메뉴 건너뛰기




Volumn 1843, Issue 1, 2014, Pages 13-25

Regulation of proteasome activity in health and disease

Author keywords

Proteasome; Protein degradation; Ubiquitin

Indexed keywords

BLM10 PA200 PROTEIN; HOLOENZYME; PA28 PROTEIN; PROTEASOME; PROTEIN; RPN4 PROTEIN; SKN 1 PROTEIN; TRANSCRIPTION FACTOR DAF 16; TRANSCRIPTION FACTOR FOXO; TRANSCRIPTION FACTOR NRF1; TRANSCRIPTION FACTOR NRF2; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 84890203542     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2013.08.012     Document Type: Review
Times cited : (362)

References (207)
  • 1
    • 84863903065 scopus 로고    scopus 로고
    • Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis
    • Lindquist S.L., Kelly J.W. Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis. Cold Spring Harb. Perspect. Biol. 2011, 3.
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3
    • Lindquist, S.L.1    Kelly, J.W.2
  • 2
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 2009, 78:477-513.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 6
    • 84862667721 scopus 로고    scopus 로고
    • An historic perspective of proteasome inhibition
    • Esseltine D.L., Mulligan G. An historic perspective of proteasome inhibition. Semin. Hematol. 2012, 49:196-206.
    • (2012) Semin. Hematol. , vol.49 , pp. 196-206
    • Esseltine, D.L.1    Mulligan, G.2
  • 7
    • 63649086487 scopus 로고    scopus 로고
    • Targeting the ubiquitin system in cancer therapy
    • Hoeller D., Dikic I. Targeting the ubiquitin system in cancer therapy. Nature 2009, 458:438-444.
    • (2009) Nature , vol.458 , pp. 438-444
    • Hoeller, D.1    Dikic, I.2
  • 12
    • 59649115172 scopus 로고    scopus 로고
    • Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination
    • Baugh J.M., Viktorova E.G., Pilipenko E.V. Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination. J. Mol. Biol. 2009, 386:814-827.
    • (2009) J. Mol. Biol. , vol.386 , pp. 814-827
    • Baugh, J.M.1    Viktorova, E.G.2    Pilipenko, E.V.3
  • 13
    • 68149164657 scopus 로고    scopus 로고
    • A tetrahedral transition state at the active sites of the 20S proteasome is coupled to opening of the alpha-ring channel
    • Osmulski P.A., Hochstrasser M., Gaczynska M. A tetrahedral transition state at the active sites of the 20S proteasome is coupled to opening of the alpha-ring channel. Structure 2009, 17:1137-1147.
    • (2009) Structure , vol.17 , pp. 1137-1147
    • Osmulski, P.A.1    Hochstrasser, M.2    Gaczynska, M.3
  • 14
    • 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., Wefes I., Pfeifer G., Cjeka Z., Baumeister W., Fried V.A., Finley D. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell 1998, 94:615-623.
    • (1998) Cell , vol.94 , 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
  • 17
    • 84876909425 scopus 로고    scopus 로고
    • Structure of the 26S proteasome with ATP-gammaS bound provides insights into the mechanism of nucleotide-dependent substrate translocation
    • Sledz P., Unverdorben P., Beck F., Pfeifer G., Schweitzer A., Forster F., Baumeister W. Structure of the 26S proteasome with ATP-gammaS bound provides insights into the mechanism of nucleotide-dependent substrate translocation. Proc. Natl. Acad. Sci. U. S. A. 2013, 110:7264-7269.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 7264-7269
    • Sledz, P.1    Unverdorben, P.2    Beck, F.3    Pfeifer, G.4    Schweitzer, A.5    Forster, F.6    Baumeister, W.7
  • 21
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao T., Cohen R.E. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 2002, 419:403-407.
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 23
    • 84880157841 scopus 로고    scopus 로고
    • Conformational switching of the 26S proteasome enables substrate degradation
    • Matyskiela M.E., Lander G.C., Martin A. Conformational switching of the 26S proteasome enables substrate degradation. Nat. Struct. Mol. Biol. 2013, 20:781-788.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 781-788
    • Matyskiela, M.E.1    Lander, G.C.2    Martin, A.3
  • 24
    • 34548274872 scopus 로고    scopus 로고
    • Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry
    • Smith D.M., Chang S.C., Park S., Finley D., Cheng Y., Goldberg A.L. Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry. Mol. Cell 2007, 27:731-744.
    • (2007) Mol. Cell , vol.27 , pp. 731-744
    • Smith, D.M.1    Chang, S.C.2    Park, S.3    Finley, D.4    Cheng, Y.5    Goldberg, A.L.6
  • 25
    • 69949136026 scopus 로고    scopus 로고
    • Subcomplexes of PA700, the 19 S regulator of the 26 S proteasome, reveal relative roles of AAA subunits in 26 S proteasome assembly and activation and ATPase activity
    • Thompson D., Hakala K., DeMartino G.N. Subcomplexes of PA700, the 19 S regulator of the 26 S proteasome, reveal relative roles of AAA subunits in 26 S proteasome assembly and activation and ATPase activity. J. Biol. Chem. 2009, 284:24891-24903.
    • (2009) J. Biol. Chem. , vol.284 , pp. 24891-24903
    • Thompson, D.1    Hakala, K.2    DeMartino, G.N.3
  • 27
    • 77649243592 scopus 로고    scopus 로고
    • Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening
    • Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P. Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening. Mol. Cell 2010, 37:728-735.
    • (2010) Mol. Cell , vol.37 , pp. 728-735
    • Sadre-Bazzaz, K.1    Whitby, F.G.2    Robinson, H.3    Formosa, T.4    Hill, C.P.5
  • 28
    • 84865094127 scopus 로고    scopus 로고
    • Identification of the Cdc48*20S proteasome as an ancient AAA+ proteolytic machine
    • Barthelme D., Sauer R.T. Identification of the Cdc48*20S proteasome as an ancient AAA+ proteolytic machine. Science 2012, 337:843-846.
    • (2012) Science , vol.337 , pp. 843-846
    • Barthelme, D.1    Sauer, R.T.2
  • 30
    • 0034090632 scopus 로고    scopus 로고
    • Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26 S proteasome
    • Strickland E., Hakala K., Thomas P.J., DeMartino G.N. Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26 S proteasome. J. Biol. Chem. 2000, 275:5565-5572.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5565-5572
    • Strickland, E.1    Hakala, K.2    Thomas, P.J.3    DeMartino, G.N.4
  • 33
    • 36849024844 scopus 로고    scopus 로고
    • The C-terminal extension of the beta7 subunit and activator complexes stabilize nascent 20 S proteasomes and promote their maturation
    • Marques A.J., Glanemann C., Ramos P.C., Dohmen R.J. The C-terminal extension of the beta7 subunit and activator complexes stabilize nascent 20 S proteasomes and promote their maturation. J. Biol. Chem. 2007, 282:34869-34876.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34869-34876
    • Marques, A.J.1    Glanemann, C.2    Ramos, P.C.3    Dohmen, R.J.4
  • 34
    • 0242522904 scopus 로고    scopus 로고
    • Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly
    • Fehlker M., Wendler P., Lehmann A., Enenkel C. Blm3 is part of nascent proteasomes and is involved in a late stage of nuclear proteasome assembly. EMBO Rep. 2003, 4:959-963.
