2    Mouton, E.3    Albigot, R.4    Roussel, L.5    Ortega, N.6    Cayrol, C.7    Burlet-Schiltz, O.8    Girard, J.-P.9    Monsarrat, B.10
  • 40
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu, H., Sadygov, R. G., and Yates, J. R., III (2004) A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 76, 4193-4201
    • (2004) Anal. Chem. , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 42
    • 36849059755 scopus 로고    scopus 로고
    • Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites
    • DOI 10.1038/nsmb1335, PII NSMB1335
    • Kleijnen, M. F., Roelofs, J., Park, S., Hathaway, N. A., Glickman, M., King, R. W., and Finley, D. (2007) Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites. Nat. Struct. Mol. Biol. 14, 1180-1188 (Pubitemid 350223335)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.12 , pp. 1180-1188
    • Kleijnen, M.F.1    Roelofs, J.2    Park, S.3    Hathaway, N.A.4    Glickman, M.5    King, R.W.6    Finley, D.7
  • 43
    • 33947712748 scopus 로고    scopus 로고
    • Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry
    • DOI 10.1002/pmic.200600410
    • Denis, N. J., Vasilescu, J., Lambert, J. P., Smith, J. C., and Figeys, D. (2007) Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry. Proteomics 7, 868-874 (Pubitemid 46506734)
    • (2007) Proteomics , vol.7 , Issue.6 , pp. 868-874
    • Denis, N.J.1    Vasilescu, J.2    Lambert, J.-P.3    Smith, J.C.4    Figeys, D.5
  • 44
    • 44449108277 scopus 로고    scopus 로고
    • Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry
    • DOI 10.1038/nmeth0608-459, PII NMETH0608-459
    • Nielsen, M. L., Vermeulen, M., Bonaldi, T., Cox, J., Moroder, L., and Mann, M. (2008) Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry. Nat. Methods 5, 459-460 (Pubitemid 351761746)
    • (2008) Nature Methods , vol.5 , Issue.6 , pp. 459-460
    • Nielsen, M.L.1    Vermeulen, M.2    Bonaldi, T.3    Cox, J.4    Moroder, L.5    Mann, M.6
  • 45
    • 0842303313 scopus 로고    scopus 로고
    • Back to the Future with Ubiquitin
    • DOI 10.1016/S0092-8674(03)01074-2
    • Pickart, C. M. (2004) Back to the future with ubiquitin. Cell 116, 181-190 (Pubitemid 38167311)
    • (2004) Cell , vol.116 , Issue.2 , pp. 181-190
    • Pickart, C.M.1
  • 46
    • 33947380146 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the affinity-purified human 26S proteasome complex
    • DOI 10.1021/bi061994u
    • Wang, X., Chen, C. F., Baker, P. R., Chen, P. L., Kaiser, P., and Huang, L. (2007) Mass spectrometric characterization of the affinity-purified human 26S proteasome complex. Biochemistry 46, 3553-3565 (Pubitemid 46449172)
    • (2007) Biochemistry , vol.46 , Issue.11 , pp. 3553-3565
    • Wang, X.1    Chen, C.-F.2    Baker, P.R.3    Chen, P.-L.4    Kaiser, P.5    Huang, L.6
  • 47
    • 0042313977 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome
    • DOI 10.1093/emboj/cdg349
    • Imai, J., Maruya, M., Yashiroda, H., Yahara, I., and Tanaka, K. (2003) The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J. 22, 3557-3567 (Pubitemid 36898333)
    • (2003) EMBO Journal , vol.22 , Issue.14 , pp. 3557-3567
    • Imai, J.1    Maruya, M.2    Yashiroda, H.3    Yahara, I.4    Tanaka, K.5
