메뉴 건너뛰기




Volumn 52, Issue 4, 2010, Pages 277-300

Proteasomes: Their role in cellular processes

Author keywords

Apoptosis; Cell cycle; Differentiation; DNA repair; Immune response; Proteasomes; Transcription

Indexed keywords

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

EID: 77952054343     PISSN: 00413771     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (15)

References (310)
  • 1
    • 77952069598 scopus 로고    scopus 로고
    • Russian source
  • 2
    • 77952033141 scopus 로고    scopus 로고
    • Russian source
  • 3
    • 77952052113 scopus 로고    scopus 로고
    • Russian source
  • 4
    • 77952071642 scopus 로고    scopus 로고
    • Russian source
  • 5
    • 77952083478 scopus 로고    scopus 로고
    • Russian source
  • 6
    • 77952054572 scopus 로고    scopus 로고
    • Russian source
  • 7
    • 77952065177 scopus 로고    scopus 로고
    • Russian source
  • 8
    • 77952038199 scopus 로고    scopus 로고
    • Russian source
  • 9
    • 77952018021 scopus 로고    scopus 로고
    • Russian source
  • 10
    • 77952078055 scopus 로고    scopus 로고
    • Russian source
  • 11
    • 77952018006 scopus 로고    scopus 로고
    • Russian source
  • 12
    • 77952033159 scopus 로고    scopus 로고
    • Russian source
  • 13
    • 0035215395 scopus 로고    scopus 로고
    • Proteasome inhibition in cancer: Development of PS-341
    • Adams J. 2001. Proteasome inhibition in cancer: development of PS-341. Semin. Oncol. 28 : 613-619.
    • (2001) Semin. Oncol. , vol.28 , pp. 613-619
    • Adams, J.1
  • 14
    • 0037376230 scopus 로고    scopus 로고
    • Potential for proteasome inhibition in the treatment of cancer
    • DOI 10.1016/S1359-6446(03)02647-3, PII S1359644603026473
    • Adams J. 2003. Potential for proteasome inhibition in the treatment of cancer. Drug Discov. Today. 8 : 307-315. (Pubitemid 36332222)
    • (2003) Drug Discovery Today , vol.8 , Issue.7 , pp. 307-315
    • Adams, J.1
  • 16
    • 4344598382 scopus 로고    scopus 로고
    • Adrain C., Creagh E. M., Cullen S. P., Martin S. J. 2004. Caspase-dependent inactivation of proteasome function during programmed cell death in Drosophila and man. J. Biol. Chem. 279 : 36 923 - 36 930.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36923-36930
    • Adrain, C.1    Creagh, E.M.2    Cullen, S.P.3    Martin, S.J.4
  • 17
    • 0023849528 scopus 로고
    • A new type of prosome-like particle, composed of small cytoplasmic RNA and multimers of a 21-kDa protein, inhibits protein synthesis in vitro
    • Akhayat O., Infante A., Infante D., Martins S. A. C., de Grossi S. A. M. F., de Scherrer K. 1987. A new tipe of prosome-like particle, composed of small cytoplasmatic RNA and multimers of 21-kDa protein, inhibits protein synthesis in vitro. Eur. J. Biochem. 170 : 23-33. (Pubitemid 18028436)
    • (1988) European Journal of Biochemistry , vol.170 , Issue.1-2 , pp. 23-33
    • Akhayat, O.1    Infante, A.A.2    Infante, D.3    Martins de Sa, C.4    Grossi de Sa, M.-F.5    Scherrer, K.6
  • 18
    • 0034844509 scopus 로고    scopus 로고
    • Proteasome inhibitor-induced apoptosis of B-chronic lymphocytic leukaemia cells involves cytochrome c release and caspase activation, accompanied by formation of an 700 kDa Apaf-1 containing apoptosome complex
    • DOI 10.1038/sj.leu.2402201
    • Almond J. B., Snowden R. T., Hunter A., Dinsdale D., Cain K., Cohen G. M. 2001. Proteasome inhibitor-induced apoptosis of B-chronic lymphocytic leukaemia cells involves cytochrome c release and caspase activation, accompanied by formation of an approximately 700 kDa Apaf-1 containing apoptosome complex. Leukemia. 15 : 1388-1397. (Pubitemid 32785308)
    • (2001) Leukemia , vol.15 , Issue.9 , pp. 1388-1397
    • Almond, J.B.1    Snowden, R.T.2    Hunter, A.3    Dinsdale, D.4    Cain, K.5    Cohen, G.M.6
  • 19
    • 24044488987 scopus 로고    scopus 로고
    • Mechanism of direct degradation of IkappaBalpha by 20S proteasome
    • DOI 10.1016/j.febslet.2005.07.060, PII S0014579305009233
    • Alvarez-Castelao B., Castaño J. G. 2005. Mechanism of direct degradation of IkappaBalpha by 20S proteasome. FEBS Lett. 579 : 4797-4802. (Pubitemid 41218666)
    • (2005) FEBS Letters , vol.579 , Issue.21 , pp. 4797-4802
    • Alvarez-Castelao, B.1    Castano, J.G.2
  • 21
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • DOI 10.1016/j.bbamcr.2004.10.003, PII S0167488904002538, The Ubiquitin-Proteasome System
    • Amerik A. Y., Hochstrasser M. 2004. Mechanism and function of deubiquitinating enzymes. Biochim. Biophys. Acta. 1695 : 189-207. (Pubitemid 39574973)
    • (2004) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1695 , Issue.1-3 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 22
    • 0032429122 scopus 로고    scopus 로고
    • Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts
    • An B., Goldfarb R. H., Siman R., Dou Q. P. 1998. Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibro-blasts. Cell Death Differ. 5: 1062-1075. (Pubitemid 29008220)
    • (1998) Cell Death and Differentiation , vol.5 , Issue.12 , pp. 1062-1075
    • An, B.1    Goldfarb, R.H.2    Siman, R.3    Ping Dou, Q.4
  • 23
    • 18344386695 scopus 로고    scopus 로고
    • SCF-mediated protein degradation and cell cycle control
    • DOI 10.1038/sj.onc.1208614
    • Ang X. L., Wade Harper J. 2005. SCF-mediated protein degradation and cell cycle control. Oncogene. 24 (17) :2860-2870. (Pubitemid 40638095)
    • (2005) Oncogene , vol.24 , Issue.17 , pp. 2860-2870
    • Ang, X.L.1    Harper, J.W.2
  • 24
    • 0033168717 scopus 로고    scopus 로고
    • Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly
    • DOI 10.1093/emboj/18.13.3575
    • Arendt C. S., Hochstrasser M. 1999. Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly. EMBO J. 18 : 3575-3585. (Pubitemid 29308838)
    • (1999) EMBO Journal , vol.18 , Issue.13 , pp. 3575-3585
    • Arendt, C.S.1    Hochstrasser, M.2
  • 25
    • 0024285837 scopus 로고
    • Identity of the 19S 'prosome' particle with the large multifunctional protease complex of mammalian cells (the proteasome)
    • Arrigo A. P., Tanaka K., Goldberg A. L., Welch W. J. 1988. Identity of the 19S «prosome» particle with the large multifunctional protease complex of mammalian cells (the proteasome). Nature. 331 : 192-194. (Pubitemid 18042153)
    • (1988) Gynecologic Oncology , vol.29 , Issue.1 , pp. 192-194
    • Arrigo, A.-P.1    Tanaka, K.2    Goldberg, A.L.3    Welch, W.J.4
  • 26
    • 0036791010 scopus 로고    scopus 로고
    • Mdm-2 and ubiquitin-independent p53 proteasomal degradation regulated by NQO1
    • Asher G., Lotem J., Sachs L., Kahana C., Shaul Y. 2002. Mdm-2 and ubiquitin-independent p53 proteasomal degradation regulated by NQO1. Proc. Nat. Acad. Sci. USA. 99: 13 125 - 13 130.
    • (2002) Proc. Nat. Acad. Sci. USA. , vol.99 , pp. 13125-13130
    • Asher, G.1    Lotem, J.2    Sachs, L.3    Kahana, C.4    Shaul, Y.5
  • 27
    • 33644857820 scopus 로고    scopus 로고
    • Genomic association of the proteasome demonstrates overlapping gene regulatory activity with transcription factor substrates
    • DOI 10.1016/j.molcel.2006.02.020, PII S1097276506001420
    • Auld K. L., Brown C. R., Casolari J. M., Komili S., Silver P. A. 2006. Genomic association of the proteasome demonstrates overlapping gene regulatory activity with transcription factor substrates. Mol. Cell. 21 : 861-871. (Pubitemid 43376135)
    • (2006) Molecular Cell , vol.21 , Issue.6 , pp. 861-871
    • Auld, K.L.1    Brown, C.R.2    Casolari, J.M.3    Komili, S.4    Silver, P.A.5
  • 28
    • 33746268117 scopus 로고    scopus 로고
    • Transcriptional regulation by the proteasome as a mechanism for cellular protein homeostasis
    • Auld K. L., Silver P. A. 2006. Transcriptional regulation by the proteasome as a mechanism for cellular protein homeostasis. Cell Cycle. 5 : 1503-1505. (Pubitemid 44091968)
    • (2006) Cell Cycle , vol.5 , Issue.14 , pp. 1503-1505
    • Auld, K.L.1    Silver, P.A.2
  • 29
    • 0037397484 scopus 로고    scopus 로고
    • Orchestrating nuclear functions: Ubiquitin sets the rhythm
    • DOI 10.1016/S0968-0004(03)00055-0
    • Bach I., Ostendorf H. P. 2003. Orchestrating nuclear functions: ubiquitin sets the rhythm. TiBS. 28 : 189-195. (Pubitemid 36507157)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.4 , pp. 189-195
    • Bach, I.1    Ostendorff, H.P.2
  • 31
    • 2442676283 scopus 로고    scopus 로고
    • Hyperphosphorylation of rat liver proteasome subunits: The effects of ethanol and okadaic acid are compared
    • DOI 10.1016/S0024-3205(04)00319-4, PII S0024320504003194
    • Bardag-Gorce F., Venkatesh R., Li J., French B. A., French S. W. 2004. Hyperphosphorylation of rat liver proteasome subunits: the effects of ethanol and okadaic acid are compared. Life Sci. 75 : 585-597. (Pubitemid 38670265)
    • (2004) Life Sciences , vol.75 , Issue.5 , pp. 585-597
    • Bardag-Gorce, F.1    Venkatesh, R.2    Li, J.3    French, B.A.4    French, S.W.5
  • 32
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a selfcompartmentalizing protease
    • Baumeister W., Walz J., Zuhl F., Seemuller E. 1998. The proteasome: paradigm of a selfcompartmentalizing protease. Cell. 92 : 367-380.