    • (2003) EMBO Rep. , vol.4 , pp. 959-963
    • Fehlker, M.1    Wendler, P.2    Lehmann, A.3    Enenkel, C.4
  • 35
    • 79952342817 scopus 로고    scopus 로고
    • Proteasomal degradation of Sfp1 contributes to the repression of ribosome biogenesis during starvation and is mediated by the proteasome activator Blm10
    • Lopez A.D., Tar K., Krugel U., Dange T., Ros I.G., Schmidt M. Proteasomal degradation of Sfp1 contributes to the repression of ribosome biogenesis during starvation and is mediated by the proteasome activator Blm10. Mol. Biol. Cell 2011, 22:528-540.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 528-540
    • Lopez, A.D.1    Tar, K.2    Krugel, U.3    Dange, T.4    Ros, I.G.5    Schmidt, M.6
  • 37
    • 84883572040 scopus 로고    scopus 로고
    • Loss of a 20S proteasome activator in Saccharomyces cerevisiae downregulates genes important for genomic integrity, increases DNA damage, and selectively sensitizes cells to agents with diverse mechanisms of action
    • Doherty K.M., Pride L.D., Lukose J., Snydsman B.E., Charles R., Pramanik A., Muller E.G., Botstein D., Moore C.W. Loss of a 20S proteasome activator in Saccharomyces cerevisiae downregulates genes important for genomic integrity, increases DNA damage, and selectively sensitizes cells to agents with diverse mechanisms of action. G3 (Bethesda) 2012, 2:943-959.
    • (2012) G3 (Bethesda) , vol.2 , pp. 943-959
    • Doherty, K.M.1    Pride, L.D.2    Lukose, J.3    Snydsman, B.E.4    Charles, R.5    Pramanik, A.6    Muller, E.G.7    Botstein, D.8    Moore, C.W.9
  • 39
    • 84878314537 scopus 로고    scopus 로고
    • Acetylation-mediated proteasomal degradation of core histones during DNA repair and spermatogenesis
    • Qian M.X., Pang Y., Liu C.H., Haratake K., Du B.Y., Ji D.Y., Wang G.F., Zhu Q.Q., Song W., Yu Y., et al. Acetylation-mediated proteasomal degradation of core histones during DNA repair and spermatogenesis. Cell 2013, 153:1012-1024.
    • (2013) Cell , vol.153 , pp. 1012-1024
    • Qian, M.X.1    Pang, Y.2    Liu, C.H.3    Haratake, K.4    Du, B.Y.5    Ji, D.Y.6    Wang, G.F.7    Zhu, Q.Q.8    Song, W.9    Yu, Y.10
  • 40
    • 19444387760 scopus 로고    scopus 로고
    • The 1.9Ǻ structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions
    • Forster A., Masters E.I., Whitby F.G., Robinson H., Hill C.P. The 1.9Ǻ structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions. Mol. Cell 2005, 18:589-599.
    • (2005) Mol. Cell , vol.18 , pp. 589-599
    • Forster, A.1    Masters, E.I.2    Whitby, F.G.3    Robinson, H.4    Hill, C.P.5
  • 41
    • 0026498493 scopus 로고
    • Purification of an 11 S regulator of the multicatalytic protease
    • Dubiel W., Pratt G., Ferrell K., Rechsteiner M. Purification of an 11 S regulator of the multicatalytic protease. J. Biol. Chem. 1992, 267:22369-22377.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22369-22377
    • Dubiel, W.1    Pratt, G.2    Ferrell, K.3    Rechsteiner, M.4
  • 42
    • 0026669739 scopus 로고
    • Identification, purification, and characterization of a protein activator (PA28) of the 20 S proteasome (macropain)
    • Ma C.P., Slaughter C.A., DeMartino G.N. Identification, purification, and characterization of a protein activator (PA28) of the 20 S proteasome (macropain). J. Biol. Chem. 1992, 267:10515-10523.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10515-10523
    • Ma, C.P.1    Slaughter, C.A.2    DeMartino, G.N.3
  • 43
    • 0034640520 scopus 로고    scopus 로고
    • Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis
    • Tanahashi N., Murakami Y., Minami Y., Shimbara N., Hendil K.B., Tanaka K. Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis. J. Biol. Chem. 2000, 275:14336-14345.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14336-14345
    • Tanahashi, N.1    Murakami, Y.2    Minami, Y.3    Shimbara, N.4    Hendil, K.B.5    Tanaka, K.6
  • 44
    • 0035955559 scopus 로고    scopus 로고
    • Reconstitution of hybrid proteasomes from purified PA700-20 S complexes and PA28alphabeta activator: ultrastructure and peptidase activities
    • Kopp F., Dahlmann B., Kuehn L. Reconstitution of hybrid proteasomes from purified PA700-20 S complexes and PA28alphabeta activator: ultrastructure and peptidase activities. J. Mol. Biol. 2001, 313:465-471.
    • (2001) J. Mol. Biol. , vol.313 , pp. 465-471
    • Kopp, F.1    Dahlmann, B.2    Kuehn, L.3
  • 45
    • 0037013955 scopus 로고    scopus 로고
    • Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes
    • Cascio P., Call M., Petre B.M., Walz T., Goldberg A.L. Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes. EMBO J. 2002, 21:2636-2645.
    • (2002) EMBO J. , vol.21 , pp. 2636-2645
    • Cascio, P.1    Call, M.2    Petre, B.M.3    Walz, T.4    Goldberg, A.L.5
  • 50
    • 34250339984 scopus 로고    scopus 로고
    • Ubiquitin- and ATP-independent proteolytic turnover of p21 by the REGgamma-proteasome pathway
    • Li X., Amazit L., Long W., Lonard D.M., Monaco J.J., O'Malley B.W. Ubiquitin- and ATP-independent proteolytic turnover of p21 by the REGgamma-proteasome pathway. Mol. Cell 2007, 26:831-842.
    • (2007) Mol. Cell , vol.26 , pp. 831-842
    • Li, X.1    Amazit, L.2    Long, W.3    Lonard, D.M.4    Monaco, J.J.5    O'Malley, B.W.6
  • 51
    • 34250342888 scopus 로고    scopus 로고
    • Ubiquitin-independent degradation of cell-cycle inhibitors by the REGgamma proteasome
    • Chen X., Barton L.F., Chi Y., Clurman B.E., Roberts J.M. Ubiquitin-independent degradation of cell-cycle inhibitors by the REGgamma proteasome. Mol. Cell 2007, 26:843-852.
    • (2007) Mol. Cell , vol.26 , pp. 843-852
    • Chen, X.1    Barton, L.F.2    Chi, Y.3    Clurman, B.E.4    Roberts, J.M.5
  • 52
    • 0025886546 scopus 로고
    • Structural and serological similarity of MHC-linked LMP and proteasome (multicatalytic proteinase) complexes
    • Brown M.G., Driscoll J., Monaco J.J. Structural and serological similarity of MHC-linked LMP and proteasome (multicatalytic proteinase) complexes. Nature 1991, 353:355-357.
    • (1991) Nature , vol.353 , pp. 355-357
    • Brown, M.G.1    Driscoll, J.2    Monaco, J.J.3
  • 53
    • 0025998206 scopus 로고
    • Subunit of the '20S' proteasome (multicatalytic proteinase) encoded by the major histocompatibility complex
    • Ortiz-Navarrete V., Seelig A., Gernold M., Frentzel S., Kloetzel P.M., Hammerling G.J. Subunit of the '20S' proteasome (multicatalytic proteinase) encoded by the major histocompatibility complex. Nature 1991, 353:662-664.
    • (1991) Nature , vol.353 , pp. 662-664
    • Ortiz-Navarrete, V.1    Seelig, A.2    Gernold, M.3    Frentzel, S.4    Kloetzel, P.M.5    Hammerling, G.J.6
  • 55
    • 0029878931 scopus 로고    scopus 로고
    • Identification of MECL-1 (LMP-10) as the third IFN-gamma-inducible proteasome subunit
    • Nandi D., Jiang H., Monaco J.J. Identification of MECL-1 (LMP-10) as the third IFN-gamma-inducible proteasome subunit. J. Immunol. 1996, 156:2361-2364.