  • 48
    • 28344456279 scopus 로고    scopus 로고
    • A genomic and functional inventory of deubiquitinating enzymes
    • DOI 10.1016/j.cell.2005.11.007, PII S0092867405011694
    • Nijman, S. M., Luna-Vargas, M. P., Velds, A., Brummelkamp, T. R., Dirac, A. M., Sixma, T. K., and Bernards, R. (2005) A genomic and functional inventory of deubiquitinating enzymes. Cell 123, 773-786 (Pubitemid 41721026)
    • (2005) Cell , vol.123 , Issue.5 , pp. 773-786
    • Nijman, S.M.B.1    Luna-Vargas, M.P.A.2    Velds, A.3    Brummelkamp, T.R.4    Dirac, A.M.G.5    Sixma, T.K.6    Bernards, R.7
  • 49
    • 31544457877 scopus 로고    scopus 로고
    • P53 ubiquitination: Mdm2 and beyond
    • DOI 10.1016/j.molcel.2006.01.020, PII S1097276506000402
    • Brooks, C. L., and Gu, W. (2006) p53 ubiquitination: Mdm2 and beyond. Mol. Cell 21, 307-315 (Pubitemid 43163526)
    • (2006) Molecular Cell , vol.21 , Issue.3 , pp. 307-315
    • Brooks, C.L.1    Gu, W.2
  • 50
    • 0030895008 scopus 로고    scopus 로고
    • A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein
    • DOI 10.1093/emboj/16.7.1519
    • Everett, R. D., Meredith, M., Orr, A., Cross, A., Kathoria, M., and Parkinson, J. (1997) A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein. EMBO J. 16, 1519-1530 (Pubitemid 27151947)
    • (1997) EMBO Journal , vol.16 , Issue.7 , pp. 1519-1530
    • Everett, R.D.1    Meredith, M.2    Orr, A.3    Cross, A.4    Kathoria, M.5    Parkinson, J.6
  • 51
    • 34249295787 scopus 로고    scopus 로고
    • Hyperubiquitylation of wild-type p53 contributes to cytoplasmic sequestration in neuroblastoma
    • DOI 10.1038/sj.cdd.4402126, PII 4402126
    • Becker, K., Marchenko, N. D., Maurice, M., and Moll, U. M. (2007) Hyperubiquitylation of wild-type p53 contributes to cytoplasmic sequestration in neuroblastoma. Cell Death Differ. 14, 1350-1360 (Pubitemid 46965264)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.7 , pp. 1350-1360
    • Becker, K.1    Marchenko, N.D.2    Maurice, M.3    Moll, U.M.4
  • 52
    • 27644554700 scopus 로고    scopus 로고
    • A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes
    • DOI 10.1038/nature04106, PII N04106
    • Hirano, Y., Hendil, K. B., Yashiroda, H., Iemura, S., Nagane, R., Hioki, Y., Natsume, T., Tanaka, K., and Murata, S. (2005) A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes. Nature 437, 1381-1385 (Pubitemid 41568686)
    • (2005) Nature , vol.437 , Issue.7063 , pp. 1381-1385
    • Hirano, Y.1    Hendil, K.B.2    Yashiroda, H.3    Iemura, S.-I.4    Nagane, R.5    Hioki, Y.6    Natsume, T.7    Tanaka, K.8    Murata, S.9
  • 55
    • 20444417275 scopus 로고    scopus 로고
    • The DNA damage-inducible UbL-UbA protein Ddi1 participates in Mec1-mediated degradation of Ho endonuclease
    • DOI 10.1128/MCB.25.13.5355-5362.2005
    • Kaplun, L., Tzirkin, R., Bakhrat, A., Shabek, N., Ivantsiv, Y., and Raveh, D. (2005) The DNA damage-inducible UbL-UbA protein DdM participates in Mec1-mediated degradation of Ho endonuclease. Mol. Cell. Biol. 25, 5355-5362 (Pubitemid 40853573)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.13 , pp. 5355-5362
