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Volumn 4, Issue 3, 2014, Pages 862-884

Regulating the 20S proteasome ubiquitin-independent degradation pathway

Author keywords

20s proteasome; Intrinsically disordered proteins; Oxidatively damaged proteins; Protein degradation; Regulatory mechanisms

Indexed keywords

PROTEASOME; REGULATOR PROTEIN; UBIQUITIN; ATP DEPENDENT 26S PROTEASE;

EID: 84924735979     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom4030862     Document Type: Review
Times cited : (266)

References (142)
  • 3
    • 84890203542 scopus 로고    scopus 로고
    • Regulation of proteasome activity in health and disease
    • Schmidt, M.; Finley, D. Regulation of proteasome activity in health and disease. Biochim. Biophys. Acta 2014, 1843, 13-25.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 13-25
    • Schmidt, M.1    Finley, D.2
  • 4
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A.L. Protein degradation and protection against misfolded or damaged proteins. Nature 2003, 426, 895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 5
    • 61449156563 scopus 로고    scopus 로고
    • Targeting proteins for destruction by the ubiquitin system: Implications for human pathobiology
    • Schwartz, A.L.; Ciechanover, A. Targeting proteins for destruction by the ubiquitin system: Implications for human pathobiology. Annu. Rev. Pharmacol. Toxicol. 2009, 49, 73-96.
    • (2009) Annu. Rev. Pharmacol. Toxicol. , vol.49 , pp. 73-96
    • Schwartz, A.L.1    Ciechanover, A.2
  • 6
    • 84876916040 scopus 로고    scopus 로고
    • Structural biology of the proteasome
    • Kish-Trier, E.; Hill, C.P. Structural biology of the proteasome. Annu. Rev. Biophys. 2013, 42, 29-49.
    • (2013) Annu. Rev. Biophys. , vol.42 , pp. 29-49
    • Kish-Trier, E.1    Hill, C.P.2
  • 7
    • 79959265889 scopus 로고    scopus 로고
    • Ubiquitin-independent proteasomal degradation during oncogenic viral infections
    • Hwang, J.; Winkler, L.; Kalejta, R.F. Ubiquitin-independent proteasomal degradation during oncogenic viral infections. Biochim. Biophys. Acta 2011, 1816, 147-157.
    • (2011) Biochim. Biophys. Acta , vol.1816 , pp. 147-157
    • Hwang, J.1    Winkler, L.2    Kalejta, R.F.3
  • 8
    • 84862736551 scopus 로고    scopus 로고
    • Degradation of damaged proteins: The main function of the 20S proteasome
    • Pickering, A.M.; Davies, K.J. Degradation of damaged proteins: The main function of the 20S proteasome. Prog. Mol. Biol. Transl. Sci. 2012, 109, 227-248.
    • (2012) Prog. Mol. Biol. Transl. Sci. , vol.109 , pp. 227-248
    • Pickering, A.M.1    Davies, K.J.2
  • 9
    • 84890174353 scopus 로고    scopus 로고
    • Ubiquitin-independent proteasomal degradation
    • Erales, J.; Coffino, P. Ubiquitin-independent proteasomal degradation. Biochim. Biophys. Acta 2014, 1843, 216-221.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 216-221
    • Erales, J.1    Coffino, P.2
  • 10
    • 13244275245 scopus 로고    scopus 로고
    • A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73
    • Asher, G.; Tsvetkov, P.; Kahana, C.; Shaul, Y. A mechanism of ubiquitin-independent proteasomal degradation of the tumor suppressors p53 and p73. Genes Dev. 2005, 19, 316-321.
    • (2005) Genes Dev. , vol.19 , pp. 316-321
    • Asher, G.1    Tsvetkov, P.2    Kahana, C.3    Shaul, Y.4
  • 11
    • 79955757695 scopus 로고    scopus 로고
    • Oxidative stress-mediated regulation of proteasome complexes
    • Aiken, C.T.; Kaake, R.M.; Wang, X.; Huang, L. Oxidative stress-mediated regulation of proteasome complexes. Mol. Cell. Proteomics 2011, doi: 10.1074/mcp.M110.006924.
    • (2011) Mol. Cell. Proteomics
    • Aiken, C.T.1    Kaake, R.M.2    Wang, X.3    Huang, L.4
  • 13
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H.J.; Wright, P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 2005, 6, 197-208.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 14
    • 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
  • 16
    • 34548855943 scopus 로고    scopus 로고
    • Cell cycle-dependent caspase-like activity that cleaves p27(KIP1) is the beta(1) subunit of the 20S proteasome
    • Tambyrajah, W.S.; Bowler, L.D.; Medina-Palazon, C.; Sinclair, A.J. Cell cycle-dependent caspase-like activity that cleaves p27(KIP1) is the beta(1) subunit of the 20S proteasome. Arch. Biochem. Biophys. 2007, 466, 186-193.
    • (2007) Arch. Biochem. Biophys. , vol.466 , pp. 186-193
    • Tambyrajah, W.S.1    Bowler, L.D.2    Medina-Palazon, C.3    Sinclair, A.J.4
  • 17
    • 44649168869 scopus 로고    scopus 로고
    • NAD(P)H quinone oxidoreductase 1 inhibits the proteasomal degradation of the tumour suppressor p33(ING1b)
    • Garate, M.; Wong, R.P.; Campos, E.I.; Wang, Y.; Li, G. NAD(P)H quinone oxidoreductase 1 inhibits the proteasomal degradation of the tumour suppressor p33(ING1b). EMBO Rep. 2008, 9, 576-581.
    • (2008) EMBO Rep. , vol.9 , pp. 576-581
    • Garate, M.1    Wong, R.P.2    Campos, E.I.3    Wang, Y.4    Li, G.5
  • 18
    • 77955321215 scopus 로고    scopus 로고
    • NAD(P)H quinone oxidoreductase protects TAp63gamma from proteasomal degradation and regulates TAp63gamma-dependent growth arrest
    • Rokah, O.H.; Shpilberg, O.; Granot, G. NAD(P)H quinone oxidoreductase protects TAp63gamma from proteasomal degradation and regulates TAp63gamma-dependent growth arrest. PLoS One 2010, 5, e11401.