    • (1996) J. Immunol. , vol.156 , pp. 2361-2364
    • Nandi, D.1    Jiang, H.2    Monaco, J.J.3
  • 56
    • 84857313367 scopus 로고    scopus 로고
    • Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity
    • Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M., Groll M. Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity. Cell 2012, 148:727-738.
    • (2012) Cell , vol.148 , pp. 727-738
    • Huber, E.M.1    Basler, M.2    Schwab, R.3    Heinemeyer, W.4    Kirk, C.J.5    Groettrup, M.6    Groll, M.7
  • 57
    • 84862750546 scopus 로고    scopus 로고
    • Immunoproteasomes: structure, function, and antigen presentation
    • Ferrington D.A., Gregerson D.S. Immunoproteasomes: structure, function, and antigen presentation. Prog. Mol. Biol. Transl. Sci. 2012, 109:75-112.
    • (2012) Prog. Mol. Biol. Transl. Sci. , vol.109 , pp. 75-112
    • Ferrington, D.A.1    Gregerson, D.S.2
  • 58
    • 84861869794 scopus 로고    scopus 로고
    • Differential roles of proteasome and immunoproteasome regulators Pa28alphabeta, Pa28gamma and Pa200 in the degradation of oxidized proteins
    • Pickering A.M., Davies K.J. Differential roles of proteasome and immunoproteasome regulators Pa28alphabeta, Pa28gamma and Pa200 in the degradation of oxidized proteins. Arch. Biochem. Biophys. 2012, 523:181-190.
    • (2012) Arch. Biochem. Biophys. , vol.523 , pp. 181-190
    • Pickering, A.M.1    Davies, K.J.2
  • 61
    • 84874787780 scopus 로고    scopus 로고
    • Immuno- and constitutive proteasomes do not differ in their abilities to degrade ubiquitinated proteins
    • Nathan J.A., Spinnenhirn V., Schmidtke G., Basler M., Groettrup M., Goldberg A.L. Immuno- and constitutive proteasomes do not differ in their abilities to degrade ubiquitinated proteins. Cell 2013, 152:1184-1194.
    • (2013) Cell , vol.152 , pp. 1184-1194
    • Nathan, J.A.1    Spinnenhirn, V.2    Schmidtke, G.3    Basler, M.4    Groettrup, M.5    Goldberg, A.L.6
  • 65
  • 67
    • 84864003919 scopus 로고    scopus 로고
    • Transfer of Ho endonuclease and Ufo1 to the proteasome by the UbL-UbA shuttle protein, Ddi1, analysed by complex formation in vitro
    • Voloshin O., Bakhrat A., Herrmann S., Raveh D. Transfer of Ho endonuclease and Ufo1 to the proteasome by the UbL-UbA shuttle protein, Ddi1, analysed by complex formation in vitro. PLoS One 2012, 7:e39210.
    • (2012) PLoS One , vol.7
    • Voloshin, O.1    Bakhrat, A.2    Herrmann, S.3    Raveh, D.4
  • 69
    • 41649091606 scopus 로고    scopus 로고
    • Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome
    • Koulich E., Li X., DeMartino G.N. Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome. Mol. Biol. Cell 2008, 19:1072-1082.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1072-1082
    • Koulich, E.1    Li, X.2    DeMartino, G.N.3
  • 71
    • 0031038169 scopus 로고    scopus 로고
    • Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
    • Lam Y.A., Xu W., DeMartino G.N., Cohen R.E. Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature 1997, 385:737-740.
    • (1997) Nature , vol.385 , pp. 737-740
    • Lam, Y.A.1    Xu, W.2    DeMartino, G.N.3    Cohen, R.E.4
  • 73
    • 0344629427 scopus 로고    scopus 로고
    • Ubiquitin depletion as a key mediator of toxicity by translational inhibitors
    • Hanna J., Leggett D.S., Finley D. Ubiquitin depletion as a key mediator of toxicity by translational inhibitors. Mol. Cell. Biol. 2003, 23:9251-9261.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 9251-9261
    • Hanna, J.1    Leggett, D.S.2    Finley, D.3
  • 75
    • 80455122748 scopus 로고    scopus 로고
    • Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins
    • Fang N.N., Ng A.H., Measday V., Mayor T. Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins. Nat. Cell Biol. 2011, 13:1344-1352.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1344-1352
    • Fang, N.N.1    Ng, A.H.2    Measday, V.3    Mayor, T.4
  • 76
    • 0034646298 scopus 로고    scopus 로고
    • Physical association of ubiquitin ligases and the 26S proteasome
    • Xie Y., Varshavsky A. Physical association of ubiquitin ligases and the 26S proteasome. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:2497-2502.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 2497-2502
    • Xie, Y.1    Varshavsky, A.2
  • 77
    • 22544466122 scopus 로고    scopus 로고
    • E3 ubiquitin ligase RNF2 interacts with the S6' proteasomal ATPase subunit and increases the ATP hydrolysis activity of S6'
    • Lee S.J., Choi D., Rhim H., Kang S. E3 ubiquitin ligase RNF2 interacts with the S6' proteasomal ATPase subunit and increases the ATP hydrolysis activity of S6'. Biochem. J. 2005, 389:457-463.
    • (2005) Biochem. J. , vol.389 , pp. 457-463
    • Lee, S.J.1    Choi, D.2    Rhim, H.3    Kang, S.4
  • 79
    • 0038268188 scopus 로고    scopus 로고
    • Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins
    • Seeger M., Hartmann-Petersen R., Wilkinson C.R., Wallace M., Samejima I., Taylor M.S., Gordon C. Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins. J. Biol. Chem. 2003, 278:16791-16796.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16791-16796
    • Seeger, M.1    Hartmann-Petersen, R.2    Wilkinson, C.R.3    Wallace, M.4    Samejima, I.5    Taylor, M.S.6    Gordon, C.7
  • 80
    • 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., Schieltz D., Yates J., Dohmen J., Deshaies R.J. Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol. Biol. Cell 2000, 11:3425-3439.
    • (2000) Mol. Biol. Cell , vol.11 , 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
  • 82
    • 0036904663 scopus 로고    scopus 로고
    • UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis
    • Xie Y., Varshavsky A. UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis. Nat. Cell Biol. 2002, 4:1003-1007.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 1003-1007
    • Xie, Y.1    Varshavsky, A.2
  • 83
    • 85027955696 scopus 로고    scopus 로고
    • A conserved 20S proteasome assembly factor requires a C-terminal HbYX motif for proteasomal precursor binding
    • Kusmierczyk A.R., Kunjappu M.J., Kim R.Y., Hochstrasser M. A conserved 20S proteasome assembly factor requires a C-terminal HbYX motif for proteasomal precursor binding. Nat. Struct. Mol. Biol. 2011, 18:622-629.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 622-629
    • Kusmierczyk, A.R.1    Kunjappu, M.J.2    Kim, R.Y.3    Hochstrasser, M.4
  • 85
    • 0032828077 scopus 로고    scopus 로고
    • The proteasome inhibitor PI31 competes with PA28 for binding to 20S proteasomes
    • Zaiss D.M., Standera S., Holzhutter H., Kloetzel P., Sijts A.J. The proteasome inhibitor PI31 competes with PA28 for binding to 20S proteasomes. FEBS Lett. 1999, 457:333-338.
    • (1999) FEBS Lett. , vol.457 , pp. 333-338
    • Zaiss, D.M.1    Standera, S.2    Holzhutter, H.3    Kloetzel, P.4    Sijts, A.J.5
  • 87
    • 79955544968 scopus 로고    scopus 로고
    • A conserved F box regulatory complex controls proteasome activity in Drosophila
    • Bader M., Benjamin S., Wapinski O.L., Smith D.M., Goldberg A.L., Steller H. A conserved F box regulatory complex controls proteasome activity in Drosophila. Cell 2011, 145:371-382.