    • (1998) Cell. , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 33
    • 0035067597 scopus 로고    scopus 로고
    • The unfolding of substrates and ubiquitin-independent protein degradation by proteasomes
    • DOI 10.1016/S0300-9084(01)01244-5
    • Benaroudj N., Tarcsa E., Cascio P., Goldberg A. L. 2001. The unfolding of substrates and ubiquitin-independent protein degradation by proteasomes. Biochimie. 83 : 311-318. (Pubitemid 32293651)
    • (2001) Biochimie , vol.83 , Issue.3-4 , pp. 311-318
    • Benaroudj, N.1    Tarcsa, E.2    Cascio, P.3    Goldberg, A.L.4
  • 34
    • 0032103504 scopus 로고    scopus 로고
    • Proteasome activities decrease during dexamethasone-induced apoptosis at thymocytes
    • Beyette J., Mason G., Murray R., Cohen G., Rivett J. 1998. Proteasome activities decrease during dexamethasone-induced apoptosis of thymocytes. Biochem. J. 332 : 315-320. (Pubitemid 28271861)
    • (1998) Biochemical Journal , vol.332 , Issue.2 , pp. 315-320
    • Beyette, J.1    Mason, G.G.F.2    Murray, R.Z.3    Cohen, G.M.4    Rivett, A.J.5
  • 36
    • 0035863064 scopus 로고    scopus 로고
    • Gamma-Interferon decreases the level of 26 S proteasomes and changes the pattern of phosphorylation
    • DOI 10.1042/0264-6021:3530291
    • Bose S., Brooks P., Mason G. G., Rivett A. J. 2001. Gamma-interferon decreases the level of 26 S proteasomes and changes the pattern of phosphorylation. Biochem. J. 353 : 291-297. (Pubitemid 32096938)
    • (2001) Biochemical Journal , vol.353 , Issue.2 , pp. 291-297
    • Bose, S.1    Brooks, P.2    Mason, G.G.F.3    Rivett, A.J.4
  • 37
    • 0033119577 scopus 로고    scopus 로고
    • Phosphorylation of proteasomes in mammalian cells
    • Bose S., Mason G. G., Rivett A. J. 1999. Phosphorylation of proteasomes in mammalian cells. Mol. Biol. Rep. 26 : 11-14. (Pubitemid 29223244)
    • (1999) Molecular Biology Reports , vol.26 , Issue.1-2 , pp. 11-14
    • Bose, S.1    Mason, G.G.F.2    Rivett, A.J.3
  • 38
    • 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
    • DOI 10.1042/BJ20031122
    • Bose S., Stratford F. L., Broadfoot K. I., Mason G. G., Rivett A. J. 2004. 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. 378 : 177-184. (Pubitemid 38299555)
    • (2004) Biochemical Journal , vol.378 , Issue.1 , pp. 177-184
    • Bose, S.1    Stratford, F.L.L.2    Broadfoot, K.I.3    Mason, G.G.F.4    Rivett, A.J.5
  • 39
    • 33645541393 scopus 로고    scopus 로고
    • Degrade to create: Developmental requirements for ubiquitin-mediated proteolysis during early C. Elegans embryogenesis
    • Bowerman B., Kurz T. 2006. Degrade to create: developmental requirements for ubiquitin-mediated proteolysis during early C. Elegans embryogenesis. Development. 133 : 773-784.
    • (2006) Development , vol.133 , pp. 773-784
    • Bowerman, B.1    Kurz, T.2
  • 42
    • 0033974063 scopus 로고    scopus 로고
    • Posttranslational modification of Bcl-2 facilitates its proteasome- dependent degradation: Molecular characterization of the involved signaling pathway
    • DOI 10.1128/MCB.20.5.1886-1896.2000
    • Breitschopf K., Haendeler J., Malchow P., Zeiher A.M., Dimmeler S. 2000a. Posttranslational modification of Bcl - 2 facilitates its proteasome-dependent degradation: molecular characterization of the involved signaling pathway. Mol. Cell. Biol. 20 : 1886-1896. (Pubitemid 30100205)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.5 , pp. 1886-1896
    • Breitschopf, K.1    Haendeler, J.2    Malchow, P.3    Zeiher, A.M.4    Dimmeler, S.5
  • 43
    • 0034647563 scopus 로고    scopus 로고
    • Ubiquitin-mediated degradation of the proapoptotic active form of bid. A functional consequence on apoptosis induction
    • DOI 10.1074/jbc.M001083200
    • Breitschopf K., Zeiher A. M., Dimmeler S. 2000b. Ubiquitin-mediated degradation of the proapoptotic active form of bid. A functional consequence on apoptosis induction. J. Biol. Chem. 275 : 21 648 - 21 652. (Pubitemid 30481872)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.28 , pp. 21648-21652
    • Breitschopf, K.1    Zeiher, A.M.2    Dimmeler, S.3
  • 45
  • 46
    • 0034641694 scopus 로고    scopus 로고
    • Identification and characterization of a mammalian protein interacting with 20S proteasome precursors
    • Burri L., Höckendorff J., Boehm U., Klamp T., Dohmen R. J., Levy F. 2000. Identification and characterization of a mammalian protein interacting with 20S proteasome precursors. Proc. Nat. Acad. Sci. USA. 97 : 10 348 - 10 353.
    • (2000) Proc. Nat. Acad. Sci. USA , vol.97 , pp. 10348-10353
    • Burri, L.1    Höckendorff, J.2    Boehm, U.3    Klamp, T.4    Dohmen, R.J.5    Levy, F.6
  • 47
    • 0034651104 scopus 로고    scopus 로고
    • Proteasome involvement and accumulation of ubiquitinated proteins in cerebellar granule neurons undergoing apoptosis
    • Canu N., Barbato C., Ciotti M. T., Serafino A., Dus L., Calissano P. 2000. Proteasome involvement and accumulation of ubiquitinated proteins in cerebellar granule neurons undergoing apoptosis. J. Neurosci. 20 : 589-599. (Pubitemid 30225561)
    • (2000) Journal of Neuroscience , vol.20 , Issue.2 , pp. 589-599
    • Canu, N.1    Barbato, C.2    Ciotti, M.T.3    Serafino, A.4    Dus, L.5    Calissano, P.6
  • 48
    • 0029876795 scopus 로고    scopus 로고
    • Phosphorylation of C8 and C9 subunits of the multicatalytic proteinase by casein kinase II and identification of the C8 phosphorylation sites by direct mutagenesis
    • DOI 10.1021/bi952540s
    • Castaño J. G., Mahillo E., Arizti P., Arribas J. 1996. Phosphorylation of C8 and C9 subunits of the multicatalytic proteinase by casein kinase II and identification of the C8 phosphorylation sites by direct mutagenesis. Biochemistry. 35 : 3782-3789. (Pubitemid 26102167)
    • (1996) Biochemistry , vol.35 , Issue.12 , pp. 3782-3789
    • Castano, J.G.1    Mahillo, E.2    Arizti, P.3    Arribas, J.4
  • 50
    • 0035315902 scopus 로고    scopus 로고
    • The levels of MDM2 protein are decreased by a proteasomemediated proteolysis prior to caspase-3-dependent pRb and PARP cleavages
    • Cho J. W., Park J. C., Lee J. C., Kwon T. K., Park J. W., Baek W.K., Suh S. I., Suh M. H. 2001. The levels of MDM2 protein are decreased by a proteasomemediated proteolysis prior to caspase-3-dependent pRb and PARP cleavages. J. Korean Med. Sci. 16 : 135-139.
    • (2001) J. Korean Med. Sci. , vol.16 , pp. 135-139
    • Cho, J.W.1    Park, J.C.2    Lee, J.C.3    Kwon, T.K.4    Park, J.W.5    Baek, W.K.6    Suh, S.I.7    Suh, M.H.8
  • 51
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • DOI 10.1016/S0896-6273(03)00606-8
    • Ciechanover A., Brundin P. 2003. The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron. 40 : 427-446. (Pubitemid 37244106)
    • (2003) Neuron , vol.40 , Issue.2 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 52
    • 9644272423 scopus 로고    scopus 로고
    • The ubiquitin system: Pathogenesis of human diseases and drug targeting
    • DOI 10.1016/j.bbamcr.2004.09.018, PII S0167488904002344, The Ubiquitin-Proteasome System
    • Ciechanover A., Schwartz A.L. 2004. The ubiquitin system: pathogenesis of human diseases and drug targeting. Biochim. biophys. acta. 1695 : 3-17. (Pubitemid 39574964)
    • (2004) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1695 , Issue.1-3 , pp. 3-17
    • Ciechanover, A.1    Schwartz, A.L.2
  • 55
    • 0035067587 scopus 로고    scopus 로고
    • Antizyme, a mediator of ubiquitin-independent proteasomal degradation
    • DOI 10.1016/S0300-9084(01)01252-4
    • Coffino P. 2001. Antizyme, a mediator of ubiquitin-independent proteasomal degradation. Biochimie. 83 : 319-323. (Pubitemid 32293652)
    • (2001) Biochimie , vol.83 , Issue.3-4 , pp. 319-323
    • Coffino, P.1
  • 56
    • 33644867538 scopus 로고    scopus 로고
    • The proteasome: A utility tool for transcription?
    • Collins G.A., Tansey W.P. 2006. The proteasome: a utility tool for transcription? Curr. Opin. Genet. Develop. 16 : 197-202.
    • (2006) Curr. Opin. Genet. Develop. , vol.16 , pp. 197-202
    • Collins, G.A.1    Tansey, W.P.2
  • 59
    • 0035074614 scopus 로고    scopus 로고
    • Subtypes of 20S proteasomes from skeletal muscle
    • DOI 10.1016/S0300-9084(01)01240-8
    • Dahlmann B., Ruppert T., Kloetzel P. M., Kuehn L. 2001. Subtypes of 20S proteasomes from skeletal muscle. Biochimie 83 : 295-299. (Pubitemid 32293649)
    • (2001) Biochimie , vol.83 , Issue.3-4 , pp. 295-299
    • Dahlmann, B.1    Ruppert, T.2    Kloetzel, P.M.3    Kuehn, L.4
  • 62
    • 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. 1998. The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNFalpha-initiated apoptosis. Br. J. Canc. 77 : 1103-1107. (Pubitemid 28116281)
    • (1998) British Journal of Cancer , vol.77 , Issue.7 , 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
  • 63
    • 0033529596 scopus 로고    scopus 로고
    • The proteasome, a novel protease regulated by multiple mechanisms
    • Demartino G. N., Slaughter C. A. 1999. The proteasome, a novel protease regulated by multiple mechanisms. J. Biol. Chem. 274 : 22 123 - 22 126. (Pubitemid 129529211)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.32 , pp. 22123-22126
    • DeMartino, G.N.1    Slaughter, C.A.2
  • 64
    • 27244462417 scopus 로고    scopus 로고
    • Glutathiolation of the proteasome is enhanced by proteolytic inhibitors
    • DOI 10.1006/abbi.2001.2332
    • Demasi M., Shringarpure R., Davies K. J. 2001. Glutathiolation of the proteasome is enhanced by proteolytic inhibitors. Arch. Biochem. Biophys. 389 : 254-263. (Pubitemid 32881951)
    • (2001) Archives of Biochemistry and Biophysics , vol.389 , Issue.2 , pp. 254-263
    • Demasi, M.1    Shringarpure, R.2    Davies, K.J.A.3
  • 65
    • 0037414784 scopus 로고    scopus 로고
    • 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated
    • Demasi M., Silva G. M., Netto L. E. 2003. 20 S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated. J. Biol. Chem. 278 : 679-685.
    • (2003) J. Biol. Chem. , vol.278 , pp. 679-685
    • Demasi, M.1    Silva, G.M.2    Netto, L.E.3
  • 66
    • 0028841492 scopus 로고
    • Make it or break it: The role of ubiquitin-dependent proteolysis in cellular regulation
    • Deshaies R. J. 1995. Make it or break it: the role of ubiquitin-dependent proteolysis in cellular regulation. Trends Cell Biol. 5 : 428-434.