    • (2010) PLoS One , vol.5
    • Rokah, O.H.1    Shpilberg, O.2    Granot, G.3
  • 19
    • 79952281710 scopus 로고    scopus 로고
    • Disruption of NAD(P)H: Quinone oxidoreductase 1 gene in mice leads to 20S proteasomal degradation of p63 resulting in thinning of epithelium and chemical-induced skin cancer
    • Patrick, B.A.; Gong, X.; Jaiswal, A.K. Disruption of NAD(P)H: Quinone oxidoreductase 1 gene in mice leads to 20S proteasomal degradation of p63 resulting in thinning of epithelium and chemical-induced skin cancer. Oncogene 2011, 30, 1098-1107.
    • (2011) Oncogene , vol.30 , pp. 1098-1107
    • Patrick, B.A.1    Gong, X.2    Jaiswal, A.K.3
  • 20
    • 0037452979 scopus 로고    scopus 로고
    • Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein
    • Kalejta, R.F.; Shenk, T. Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein. Proc. Natl. Acad. Sci. USA 2003, 100, 3263-3268.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3263-3268
    • Kalejta, R.F.1    Shenk, T.2
  • 23
    • 77955286666 scopus 로고    scopus 로고
    • c-Fos proteasomal degradation is activated by a default mechanism, and its regulation by NAD(P)H: Quinone oxidoreductase 1 determines c-Fos serum response kinetics
    • Adler, J.; Reuven, N.; Kahana, C.; Shaul, Y. c-Fos proteasomal degradation is activated by a default mechanism, and its regulation by NAD(P)H: Quinone oxidoreductase 1 determines c-Fos serum response kinetics. Mol. Cell. Biol. 2010, 30, 3767-3778.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3767-3778
    • Adler, J.1    Reuven, N.2    Kahana, C.3    Shaul, Y.4
  • 24
    • 24044488987 scopus 로고    scopus 로고
    • Mechanism of direct degradation of Ikappabalpha by 20S proteasome
    • Alvarez-Castelao, B.; Castano, J.G. Mechanism of direct degradation of Ikappabalpha by 20S proteasome. FEBS Lett. 2005, 579, 4797-4802.
    • (2005) FEBS Lett. , vol.579 , pp. 4797-4802
    • Alvarez-Castelao, B.1    Castano, J.G.2
  • 25
    • 14644446056 scopus 로고    scopus 로고
    • 20S proteasomal degradation of ornithine decarboxylase is regulated by NQO1
    • Asher, G.; Bercovich, Z.; Tsvetkov, P.; Shaul, Y.; Kahana, C. 20S proteasomal degradation of ornithine decarboxylase is regulated by NQO1. Mol. Cell 2005, 17, 645-655.
    • (2005) Mol. Cell , vol.17 , pp. 645-655
    • Asher, G.1    Bercovich, Z.2    Tsvetkov, P.3    Shaul, Y.4    Kahana, C.5
  • 26
    • 34447522124 scopus 로고    scopus 로고
    • Constitutive/hypoxic degradation of HIF-alpha proteins by the proteasome is independent of von hippel lindau protein ubiquitylation and the transactivation activity of the protein
    • Kong, X.; Alvarez-Castelao, B.; Lin, Z.; Castano, J.G.; Caro, J. Constitutive/hypoxic degradation of HIF-alpha proteins by the proteasome is independent of von hippel lindau protein ubiquitylation and the transactivation activity of the protein. J. Biol. Chem. 2007, 282, 15498-15505.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15498-15505
    • Kong, X.1    Alvarez-Castelao, B.2    Lin, Z.3    Castano, J.G.4    Caro, J.5
  • 27
    • 84871337647 scopus 로고    scopus 로고
    • NAD(P)H: Quinone oxidoreductase 1 (NQO1) competes with 20S proteasome for binding with C/EBPalpha leading to its stabilization and protection against radiation-induced myeloproliferative disease
    • Xu, J.; Jaiswal, A.K. NAD(P)H: Quinone oxidoreductase 1 (NQO1) competes with 20S proteasome for binding with C/EBPalpha leading to its stabilization and protection against radiation-induced myeloproliferative disease. J. Biol. Chem. 2012, 287, 41608-41618.
    • (2012) J. Biol. Chem. , vol.287 , pp. 41608-41618
    • Xu, J.1    Jaiswal, A.K.2
  • 30
    • 0036942289 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of tau proteins occurs independently of the chymotrypsin-like activity by a nonprocessive pathway
    • Cardozo, C.; Michaud, C. Proteasome-mediated degradation of tau proteins occurs independently of the chymotrypsin-like activity by a nonprocessive pathway. Arch. Biochem. Biophys. 2002, 408, 103-110.
    • (2002) Arch. Biochem. Biophys. , vol.408 , pp. 103-110
    • Cardozo, C.1    Michaud, C.2
  • 31
    • 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
  • 33
    • 56249108370 scopus 로고    scopus 로고
    • Ubiquitin-independent degradation of proteins by the proteasome
    • Jariel-Encontre, I.; Bossis, G.; Piechaczyk, M. Ubiquitin-independent degradation of proteins by the proteasome. Biochim. Biophys. Acta 2008, 1786, 153-177.
    • (2008) Biochim. Biophys. Acta , vol.1786 , pp. 153-177
    • Jariel-Encontre, I.1    Bossis, G.2    Piechaczyk, M.3
  • 34
    • 84874620572 scopus 로고    scopus 로고
    • Subcellular distribution and dynamics of active proteasome complexes unraveled by a workflow combining in vivo complex cross-linking and quantitative proteomics
    • Fabre, B.; Lambour, T.; Delobel, J.; Amalric, F.; Monsarrat, B.; Burlet-Schiltz, O.; Bousquet-Dubouch, M.P. Subcellular distribution and dynamics of active proteasome complexes unraveled by a workflow combining in vivo complex cross-linking and quantitative proteomics. Mol. Cell. Proteomics 2012, 12, 687-699.