    • (2011) Cell , vol.145 , pp. 371-382
    • Bader, M.1    Benjamin, S.2    Wapinski, O.L.3    Smith, D.M.4    Goldberg, A.L.5    Steller, H.6
  • 88
    • 84855206731 scopus 로고    scopus 로고
    • Recent advances in p97/VCP/Cdc48 cellular functions
    • Yamanaka K., Sasagawa Y., Ogura T. Recent advances in p97/VCP/Cdc48 cellular functions. Biochim. Biophys. Acta 2012, 1823:130-137.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 130-137
    • Yamanaka, K.1    Sasagawa, Y.2    Ogura, T.3
  • 89
    • 84887405374 scopus 로고    scopus 로고
    • Roles of cdc48 in regulated protein degradation in yeast
    • Buchberger A. Roles of cdc48 in regulated protein degradation in yeast. Subcell. Biochem. 2013, 66:195-222.
    • (2013) Subcell. Biochem. , vol.66 , pp. 195-222
    • Buchberger, A.1
  • 90
    • 84874452437 scopus 로고    scopus 로고
    • Bipartite determinants mediate an evolutionarily conserved interaction between Cdc48 and the 20S peptidase
    • Barthelme D., Sauer R.T. Bipartite determinants mediate an evolutionarily conserved interaction between Cdc48 and the 20S peptidase. Proc. Natl. Acad. Sci. U. S. A. 2013, 110:3327-3332.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 3327-3332
    • Barthelme, D.1    Sauer, R.T.2
  • 92
    • 0037821846 scopus 로고    scopus 로고
    • Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of mammalian proteasomes
    • Meiners S., Heyken D., Weller A., Ludwig A., Stangl K., Kloetzel P.M., Kruger E. Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of mammalian proteasomes. J. Biol. Chem. 2003, 278:21517-21525.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21517-21525
    • Meiners, S.1    Heyken, D.2    Weller, A.3    Ludwig, A.4    Stangl, K.5    Kloetzel, P.M.6    Kruger, E.7
  • 93
    • 0033004441 scopus 로고    scopus 로고
    • Rpn4p acts as a transcription factor by binding to PACE, a nonamer box found upstream of 26S proteasomal and other genes in yeast
    • Mannhaupt G., Schnall R., Karpov V., Vetter I., Feldmann H. Rpn4p acts as a transcription factor by binding to PACE, a nonamer box found upstream of 26S proteasomal and other genes in yeast. FEBS Lett. 1999, 450:27-34.
    • (1999) FEBS Lett. , vol.450 , pp. 27-34
    • Mannhaupt, G.1    Schnall, R.2    Karpov, V.3    Vetter, I.4    Feldmann, H.5
  • 95
    • 0033772765 scopus 로고    scopus 로고
    • Regulatory networks revealed by transcriptional profiling of damaged Saccharomyces cerevisiae cells: Rpn4 links base excision repair with proteasomes
    • Jelinsky S.A., Estep P., Church G.M., Samson L.D. Regulatory networks revealed by transcriptional profiling of damaged Saccharomyces cerevisiae cells: Rpn4 links base excision repair with proteasomes. Mol. Cell. Biol. 2000, 20:8157-8167.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8157-8167
    • Jelinsky, S.A.1    Estep, P.2    Church, G.M.3    Samson, L.D.4
  • 96
    • 3543037588 scopus 로고    scopus 로고
    • Homeostatic regulation of the proteasome via an Rpn4-dependent feedback circuit
    • Ju D., Wang L., Mao X., Xie Y. Homeostatic regulation of the proteasome via an Rpn4-dependent feedback circuit. Biochem. Biophys. Res. Commun. 2004, 321:51-57.
    • (2004) Biochem. Biophys. Res. Commun. , vol.321 , pp. 51-57
    • Ju, D.1    Wang, L.2    Mao, X.3    Xie, Y.4
  • 97
    • 2642560445 scopus 로고    scopus 로고
    • Proteasomal degradation of RPN4 via two distinct mechanisms, ubiquitin-dependent and -independent
    • Ju D., Xie Y. Proteasomal degradation of RPN4 via two distinct mechanisms, ubiquitin-dependent and -independent. J. Biol. Chem. 2004, 279:23851-23854.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23851-23854
    • Ju, D.1    Xie, Y.2
  • 98
    • 11244343965 scopus 로고    scopus 로고
    • Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase
    • Wang L., Mao X., Ju D., Xie Y. Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase. J. Biol. Chem. 2004, 279:55218-55223.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55218-55223
    • Wang, L.1    Mao, X.2    Ju, D.3    Xie, Y.4
  • 99
    • 78549260740 scopus 로고    scopus 로고
    • Comparative transcriptome profiling analyses during the lag phase uncover YAP1, PDR1, PDR3, RPN4, and HSF1 as key regulatory genes in genomic adaptation to the lignocellulose derived inhibitor HMF for Saccharomyces cerevisiae
    • Ma M., Liu Z.L. Comparative transcriptome profiling analyses during the lag phase uncover YAP1, PDR1, PDR3, RPN4, and HSF1 as key regulatory genes in genomic adaptation to the lignocellulose derived inhibitor HMF for Saccharomyces cerevisiae. BMC Genomics 2010, 11:660.
    • (2010) BMC Genomics , vol.11 , pp. 660
    • Ma, M.1    Liu, Z.L.2
  • 100
    • 77950366349 scopus 로고    scopus 로고
    • Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells
    • Radhakrishnan S.K., Lee C.S., Young P., Beskow A., Chan J.Y., Deshaies R.J. Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells. Mol. Cell 2010, 38:17-28.
    • (2010) Mol. Cell , vol.38 , pp. 17-28
    • Radhakrishnan, S.K.1    Lee, C.S.2    Young, P.3    Beskow, A.4    Chan, J.Y.5    Deshaies, R.J.6
  • 101
    • 77957341511 scopus 로고    scopus 로고
    • Proteasomal degradation is transcriptionally controlled by TCF11 via an ERAD-dependent feedback loop
    • Steffen J., Seeger M., Koch A., Kruger E. Proteasomal degradation is transcriptionally controlled by TCF11 via an ERAD-dependent feedback loop. Mol. Cell 2010, 40:147-158.
    • (2010) Mol. Cell , vol.40 , pp. 147-158
    • Steffen, J.1    Seeger, M.2    Koch, A.3    Kruger, E.4
  • 102
    • 33744477355 scopus 로고    scopus 로고
    • Preincubation with the proteasome inhibitor MG-132 enhances proteasome activity via the Nrf2 transcription factor in aging human skin fibroblasts
    • Kraft D.C., Deocaris C.C., Wadhwa R., Rattan S.I. Preincubation with the proteasome inhibitor MG-132 enhances proteasome activity via the Nrf2 transcription factor in aging human skin fibroblasts. Ann. N. Y. Acad. Sci. 2006, 1067:420-424.
    • (2006) Ann. N. Y. Acad. Sci. , vol.1067 , pp. 420-424
    • Kraft, D.C.1    Deocaris, C.C.2    Wadhwa, R.3    Rattan, S.I.4
  • 103
    • 84858972249 scopus 로고    scopus 로고
    • Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress
    • Pickering A.M., Linder R.A., Zhang H., Forman H.J., Davies K.J. Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress. J. Biol. Chem. 2012, 287:10021-10031.