    • (1995) Trends Cell Biol. , vol.5 , pp. 428-434
    • Deshaies, R.J.1
  • 68
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Deveraux Q. L., Takahashi R., Salvesen G. S., Reed J. C. 1997. X-linked IAP is a direct inhibitor of cell-death proteases. Nature. 388 : 300-304.
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 71
    • 0026775928 scopus 로고
    • Identification and localization of a cysteinyl residue critical for the trypsin-like catalytic activity of the proteasome
    • Dick L. R., Moomaw C. R., Pramanik B. C., DeMartino G. N., Slaughter C. A. 1992. Identification and localization of a cysteinyl residue critical for the trypsin-like catalytic activity of the proteasome. Biochemistry. 31 : 7347-7355.
    • (1992) Biochemistry , vol.31 , pp. 7347-7355
    • Dick, L.R.1    Moomaw, C.R.2    Pramanik, B.C.3    Demartino, G.N.4    Slaughter, C.A.5
  • 72
    • 0033532543 scopus 로고    scopus 로고
    • Dephosphorylation targets Bcl-2 for ubiquitin-dependent degradation: A link between the apoptosome and the proteasome pathway
    • Dimmeler S., Breitschopf K., Haendeler J., Zeiher A. M. 1999. Dephosphorylation targets Bcl-2 for ubiquitin-dependent degradation: a link between the apoptosome and the proteasome pathway. J. Exp. Med. 189 : 1815-1822.
    • (1999) J. Exp. Med. , vol.189 , pp. 1815-1822
    • Dimmeler, S.1    Breitschopf, K.2    Haendeler, J.3    Zeiher, A.M.4
  • 73
    • 0036143203 scopus 로고    scopus 로고
    • Recent insights into the mechanism of glucocorticosteroid-induced apoptosis
    • Distelhorst C. W. 2002. Recent insights into the mechanism of glucocorticosteroid-induced apoptosis. Cell Death Differ. 9 : 6-19.
    • (2002) Cell Death Differ , vol.9 , pp. 6-19
    • Distelhorst, C.W.1
  • 74
    • 0031034160 scopus 로고    scopus 로고
    • Activation of the cell death program by inhibition of proteasome function
    • Drexler H. C. 1997. Activation of the cell death program by inhibition of proteasome function.Proc. Nat. Acad. Sci. USA. 94 : 855-860.
    • (1997) Proc. Nat. Acad. Sci. USA. , Issue.94 , pp. 855-860
    • Drexler, H.C.1
  • 75
    • 0001842889 scopus 로고    scopus 로고
    • Programmed cell death and the proteasome
    • Drexler H. C. A. 1998. Programmed cell death and the proteasome. Apoptosis. 3 : 1-7.
    • (1998) Apoptosis , vol.3 , pp. 1-7
    • Drexler, H.C.A.1
  • 76
    • 0033965742 scopus 로고    scopus 로고
    • Inhibition of proteasome function induces programmed cell death in proliferating endothelial cells
    • Drexler H. C., Risau W., Konerding M. A. 2000. Inhibition of proteasome function induces programmed cell death in proliferating endothelial cells. FASEB J. 14 : 65-77.
    • (2000) FASEB J. , vol.14 , pp. 65-77
    • Drexler, H.C.1    Risau, W.2    Konerding, M.A.3
  • 78
    • 0342265782 scopus 로고
    • A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes
    • Etlinger J. D., Goldberg A. L. 1977. A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes. Proc. Nat. Acad. Sci. USA. 74 : 54-58.
    • (1977) Proc. Nat. Acad. Sci. USA. , vol.74 , pp. 54-58
    • Etlinger, J.D.1    Goldberg, A.L.2
  • 79
    • 33144478094 scopus 로고    scopus 로고
    • Roles of the anaphase-promoting complex/cyclosome and of its activator Cdc20 in functional substrate binding
    • Eytan E., Moshe Y., Braunstein I., Hershko A. 2006. Roles of the anaphase-promoting complex/cyclosome and of its activator Cdc20 in functional substrate binding. Proc. Nat. Acad. Sci. USA. 103 (7) : 2081-2086.
    • (2006) Proc. Nat. Acad. Sci. USA. , vol.103 , Issue.7 , pp. 2081-2086
    • Eytan, E.1    Moshe, Y.2    Braunstein, I.3    Hershko, A.4
  • 80
    • 1242271997 scopus 로고    scopus 로고
    • Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3
    • Ezhkova E., Tansey W. P. 2004. Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3. Mol. Cell. 13 : 435-442.
    • (2004) Mol. Cell. , vol.13 , pp. 435-442
    • Ezhkova, E.1    Tansey, W.P.2
  • 81
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang S., Jensen J. P., Ludwig R. L., Vousden K. H., Weissman A. M. 2000. Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J. Biol. Chem. 275 : 8945-8951.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 82
    • 33747770049 scopus 로고    scopus 로고
    • Inactivation of the proteasome by 4-hydroxy-2-nonenal is site specific and dependant on 20S proteasome subtypes
    • Farout L., Mary J., Vinh J., Szweda L. I., Friguet B. 2006. Inactivation of the proteasome by 4-hydroxy-2-nonenal is site specific and dependant on 20S proteasome subtypes. Arch. Biochem. Biophys. 453 : 135-142.
    • (2006) Arch. Biochem. Biophys. , vol.453 , pp. 135-142
    • Farout, L.1    Mary, J.2    Vinh, J.3    Szweda, L.I.4    Friguet, B.5
  • 83
    • 0035947238 scopus 로고    scopus 로고
    • The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II
    • Ferdous A., Gonzalez F., Sun L., Kodadek T., Johnston S. A. 2001. The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II. Mol. Cell. 7 : 981-991.
    • (2001) Mol. Cell. , vol.7 , pp. 981-991
    • Ferdous, A.1    Gonzalez, F.2    Sun, L.3    Kodadek, T.4    Johnston, S.A.5
  • 84
    • 0037159223 scopus 로고    scopus 로고
    • A nonproteolytic function of the 19S regulatory subunit of the 26S proteasome is required for efficient activated transcription by human RNA polymerase II
    • Ferdous A., Kodadek T., Johnston S.A. 2002. A nonproteolytic function of the 19S regulatory subunit of the 26S proteasome is required for efficient activated transcription by human RNA polymerase II. Biochemistry. 41 : 12 798 - 12 805.
    • (2002) Biochemistry , vol.41 , pp. 12798-12805
    • Ferdous, A.1    Kodadek, T.2    Johnston, S.A.3
  • 85
    • 33846132939 scopus 로고    scopus 로고
    • The role of the proteasomal ATPases and activator monoubiquitylation in regulating Gal4 binding to promoters
    • Ferdous A., Sikder D., Gillette T., Nalley K., Kodadek T., Johnston S. A. 2007. The role of the proteasomal ATPases and activator monoubiquitylation in regulating Gal4 binding to promoters. Genes Develop. 21 : 112-123.
    • (2007) Genes Develop. , vol.21 , pp. 112-123
    • Ferdous, A.1    Sikder, D.2    Gillette, T.3    Nalley, K.4    Kodadek, T.5    Johnston, S.A.6
  • 86
    • 0036683779 scopus 로고    scopus 로고
    • In vivo and in vitro phosphorylation of Candida albicans 20S proteasome
    • Fernandez Murray P., Biscoglio M. J., Passeron S. 2002. In vivo and in vitro phosphorylation of Candida albicans 20S proteasome. Arch. Biochem. Biophys. 404 : 116-125.
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 116-125
    • Fernandez Murray, P.1    Biscoglio, M.J.2    Passeron, S.3
  • 87
    • 0028925398 scopus 로고
    • A novel chymotrypsin-like component of the multicatalytic proteinase complex optimally active at acidic pH
    • Figueiredo-Pereira M. E., Chen W. E., Yuan H. M., Wilk S. 1995. A novel chymotrypsin-like component of the multicatalytic proteinase complex optimally active at acidic pH. Arch. Biochem. Biophys. 317 : 69-78.
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 69-78
    • Figueiredo-Pereira, M.E.1    Chen, W.E.2    Yuan, H.M.3    Wilk, S.4
  • 90
    • 0030948085 scopus 로고    scopus 로고
    • SUG1, a putative transcriptional mediator and subunit of the PA700 proteasome regulatory complex, is a DNA helicase
    • Fraser R. A., Rossignol M., Heard D. J., Egly J. M., Chambon P. 1997. SUG1, a putative transcriptional mediator and subunit of the PA700 proteasome regulatory complex, is a DNA helicase. J. Biol. Chem. 272 : 7122-7126.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7122-7126
    • Fraser, R.A.1    Rossignol, M.2    Heard, D.J.3    Egly, J.M.4    Chambon, P.5
  • 91
    • 0028241569 scopus 로고
    • Displacement of housekeeping proteasome subunits by MHC-encoded LMPs: A newly discovered mechanism for modulating the multicatalytic proteinase complex
    • Früh K., Gossen M., Wang K., Bujard H., Peterson P. A., Yang Y. 1994. Displacement of housekeeping proteasome subunits by MHC-encoded LMPs: a newly discovered mechanism for modulating the multicatalytic proteinase complex. EMBO J. 13 : 3236-3244.
    • (1994) EMBO J. , vol.13 , pp. 3236-3244
    • Früh, K.1    Gossen, M.2    Wang, K.3    Bujard, H.4    Peterson, P.A.5    Yang, Y.6
  • 92
    • 0037126632 scopus 로고    scopus 로고
    • Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome reveal a conserved core structure
    • Fu H. Y., Reis N., Lee Y., Glickman M. H., Vierstra R. 2001. Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome reveal a conserved core structure. J. EMBO. 20 : 7096-7107.
    • (2001) J. EMBO. , vol.20 , pp. 7096-7107
    • Fu, H.Y.1    Reis, N.2    Lee, Y.3    Glickman, M.H.4    Vierstra, R.5
  • 95
    • 33645823654 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in viral infections
    • Gao G., Luo H. 2006. The ubiquitin-proteasome pathway in viral infections. Can. J. Physiol. Pharmacol. 84 : 5-14.
    • (2006) Can. J. Physiol. Pharmacol. , vol.84 , pp. 5-14
    • Gao, G.1    Luo, H.2
  • 96
    • 2142715911 scopus 로고    scopus 로고
    • Purification procedures determine the proteasome activation properties of REGγ (PA28γ)
    • Gao X., Li J., Pratt G., Wilk S., Rechsteiner M. 2004. Purification procedures determine the proteasome activation properties of REGγ (PA28γ). Arch. Biochem. Biophys. 425 : 158-164.
    • (2004) Arch. Biochem. Biophys. , vol.425 , pp. 158-164
    • Gao, X.1    Li, J.2    Pratt, G.3    Wilk, S.4    Rechsteiner, M.5
  • 100
    • 33745763117 scopus 로고    scopus 로고
    • Distinct functions of the ubiquitin-proteasome pathway influence nucleotide excision repair
    • Gillette T. G., Yu S., Zhou Z., Waters R., Johnston S. A., Reed S. H. 2006. Distinct functions of the ubiquitin-proteasome pathway influence nucleotide excision repair. EMBO J. 25 : 2529-2538.