    • Kaplun, L.1    Tzirkin, R.2    Bakhrat, A.3    Shabek, N.4    Ivantsiv, Y.5    Raveh, D.6
  • 57
    • 0028267689 scopus 로고
    • Cytolocation of prosome antigens on intermediate filament subnetworks of cytokeratin, vimentin and desmin type
    • Olink-Coux, M., Arcangeletti, C., Pinardi, F., Minisini, R., Huesca, M., Chezzi, C., and Scherrer, K. (1994) Cytolocation of prosome antigens on intermediate filament subnetworks of cytokeratin, vimentin and desmin type. J. Cell Sci. 107, 353-366 (Pubitemid 24091843)
    • (1994) Journal of Cell Science , vol.107 , Issue.3 , pp. 353-366
    • Olink-Coux, M.1    Arcangeletti, C.2    Pinardi, F.3    Minisini, R.4    Huesca, M.5    Chezzi, C.6    Scherrer, K.7
  • 58
    • 35448935186 scopus 로고    scopus 로고
    • Characterisation of the nascent polypeptide-associated complex in fission yeast
    • DOI 10.1007/s11033-006-9043-5
    • Andersen, K. M., Semple, C. A., and Hartmann-Petersen, R. (2007) Characterisation of the nascent polypeptide-associated complex in fission yeast. Mol. Biol. Rep. 34, 275-281 (Pubitemid 47624290)
    • (2007) Molecular Biology Reports , vol.34 , Issue.4 , pp. 275-281
    • Andersen, K.M.1    Semple, C.A.2    Hartmann-Petersen, R.3
  • 61
    • 0028894198 scopus 로고
    • Human proteasomes analysed with monoclonal antibodies
    • Hendil, K. B., Kristensen, P., and Uerkvitz, W. (1995) Human proteasomes analysed with monoclonal antibodies. Biochem. J. 305, 245-252
    • (1995) Biochem. J. , vol.305 , pp. 245-252
    • Hendil, K.B.1    Kristensen, P.2    Uerkvitz, W.3
  • 63
    • 41649091606 scopus 로고    scopus 로고
    • Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome
    • Koulich, E., Li, X., and DeMartino, G. N. (2008) Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome. Mol. Biol. Cell 19, 1072-1082
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1072-1082
    • Koulich, E.1    Li, X.2    DeMartino, G.N.3
  • 65
    • 19444367393 scopus 로고    scopus 로고
    • Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2
    • DOI 10.1016/j.molcel.2005.04.024, PII S1097276505012876
    • Meulmeester, E., Maurice, M. M., Boutell, C., Teunisse, A. F., Ovaa, H., Abraham, T. E., Dirks, R. W., and Jochemsen, A. G. (2005) Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2. Mol. Cell 18, 565-576 (Pubitemid 40726233)
    • (2005) Molecular Cell , vol.18 , Issue.5 , pp. 565-576
    • Meulmeester, E.1    Maurice, M.M.2    Boutell, C.3    Teunisse, A.F.A.S.4    Ovaa, H.5    Abraham, T.E.6    Dirks, R.W.7    Jochemsen, A.G.8
  • 66
    • 36049010619 scopus 로고    scopus 로고
    • The p53-Mdm2-HAUSP complex is involved in p53 stabilization by HAUSP
    • Brooks, C. L., Li, M., Hu, M., Shi, Y., and Gu, W. (2007) The p53-Mdm2-HAUSP complex is involved in p53 stabilization by HAUSP. Oncogene 26, 7262-7266
    • (2007) Oncogene , vol.26 , pp. 7262-7266
    • Brooks, C.L.1    Li, M.2    Hu, M.3    Shi, Y.4    Gu, W.5
  • 67
    • 33749049581 scopus 로고    scopus 로고
    • Deubiquitinating Enzyme Ubp6 Functions Noncatalytically to Delay Proteasomal Degradation
    • DOI 10.1016/j.cell.2006.07.038, PII S0092867406012086