    • (2012) J. Biol. Chem. , vol.287 , pp. 10021-10031
    • Pickering, A.M.1    Linder, R.A.2    Zhang, H.3    Forman, H.J.4    Davies, K.J.5
  • 104
    • 77950907407 scopus 로고    scopus 로고
    • Nuclear erythroid factor 2-mediated proteasome activation delays senescence in human fibroblasts
    • Kapeta S., Chondrogianni N., Gonos E.S. Nuclear erythroid factor 2-mediated proteasome activation delays senescence in human fibroblasts. J. Biol. Chem. 2010, 285:8171-8184.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8171-8184
    • Kapeta, S.1    Chondrogianni, N.2    Gonos, E.S.3
  • 105
    • 0242721624 scopus 로고    scopus 로고
    • Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway
    • Kwak M.K., Wakabayashi N., Greenlaw J.L., Yamamoto M., Kensler T.W. Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway. Mol. Cell. Biol. 2003, 23:8786-8794.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8786-8794
    • Kwak, M.K.1    Wakabayashi, N.2    Greenlaw, J.L.3    Yamamoto, M.4    Kensler, T.W.5
  • 106
    • 77953012548 scopus 로고    scopus 로고
    • Stress-activated cap'n'collar transcription factors in aging and human disease
    • Sykiotis G.P., Bohmann D. Stress-activated cap'n'collar transcription factors in aging and human disease. Sci. Signal. 2010, 3:re3.
    • (2010) Sci. Signal. , vol.3
    • Sykiotis, G.P.1    Bohmann, D.2
  • 107
    • 57749120460 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 play distinct roles in activation of antioxidant response element-dependent genes
    • Ohtsuji M., Katsuoka F., Kobayashi A., Aburatani H., Hayes J.D., Yamamoto M. Nrf1 and Nrf2 play distinct roles in activation of antioxidant response element-dependent genes. J. Biol. Chem. 2008, 283:33554-33562.
    • (2008) J. Biol. Chem. , vol.283 , pp. 33554-33562
    • Ohtsuji, M.1    Katsuoka, F.2    Kobayashi, A.3    Aburatani, H.4    Hayes, J.D.5    Yamamoto, M.6
  • 108
    • 33745807575 scopus 로고    scopus 로고
    • Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain. Inhibition of nuclear translocation and transacting function
    • Wang W., Chan J.Y. Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain. Inhibition of nuclear translocation and transacting function. J. Biol. Chem. 2006, 281:19676-19687.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19676-19687
    • Wang, W.1    Chan, J.Y.2
  • 109
    • 42649130014 scopus 로고    scopus 로고
    • PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria
    • Lo S.C., Hannink M. PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria. Exp. Cell Res. 2008, 314:1789-1803.
    • (2008) Exp. Cell Res. , vol.314 , pp. 1789-1803
    • Lo, S.C.1    Hannink, M.2
  • 110
    • 0032536783 scopus 로고    scopus 로고
    • Targeted disruption of the ubiquitous CNC-bZIP transcription factor, Nrf-1, results in anemia and embryonic lethality in mice
    • Chan J.Y., Kwong M., Lu R., Chang J., Wang B., Yen T.S., Kan Y.W. Targeted disruption of the ubiquitous CNC-bZIP transcription factor, Nrf-1, results in anemia and embryonic lethality in mice. EMBO J. 1998, 17:1779-1787.
    • (1998) EMBO J. , vol.17 , pp. 1779-1787
    • Chan, J.Y.1    Kwong, M.2    Lu, R.3    Chang, J.4    Wang, B.5    Yen, T.S.6    Kan, Y.W.7
  • 113
    • 83255185776 scopus 로고    scopus 로고
    • Dual regulation of the transcriptional activity of Nrf1 by beta-TrCP- and Hrd1-dependent degradation mechanisms
    • Tsuchiya Y., Morita T., Kim M., Iemura S., Natsume T., Yamamoto M., Kobayashi A. Dual regulation of the transcriptional activity of Nrf1 by beta-TrCP- and Hrd1-dependent degradation mechanisms. Mol. Cell. Biol. 2011, 31:4500-4512.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 4500-4512
    • Tsuchiya, Y.1    Morita, T.2    Kim, M.3    Iemura, S.4    Natsume, T.5    Yamamoto, M.6    Kobayashi, A.7
  • 114
    • 11144264663 scopus 로고    scopus 로고
    • BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase
    • Furukawa M., Xiong Y. BTB protein Keap1 targets antioxidant transcription factor Nrf2 for ubiquitination by the Cullin 3-Roc1 ligase. Mol. Cell. Biol. 2005, 25:162-171.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 162-171
    • Furukawa, M.1    Xiong, Y.2
  • 115
    • 38149092669 scopus 로고    scopus 로고
    • Proteasomal dysfunction activates the transcription factor SKN-1 and produces a selective oxidative-stress response in Caenorhabditis elegans
    • Kahn N.W., Rea S.L., Moyle S., Kell A., Johnson T.E. Proteasomal dysfunction activates the transcription factor SKN-1 and produces a selective oxidative-stress response in Caenorhabditis elegans. Biochem. J. 2008, 409:205-213.
    • (2008) Biochem. J. , vol.409 , pp. 205-213
    • Kahn, N.W.1    Rea, S.L.2    Moyle, S.3    Kell, A.4    Johnson, T.E.5
  • 116
    • 79959823394 scopus 로고    scopus 로고
    • Specific SKN-1/Nrf stress responses to perturbations in translation elongation and proteasome activity
    • Li X., Matilainen O., Jin C., Glover-Cutter K.M., Holmberg C.I., Blackwell T.K. Specific SKN-1/Nrf stress responses to perturbations in translation elongation and proteasome activity. PLoS Genet. 2011, 7:e1002119.
    • (2011) PLoS Genet. , vol.7
    • Li, X.1    Matilainen, O.2    Jin, C.3    Glover-Cutter, K.M.4    Holmberg, C.I.5    Blackwell, T.K.6
  • 117
    • 84873417130 scopus 로고    scopus 로고
    • A conserved role for the 20S proteasome and Nrf2 transcription factor in oxidative-stress adaptation in mammals, C. elegans and D. melanogaster
    • Pickering A.M., Staab T.A., Tower J., Sieburth D.S., Davies K.J. A conserved role for the 20S proteasome and Nrf2 transcription factor in oxidative-stress adaptation in mammals, C. elegans and D. melanogaster. J. Exp. Biol. 2012, 216:543-553.
    • (2012) J. Exp. Biol. , vol.216 , pp. 543-553
    • Pickering, A.M.1    Staab, T.A.2    Tower, J.3    Sieburth, D.S.4    Davies, K.J.5
  • 118
    • 66349105688 scopus 로고    scopus 로고
    • The WD40 repeat protein WDR-23 functions with the CUL4/DDB1 ubiquitin ligase to regulate nuclear abundance and activity of SKN-1 in Caenorhabditis elegans
    • Choe K.P., Przybysz A.J., Strange K. The WD40 repeat protein WDR-23 functions with the CUL4/DDB1 ubiquitin ligase to regulate nuclear abundance and activity of SKN-1 in Caenorhabditis elegans. Mol. Cell. Biol. 2009, 29:2704-2715.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 2704-2715
    • Choe, K.P.1    Przybysz, A.J.2    Strange, K.3
  • 121
    • 80052968161 scopus 로고    scopus 로고
    • Regulation of FOXO protein stability via ubiquitination and proteasome degradation
    • Huang H., Tindall D.J. Regulation of FOXO protein stability via ubiquitination and proteasome degradation. Biochim. Biophys. Acta 2011, 1813:1961-1964.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1961-1964
    • Huang, H.1    Tindall, D.J.2
  • 122
    • 41449113346 scopus 로고    scopus 로고
    • Coordinate activation of autophagy and the proteasome pathway by FoxO transcription factor
    • Zhao J., Brault J.J., Schild A., Goldberg A.L. Coordinate activation of autophagy and the proteasome pathway by FoxO transcription factor. Autophagy 2008, 4:378-380.