    • (2006) EMBO J. , vol.25 , pp. 2529-2538
    • Gillette, T.G.1    Yu, S.2    Zhou, Z.3    Waters, R.4    Johnston, S.A.5    Reed, S.H.6
  • 101
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin - Proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman M. H., Ciechanover A. 2002. The ubiquitin - proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 82 : 373-428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 102
    • 20444384416 scopus 로고    scopus 로고
    • Proteasome plasticity
    • Glickman M. H., Raveh D. 2005. Proteasome plasticity. FEBS Lett. 579 : 3214-3223.
    • (2005) FEBS Lett. , vol.579 , pp. 3214-3223
    • Glickman, M.H.1    Raveh, D.2
  • 103
    • 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. 1998. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell. 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
  • 105
    • 0034059667 scopus 로고    scopus 로고
    • C-Myc proteolysis by the ubiquitin-proteasome pathway: Stabilization of c-Myc in Burkitt's lymphoma cells
    • Gregory M. A., Hann S. R. 2000. c-Myc proteolysis by the ubiquitin - proteasome pathway: stabilization of c-Myc in Burkitt's lymphoma cells. Mol. Cell. Biol. 20 : 2423-2435.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2423-2435
    • Gregory, M.A.1    Hann, S.R.2
  • 107
    • 0035067590 scopus 로고    scopus 로고
    • Interferon-gamma inducible exchanges of20S proteasome active site subunits: Why?
    • Groettrup M., Khan S., Schwarz K., Schmidtke G. 2001a. Interferon-gamma inducible exchanges of20S proteasome active site subunits: why? Biochimie. 83 : 367-372.
    • (2001) Biochimie. , vol.83 , pp. 367-372
    • Groettrup, M.1    Khan, S.2    Schwarz, K.3    Schmidtke, G.4
  • 111
    • 9644262422 scopus 로고    scopus 로고
    • Inhibitors of the eukaryotic 20S proteasome core particle: A structural approach
    • Groll M., Huber R. 2004. Inhibitors of the eukaryotic 20S proteasome core particle: a structural approach. Biochim. biophys. acta. 1695 : 33-44.
    • (2004) Biochim. Biophys. Acta. , vol.1695 , pp. 33-44
    • Groll, M.1    Huber, R.2
  • 112
    • 0024497473 scopus 로고
    • The Drosophila proteasome undergoes changes in its subunit pattern during development
    • Haass C., Kloetzel P. M. 1989. The Drosophila proteasome undergoes changes in its subunit pattern during development. Exp. Cell. Res. 180 : 243-252.
    • (1989) Exp. Cell. Res. , vol.180 , pp. 243-252
    • Haass, C.1    Kloetzel, P.M.2
  • 114
    • 0030774890 scopus 로고    scopus 로고
    • The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing
    • Heinemeyer W., Fischer M., Krimmer T., Stachon U., Wolf D. H. 1997. The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing. J. Biol. Chem. 272 : 25 200 - 25 209.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25200-25209
    • Heinemeyer, W.1    Fischer, M.2    Krimmer, T.3    Stachon, U.4    Wolf, D.H.5
  • 115
    • 3242714839 scopus 로고    scopus 로고
    • The ultimate nanoscale mincer: Assembly, structure and active sites of the 20S proteasome core
    • Heinemeyer W., Ramos P. C., Dohmen R. J. 2004. The ultimate nanoscale mincer: assembly, structure and active sites of the 20S proteasome core. Cell Mol. Life Sci. 61: 1562-1578.
    • (2004) Cell Mol. Life Sci. , vol.61 , pp. 1562-1578
    • Heinemeyer, W.1    Ramos, P.C.2    Dohmen, R.J.3
  • 116
    • 21544475903 scopus 로고    scopus 로고
    • IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response
    • Heink S., Ludwig D., Kloetzel P.M., Kruger E. 2005. IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response. Proc. Nat. Acad. Sci. USA. 102 : 9241-9246.
    • (2005) Proc. Nat. Acad. Sci. USA , vol.102 , pp. 9241-9246
    • Heink, S.1    Ludwig, D.2    Kloetzel, P.M.3    Kruger, E.4
  • 117
    • 0032526238 scopus 로고    scopus 로고
    • Simultaneous binding of PA28 and PA700 activators to 20S proteasomes
    • Hendil K. B., Khan S., Tanaka K. 1998. Simultaneous binding of PA28 and PA700 activators to 20S proteasomes. Biochem. J. 332 : 749-754.
    • (1998) Biochem. J. , vol.332 , pp. 749-754
    • Hendil, K.B.1    Khan, S.2    Tanaka, K.3
  • 118
    • 0032481131 scopus 로고    scopus 로고
    • Prostate carcinoma cell death resulting from inhibition of proteasome activity is independent of functional Bcl-2 and p53
    • Herrmann J. L., Briones F. J., Brisbay S., Logothetis C. J., McDonnell T. J. 1998. Prostate carcinoma cell death resulting from inhibition of proteasome activity is independent of functional Bcl-2 and p53. Oncogene. 17 : 2889-2899.
    • (1998) Oncogene , vol.17 , pp. 2889-2899
    • Herrmann, J.L.1    Briones, F.J.2    Brisbay, S.3    Logothetis, C.J.4    McDonnell, T.J.5
  • 119
    • 0347987907 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in cardiovascular diseases - A hypothesis extended
    • Herrmann J., Ciechanover A., Lerman O., Lerman A. 2004. The ubiquitin-proteasome system in cardiovascular diseases - a hypothesis extended. Cardiovascular Res. 61 : 11-12.
    • (2004) Cardiovascular Res. , vol.61 , pp. 11-12
    • Herrmann, J.1    Ciechanover, A.2    Lerman, O.3    Lerman, A.4
  • 120
    • 0030724422 scopus 로고    scopus 로고
    • Roles of ubiquitin-mediated proteolysis in cell cycle control
    • Hershko A. 1997. Roles of ubiquitin-mediated proteolysis in cell cycle control. Curr. Opin. Cell Biol. 9 : 788-799.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 788-799
    • Hershko, A.1
  • 122
    • 0034296394 scopus 로고    scopus 로고
    • Basic medical research award. The ubiquitin system
    • Hershko A., Ciechanover A., Varshavsky A. 2000. Basic medical research award. The ubiquitin system. Nat. Med. 6 : 1073-1081.
    • (2000) Nat. Med. , vol.6 , pp. 1073-1081
    • Hershko, A.1    Ciechanover, A.2    Varshavsky, A.3
  • 124
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochshtrasser M. 1996. Ubiquitin-dependent protein degradation. Annu. Rev. Immunol. 17 : 405-439.
    • (1996) Annu. Rev. Immunol. , vol.17 , pp. 405-439
    • Hochshtrasser, M.1
  • 125
    • 16244373679 scopus 로고    scopus 로고
    • Multiubiquitylation by E4 enzymes: «One size» doesn't fit all
    • Hoppe T. 2005. Multiubiquitylation by E4 enzymes: «one size» doesn't fit all. Trends Biochem. Sci. 30 : 183-187.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 183-187
    • Hoppe, T.1
  • 126
    • 5644266525 scopus 로고    scopus 로고
    • Identification of a protein kinase which phosphorylates a subunit of the 26S proteasome and changes in its activity during meiotic cell cycle in goldfish oocytes
    • Horiguchi R., Yoshikuni M., Tokumoto M., Nagahama Y., Tokumoto T. 2005. Identification of a protein kinase which phosphorylates a subunit of the 26S proteasome and changes in its activity during meiotic cell cycle in goldfish oocytes. Cell Signal. 17 : 205-215.
    • (2005) Cell Signal. , vol.17 , pp. 205-215
    • Horiguchi, R.1    Yoshikuni, M.2    Tokumoto, M.3    Nagahama, Y.4    Tokumoto, T.5
  • 127
    • 3242732010 scopus 로고    scopus 로고
    • Ubiquitin-free routes into the proteasome
    • Hoyt M. A., Coffino P. 2004. Ubiquitin-free routes into the proteasome. Cell Mol. Life Sci. 61 : 1596-1600.
    • (2004) Cell Mol. Life Sci. , vol.61 , pp. 1596-1600
    • Hoyt, M.A.1    Coffino, P.2
  • 128
    • 8244241099 scopus 로고    scopus 로고
    • Evolution of the proteasome components
    • Hughes A. L. 1997. Evolution of the proteasome components. Immunogenetics. 46 : 82-92.
    • (1997) Immunogenetics , Issue.46 , pp. 82-92
    • Hughes, A.L.1
  • 129
    • 33750464206 scopus 로고    scopus 로고
    • Posttranslational modification of the 20S proteasomal proteins of the archaeon Haloferax volcanii
    • Humbard M. A., Stevens S. M., Jr., Maupin-Furlow J. A. 2006. Posttranslational modification of the 20S proteasomal proteins of the archaeon Haloferax volcanii. J. Bacteriol. 188 : 7521-7530.
    • (2006) J. Bacteriol. , vol.188 , pp. 7521-7530
    • Humbard, M.A.1    Stevens Jr., S.M.2    Maupin-Furlow, J.A.3
  • 130
    • 0027360689 scopus 로고
    • Regulation of proteasome expression in developing and transformed cells
    • Ichihara A., Tanaka K., Andoh T., Shimbara N. 1993. Regulation of proteasome expression in developing and transformed cells. Adv. Enzyme Regul. 33 : 173-180.
    • (1993) Adv. Enzyme Regul. , vol.33 , pp. 173-180
    • Ichihara, A.1    Tanaka, K.2    Andoh, T.3    Shimbara, N.4
  • 131
    • 0029564960 scopus 로고
    • Lactacystin, a specific inhibitor of the proteasome, induces apoptosis in human monoblast U937 cells
    • Imajoh-Ohmi S., Kawaguchi T., Sugiyama S., TanakaK., Omura S., Kikuchi H. 1995. Lactacystin, a specific inhibitor of the proteasome, induces apoptosis in human monoblast U937 cells. Biochem. Biophys. Res. Commun. 217 : 1070-1077.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 1070-1077
    • Imajoh-Ohmi, S.1    Kawaguchi, T.2    Tanakak., S.S.3    Omura, S.4    Kikuchi, H.5
  • 132
    • 0036177305 scopus 로고    scopus 로고
    • Electrophoretic analysis of phosphorylation of the yeast 20S proteasome
    • Iwafune Y., Kawasaki H., Hirano H. 2002. Electrophoretic analysis of phosphorylation of the yeast 20S proteasome. Electrophoresis. 23 : 329-338.
    • (2002) Electrophoresis , vol.23 , pp. 329-338
    • Iwafune, Y.1    Kawasaki, H.2    Hirano, H.3
  • 133
    • 5344237367 scopus 로고    scopus 로고
    • Identification of three phosphorylation sites in the alpha7 subunit of the yeast 20S proteasome in vivo using mass spectrometry
    • Iwafune Y., Kawasaki H., Hirano H. 2004. Identification of three phosphorylation sites in the alpha7 subunit of the yeast 20S proteasome in vivo using mass spectrometry. Arch. Biochem. Biophys. 431 : 9-15.
    • (2004) Arch. Biochem. Biophys. , vol.431 , pp. 9-15
    • Iwafune, Y.1    Kawasaki, H.2    Hirano, H.3
  • 134
  • 135
    • 0029068172 scopus 로고
    • Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26 S proteasome
    • Jariel-Encontre I., Pariat M., Martin F., Carillo S., Salvat C., Piechaczyk M. 1995. Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26 S proteasome. J. Biol. Chem. 270 : 11 623 - 11 627.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11623-11627
    • Jariel-Encontre, I.1    Pariat, M.2    Martin, F.3    Carillo, S.4    Salvat, C.5    Piechaczyk, M.6
  • 136
  • 138
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro C. A., Weissman A. M. 2000. RING finger proteins: mediators of ubiquitin ligase activity. Cell. 102 : 549-552.