    • (2012) Mol. Cell. Proteomics , vol.12 , pp. 687-699
    • Fabre, B.1    Lambour, T.2    Delobel, J.3    Amalric, F.4    Monsarrat, B.5    Burlet-Schiltz, O.6    Bousquet-Dubouch, M.P.7
  • 36
    • 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
  • 38
    • 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
  • 39
    • 84896732643 scopus 로고    scopus 로고
    • The proteasome and the degradation of oxidized proteins: Part III-redox regulation of the proteasomal system
    • Hohn, T.J.; Grune, T. The proteasome and the degradation of oxidized proteins: Part III-redox regulation of the proteasomal system. Redox Biol. 2014, 2, 388-394.
    • (2014) Redox Biol. , vol.2 , pp. 388-394
    • Hohn, T.J.1    Grune, T.2
  • 40
    • 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 , pp. ra88
    • Wang, X.1    Yen, J.2    Kaiser, P.3    Huang, L.4
  • 41
    • 80052265819 scopus 로고    scopus 로고
    • HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress
    • Grune, T.; Catalgol, B.; Licht, A.; Ermak, G.; Pickering, A.M.; Ngo, J.K.; Davies, K.J. HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress. Free Radic. Biol. Med. 2011, 51, 1355-1364.
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 1355-1364
    • Grune, T.1    Catalgol, B.2    Licht, A.3    Ermak, G.4    Pickering, A.M.5    Ngo, J.K.6    Davies, K.J.7
  • 42
    • 84876903554 scopus 로고    scopus 로고
    • Negative regulation of 26S proteasome stability via calpain-mediated cleavage of Rpn10 subunit upon mitochondrial dysfunction in neurons
    • Huang, Q.; Wang, H.; Perry, S.W.; Figueiredo-Pereira, M.E. Negative regulation of 26S proteasome stability via calpain-mediated cleavage of Rpn10 subunit upon mitochondrial dysfunction in neurons. J. Biol. Chem. 2013, 288, 12161-12174.
    • (2013) J. Biol. Chem. , vol.288 , pp. 12161-12174
    • Huang, Q.1    Wang, H.2    Perry, S.W.3    Figueiredo-Pereira, M.E.4
  • 43
    • 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
  • 44
    • 0042313977 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome
    • Imai, J.; Maruya, M.; Yashiroda, H.; Yahara, I.; Tanaka, K. The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J. 2003, 22, 3557-3567.
    • (2003) EMBO J. , vol.22 , pp. 3557-3567
    • Imai, J.1    Maruya, M.2    Yashiroda, H.3    Yahara, I.4    Tanaka, K.5
  • 45
    • 0037102467 scopus 로고    scopus 로고
    • Increased degradation of oxidized proteins in yeast defective in 26S proteasome assembly
    • Inai, Y.; Nishikimi, M. Increased degradation of oxidized proteins in yeast defective in 26S proteasome assembly. Arch. Biochem. Biophys. 2002, 404, 279-284.
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 279-284
    • Inai, Y.1    Nishikimi, M.2
  • 46
    • 0037414834 scopus 로고    scopus 로고
    • Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome
    • Shringarpure, R.; Grune, T.; Mehlhase, J.; Davies, K.J. Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome. J. Biol. Chem. 2003, 278, 311-318.
    • (2003) J. Biol. Chem. , vol.278 , pp. 311-318
    • Shringarpure, R.1    Grune, T.2    Mehlhase, J.3    Davies, K.J.4
  • 48
    • 0026669739 scopus 로고
    • Identification, purification, and characterization of a protein activator (PA28) of the 20S proteasome (macropain)
    • Ma, C.P.; Slaughter, C.A.; DeMartino, G.N. Identification, purification, and characterization of a protein activator (PA28) of the 20S 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
  • 54
    • 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
  • 55
    • 31044449824 scopus 로고    scopus 로고
    • The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP-independent manner by the REGgamma proteasome
    • Li, X.; Lonard, D.M.; Jung, S.Y.; Malovannaya, A.; Feng, Q.; Qin, J.; Tsai, S.Y.; Tsai, M.J.; O’Malley, B.W. The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP-independent manner by the REGgamma proteasome. Cell 2006, 124, 381-392.
    • (2006) Cell , vol.124 , pp. 381-392
    • Li, X.1    Lonard, D.M.2    Jung, S.Y.3    Malovannaya, A.4    Feng, Q.5    Qin, J.6    Tsai, S.Y.7    Tsai, M.J.8    O’Malley, B.W.9
  • 57
    • 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
  • 58
    • 84899411254 scopus 로고    scopus 로고
    • Proteasomes associated with the Blm10 activator protein antagonize mitochondrial fission through degradation of the fission protein Dnm1
    • Tar, K.; Dange, T.; Yang, C.; Yao, Y.; Bulteau, A.L.; Salcedo, E.F.; Braigen, S.; Bouillaud, F.; Finley, D.; Schmidt, M. Proteasomes associated with the Blm10 activator protein antagonize mitochondrial fission through degradation of the fission protein Dnm1. J. Biol. Chem. 2014, 289, 12145-12156.
    • (2014) J. Biol. Chem. , vol.289 , pp. 12145-12156
    • Tar, K.1    Dange, T.2    Yang, C.3    Yao, Y.4    Bulteau, A.L.5    Salcedo, E.F.6    Braigen, S.7    Bouillaud, F.8    Finley, D.9    Schmidt, M.10
  • 59
    • 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
  • 60
    • 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. Investig. 2011, 121, 3689-3700.