    • Hanna, J., Hathaway, N. A., Tone, Y., Crosas, B., Elsasser, S., Kirkpatrick, D. S., Leggett, D. S., Gygi, S. P., King, R. W., and Finley, D. (2006) Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation. Cell 127, 99-111 (Pubitemid 44466645)
    • (2006) Cell , vol.127 , Issue.1 , pp. 99-111
    • Hanna, J.1    Hathaway, N.A.2    Tone, Y.3    Crosas, B.4    Elsasser, S.5    Kirkpatrick, D.6    Leggett, D.S.7    Gygi, S.P.8    King, R.W.9    Finley, D.10
  • 68
    • 34548354844 scopus 로고    scopus 로고
    • High incidence of ubiquitin-like domains in human ubiquitin-specific proteases
    • DOI 10.1002/prot.21546
    • Zhu, X., Menard, R., and Sulea, T. (2007) High incidence of ubiquitin-like domains in human ubiquitin-specific proteases. Proteins 69, 1-7 (Pubitemid 47339134)
    • (2007) Proteins: Structure, Function and Genetics , vol.69 , Issue.1 , pp. 1-7
    • Zhu, X.1    Menard, R.2    Sulea, T.3
  • 69
    • 33646835771 scopus 로고    scopus 로고
    • HAUSP as a therapeutic target for hematopoietic tumors
    • Cheon, K. W., and Baek, K. H. (2006) HAUSP as a therapeutic target for hematopoietic tumors. Int. J. Oncol. 28, 1209-1215
    • (2006) Int. J. Oncol. , vol.28 , pp. 1209-1215
    • Cheon, K.W.1    Baek, K.H.2
  • 70
    • 11144225834 scopus 로고    scopus 로고
    • Characterization of mammalian Ecm29, a 26 S proteasome-associated protein that localizes to the nucleus and membrane vesicles
    • DOI 10.1074/jbc.M410444200
    • Gorbea, C., Goellner, G. M., Teter, K., Holmes, R. K., and Rechsteiner, M. (2004) Characterization of mammalian Ecm29, a 26 S proteasome-associated protein that localizes to the nucleus and membrane vesicles. J. Biol. Chem. 279, 54849-54861 (Pubitemid 40053231)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.52 , pp. 54849-54861
    • Gorbea, C.1    Goellner, G.M.2    Teter, K.3    Holmes, R.K.4    Rechsteiner, M.5
  • 71
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • DOI 10.1016/S0092-8674(00)80929-0
    • Baumeister, W., Walz, J., Zuhl, F., and Seemuller, E. (1998) The proteasome: paradigm of a self-compartmentalizing protease. Cell 92, 367-380 (Pubitemid 28093014)
    • (1998) Cell , vol.92 , Issue.3 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 72
    • 0029186099 scopus 로고
    • Subunits of the regulatory complex of the 26S protease
    • Dubiel, W., Ferrell, K., and Rechsteiner, M. (1995) Subunits of the regulatory complex of the 26S protease. Mol. Biol. Rep. 21, 27-34
    • (1995) Mol. Biol. Rep. , vol.21 , pp. 27-34
    • Dubiel, W.1    Ferrell, K.2    Rechsteiner, M.3
  • 74
    • 15444361471 scopus 로고    scopus 로고
    • Involvement of valosin-containing protein, an ATPase co-purified with IκBα and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IκBα
    • DOI 10.1074/jbc.273.6.3562
    • Dai, R. M., Chen, E., Longo, D. L., Gorbea, C. M., and Li, C. C. (1998) Involvement of valosin-containing protein, an ATPase Co-purified with IκBα and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IκBα. J. Biol. Chem. 273, 3562-3573 (Pubitemid 28109780)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.6 , pp. 3562-3573
    • Dai, R.-M.1    Chen, E.2    Longo, D.L.3    Gorbea, C.M.4    Li, C.-C.H.5


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