    • (2000) Cell. , Issue.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 140
    • 0029043988 scopus 로고
    • Changes in the structure and function of the multicatalytic proteinase (proteasome) during programmed cell death in the intersegmental muscles of the hawkmoth, Manduca sexta
    • Jones M. E., Haire M. F., Kloetzel P. M., Mykles D. L., Schwartz L. M. 1995. Changes in the structure and function of the multicatalytic proteinase (proteasome) during programmed cell death in the intersegmental muscles of the hawkmoth, Manduca sexta. Develop. Biol. 169 : 436-447.
    • (1995) Develop. Biol. , Issue.169 , pp. 436-447
    • Jones, M.E.1    Haire, M.F.2    Kloetzel, P.M.3    Mykles, D.L.4    Schwartz, L.M.5
  • 141
    • 0034094314 scopus 로고    scopus 로고
    • The proteasome is involved in the first metaphase-to-anaphase transition of meiosis in rat oocytes
    • Josefsberg L. B., Galiani D., Dantes A., Amsterdam A., Dekel N. 2000. The proteasome is involved in the first metaphase-to-anaphase transition of meiosis in rat oocytes. Biol. Reprod. 62 : 1270-1277.
    • (2000) Biol. Reprod. , vol.62 , pp. 1270-1277
    • Josefsberg, L.B.1    Galiani, D.2    Dantes, A.3    Amsterdam, A.4    Dekel, N.5
  • 142
    • 0035119172 scopus 로고    scopus 로고
    • Inactivation of M-phase promoting factor at exit from first embryonic mitosis in the rat is independent of cyclin B1 degradation
    • JosefsbergL. B., Kaufman O., Galiani D., Kovo M., Dekel N. 2001. Inactivation of M-phase promoting factor at exit from first embryonic mitosis in the rat is independent of cyclin B1 degradation. Biol. Reprod. 64 : 871-878.
    • (2001) Biol. Reprod. , vol.64 , pp. 871-878
    • Josefsbergl., B.1    Kaufman, O.2    Galiani, D.3    Kovo, M.4    Dekel, N.5
  • 144
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-[kappa]B activity
    • Karin M., Ben-Neriah Y. 2000. Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu. Rev. Immunol. 18 : 621-663.
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 146
    • 0033845768 scopus 로고    scopus 로고
    • Inhibiting proteasome activity causes overreplication of DNA and blocks entry into mitosis in sea urchin embryos
    • Kawahara H., Philipova R., Yokosawa H., Patel R., Tanaka K., Whitaker M. 2000b. Inhibiting proteasome activity causes overreplication of DNA and blocks entry into mitosis in sea urchin embryos. J Cell Sci. 113 : 2659-2670.
    • (2000) J Cell Sci. , vol.113 , pp. 2659-2670
    • Kawahara, H.1    Philipova, R.2    Yokosawa, H.3    Patel, R.4    Tanaka, K.5    Whitaker, M.6
  • 147
    • 0030566824 scopus 로고    scopus 로고
    • Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator
    • Kessel M., Wu W., Gottesman S., Kocsis E., Steven A. C., Maurizi M. R. 1996. Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY. FEBS Lett. 398 : 274-278.
    • (1996) ClpY. FEBS Lett. , vol.398 , pp. 274-278
    • Kessel, M.1    Wu, W.2    Gottesman, S.3    Kocsis, E.4    Steven, A.C.5    Maurizi, M.R.6
  • 152
    • 34347327136 scopus 로고    scopus 로고
    • Proteasome activity modulates chromatin modifications and RNA polymerase II phosphorylation to enhance glucocorticoid receptor-mediated transcription
    • Kinyamu H. K., Archer T. K. 2007. Proteasome activity modulates chromatin modifications and RNA polymerase II phosphorylation to enhance glucocorticoid receptor-mediated transcription. Mol. Cell. Biol. 27 : 4891-4904.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4891-4904
    • Kinyamu, H.K.1    Archer, T.K.2
  • 153
    • 17844365062 scopus 로고    scopus 로고
    • Linking the ubiquitin - Proteasome pathway to chromatin remodeling/modification by nuclear receptors
    • Kinyamu H.K., Chen J., Archer T.K. 2005. Linking the ubiquitin - proteasome pathway to chromatin remodeling/modification by nuclear receptors. J. Mol. Endocrinol. 34 : 281-297.
    • (2005) J. Mol. Endocrinol. , vol.34 , pp. 281-297
    • Kinyamu, H.K.1    Chen, J.2    Archer, T.K.3
  • 154
    • 0033038942 scopus 로고    scopus 로고
    • Proteasome inhibitors induce mitochondria-independent apoptosis in human glioma cells
    • Kitagawa H., Tani E., Ikemoto H., Ozaki I., Nakano A., Omura S. 1999. Proteasome inhibitors induce mitochondria-independent apoptosis in human glioma cells. FEBS Lett. 443 : 181-186.
    • (1999) FEBS Lett. , vol.443 , pp. 181-186
    • Kitagawa, H.1    Tani, E.2    Ikemoto, H.3    Ozaki, I.4    Nakano, A.5    Omura, S.6
  • 155
    • 0036615963 scopus 로고    scopus 로고
    • The role of the proteasome in apoptosis induced by anthracycline anticancer agents
    • Kiyomiya K., Kurebe M., Nakagawa H., Matsuo S. 2002. The role of the proteasome in apoptosis induced by anthracycline anticancer agents. Int. J. Oncol. 20 : 1205-1259.
    • (2002) Int. J. Oncol. , vol.20 , pp. 1205-1259
    • Kiyomiya, K.1    Kurebe, M.2    Nakagawa, H.3    Matsuo, S.4
  • 156
    • 0025633196 scopus 로고
    • Cell-specific accumulation of Drosophila proteasomes (MCP) during early development
    • Klein U., Gernold M., Kloetzel P. M. 1990. Cell-specific accumulation of Drosophila proteasomes (MCP) during early development. J. Cell. Biol. 111 : 2275-2282.
    • (1990) J. Cell. Biol. , vol.111 , pp. 2275-2282
    • Klein, U.1    Gernold, M.2    Kloetzel, P.M.3
  • 157
    • 0035290730 scopus 로고    scopus 로고
    • Antigen processing by the proteasome
    • Kloetzel P. M. 2001. Antigen processing by the proteasome. Nat. Rev. Mol. Cell. Biol. 2 : 179-187.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 179-187
    • Kloetzel, P.M.1
  • 158
    • 9644289334 scopus 로고    scopus 로고
    • The proteasome and MHC class i antigen processing
    • Kloetzel P. M. 2004. The proteasome and MHC class I antigen processing. Biochim. biophys. acta. 1695 : 225-233.
    • (2004) Biochim. Biophys. Acta. , vol.1695 , pp. 225-233
    • Kloetzel, P.M.1
  • 159
    • 0033011162 scopus 로고    scopus 로고
    • The role of the proteasome system and the proteasome activator PA28 complex in the cellular immune response
    • Kloetzel P. M., Soza A., Stohwasser R. 1999. The role of the proteasome system and the proteasome activator PA28 complex in the cellular immune response. Biol. Chem. 380 : 293-297. (Pubitemid 29145942)
    • (1999) Biological Chemistry , vol.380 , Issue.3 , pp. 293-297
    • Kloetzel, P.-M.1    Soza, A.2    Stohwasser, R.3
  • 160
    • 0029934284 scopus 로고    scopus 로고
    • Functional analysis of eukaryotic 20S proteasome nuclear localization signal
    • DOI 10.1006/excr.1996.0157
    • Knuehl C., Seelig A., Brecht B., Henklein P., Kloetzel P. M. 1996. Functional analysis of eukaryotic 20S proteasome nuclear localization signal.Exp. Cell Res. 225 (1) : 67-74. (Pubitemid 26158456)
    • (1996) Experimental Cell Research , vol.225 , Issue.1 , pp. 67-74
    • Knuehl, C.1    Seelig, A.2    Brecht, B.3    Henklein, P.4    Kloetzel, P.-M.5
  • 163
    • 0032764099 scopus 로고    scopus 로고
    • Induction of G1 arrest and selective growth inhibition by lactacystin in human umbilical vein endothelial cells
    • Kumeda S. I., Deguchi A., Toi M., Omura S., Umezawa K. 1999. Induction of G1 arrest and selective growth inhibition by lactacystin in human umbilical vein endothelial cells. Anticancer Res. 19 : 3961-3968.
    • (1999) Anticancer Res. , vol.19 , pp. 3961-3968
    • Kumeda, S.I.1    Deguchi, A.2    Toi, M.3    Omura, S.4    Umezawa, K.5
  • 165
    • 27544486193 scopus 로고    scopus 로고
    • The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators
    • DOI 10.1016/j.cell.2005.08.015, PII S0092867405008196
    • Lee D., Ezhkova E., Li B., Pattenden S.G., TanseyW.P., Workman J. L. 2005. The proteasome regulatory particle alters the SAGA coactivator to enhance its interactions with transcriptional activators. Cell. 123 : 423-436. (Pubitemid 41546673)
    • (2005) Cell , vol.123 , Issue.3 , pp. 423-436
    • Lee, D.1    Ezhkova, E.2    Li, B.3    Pattenden, S.G.4    Tansey, W.P.5    Workman, J.L.6
  • 166
    • 0035894104 scopus 로고    scopus 로고
    • Effect of overexpression of Bcl-2 on cellular oxidative damage, nitric oxide production, antioxidant defenses, and the proteasome
    • DOI 10.1016/S0891-5849(01)00633-5, PII S0891584901006335
    • Lee M., Hyun D. H., Marshall K. A., Ellerby L. M., Bredesen D. E., Jenner P., Halliwell B. 2001. Effect of overexpression of Bcl-2 on cellular oxidative damage, nitric oxide production, antioxidant defenses, and the proteasome. Free Radic. Biol. Med. 31 : 1550-1559. (Pubitemid 34024977)
    • (2001) Free Radical Biology and Medicine , vol.31 , Issue.12 , pp. 1550-1559
    • Lee, M.1    Hyun, D.-H.2    Marshall, K.-A.3    Ellerby, L.M.4    Bredesen, D.E.5    Jenner, P.6    Halliwell, B.7
  • 167
    • 33846599294 scopus 로고    scopus 로고
    • A novel interaction between N-myristoylation and the 26S proteasome during cell morphogenesis
    • Lee S. C., Shaw B. D. 2007. A novel interaction between N-myristoylation and the 26S proteasome during cell morphogenesis. Mol. Microbiol. 63 : 1039-1053.