    • (2008) Autophagy , vol.4 , pp. 378-380
    • Zhao, J.1    Brault, J.J.2    Schild, A.3    Goldberg, A.L.4
  • 125
    • 0346965700 scopus 로고    scopus 로고
    • O-GlcNAc modification is an endogenous inhibitor of the proteasome
    • Zhang F., Su K., Yang X., Bowe D.B., Paterson A.J., Kudlow J.E. O-GlcNAc modification is an endogenous inhibitor of the proteasome. Cell 2003, 115:715-725.
    • (2003) Cell , vol.115 , pp. 715-725
    • Zhang, F.1    Su, K.2    Yang, X.3    Bowe, D.B.4    Paterson, A.J.5    Kudlow, J.E.6
  • 128
    • 78649980437 scopus 로고    scopus 로고
    • Regulation of the 26S proteasome complex during oxidative stress
    • Wang X., Yen J., Kaiser P., Huang L. Regulation of the 26S proteasome complex during oxidative stress. Sci. Signal. 2010, 3:ra88.
    • (2010) Sci. Signal. , vol.3
    • Wang, X.1    Yen, J.2    Kaiser, P.3    Huang, L.4
  • 129
    • 84868534561 scopus 로고    scopus 로고
    • N-myristoylation of the Rpt2 subunit regulates intracellular localization of the yeast 26S proteasome
    • Kimura A., Kato Y., Hirano H. N-myristoylation of the Rpt2 subunit regulates intracellular localization of the yeast 26S proteasome. Biochemistry 2012, 51:8856-8866.
    • (2012) Biochemistry , vol.51 , pp. 8856-8866
    • Kimura, A.1    Kato, Y.2    Hirano, H.3
  • 131
    • 84859184764 scopus 로고    scopus 로고
    • Ubiquitylation of Drosophila p54/Rpn10/S5a regulates its interaction with the UBA-UBL polyubiquitin receptors
    • Lipinszki Z., Kovacs L., Deak P., Udvardy A. Ubiquitylation of Drosophila p54/Rpn10/S5a regulates its interaction with the UBA-UBL polyubiquitin receptors. Biochemistry 2012, 51:2461-2470.
    • (2012) Biochemistry , vol.51 , pp. 2461-2470
    • Lipinszki, Z.1    Kovacs, L.2    Deak, P.3    Udvardy, A.4
  • 134
    • 84876935501 scopus 로고    scopus 로고
    • Proteasome regulation by ADP-ribosylation
    • Cho-Park P.F., Steller H. Proteasome regulation by ADP-ribosylation. Cell 2013, 153:614-627.
    • (2013) Cell , vol.153 , pp. 614-627
    • Cho-Park, P.F.1    Steller, H.2
  • 135
    • 34547953209 scopus 로고    scopus 로고
    • Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6
    • Zhang F., Hu Y., Huang P., Toleman C.A., Paterson A.J., Kudlow J.E. Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6. J. Biol. Chem. 2007, 282:22460-22471.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22460-22471
    • Zhang, F.1    Hu, Y.2    Huang, P.3    Toleman, C.A.4    Paterson, A.J.5    Kudlow, J.E.6
  • 137
    • 0025012292 scopus 로고
    • Phosphorylation of the multicatalytic proteinase complex from bovine pituitaries by a copurifying cAMP-dependent protein kinase
    • Pereira M.E., Wilk S. Phosphorylation of the multicatalytic proteinase complex from bovine pituitaries by a copurifying cAMP-dependent protein kinase. Arch. Biochem. Biophys. 1990, 283:68-74.
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 68-74
    • Pereira, M.E.1    Wilk, S.2
  • 140
    • 0035895354 scopus 로고    scopus 로고
    • Assembly of the 26S proteasome is regulated by phosphorylation of the p45/Rpt6 ATPase subunit
    • Satoh K., Sasajima H., Nyoumura K.I., Yokosawa H., Sawada H. Assembly of the 26S proteasome is regulated by phosphorylation of the p45/Rpt6 ATPase subunit. Biochemistry 2001, 40:314-319.
    • (2001) Biochemistry , vol.40 , pp. 314-319
    • Satoh, K.1    Sasajima, H.2    Nyoumura, K.I.3    Yokosawa, H.4    Sawada, H.5
  • 141
    • 33646145066 scopus 로고    scopus 로고
    • Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit PSMA7 regulates proteasome degradation
    • Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q., Cao C. Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit PSMA7 regulates proteasome degradation. Mol. Cell 2006, 22:317-327.
    • (2006) Mol. Cell , vol.22 , pp. 317-327
    • Liu, X.1    Huang, W.2    Li, C.3    Li, P.4    Yuan, J.5    Li, X.6    Qiu, X.B.7    Ma, Q.8    Cao, C.9
  • 142
    • 78650632460 scopus 로고    scopus 로고
    • Osmotic stress inhibits proteasome by p38 MAPK-dependent phosphorylation
    • Lee S.H., Park Y., Yoon S.K., Yoon J.B. Osmotic stress inhibits proteasome by p38 MAPK-dependent phosphorylation. J. Biol. Chem. 2010, 285:41280-41289.
    • (2010) J. Biol. Chem. , vol.285 , pp. 41280-41289
    • Lee, S.H.1    Park, Y.2    Yoon, S.K.3    Yoon, J.B.4
  • 143
    • 59949100645 scopus 로고    scopus 로고
    • Regulation of global protein translation and protein degradation in aerobic dormancy
    • Ramnanan C.J., Allan M.E., Groom A.G., Storey K.B. Regulation of global protein translation and protein degradation in aerobic dormancy. Mol. Cell. Biochem. 2009, 323:9-20.
    • (2009) Mol. Cell. Biochem. , vol.323 , pp. 9-20
    • Ramnanan, C.J.1    Allan, M.E.2    Groom, A.G.3    Storey, K.B.4
  • 145
    • 0031906567 scopus 로고    scopus 로고
    • The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-alpha-initiated apoptosis
    • Delic J., Masdehors P., Omura S., Cosset J.M., Dumont J., Binet J.L., Magdelenat H. The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-alpha-initiated apoptosis. Br. J. Cancer 1998, 77:1103-1107.
    • (1998) Br. J. Cancer , vol.77 , pp. 1103-1107
    • Delic, J.1    Masdehors, P.2    Omura, S.3    Cosset, J.M.4    Dumont, J.5    Binet, J.L.6    Magdelenat, H.7
  • 146
    • 0032189685 scopus 로고    scopus 로고
    • Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor
    • Orlowski R.Z., Eswara J.R., Lafond-Walker A., Grever M.R., Orlowski M., Dang C.V. Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor. Cancer Res. 1998, 58:4342-4348.
    • (1998) Cancer Res. , vol.58 , pp. 4342-4348
    • Orlowski, R.Z.1    Eswara, J.R.2    Lafond-Walker, A.3    Grever, M.R.4    Orlowski, M.5    Dang, C.V.6
  • 147
    • 21344469230 scopus 로고    scopus 로고
    • Increased proteasome activity, ubiquitin-conjugating enzymes, and eEF1A translation factor detected in breast cancer tissue
    • Chen L., Madura K. Increased proteasome activity, ubiquitin-conjugating enzymes, and eEF1A translation factor detected in breast cancer tissue. Cancer Res. 2005, 65:5599-5606.