    • (2011) J. Clin. Investig. , vol.121 , pp. 3689-3700
    • Li, J.1    Horak, K.M.2    Su, H.3    Sanbe, A.4    Robbins, J.5    Wang, X.6
  • 62
    • 84907543398 scopus 로고    scopus 로고
    • Regulation of the proteasome: Evaluating the lung proteasome as a new therapeutic target
    • Meiners, S.; Keller, I.E.; Semren, N.; Caniard, A. Regulation of the proteasome: Evaluating the lung proteasome as a new therapeutic target. Antioxid. Redox Signal. 2014, doi: 10.1089/ars.2013.5798.
    • (2014) Antioxid. Redox Signal.
    • Meiners, S.1    Keller, I.E.2    Semren, N.3    Caniard, A.4
  • 64
    • 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
  • 65
    • 0037424262 scopus 로고    scopus 로고
    • Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway. Identification of novel gene clusters for cell survival
    • Kwak, M.K.; Wakabayashi, N.; Itoh, K.; Motohashi, H.; Yamamoto, M.; Kensler, T.W. Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway. Identification of novel gene clusters for cell survival. J. Biol. Chem. 2003, 278, 8135-8145.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8135-8145
    • Kwak, M.K.1    Wakabayashi, N.2    Itoh, K.3    Motohashi, H.4    Yamamoto, M.5    Kensler, T.W.6
  • 66
    • 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
  • 67
    • 34547092719 scopus 로고    scopus 로고
    • Role of increased expression of the proteasome in the protective effects of sulforaphane against hydrogen peroxide-mediated cytotoxicity in murine neuroblastoma cells
    • Kwak, M.K.; Cho, J.M.; Huang, B.; Shin, S.; Kensler, T.W. Role of increased expression of the proteasome in the protective effects of sulforaphane against hydrogen peroxide-mediated cytotoxicity in murine neuroblastoma cells. Free Radic. Biol. Med. 2007, 43, 809-817.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 809-817
    • Kwak, M.K.1    Cho, J.M.2    Huang, B.3    Shin, S.4    Kensler, T.W.5
  • 68
    • 79957676924 scopus 로고    scopus 로고
    • Loss of nuclear factor E2-related factor 1 in the brain leads to dysregulation of proteasome gene expression and neurodegeneration
    • Lee, C.S.; Lee, C.; Hu, T.; Nguyen, J.M.; Zhang, J.; Martin, M.V.; Vawter, M.P.; Huang, E.J.; Chan, J.Y. Loss of nuclear factor E2-related factor 1 in the brain leads to dysregulation of proteasome gene expression and neurodegeneration. Proc. Natl. Acad. Sci. USA 2011, 108, 8408-8413.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 8408-8413
    • Lee, C.S.1    Lee, C.2    Hu, T.3    Nguyen, J.M.4    Zhang, J.5    Martin, M.V.6    Vawter, M.P.7    Huang, E.J.8    Chan, J.Y.9
  • 69
    • 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
  • 70
    • 84880327440 scopus 로고    scopus 로고
    • Nuclear factor-erythroid 2-related factor 1 regulates expression of proteasome genes in hepatocytes and protects against endoplasmic reticulum stress and steatosis in mice
    • Lee, C.S.; Ho, D.V.; Chan, J.Y. Nuclear factor-erythroid 2-related factor 1 regulates expression of proteasome genes in hepatocytes and protects against endoplasmic reticulum stress and steatosis in mice. FEBS J. 2013, 280, 3609-3620.
    • (2013) FEBS J. , vol.280 , pp. 3609-3620
    • Lee, C.S.1    Ho, D.V.2    Chan, J.Y.3
  • 72
    • 83755229096 scopus 로고    scopus 로고
    • The Nrf1 CNC-bZIP protein is regulated by the proteasome and activated by hypoxia
    • Chepelev, N.L.; Bennitz, J.D.; Huang, T.; McBride, S.; Willmore, W.G. The Nrf1 CNC-bZIP protein is regulated by the proteasome and activated by hypoxia. PLoS One 2011, 6, e29167.
    • (2011) PLoS One , vol.6
    • Chepelev, N.L.1    Bennitz, J.D.2    Huang, T.3    McBride, S.4    Willmore, W.G.5
  • 73
    • 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
  • 74
    • 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
  • 75
    • 84864357735 scopus 로고    scopus 로고
    • Emerging roles of immunoproteasomes beyond MHC class I antigen processing
    • Ebstein, F.; Kloetzel, P.M.; Kruger, E.; Seifert, U. Emerging roles of immunoproteasomes beyond MHC class I antigen processing. Cell. Mol. Life Sci. 2012, 69, 2543-2558.
    • (2012) Cell. Mol. Life Sci. , vol.69 , pp. 2543-2558
    • Ebstein, F.1    Kloetzel, P.M.2    Kruger, E.3    Seifert, U.4
  • 76
    • 84890859839 scopus 로고    scopus 로고
    • The unique functions of tissue-specific proteasomes
    • Kniepert, A.; Groettrup, M. The unique functions of tissue-specific proteasomes. Trends Biochem. Sci. 2014, 39, 17-24.
    • (2014) Trends Biochem. Sci. , vol.39 , pp. 17-24
    • Kniepert, A.1    Groettrup, M.2
  • 78
    • 78649848069 scopus 로고    scopus 로고
    • The immunoproteasome, the 20S proteasome and the PA28alphabeta proteasome regulator are oxidative-stress-adaptive proteolytic complexes
    • Pickering, A.M.; Koop, A.L.; Teoh, C.Y.; Ermak, G.; Grune, T.; Davies, K.J. The immunoproteasome, the 20S proteasome and the PA28alphabeta proteasome regulator are oxidative-stress-adaptive proteolytic complexes. Biochem. J. 2010, 432, 585-594.