    • (2007) Mol. Microbiol. , Issue.63 , pp. 1039-1053
    • Lee, S.C.1    Shaw, B.D.2
  • 168
    • 0036296150 scopus 로고    scopus 로고
    • 20 S proteasomes are imported as precursor complexes into the nucleus of yeast
    • DOI 10.1006/jmbi.2002.5443
    • Lehmann A., Janek K., Braun B., Kloetzel P. M., Enenkel C. 2002. 20S proteasomes are imported as precursor complexes into the nucleus of yeast. J. Mol. Biol. 317 : 401-413. (Pubitemid 34722179)
    • (2002) Journal of Molecular Biology , vol.317 , Issue.3 , pp. 401-413
    • Lehmann, A.1    Janek, K.2    Braun, B.3    Kloetzel, P.-M.4    Enenkel, C.5
  • 169
    • 0034635952 scopus 로고    scopus 로고
    • Bax degradation by the ubiquitin/proteasome-dependent pathway: Involvement in tumor survival and progression
    • DOI 10.1073/pnas.070047997
    • Li B., Dou Q. P. 2000. Bax degradation by the ubiquitin/proteasome- dependent pathway: involvement in tumor survival and progression. Proc. Nat. Acad. Sci. USA. 97 : 3850-3855. (Pubitemid 30226050)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.8 , pp. 3850-3855
    • Li, B.1    Dou, Q.P.2
  • 170
    • 0030598901 scopus 로고    scopus 로고
    • Phosphorylation of the proteasome activator PA28 is required for proteasome activation
    • DOI 10.1006/bbrc.1996.1263
    • Li N., Lerea K. M., Etlinger J. D. 1996. Phosphorylation of the proteasome activator PA28 is required for proteasome activation. Biochem. Biophys. Res. Commun. 225 : 855-860. (Pubitemid 26319195)
    • (1996) Biochemical and Biophysical Research Communications , vol.225 , Issue.3 , pp. 855-860
    • Li, N.1    Lerea, K.M.2    Etlinger, J.D.3
  • 171
    • 0141729263 scopus 로고    scopus 로고
    • Diverse roles for ubiquitin-dependent proteolysis in transcriptional activation
    • Lipford J. R., Deshaies R. J. 2003. Diverse roles for ubiquitin-dependent proteolysis in transcriptional activation. Nature Cell Biol. 5 : 845-850.
    • (2003) Nature Cell Biol. , vol.5 , pp. 845-850
    • Lipford, J.R.1    Deshaies, R.J.2
  • 172
    • 27744495040 scopus 로고    scopus 로고
    • A putative stimulatory role for activator turnover in gene expression
    • DOI 10.1038/nature04098, PII N04098
    • Lipford J. R., Smith G. T., Chi Y., Deshaies R. J. 2005. A putative stimulatory role for activator turnover in gene expression. Nature. 438 : 113-116. (Pubitemid 41599830)
    • (2005) Nature , vol.438 , Issue.7064 , pp. 113-116
    • Lipford, J.R.1    Smith, G.T.2    Chi, Y.3    Deshaies, R.J.4
  • 174
    • 12244309062 scopus 로고    scopus 로고
    • Proteolysis of a nucleotide excision repair protein by the 26S proteasome
    • DOI 10.1007/s00294-002-0332-9
    • Lommel L., Ortolan T., Chen L., Madura K., Sweder K. S. 2002. Proteolysis of a nucleotide excision repair protein by the 26S proteasome. Curr. Genet. 42 : 9-20. (Pubitemid 36075988)
    • (2002) Current Genetics , vol.42 , Issue.1 , pp. 9-20
    • Lommel, L.1    Ortolan, T.2    Chen, L.3    Madura, K.4    Sweder, K.S.5
  • 175
    • 0030614801 scopus 로고    scopus 로고
    • Expression of a 268 proteasome ATPase subunit, MS73, in muscles that undergo developmentally programmed cell death, and its control by ecdysteroid hormones in the insect Manduca sexta
    • DOI 10.1016/S0014-5793(96)01413-5, PII S0014579396014135
    • Löw P., Bussell K., Dawson S. P., Billett M. A., Mayer R. J., Reynolds S. E. 1997. Expression ofa 26S proteasome ATPase subunit, MS73, in muscles that undergo developmentally programmed cell death, and its control by ecdysteroid hormones in the insect Manduca sexta. FEBS Lett. 400 : 345-349. (Pubitemid 27039381)
    • (1997) FEBS Letters , vol.400 , Issue.3 , pp. 345-349
    • Low, P.1    Bussell, K.2    Dawson, S.P.3    Billett, M.A.4    Mayer, R.J.5    Reynolds, S.E.6
  • 176
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Lowe J., Stock D., Jap B., Zwickl P., Baumeister W., Huber R. 1995. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science. 268 : 533-539.
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 177
    • 0027267492 scopus 로고
    • Copurification of casein kinase II with 20 S proteasomes and phosphorylation of a 30-kDa proteasome subunit
    • Ludemann R., Lerea K. M., Etlinger J. D. 1993. Copurification of casein kinase II with 20S proteasomes and phosphorylation of a 30-kDa proteasome subunit. J. Biol. Chem. 268 : 17413-17417. (Pubitemid 23236982)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.23 , pp. 17413-17417
    • Ludemann, R.1    Lerea, K.M.2    Etlinger, J.D.3
  • 178
    • 0034902852 scopus 로고    scopus 로고
    • A proteasome inhibitor effectively prevents mouse heart allograft rejection
    • Luo H., Wu Y., Qi S., Wan X., Chen H., Wu J. 2001. A proteasome inhibitor effectively prevents mouse heart allograft rejection. Transplantation. 72 : 196-202. (Pubitemid 32729334)
    • (2001) Transplantation , vol.72 , Issue.2 , pp. 196-202
    • Luo, H.1    Wu, Y.2    Qi, S.3    Wan, X.4    Chen, H.5    Wu, J.6
  • 181
    • 0035072563 scopus 로고    scopus 로고
    • P53-dependent apoptosis induced by proteasome inhibition in mammary epithelial cells
    • DOI 10.1038/sj.cdd.4400801
    • MacLaren A. P., Chapman R. S., Wyllie A. H., Watson C. J. 2001. p53-dependent apoptosis induced by proteasome inhibition in mammary epithelial cells. Cell Death Differ. 8 : 210-218. (Pubitemid 32288166)
    • (2001) Cell Death and Differentiation , vol.8 , Issue.3 , pp. 210-218
    • MacLaren, A.P.1    Chapman, R.S.2    Wyllie, A.H.3    Watson, C.J.4
  • 182
    • 0032711876 scopus 로고    scopus 로고
    • Multiple mammalian proteasomal ATPases, but not proteasome itself, are associated with TATA-binding protein and a novel transcriptional activator, TIP120
    • DOI 10.1046/j.1365-2443.1999.00277.x
    • Makino Y., Yoshida T., Yogosawa S., Tanaka K., Muramatsu M., Tamura T. A. 1999. Multiple mammalian proteasomal ATPases, but not proteasome itself, are associated with TATA-binding protein and a novel transcriptional activator, TIP120. Genes Cells. 4 : 529-539. (Pubitemid 29521204)
    • (1999) Genes to Cells , vol.4 , Issue.9 , pp. 529-539
    • Makino, Y.1    Yoshida, T.2    Yogosawa, S.3    Tanaka, K.4    Muramatsu, M.5    Tamura, T.-A.6
  • 183
    • 0035976930 scopus 로고    scopus 로고
    • Cyclic AMP Regulation of Neutrophil Apoptosis Occurs via a Novel Protein Kinase A-independent Signaling Pathway
    • DOI 10.1074/jbc.M105197200
    • Martin M. C., Dransfield I., Haslett C., Rossi A. G. 2001. Cyclic AMP regulation of neutrophil apoptosis occurs via a novel PKA-independent signaling pathway. J. Biol. Chem. 276 (48) : 45 041 - 45 050. (Pubitemid 37391295)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.48 , pp. 45041-45050
    • Martin, M.C.1    Dransfield, I.2    Haslett, C.3    Rossi, A.G.4
  • 184
    • 0029892643 scopus 로고    scopus 로고
    • Phosphorylation of proteasomes in mammalian cells Identification of two phosphorylated subunits and the effect of phosphorylation on activity
    • Mason G. G., Hendil K. B., Rivett A. J. 1996. Phosphorylation of proteasomes in mammalian cells. Identification of two phospho-rylated subunits and the effect of phosphorylation on activity. Eur. J. Biochem. 238 : 453-462. (Pubitemid 126425462)
    • (1996) European Journal of Biochemistry , vol.238 , Issue.2 , pp. 453-462
    • Mason, G.G.F.1    Hendil, K.B.2    Rivett, A.J.3
  • 185
    • 0032479207 scopus 로고    scopus 로고
    • Phosphorylation of ATPase subunits of the 26S proteasome
    • DOI 10.1016/S0014-5793(98)00676-0, PII S0014579398006760
    • Mason G., Murray R., Pappin D., Rivett A. J. 1998. Phosphorylation of ATPase subunits of the 26S proteasome. FEBS. 430 : 269-274. (Pubitemid 28337927)
    • (1998) FEBS Letters , vol.430 , Issue.3 , pp. 269-274
    • Mason, G.G.F.1    Murray, R.Z.2    Pappin, D.3    Rivett, A.J.4
  • 186
    • 0035847095 scopus 로고    scopus 로고
    • Identification and characterization of a Drosophila nuclear proteasome regulator. A homolog of human 11 S REGgamma (PA28gamma)
    • DOI 10.1074/jbc.M007379200
    • Masson P., Andersson O., Petersen U. M., Young P. 2001. Identification and characterization of a Drosophila nuclear protea-some regulator. A homolog of human 11 S REGgamma (PA28gamma ). J. Biol. Chem. 276 : 1383-1390. (Pubitemid 32096569)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.2 , pp. 1383-1390
    • Masson, P.1    Andersson, O.2    Petersen, U.-M.3    Young, P.4
  • 187
    • 0031918337 scopus 로고    scopus 로고
    • Biochemical characterization of the 20S proteasome from the methanoarchaeon Methanosarcina thermophila
    • Maupin-Furlow J. A., Aldrich H. C., Ferry J. G. 1998. Biochemical characterization of the 20S proteasome from the methanoarchaeon Methanosarcina thermophila. J. Bacteriol. 180 : 1480-1487.
    • (1998) J. Bacteriol. , vol.180 , pp. 1480-1487
    • Maupin-Furlow, J.A.1    Aldrich, H.C.2    Ferry, J.G.3
  • 190
    • 0026714435 scopus 로고
    • Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination
    • DOI 10.1038/360597a0
    • Murakami Y., Matsufuji S., Kameji T., Hayashi S., Igarashi K., Tamura T., Tanaka K., Ichihara A. 1992. Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination. Nature. 360 : 597-599. (Pubitemid 23000711)
    • (1992) Nature , vol.360 , Issue.6404 , pp. 597-599
    • Murakami, Y.1    Matsufuji, S.2    Kameji, T.3    Hayashi, S.4    Igarashi, K.5    Tamura, T.6    Tanaka, K.7    Ichihara, A.8
  • 191
    • 33745080323 scopus 로고    scopus 로고
    • Multiple chaperone-assisted formation of mammalian 20S proteasomes
    • Murata S. 2006. Multiple chaperone-assisted formation of mammalian 20S proteasomes. IUBMB Life. 58 : 344-348.
    • (2006) IUBMB Life , vol.58 , pp. 344-348
    • Murata, S.1
  • 192
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • Muratani M., Tansey W. P. 2003. How the ubiquitin-proteasome system controls transcription. Nat. Rev. Mol. Cell Biol. 4 : 192-201.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 194
    • 0030880547 scopus 로고    scopus 로고
    • Intermediates in the formation of mouse 20S proteasomes: Implications for the assembly of precursor beta subunits
    • Nandi D., Woodward E., Ginsburg D. B., Monaco J. J. 1997. Intermediates in the formation of mouse 20S proteasomes: implications for the assembly of precursor beta subunits. EMBO J. 16 : 5363-5375.