    • (2005) Cancer Res. , vol.65 , pp. 5599-5606
    • Chen, L.1    Madura, K.2
  • 150
    • 84865405382 scopus 로고    scopus 로고
    • Inhibitors for the immuno- and constitutive proteasome: current and future trends in drug development
    • Huber E.M., Groll M. Inhibitors for the immuno- and constitutive proteasome: current and future trends in drug development. Angew. Chem. Int. Ed. Engl. 2012, 51:8708-8720.
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 8708-8720
    • Huber, E.M.1    Groll, M.2
  • 151
    • 81255179936 scopus 로고    scopus 로고
    • The 26S proteasome complex: an attractive target for cancer therapy
    • Frankland-Searby S., Bhaumik S.R. The 26S proteasome complex: an attractive target for cancer therapy. Biochim. Biophys. Acta 2012, 1825:64-76.
    • (2012) Biochim. Biophys. Acta , vol.1825 , pp. 64-76
    • Frankland-Searby, S.1    Bhaumik, S.R.2
  • 154
    • 80052098744 scopus 로고    scopus 로고
    • Depletion of alloreactive T-cells in vitro using the proteasome inhibitor bortezomib preserves the immune response against pathogens
    • Blanco B., Sanchez-Abarca L.I., Caballero-Velazquez T., Santamaria C., Inoges S., Perez-Simon J.A. Depletion of alloreactive T-cells in vitro using the proteasome inhibitor bortezomib preserves the immune response against pathogens. Leuk. Res. 2011, 35:1412-1415.
    • (2011) Leuk. Res. , vol.35 , pp. 1412-1415
    • Blanco, B.1    Sanchez-Abarca, L.I.2    Caballero-Velazquez, T.3    Santamaria, C.4    Inoges, S.5    Perez-Simon, J.A.6
  • 155
    • 84862653224 scopus 로고    scopus 로고
    • Proteasome inhibitors as immunosuppressants: biological rationale and clinical experience
    • Moran E., Carbone F., Augusti V., Patrone F., Ballestrero A., Nencioni A. Proteasome inhibitors as immunosuppressants: biological rationale and clinical experience. Semin. Hematol. 2012, 49:270-276.
    • (2012) Semin. Hematol. , vol.49 , pp. 270-276
    • Moran, E.1    Carbone, F.2    Augusti, V.3    Patrone, F.4    Ballestrero, A.5    Nencioni, A.6
  • 156
    • 67650388103 scopus 로고    scopus 로고
    • A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis
    • Muchamuel T., Basler M., Aujay M.A., Suzuki E., Kalim K.W., Lauer C., Sylvain C., Ring E.R., Shields J., Jiang J., et al. A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis. Nat. Med. 2009, 15:781-787.
    • (2009) Nat. Med. , vol.15 , pp. 781-787
    • Muchamuel, T.1    Basler, M.2    Aujay, M.A.3    Suzuki, E.4    Kalim, K.W.5    Lauer, C.6    Sylvain, C.7    Ring, E.R.8    Shields, J.9    Jiang, J.10
  • 157
    • 77956198116 scopus 로고    scopus 로고
    • Prevention of experimental colitis by a selective inhibitor of the immunoproteasome
    • Basler M., Dajee M., Moll C., Groettrup M., Kirk C.J. Prevention of experimental colitis by a selective inhibitor of the immunoproteasome. J. Immunol. 2010, 185:634-641.
    • (2010) J. Immunol. , vol.185 , pp. 634-641
    • Basler, M.1    Dajee, M.2    Moll, C.3    Groettrup, M.4    Kirk, C.J.5
  • 158
    • 78650034178 scopus 로고    scopus 로고
    • Ubiquitin/proteasome pathway impairment in neurodegeneration: therapeutic implications
    • Huang Q., Figueiredo-Pereira M.E. Ubiquitin/proteasome pathway impairment in neurodegeneration: therapeutic implications. Apoptosis 2010, 15:1292-1311.
    • (2010) Apoptosis , vol.15 , pp. 1292-1311
    • Huang, Q.1    Figueiredo-Pereira, M.E.2
  • 159
    • 84879077265 scopus 로고    scopus 로고
    • Alzheimer disease in the United States (2010-2050) estimated using the 2010 census
    • Hebert L.E., Weuve J., Scherr P.A., Evans D.A. Alzheimer disease in the United States (2010-2050) estimated using the 2010 census. Neurology 2013, 80:1778-1783.
    • (2013) Neurology , vol.80 , pp. 1778-1783
    • Hebert, L.E.1    Weuve, J.2    Scherr, P.A.3    Evans, D.A.4
  • 161
    • 27344441173 scopus 로고    scopus 로고
    • Metabolism of amyloid-beta peptide and Alzheimer's disease
    • Iwata N., Higuchi M., Saido T.C. Metabolism of amyloid-beta peptide and Alzheimer's disease. Pharmacol. Ther. 2005, 108:129-148.
    • (2005) Pharmacol. Ther. , vol.108 , pp. 129-148
    • Iwata, N.1    Higuchi, M.2    Saido, T.C.3
  • 162
    • 77949764687 scopus 로고    scopus 로고
    • Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation
    • Kaneko M., Koike H., Saito R., Kitamura Y., Okuma Y., Nomura Y. Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation. J. Neurosci. 2010, 30:3924-3932.
    • (2010) J. Neurosci. , vol.30 , pp. 3924-3932
    • Kaneko, M.1    Koike, H.2    Saito, R.3    Kitamura, Y.4    Okuma, Y.5    Nomura, Y.6
  • 164
    • 0034605045 scopus 로고    scopus 로고
    • Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes
    • Takei Y., Teng J., Harada A., Hirokawa N. Defects in axonal elongation and neuronal migration in mice with disrupted tau and map1b genes. J. Cell Biol. 2000, 150:989-1000.
    • (2000) J. Cell Biol. , vol.150 , pp. 989-1000
    • Takei, Y.1    Teng, J.2    Harada, A.3    Hirokawa, N.4
  • 166
    • 84878114130 scopus 로고    scopus 로고
    • Tau degradation: the ubiquitin-proteasome system versus the autophagy-lysosome system
    • Lee M.J., Lee J.H., Rubinsztein D.C. Tau degradation: the ubiquitin-proteasome system versus the autophagy-lysosome system. Prog. Neurobiol. 2013, 105:600-604.
    • (2013) Prog. Neurobiol. , vol.105 , pp. 600-604
    • Lee, M.J.1    Lee, J.H.2    Rubinsztein, D.C.3
  • 170
    • 0037381710 scopus 로고    scopus 로고
    • Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease
    • Keck S., Nitsch R., Grune T., Ullrich O. Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J. Neurochem. 2003, 85:115-122.
    • (2003) J. Neurochem. , vol.85 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3    Ullrich, O.4
  • 171
    • 80052398365 scopus 로고    scopus 로고
    • Alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • Bartels T., Choi J.G., Selkoe D.J. alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 2011, 477:107-110.
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 172
    • 0035976835 scopus 로고    scopus 로고
    • Alpha-Synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome
    • Tofaris G.K., Layfield R., Spillantini M.G. alpha-Synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Lett. 2001, 509:22-26.
    • (2001) FEBS Lett. , vol.509 , pp. 22-26
    • Tofaris, G.K.1    Layfield, R.2    Spillantini, M.G.3
  • 173
    • 51149121890 scopus 로고    scopus 로고
    • Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies
    • Bedford L., Hay D., Devoy A., Paine S., Powe D.G., Seth R., Gray T., Topham I., Fone K., Rezvani N., et al. Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies. J. Neurosci. 2008, 28:8189-8198.