    • (2010) Biochem. J. , vol.432 , pp. 585-594
    • Pickering, A.M.1    Koop, A.L.2    Teoh, C.Y.3    Ermak, G.4    Grune, T.5    Davies, K.J.6
  • 81
    • 72949104779 scopus 로고    scopus 로고
    • Antigen presentation in the thymus for positive selection and central tolerance induction
    • Klein, L.; Hinterberger, M.; Wirnsberger, G.; Kyewski, B. Antigen presentation in the thymus for positive selection and central tolerance induction. Nat. Rev. Immunol. 2009, 9, 833-844.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 833-844
    • Klein, L.1    Hinterberger, M.2    Wirnsberger, G.3    Kyewski, B.4
  • 82
    • 35649014794 scopus 로고    scopus 로고
    • The testis-specific proteasome subunit Prosalpha6T of D. Melanogaster is required for individualization and nuclear maturation during spermatogenesis
    • Zhong, L.; Belote, J.M. The testis-specific proteasome subunit Prosalpha6T of D. Melanogaster is required for individualization and nuclear maturation during spermatogenesis. Development 2007, 134, 3517-3525.
    • (2007) Development , vol.134 , pp. 3517-3525
    • Zhong, L.1    Belote, J.M.2
  • 85
    • 84867230539 scopus 로고    scopus 로고
    • Stress-induced NQO1 controls stability of C/EBPalpha against 20S proteasomal degradation to regulate p63 expression with implications in protection against chemical-induced skin cancer
    • Patrick, B.A.; Jaiswal, A.K. Stress-induced NQO1 controls stability of C/EBPalpha against 20S proteasomal degradation to regulate p63 expression with implications in protection against chemical-induced skin cancer. Oncogene 2012, 31, 4362-4371.
    • (2012) Oncogene , vol.31 , pp. 4362-4371
    • Patrick, B.A.1    Jaiswal, A.K.2
  • 87
    • 0001075830 scopus 로고
    • Induction of NAD(P)H: Quinone reductase in murine hepatoma cells by phenolic antioxidants, azo dyes, and other chemoprotectors: A model system for the study of anticarcinogens
    • De Long, M.J.; Prochaska, H.J.; Talalay, P. Induction of NAD(P)H: Quinone reductase in murine hepatoma cells by phenolic antioxidants, azo dyes, and other chemoprotectors: A model system for the study of anticarcinogens. Proc. Natl. Acad. Sci. USA 1986, 83, 787-791.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 787-791
    • De Long, M.J.1    Prochaska, H.J.2    Talalay, P.3
  • 88
    • 33646857902 scopus 로고    scopus 로고
    • The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol
    • Asher, G.; Dym, O.; Tsvetkov, P.; Adler, J.; Shaul, Y. The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol. Biochemistry 2006, 45, 6372-6378.
    • (2006) Biochemistry , vol.45 , pp. 6372-6378
    • Asher, G.1    Dym, O.2    Tsvetkov, P.3    Adler, J.4    Shaul, Y.5
  • 89
    • 84888984200 scopus 로고    scopus 로고
    • NRH: Quinone oxidoreductase 2 (NQO2) protein competes with the 20S proteasome to stabilize transcription factor CCAAT enhancer-binding protein alpha (C/EBPalpha), leading to protection against gamma radiation-induced myeloproliferative disease
    • Xu, J.; Patrick, B.A.; Jaiswal, A.K. NRH: Quinone oxidoreductase 2 (NQO2) protein competes with the 20S proteasome to stabilize transcription factor CCAAT enhancer-binding protein alpha (C/EBPalpha), leading to protection against gamma radiation-induced myeloproliferative disease. J. Biol. Chem. 2013, 288, 34799-34808.
    • (2013) J. Biol. Chem. , vol.288 , pp. 34799-34808
    • Xu, J.1    Patrick, B.A.2    Jaiswal, A.K.3
  • 90
    • 34347225583 scopus 로고    scopus 로고
    • NRH: Quinone oxidoreductase 2 and NAD(P)H: Quinone oxidoreductase 1 protect tumor suppressor p53 against 20S proteasomal degradation leading to stabilization and activation of p53
    • Gong, X.; Kole, L.; Iskander, K.; Jaiswal, A.K. NRH: Quinone oxidoreductase 2 and NAD(P)H: Quinone oxidoreductase 1 protect tumor suppressor p53 against 20S proteasomal degradation leading to stabilization and activation of p53. Cancer Res. 2007, 67, 5380-5388.
    • (2007) Cancer Res. , vol.67 , pp. 5380-5388
    • Gong, X.1    Kole, L.2    Iskander, K.3    Jaiswal, A.K.4
  • 91
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review
    • Csermely, P.; Schnaider, T.; Soti, C.; Prohaszka, Z.; Nardai, G. The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review. Pharmacol. Ther. 1998, 79, 129-168.
    • (1998) Pharmacol. Ther. , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohaszka, Z.4    Nardai, G.5
  • 92
    • 84886728386 scopus 로고    scopus 로고
    • Hsp90 inhibits alpha-synuclein aggregation by interacting with soluble oligomers
    • Daturpalli, S.; Waudby, C.A.; Meehan, S.; Jackson, S.E. Hsp90 inhibits alpha-synuclein aggregation by interacting with soluble oligomers. J. Mol. Biol. 2013, 425, 4614-4628.
    • (2013) J. Mol. Biol. , vol.425 , pp. 4614-4628
    • Daturpalli, S.1    Waudby, C.A.2    Meehan, S.3    Jackson, S.E.4
  • 93
    • 8544273285 scopus 로고    scopus 로고
    • Hsp90 enhances degradation of oxidized calmodulin by the 20S proteasome
    • Whittier, J.E.; Xiong, Y.; Rechsteiner, M.C.; Squier, T.C. Hsp90 enhances degradation of oxidized calmodulin by the 20S proteasome. J. Biol. Chem. 2004, 279, 46135-46142.
    • (2004) J. Biol. Chem. , vol.279 , pp. 46135-46142
    • Whittier, J.E.1    Xiong, Y.2    Rechsteiner, M.C.3    Squier, T.C.4
  • 94
    • 0036681384 scopus 로고    scopus 로고
    • Interaction of Hsp90 with 20S proteasome: Thermodynamic and kinetic characterization
    • Eleuteri, A.M.; Cuccioloni, M.; Bellesi, J.; Lupidi, G.; Fioretti, E.; Angeletti, M. Interaction of Hsp90 with 20S proteasome: Thermodynamic and kinetic characterization. Proteins 2002, 48, 169-177.