    • (1997) EMBO J. , vol.16 , pp. 5363-5375
    • Nandi, D.1    Woodward, E.2    Ginsburg, D.B.3    Monaco, J.J.4
  • 195
    • 0036678959 scopus 로고    scopus 로고
    • Role and function of the 26S proteasome in proliferation and apoptosis
    • Naujokat C., Hoffmann S. 2002. Role and function of the 26S proteasome in proliferation and apoptosis. Lab. Invest. 82 : 965-980.
    • (2002) Lab. Invest. , vol.82 , pp. 965-980
    • Naujokat, C.1    Hoffmann, S.2
  • 196
    • 0033623487 scopus 로고    scopus 로고
    • Proteasome inhibitors induced caspase-dependent apoptosis and accumulation of p21WAF1/Cip1 in human immature leukemic cells
    • Naujokat C., Sezer O., Zinke H., Leclere A., Hauptmann S., Possinger K. 2000. Proteasome inhibitors induced caspase-dependent apoptosis and accumulation of p21WAF1/Cip1 in human immature leukemic cells. Eur. J. Haematol. 65 : 221-236.
    • (2000) Eur. J. Haematol. , vol.65 , pp. 221-236
    • Naujokat, C.1    Sezer, O.2    Zinke, H.3    Leclere, A.4    Hauptmann, S.5    Possinger, K.6
  • 197
    • 1542297619 scopus 로고    scopus 로고
    • Urban renewal in the nucleus: Is protein turnover by proteasomes absolutely required for nuclear receptor-regulated transcription?
    • Nawaz Z., O'Malley B. W. 2004. Urban renewal in the nucleus: is protein turnover by proteasomes absolutely required for nuclear receptor-regulated transcription? Mol. Endocrinol. 18 : 493-499.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 493-499
    • Nawaz, Z.1    O'Malley, B.W.2
  • 198
    • 0029558611 scopus 로고
    • Nuclear localization signals of human and Thermoplasma proteasomal alpha subunits are functional in vitro
    • Nederlof P. M., WangH. R., Baumeister W. 1995. Nuclear localization signals of human and Thermoplasma proteasomal alpha subunits are functional in vitro. Proc. Nat. Acad. Sci. USA. 92 : 12 060 - 12 064.
    • (1995) Proc. Nat. Acad. Sci. USA. , vol.92 , pp. 12060-12064
    • Nederlof, P.M.1    Wangh., R.2    Baumeister, W.3
  • 199
    • 0025157203 scopus 로고
    • Cloning and nucleotide sequence of cDNA for Ki antigen, a highly conserved nuclear protein detected with sera from patients with systemic lupus erythematosus
    • Nikaido T., Shimada K., Shibata M., Hata M., Sakamoto M., Takasaki Y., Sato C., Takahashi T., Nishida Y. 1990. Cloning and nucleotide sequence of cDNA for Ki antigen, a highly conserved nuclear protein detected with sera from patients with systemic lupus erythematosus. Clin. Exp. Immunol. 79 : 209-214.
    • (1990) Clin. Exp. Immunol. , vol.79 , pp. 209-214
    • Nikaido, T.1    Shimada, K.2    Shibata, M.3    Hata, M.4    Sakamoto, M.5    Takasaki, Y.6    Sato, C.7    Takahashi, T.8    Nishida, Y.9
  • 200
    • 0034327510 scopus 로고    scopus 로고
    • Catalytic activities of the 20S proteasome, a multicatalytic proteinase complex
    • Orlowski M., Wilk S. 2000. Catalytic activities of the 20S proteasome, a multicatalytic proteinase complex. Arch. Biochem. Biophys. 383 : 1-16.
    • (2000) Arch. Biochem. Biophys. , vol.383 , pp. 1-16
    • Orlowski, M.1    Wilk, S.2
  • 201
    • 0037834898 scopus 로고    scopus 로고
    • Ubiquitin-independent proteolytic functions of the proteasome
    • Orlowski M., Wilk S. 2003. Ubiquitin-independent proteolytic functions of the proteasome. Arch. Biochem. Biophys. 415 : 1-5.
    • (2003) Arch. Biochem. Biophys. , vol.415 , pp. 1-5
    • Orlowski, M.1    Wilk, S.2
  • 202
    • 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. 1998. Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor. Cancer Res. 58 : 4342-4348.
    • (1998) Cancer Res. , Issue.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
  • 203
    • 0034759491 scopus 로고    scopus 로고
    • The proteasome in cancer biology and treatment
    • Pajonk F., McBride W. H. 2001. The proteasome in cancer biology and treatment. Radiat. Res. 156 : 447-459.
    • (2001) Radiat. Res. , vol.156 , pp. 447-459
    • Pajonk, F.1    McBride, W.H.2
  • 205
    • 0026538022 scopus 로고
    • Enzymatic changes of the bovine pituitary multicatalytic proteinase complex, induced by magnesium ions
    • Pereira M. E., Yu B., Wilk S. 1992. Enzymatic changes of the bovine pituitary multicatalytic proteinase complex, induced by magnesium ions. Arch. Biochem. Biophys. 294 : 1-8.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 1-8
    • Pereira, M.E.1    Yu, B.2    Wilk, S.3
  • 206
    • 0025012292 scopus 로고
    • Phosphorylation of the multicatalytic proteinase complex from bovine pituitaries by a copurifying cAMP-dependent protein kinase
    • Pereira M. E., Wilk S. 1990. Phosphorylation of the multicatalytic proteinase complex from bovine pituitaries by a copurifying cAMP-dependent protein kinase. Arch. Biochem. Biophys. 283 : 68-74.
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 68-74
    • Pereira, M.E.1    Wilk, S.2
  • 208
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C. M. 2001. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70 : 503-533.
    • (2001) Annu. Rev. Biochem. , Issue.70 , pp. 503-533
    • Pickart, C.M.1
  • 209
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • Pickart C. M., Eddins M. J. 2004. Ubiquitin: structures, functions, mechanisms. Biochim. biophys. acta. 1695 : 55-72.
    • (2004) Biochim. Biophys. Acta. , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 210
    • 0035034677 scopus 로고    scopus 로고
    • Effects of proteasome inhibitor PSI on neoplastic and non-transformed cell lines
    • Pleban E., Bury M., Mlynarczuk I., Wojcik C. 2001. Effects of proteasome inhibitor PSI on neoplastic and non-transformed cell lines. Folia Histochem. Cytobiol. 39 : 133-134.
    • (2001) Folia Histochem. Cytobiol. , vol.39 , pp. 133-134
    • Pleban, E.1    Bury, M.2    Mlynarczuk, I.3    Wojcik, C.4
  • 211
    • 0000991680 scopus 로고    scopus 로고
    • Proteasome inhibitors induce cytochrome c-caspase - 3-like protease-mediated apoptosis in cultured cortical neurons
    • Qiu J. H., Asai A., Chi S., Saito N., Hamada H., Kirino T. 2000. Proteasome inhibitors induce cytochrome c-caspase - 3-like protease-mediated apoptosis in cultured cortical neurons. J. Neurosci. 20 : 259-265.
    • (2000) J. Neurosci. , vol.20 , pp. 259-265
    • Qiu, J.H.1    Asai, A.2    Chi, S.3    Saito, N.4    Hamada, H.5    Kirino, T.6
  • 213
    • 0032548998 scopus 로고    scopus 로고
    • Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly
    • Ramos P. C., Höckendorff J., Johnson E. S., Varshavsky A., Dohmen R. J. 1998. Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell. 92 : 489-499.
    • (1998) Cell , vol.92 , pp. 489-499
    • Ramos, P.C.1    Höckendorff, J.2    Johnson, E.S.3    Varshavsky, A.4    Dohmen, R.J.5
  • 214
    • 0033529171 scopus 로고    scopus 로고
    • Lovastatin-mediated G1 arrest is through inhibition of the proteasome, independent of hydroxymethyl glutaryl-CoA reductase
    • Rao S., Porter D. C., Chen X., Herliczek T., Lowe M., Keyomarsi K. 1999. Lovastatin-mediated G1 arrest is through inhibition of the proteasome, independent of hydroxymethyl glutaryl-CoA reductase. Proc. Nat. Acad. Sci. USA. 96 : 7797-7802.
    • (1999) Proc. Nat. Acad. Sci. USA , vol.96 , pp. 7797-7802
    • Rao, S.1    Porter, D.C.2    Chen, X.3    Herliczek, T.4    Lowe, M.5    Keyomarsi, K.6
  • 215
    • 9644302406 scopus 로고    scopus 로고
    • Productive RUPture: Activation of transcription factors by proteasomal processing
    • Rape M., Jentsch S. 2004. Productive RUPture: activation of transcription factors by proteasomal processing. Biochim. biophys. acta. 1695 : 209-213.
    • (2004) Biochim. Biophys. Acta. , vol.1695 , pp. 209-213
    • Rape, M.1    Jentsch, S.2
  • 217
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: Cell biological roles of proteasome activators and inhibitors
    • Rechsteiner M., Hill C.P. 2005. Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. Trends Cell Biol. 15 : 27-33.
    • (2005) Trends Cell Biol. , vol.15 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 219
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner M., Rogers S. W. 1996. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21 : 267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 220
    • 33846042439 scopus 로고    scopus 로고
    • Nucleotide excision repair and the ubiquitin proteasome pathway - Do all roads lead to Rome?
    • Reed S. H., Gillette T. G. 2007. Nucleotide excision repair and the ubiquitin proteasome pathway - do all roads lead to Rome? DNA Repair (Amst.). 6 : 149-156.
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 149-156
    • Reed, S.H.1    Gillette, T.G.2
  • 221
    • 33748336875 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in cell cycle control
    • Reed S. I. 2006. The ubiquitin-proteasome pathway in cell cycle control. Results Probl. Cell Differ. 42 : 147-181.
    • (2006) Results Probl. Cell Differ. , vol.42 , pp. 147-181
    • Reed, S.I.1
  • 222
    • 3142691854 scopus 로고    scopus 로고
    • DNA damage-induced Def1- RNA polymerase II interaction and Def1 requirement forpolymerase ubiquitylation in vitro
    • Reid J., Svejstrup J. Q. 2004. DNA damage-induced Def1- RNA polymerase II interaction and Def1 requirement forpolymerase ubiquitylation in vitro. J. Biol. Chem. 279 : 29 875 - 29 878.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29875-29878
    • Reid, J.1    Svejstrup, J.Q.2
  • 223
    • 0035869581 scopus 로고    scopus 로고
    • CPEB degradation during Xenopus oocyte maturation requires a PEST domain and the 26S proteasome
    • Reverte C. G., Ahearn M. D., Hake L. E. 2001. CPEB degradation during Xenopus oocyte maturation requires a PEST domain and the 26S proteasome. Develop. Biol. 231 : 447-458.
    • (2001) Develop. Biol. , vol.231 , pp. 447-458
    • Reverte, C.G.1    Ahearn, M.D.2    Hake, L.E.3
  • 224
    • 0032006110 scopus 로고    scopus 로고
    • Intracellular distribution of proteasomes
    • Rivett A. J. 1998. Intracellular distribution of proteasomes. Curr. Opin. Immunol. 10 : 110-114.