    • (2008) J. Neurosci. , vol.28 , pp. 8189-8198
    • Bedford, L.1    Hay, D.2    Devoy, A.3    Paine, S.4    Powe, D.G.5    Seth, R.6    Gray, T.7    Topham, I.8    Fone, K.9    Rezvani, N.10
  • 174
    • 84873844495 scopus 로고    scopus 로고
    • Pale body-like inclusion formation and neurodegeneration following depletion of 26S proteasomes in mouse brain neurons are independent of alpha-synuclein
    • Paine S.M., Anderson G., Bedford K., Lawler K., Mayer R.J., Lowe J., Bedford L. Pale body-like inclusion formation and neurodegeneration following depletion of 26S proteasomes in mouse brain neurons are independent of alpha-synuclein. PLoS One 2013, 8:e54711.
    • (2013) PLoS One , vol.8
    • Paine, S.M.1    Anderson, G.2    Bedford, K.3    Lawler, K.4    Mayer, R.J.5    Lowe, J.6    Bedford, L.7
  • 176
    • 84867386032 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in Huntington's disease: are proteasomes impaired, initiators of disease, or coming to the rescue?
    • Schipper-Krom S., Juenemann K., Reits E.A. The ubiquitin-proteasome system in Huntington's disease: are proteasomes impaired, initiators of disease, or coming to the rescue?. Biochem. Res. Int. 2012, 2012:837015.
    • (2012) Biochem. Res. Int. , vol.2012 , pp. 837015
    • Schipper-Krom, S.1    Juenemann, K.2    Reits, E.A.3
  • 177
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group. Cell 1993, 72:971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 179
    • 0037461730 scopus 로고    scopus 로고
    • Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders
    • Sanchez I., Mahlke C., Yuan J. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 2003, 421:373-379.
    • (2003) Nature , vol.421 , pp. 373-379
    • Sanchez, I.1    Mahlke, C.2    Yuan, J.3
  • 183
    • 34249802905 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system alterations in a striatal cell model of Huntington's disease
    • Hunter J.M., Lesort M., Johnson G.V. Ubiquitin-proteasome system alterations in a striatal cell model of Huntington's disease. J. Neurosci. Res. 2007, 85:1774-1788.
    • (2007) J. Neurosci. Res. , vol.85 , pp. 1774-1788
    • Hunter, J.M.1    Lesort, M.2    Johnson, G.V.3
  • 184
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 2001, 292:1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 186
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • Venkatraman P., Wetzel R., Tanaka M., Nukina N., Goldberg A.L. Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol. Cell 2004, 14:95-104.
    • (2004) Mol. Cell , vol.14 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3    Nukina, N.4    Goldberg, A.L.5
  • 187
    • 45149115090 scopus 로고    scopus 로고
    • Proteasomes cleave at multiple sites within polyglutamine tracts: activation by PA28gamma(K188E)
    • Pratt G., Rechsteiner M. Proteasomes cleave at multiple sites within polyglutamine tracts: activation by PA28gamma(K188E). J. Biol. Chem. 2008, 283:12919-12925.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12919-12925
    • Pratt, G.1    Rechsteiner, M.2
  • 188
    • 34948845308 scopus 로고    scopus 로고
    • Proteasome activator enhances survival of Huntington's disease neuronal model cells
    • Seo H., Sonntag K.C., Kim W., Cattaneo E., Isacson O. Proteasome activator enhances survival of Huntington's disease neuronal model cells. PLoS One 2007, 2:e238.
    • (2007) PLoS One , vol.2
    • Seo, H.1    Sonntag, K.C.2    Kim, W.3    Cattaneo, E.4    Isacson, O.5
  • 191
    • 79955060100 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in cardiomyopathies
    • Schlossarek S., Carrier L. The ubiquitin-proteasome system in cardiomyopathies. Curr. Opin. Cardiol. 2011, 26:190-195.
    • (2011) Curr. Opin. Cardiol. , vol.26 , pp. 190-195
    • Schlossarek, S.1    Carrier, L.2
  • 193
    • 84865497050 scopus 로고    scopus 로고
    • Genetically induced moderate inhibition of the proteasome in cardiomyocytes exacerbates myocardial ischemia-reperfusion injury in mice
    • Tian Z., Zheng H., Li J., Li Y., Su H., Wang X. Genetically induced moderate inhibition of the proteasome in cardiomyocytes exacerbates myocardial ischemia-reperfusion injury in mice. Circ. Res. 2012, 111:532-542.
    • (2012) Circ. Res. , vol.111 , pp. 532-542
    • Tian, Z.1    Zheng, H.2    Li, J.3    Li, Y.4    Su, H.5    Wang, X.6
  • 194
    • 80052386730 scopus 로고    scopus 로고
    • Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/reperfusion injury in mice
    • Li J., Horak K.M., Su H., Sanbe A., Robbins J., Wang X. Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/reperfusion injury in mice. J. Clin. Invest. 2011, 121:3689-3700.
    • (2011) J. Clin. Invest. , vol.121 , pp. 3689-3700
    • Li, J.1    Horak, K.M.2    Su, H.3    Sanbe, A.4    Robbins, J.5    Wang, X.6
  • 195
    • 84869051809 scopus 로고    scopus 로고
    • Protein oxidative damage at the crossroads of cellular senescence, aging, and age-related diseases
    • Baraibar M.A., Liu L., Ahmed E.K., Friguet B. Protein oxidative damage at the crossroads of cellular senescence, aging, and age-related diseases. Oxidative Med. Cell. Longev. 2012, 2012:919832.
    • (2012) Oxidative Med. Cell. Longev. , vol.2012 , pp. 919832
    • Baraibar, M.A.1    Liu, L.2    Ahmed, E.K.3    Friguet, B.4
  • 196
    • 0033610079 scopus 로고    scopus 로고
    • Gene expression profile of aging and its retardation by caloric restriction
    • Lee C.K., Klopp R.G., Weindruch R., Prolla T.A. Gene expression profile of aging and its retardation by caloric restriction. Science 1999, 285:1390-1393.
    • (1999) Science , vol.285 , pp. 1390-1393
    • Lee, C.K.1    Klopp, R.G.2    Weindruch, R.3    Prolla, T.A.4
  • 198
    • 0038686574 scopus 로고    scopus 로고
    • Proteasome disassembly and downregulation is correlated with viability during stationary phase
    • Bajorek M., Finley D., Glickman M.H. Proteasome disassembly and downregulation is correlated with viability during stationary phase. Curr. Biol. 2003, 13:1140-1144.
    • (2003) Curr. Biol. , vol.13 , pp. 1140-1144
    • Bajorek, M.1    Finley, D.2    Glickman, M.H.3
  • 199
    • 4344677922 scopus 로고    scopus 로고
    • Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease
    • Grune T., Jung T., Merker K., Davies K.J. Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int. J. Biochem. Cell Biol. 2004, 36:2519-2530.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2519-2530
    • Grune, T.1    Jung, T.2    Merker, K.3    Davies, K.J.4
  • 205
    • 28744438867 scopus 로고    scopus 로고
    • Ump1 extends yeast lifespan and enhances viability during oxidative stress: central role for the proteasome?
    • Chen Q., Thorpe J., Dohmen J.R., Li F., Keller J.N. Ump1 extends yeast lifespan and enhances viability during oxidative stress: central role for the proteasome?. Free Radic. Biol. Med. 2006, 40:120-126.
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 120-126
    • Chen, Q.1    Thorpe, J.2    Dohmen, J.R.3    Li, F.4    Keller, J.N.5
  • 206
    • 59449095881 scopus 로고    scopus 로고
    • Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process
    • Tonoki A., Kuranaga E., Tomioka T., Hamazaki J., Murata S., Tanaka K., Miura M. Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process. Mol. Cell. Biol. 2009, 29:1095-1106.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1095-1106
    • Tonoki, A.1    Kuranaga, E.2    Tomioka, T.3    Hamazaki, J.4    Murata, S.5    Tanaka, K.6    Miura, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.