    • (2002) Proteins , vol.48 , pp. 169-177
    • Eleuteri, A.M.1    Cuccioloni, M.2    Bellesi, J.3    Lupidi, G.4    Fioretti, E.5    Angeletti, M.6
  • 95
    • 0028889670 scopus 로고
    • Age-dependent association of isolated bovine lens multicatalytic proteinase complex (proteasome) with heat-shock protein 90, an endogenous inhibitor
    • Wagner, B.J.; Margolis, J.W. Age-dependent association of isolated bovine lens multicatalytic proteinase complex (proteasome) with heat-shock protein 90, an endogenous inhibitor. Arch. Biochem. Biophys. 1995, 323, 455-462.
    • (1995) Arch. Biochem. Biophys. , vol.323 , pp. 455-462
    • Wagner, B.J.1    Margolis, J.W.2
  • 96
    • 0030586350 scopus 로고    scopus 로고
    • Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90
    • Conconi, M.; Szweda, L.I.; Levine, R.L.; Stadtman, E.R.; Friguet, B. Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90. Arch. Biochem. Biophys. 1996, 331, 232-240.
    • (1996) Arch. Biochem. Biophys. , vol.331 , pp. 232-240
    • Conconi, M.1    Szweda, L.I.2    Levine, R.L.3    Stadtman, E.R.4    Friguet, B.5
  • 97
    • 0032527963 scopus 로고    scopus 로고
    • Protection from oxidative inactivation of the 20S proteasome by heat-shock protein 90
    • Conconi, M.; Petropoulos, I.; Emod, I.; Turlin, E.; Biville, F.; Friguet, B. Protection from oxidative inactivation of the 20S proteasome by heat-shock protein 90. Biochem. J. 1998, 333, 407-415.
    • (1998) Biochem. J. , vol.333 , pp. 407-415
    • Conconi, M.1    Petropoulos, I.2    Emod, I.3    Turlin, E.4    Biville, F.5    Friguet, B.6
  • 98
    • 0033033698 scopus 로고    scopus 로고
    • Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones
    • Ullrich, O.; Reinheckel, T.; Sitte, N.; Hass, R.; Grune, T.; Davies, K.J. Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones. Proc. Natl. Acad. Sci. USA 1999, 96, 6223-6228.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6223-6228
    • Ullrich, O.1    Reinheckel, T.2    Sitte, N.3    Hass, R.4    Grune, T.5    Davies, K.J.6
  • 99
    • 75149149780 scopus 로고    scopus 로고
    • Chromatin repair after oxidative stress: Role of PARP-mediated proteasome activation
    • Catalgol, B.; Wendt, B.; Grimm, S.; Breusing, N.; Ozer, N.K.; Grune, T. Chromatin repair after oxidative stress: Role of PARP-mediated proteasome activation. Free Radic. Biol. Med. 2010, 48, 673-680.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 673-680
    • Catalgol, B.1    Wendt, B.2    Grimm, S.3    Breusing, N.4    Ozer, N.K.5    Grune, T.6
  • 100
    • 0026601666 scopus 로고
    • Specific inhibitors of poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferase
    • Banasik, M.; Komura, H.; Shimoyama, M.; Ueda, K. Specific inhibitors of poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferase. J. Biol. Chem. 1992, 267, 1569-1575.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1569-1575
    • Banasik, M.1    Komura, H.2    Shimoyama, M.3    Ueda, K.4
  • 103
    • 51949098691 scopus 로고    scopus 로고
    • PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex
    • Abbas, T.; Sivaprasad, U.; Terai, K.; Amador, V.; Pagano, M.; Dutta, A. PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex. Genes Dev. 2008, 22, 2496-2506.
    • (2008) Genes Dev. , vol.22 , pp. 2496-2506
    • Abbas, T.1    Sivaprasad, U.2    Terai, K.3    Amador, V.4    Pagano, M.5    Dutta, A.6
  • 104
    • 77953309753 scopus 로고    scopus 로고
    • MDM2 promotes proteasomal degradation of p21WAF1 via a conformation change
    • Xu, H.; Zhang, Z.; Li, M.; Zhang, R. MDM2 promotes proteasomal degradation of p21WAF1 via a conformation change. J. Biol. Chem. 2010, 285, 18407-18414.
    • (2010) J. Biol. Chem. , vol.285 , pp. 18407-18414
    • Xu, H.1    Zhang, Z.2    Li, M.3    Zhang, R.4
  • 105
    • 0346243936 scopus 로고    scopus 로고
    • MDM2 promotes p21WAF1/CIP1 proteasomal turnover independently of ubiquitylation
    • Jin, Y.; Lee, H.; Zeng, S.X.; Dai, M.S.; Lu, H. MDM2 promotes p21WAF1/CIP1 proteasomal turnover independently of ubiquitylation. EMBO J. 2003, 22, 6365-6377.
    • (2003) EMBO J. , vol.22 , pp. 6365-6377
    • Jin, Y.1    Lee, H.2    Zeng, S.X.3    Dai, M.S.4    Lu, H.5
  • 106
    • 1942437554 scopus 로고    scopus 로고
    • MDM2 is a negative regulator of p21WAF1/CIP1, independent of p53
    • Zhang, Z.; Wang, H.; Li, M.; Agrawal, S.; Chen, X.; Zhang, R. MDM2 is a negative regulator of p21WAF1/CIP1, independent of p53. J. Biol. Chem. 2004, 279, 16000-16006.
    • (2004) J. Biol. Chem. , vol.279 , pp. 16000-16006
    • Zhang, Z.1    Wang, H.2    Li, M.3    Agrawal, S.4    Chen, X.5    Zhang, R.6
  • 107
    • 0035872863 scopus 로고    scopus 로고
    • A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome
    • Touitou, R.; Richardson, J.; Bose, S.; Nakanishi, M.; Rivett, J.; Allday, M.J. A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome. EMBO J. 2001, 20, 2367-2375.
    • (2001) EMBO J. , vol.20 , pp. 2367-2375
    • Touitou, R.1    Richardson, J.2    Bose, S.3    Nakanishi, M.4    Rivett, J.5    Allday, M.J.6
  • 108
    • 77749320340 scopus 로고    scopus 로고
    • 14-3-3Tau regulates ubiquitin-independent proteasomal degradation of p21, a novel mechanism of p21 downregulation in breast cancer
    • Wang, B.; Liu, K.; Lin, H.Y.; Bellam, N.; Ling, S.; Lin, W.C. 14-3-3Tau regulates ubiquitin-independent proteasomal degradation of p21, a novel mechanism of p21 downregulation in breast cancer. Mol. Cell. Biol. 2010, 30, 1508-1527.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1508-1527
    • Wang, B.1    Liu, K.2    Lin, H.Y.3    Bellam, N.4    Ling, S.5    Lin, W.C.6
  • 110
    • 77953496625 scopus 로고    scopus 로고
    • The NF-κB family of transcription factors and its regulation
    • Oeckinghaus, A.; Ghosh, S. The NF-κB family of transcription factors and its regulation. Cold Spring Harb. Perspect. Biol. 2009, doi: 10.1101/cshperspect.a000034.
    • (2009) Cold Spring Harb. Perspect. Biol.
    • Oeckinghaus, A.1    Ghosh, S.2
  • 111
    • 0032488219 scopus 로고    scopus 로고
    • Association between HTLV-1 Tax and I kappa B alpha is dependent on the I kappa B alpha phosphorylation state
    • Petropoulos, L.; Hiscott, J. Association between HTLV-1 Tax and I kappa B alpha is dependent on the I kappa B alpha phosphorylation state. Virology 1998, 252, 189-199.
    • (1998) Virology , vol.252 , pp. 189-199
    • Petropoulos, L.1    Hiscott, J.2
  • 112
    • 0029902650 scopus 로고    scopus 로고
    • Effects on NF-kappa B1/p105 processing of the interaction between the HTLV-1 transactivator Tax and the proteasome
    • Rousset, R.; Desbois, C.; Bantignies, F.; Jalinot, P. Effects on NF-kappa B1/p105 processing of the interaction between the HTLV-1 transactivator Tax and the proteasome. Nature 1996, 381, 328-331.
    • (1996) Nature , vol.381 , pp. 328-331
    • Rousset, R.1    Desbois, C.2    Bantignies, F.3    Jalinot, P.4
  • 114
    • 84899928291 scopus 로고    scopus 로고
    • Regulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyond
    • Cui, Z.; Scruggs, S.B.; Gilda, J.E.; Ping, P.; Gomes, A.V. Regulation of cardiac proteasomes by ubiquitination, SUMOylation, and beyond. J. Mol. Cell. Cardiol. 2013, 71, 32-42.
    • (2013) J. Mol. Cell. Cardiol. , vol.71 , pp. 32-42
    • Cui, Z.1    Scruggs, S.B.2    Gilda, J.E.3    Ping, P.4    Gomes, A.V.5
  • 115
    • 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
  • 116
    • 0035143449 scopus 로고    scopus 로고
    • Polo-like kinase interacts with proteasomes and regulates their activity
    • Feng, Y.; Longo, D.L.; Ferris, D.K. Polo-like kinase interacts with proteasomes and regulates their activity. Cell Growth Differ. 2001, 12, 29-37.
    • (2001) Cell Growth Differ. , vol.12 , pp. 29-37
    • Feng, Y.1    Longo, D.L.2    Ferris, D.K.3
  • 117
    • 84879201308 scopus 로고    scopus 로고
    • Impaired assembly and post-translational regulation of 26S proteasome in human end-stage heart failure
    • Day, S.M.; Divald, A.; Wang, P.; Davis, F.; Bartolone, S.; Jones, R.; Powell, S.R. Impaired assembly and post-translational regulation of 26S proteasome in human end-stage heart failure. Circ. Heart Fail. 2013, 6, 544-549.
    • (2013) Circ. Heart Fail. , vol.6 , pp. 544-549
    • Day, S.M.1    Divald, A.2    Wang, P.3    Davis, F.4    Bartolone, S.5    Jones, R.6    Powell, S.R.7
  • 118
    • 1542344946 scopus 로고    scopus 로고
    • Phosphorylation of 20S proteasome alpha subunit C8 (alpha7) stabilizes the 26S proteasome and plays a role in the regulation of proteasome complexes by gamma-interferon
    • Bose, S.; Stratford, F.L.; Broadfoot, K.I.; Mason, G.G.; Rivett, A.J. Phosphorylation of 20S proteasome alpha subunit C8 (alpha7) stabilizes the 26S proteasome and plays a role in the regulation of proteasome complexes by gamma-interferon. Biochem. J. 2004, 378, 177-184.
    • (2004) Biochem. J. , vol.378 , pp. 177-184
    • Bose, S.1    Stratford, F.L.2    Broadfoot, K.I.3    Mason, G.G.4    Rivett, A.J.5
  • 120
    • 0037414784 scopus 로고    scopus 로고
    • 20S proteasome from saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated
    • Demasi, M.; Silva, G.M.; Netto, L.E. 20S proteasome from saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated. J. Biol. Chem. 2003, 278, 679-685.
    • (2003) J. Biol. Chem. , vol.278 , pp. 679-685
    • Demasi, M.1    Silva, G.M.2    Netto, L.E.3
  • 121
    • 43549092673 scopus 로고    scopus 로고
    • Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome
    • Silva, G.M.; Netto, L.E.; Discola, K.F.; Piassa-Filho, G.M.; Pimenta, D.C.; Barcena, J.A.; Demasi, M. Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome. FEBS J. 2008, 275, 2942-2955.
    • (2008) FEBS J. , vol.275 , pp. 2942-2955
    • Silva, G.M.1    Netto, L.E.2    Discola, K.F.3    Piassa-Filho, G.M.4    Pimenta, D.C.5    Barcena, J.A.6    Demasi, M.7
  • 122
    • 0024094566 scopus 로고
    • The association of prosomes with some of the intermediate filament networks of the animal cell
    • De Sa, M.F.G.; de Sa, C.M.; Harper, F.; Olink-Coux, M.; Huesca, M.; Scherrer, K. The association of prosomes with some of the intermediate filament networks of the animal cell. J. Cell Biol. 1988, 107, 1517-1530.
    • (1988) J. Cell Biol. , vol.107 , pp. 1517-1530
    • De Sa, M.F.G.1    de Sa, C.M.2    Harper, F.3    Olink-Coux, M.4    Huesca, M.5    Scherrer, K.6
  • 123
    • 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.; Scherrer, K. Cytolocation of prosome antigens on intermediate filament subnetworks of cytokeratin, vimentin and desmin type. J. Cell Sci. 1994, 107, 353-366.
    • (1994) J. Cell Sci. , vol.107 , 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
  • 124
    • 0034672211 scopus 로고    scopus 로고
    • Association of immunoproteasomes with the endoplasmic reticulum
    • Brooks, P.; Murray, R.Z.; Mason, G.G.; Hendil, K.B.; Rivett, A.J. Association of immunoproteasomes with the endoplasmic reticulum. Biochem. J. 2000, 352, 611-615.
    • (2000) Biochem. J. , vol.352 , pp. 611-615
    • Brooks, P.1    Murray, R.Z.2    Mason, G.G.3    Hendil, K.B.4    Rivett, A.J.5
  • 128
    • 0036735384 scopus 로고    scopus 로고
    • Nuclear localization of proteasomes participates in stress-inducible resistance of solid tumor cells to topoisomerase II-directed drugs
    • Ogiso, Y.; Tomida, A.; Tsuruo, T. Nuclear localization of proteasomes participates in stress-inducible resistance of solid tumor cells to topoisomerase II-directed drugs. Cancer Res. 2002, 62, 5008-5012.
    • (2002) Cancer Res. , vol.62 , pp. 5008-5012
    • Ogiso, Y.1    Tomida, A.2    Tsuruo, T.3
  • 130
    • 79957472437 scopus 로고    scopus 로고
    • Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane
    • Yoshii, S.R.; Kishi, C.; Ishihara, N.; Mizushima, N. Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane. J. Biol. Chem. 2011, 286, 19630-19640.
    • (2011) J. Biol. Chem. , vol.286 , pp. 19630-19640
    • Yoshii, S.R.1    Kishi, C.2    Ishihara, N.3    Mizushima, N.4
  • 131
    • 84891373742 scopus 로고    scopus 로고
    • T lymphocytes export proteasomes by way of microparticles: A possible mechanism for generation of extracellular proteasomes
    • Bochmann, I.; Ebstein, F.; Lehmann, A.; Wohlschlaeger, J.; Sixt, S.U.; Kloetzel, P.M.; Dahlmann, B. T lymphocytes export proteasomes by way of microparticles: A possible mechanism for generation of extracellular proteasomes. J. Cell. Mol. Med. 2014, 18, 59-68.
    • (2014) J. Cell. Mol. Med. , vol.18 , pp. 59-68
    • Bochmann, I.1    Ebstein, F.2    Lehmann, A.3    Wohlschlaeger, J.4    Sixt, S.U.5    Kloetzel, P.M.6    Dahlmann, B.7
  • 132
    • 51649096925 scopus 로고    scopus 로고
    • Circulating 20S proteasome levels in patients with mixed connective tissue disease and systemic lupus erythematosus
    • Majetschak, M.; Perez, M.; Sorell, L.T.; Lam, J.; Maldonado, M.E.; Hoffman, R.W. Circulating 20S proteasome levels in patients with mixed connective tissue disease and systemic lupus erythematosus. Clin. Vaccine Immunol. 2008, 15, 1489-1493.
    • (2008) Clin. Vaccine Immunol. , vol.15 , pp. 1489-1493
    • Majetschak, M.1    Perez, M.2    Sorell, L.T.3    Lam, J.4    Maldonado, M.E.5    Hoffman, R.W.6
  • 136
    • 56449112645 scopus 로고    scopus 로고
    • Extracellular, circulating proteasomes and ubiquitin-incidence and relevance
    • Sixt, S.U.; Dahlmann, B. Extracellular, circulating proteasomes and ubiquitin-incidence and relevance. Biochim. Biophys. Acta 2008, 1782, 817-823.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 817-823
    • Sixt, S.U.1    Dahlmann, B.2
  • 137
    • 84890282151 scopus 로고    scopus 로고
    • Mechanism of cleavage of alpha-synuclein by the 20S proteasome and modulation of its degradation by the redox state of the N-terminal methionines
    • Alvarez-Castelao, B.; Goethals, M.; Vandekerckhove, J.; Castano, J.G. Mechanism of cleavage of alpha-synuclein by the 20S proteasome and modulation of its degradation by the redox state of the N-terminal methionines. Biochim. Biophys. Acta 2014, 1843, 352-365.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 352-365
    • Alvarez-Castelao, B.1    Goethals, M.2    Vandekerckhove, J.3    Castano, J.G.4
  • 139
    • 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
  • 140
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: From research tools to drug candidates
    • Kisselev, A.F.; Goldberg, A.L. Proteasome inhibitors: From research tools to drug candidates. Chem. Biol. 2001, 8, 739-758.
    • (2001) Chem. Biol. , vol.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 142
    • 84890207562 scopus 로고    scopus 로고
    • Applied techniques for mining natural proteasome inhibitors
    • Stein, M.L.; Groll, M. Applied techniques for mining natural proteasome inhibitors. Biochim. Biophys. Acta 2014, 1843, 26-38.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 26-38
    • Stein, M.L.1    Groll, M.2


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