    • (1998) Curr. Opin. Immunol. , vol.10 , pp. 110-114
    • Rivett, A.J.1
  • 225
    • 0035070697 scopus 로고    scopus 로고
    • Regulation of proteasome complexes by γ-interferon and phosphorylation
    • Rivett A., Bose S., Brooks P., Broadfoot K. I. 2001. Regulation of proteasome complexes by γ-interferon and phosphorylation. Biochimie. 83 : 363-366.
    • (2001) Biochimie. , Issue.83 , pp. 363-366
    • Rivett, A.1    Bose, S.2    Brooks, P.3    Broadfoot, K.I.4
  • 226
    • 0026651895 scopus 로고
    • Electron microscopic localization of the multicatalytic proteinase complex in rat liver and in cultured cells
    • Rivett A. J., Palmer A., Knecht E. 1992. Electron microscopic localization of the multicatalytic proteinase complex in rat liver and in cultured cells. J. Histochem. Cytochem. 40 : 1165-1172.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 1165-1172
    • Rivett, A.J.1    Palmer, A.2    Knecht, E.3
  • 227
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I-presented peptides
    • Rock K. L., Goldberg A. L. 1999. Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu. Rev. Immunol. 17 : 739-779.
    • (1999) Annu. Rev. Immunol. , Issue.17 , pp. 739-779
    • Rock, K.L.1    Goldberg, A.L.2
  • 228
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class i molecules
    • Rock K. L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., Goldberg A. L. 1994. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell. 78 : 761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 229
    • 0029973122 scopus 로고    scopus 로고
    • HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome
    • Rohrwild M., Coux O., Huang H. C., Moerschell R. P., Yoo S. J., Seol J. H. 1996. HslV-HslU: a novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome. Proc. Nat. Acad. Sci. USA. 93 : 5808-5813.
    • (1996) Proc. Nat. Acad. Sci. USA , vol.93 , pp. 5808-5813
    • Rohrwild, M.1    Coux, O.2    Huang, H.C.3    Moerschell, R.P.4    Yoo, S.J.5    Seol, J.H.6
  • 231
    • 0010586475 scopus 로고    scopus 로고
    • The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair
    • Russell S. J., Reed S. H., Huang W., Friedberg E. C., Johnston S. A. 1999. The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair. Mol. Cell. 3 : 687-695.
    • (1999) Mol. Cell. , vol.3 , pp. 687-695
    • Russell, S.J.1    Reed, S.H.2    Huang, W.3    Friedberg, E.C.4    Johnston, S.A.5
  • 232
    • 0028346790 scopus 로고
    • Distribution of prosome proteins and theirrelationship with the cytoskeleton in oogenesis of Xenopus laevis
    • Ryabova L. V., Virtanen I., Olink-Coux M., Scherrer K., Vas- setzky S. G. 1994. Distribution of prosome proteins and theirrelationship with the cytoskeleton in oogenesis of Xenopus laevis. Mol. Reprod. Develop. 37 : 195-203.
    • (1994) Mol. Reprod. Develop. , vol.37 , pp. 195-203
    • Ryabova, L.V.1    Virtanen, I.2    Olink-Coux, M.3    Scherrer, K.4    Vassetzky, S.G.5
  • 234
    • 0033081027 scopus 로고    scopus 로고
    • Destruction of Myc by ubiquitin-mediated proteolysis: Cancer-associated and transforming mutations stabilize Myc
    • Salghetti S. E., Kim S. Y., Tansey W. P. 1999. Destruction of Myc by ubiquitin-mediated proteolysis: cancer-associated and transforming mutations stabilize Myc. EMBO J. 18 : 717-726.
    • (1999) EMBO J. , vol.18 , pp. 717-726
    • Salghetti, S.E.1    Kim, S.Y.2    Tansey, W.P.3
  • 235
    • 0029132743 scopus 로고
    • Phosphorylation of proteasome substrate by a protein kinase associated with the 26 S proteasome is linked to the ATP-dependent proteolysis of the 26 S proteasome
    • Satoh K., Nishikawa T., Yokosawa H., Sawada H. 1995. Phosphorylation of proteasome substrate by a protein kinase associated with the 26 S proteasome is linked to the ATP-dependent proteolysis of the 26 S proteasome. Biochem. Biophys. Res. Commun. 213 : 7-14.
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 7-14
    • Satoh, K.1    Nishikawa, T.2    Yokosawa, H.3    Sawada, H.4
  • 236
    • 0002892252 scopus 로고    scopus 로고
    • The 26S proteasome assembly is regulated by a maturation-inducing hormone in starfish oocytes
    • Sawada M. T., Morinaga C., Izumi K., Sawada H. 1999. The 26S proteasome assembly is regulated by a maturation-inducing hormone in starfish oocytes. Biochem. Biophys. Res. Commun. 254 : 338-344.
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 338-344
    • Sawada, M.T.1    Morinaga, C.2    Izumi, K.3    Sawada, H.4
  • 238
    • 26844433577 scopus 로고    scopus 로고
    • Proteasome-associated proteins: Regulation of a proteolytic machine
    • Schmidt M., Hanna J., Elsasser S., Finley D. 2005. Proteasome-associated proteins: regulation of a proteolytic machine. Biol. Chem. 386 : 725-737.
    • (2005) Biol. Chem. , vol.386 , pp. 725-737
    • Schmidt, M.1    Hanna, J.2    Elsasser, S.3    Finley, D.4
  • 239
    • 11144245311 scopus 로고    scopus 로고
    • Regulated proteolysis and plant development
    • Schwechheimer C., Schwager K. 2004. Regulated proteolysis and plant development. Plant Cell Rep. 23 : 353-364.
    • (2004) Plant Cell Rep. , vol.23 , pp. 353-364
    • Schwechheimer, C.1    Schwager, K.2
  • 240
    • 0033590632 scopus 로고    scopus 로고
    • A rate limiting function of cdc25A for S phase entry inversely correlates with tyrosine dephosphorylation of Cdk2
    • Sexl V., Diehl J. A., Sherr C. J., Ashmun R., Beach D., Roussel M. F. 1999. A rate limiting function of cdc25A for S phase entry inversely correlates with tyrosine dephosphorylation of Cdk2. Oncogene. 18 : 573-582.
    • (1999) Oncogene. , vol.18 , pp. 573-582
    • Sexl, V.1    Diehl, J.A.2    Sherr, C.J.3    Ashmun, R.4    Beach, D.5    Roussel, M.F.6
  • 241
    • 0035180374 scopus 로고    scopus 로고
    • Ubiquitin proteasome pathway: Implications and advances in cancer therapy
    • Shah S. A., Potter M. W., Callery M. P. 2001a. Ubiquitin proteasome pathway: implications and advances in cancer therapy. Surg. Oncol. 10 : 43-52.
    • (2001) Surg. Oncol. , vol.10 , pp. 43-52
    • Shah, S.A.1    Potter, M.W.2    Callery, M.P.3
  • 244
    • 0034958237 scopus 로고    scopus 로고
    • P53-dependent apoptosis pathways
    • Shen Y., White E. 2001. p53-dependent apoptosis pathways. Adv. Cancer Res. 82 : 55-84.
    • (2001) Adv. Cancer Res. , vol.82 , pp. 55-84
    • Shen, Y.1    White, E.2
  • 245
    • 0036124032 scopus 로고    scopus 로고
    • Identification of the 19S regulatory particle subunits from the rice 26S proteasome
    • Shibahara T., Kawasaki H., Hirano H. 2002. Identification of the 19S regulatory particle subunits from the rice 26S proteasome. Eur. J. Biochem. 269 : 1474-1483.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1474-1483
    • Shibahara, T.1    Kawasaki, H.2    Hirano, H.3
  • 246
    • 0346218256 scopus 로고    scopus 로고
    • Mass spectrometric analysis of expression of ATPase subunits encoded by duplicated genes in the 19S regulatory particle of rice 26S proteasome
    • Shibahara T., Kawasaki H., Hirano H. 2004. Mass spectrometric analysis of expression of ATPase subunits encoded by duplicated genes in the 19S regulatory particle of rice 26S proteasome. Arch. Biochem. Biophys. 421 : 34-41.
    • (2004) Arch. Biochem. Biophys. , vol.421 , pp. 34-41
    • Shibahara, T.1    Kawasaki, H.2    Hirano, H.3
  • 247
    • 0029086522 scopus 로고
    • Sodium dodecyl sulfate (SDS) activation of the 20S proteasome in rat liver
    • Shibatani T., Ward W.F. 1995. Sodium dodecyl sulfate (SDS) activation of the 20S proteasome in rat liver. Arch. Biochem. Biophys. 321 : 160-166.
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 160-166
    • Shibatani, T.1    Ward, W.F.2
  • 248
    • 0026783274 scopus 로고
    • Regulation of gene expression of proteasomes (multi-protease complexes) during growth and differentiation of human hematopoietic cells
    • Shimbara N., Orino E., Sone S., Ogura T., Takashina M., Shono M., Tamura T., Yasuda H., Tanaka K., Ichihara A. 1992. Regulation of gene expression of proteasomes (multi-protease complexes) during growth and differentiation of human hematopoietic cells. J. Biol. Chem. 267 : 18 100 - 18 109.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18100-18109
    • Shimbara, N.1    Orino, E.2    Sone, S.3    Ogura, T.4    Takashina, M.5    Shono, M.6    Tamura, T.7    Yasuda, H.8    Tanaka, K.9    Ichihara, A.10
  • 250
    • 33748753648 scopus 로고    scopus 로고
    • Widespread, but non-identical, association of proteasomal 19 and 20 S proteins with yeast chromatin
    • Sikder D., Johnston S. A., Kodadek T. 2006. Widespread, but non-identical, association of proteasomal 19 and 20 S proteins with yeast chromatin. J. Biol. Chem. 281 : 27 346 - 27 355.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27346-27355
    • Sikder, D.1    Johnston, S.A.2    Kodadek, T.3
  • 251
    • 3242665372 scopus 로고    scopus 로고
    • The ubiquitin 26S proteasome proteolytic pathway
    • Smalle J., Vierstra D. 2004. The ubiquitin 26S proteasome proteolytic pathway. Annu. Rev. Plant Biol. 55 : 555-590.
    • (2004) Annu. Rev. Plant Biol. , vol.55 , pp. 555-590
    • Smalle, J.1    Vierstra, D.2
  • 253
    • 33746643854 scopus 로고    scopus 로고
    • Friend or foe? The proteasome in combined cancer therapy
    • Sohn D., Totzke G., Schulze-OsthoffK., Janicke R. U. 2006b. Friend or foe? The proteasome in combined cancer therapy. Cell Cycle. 5 : 841-845.
    • (2006) Cell Cycle , vol.5 , pp. 841-845
    • Sohn, D.1    Schulze-Osthoffk, T.G.2    Janicke, R.U.3
  • 254
    • 0030840661 scopus 로고    scopus 로고
    • Expression and subcellular localization of mouse 20S proteasome activator complex PA28
    • Soza A., Knuehl C., Groettrup M., Henklein P., Tanaka K., Kloetzel P.-M. 1997. Expression and subcellular localization of mouse 20S proteasome activator complex PA28. FEBS Lett. 413 : 27-34.
    • (1997) FEBS Lett. , vol.413 , pp. 27-34
    • Soza, A.1    Knuehl, C.2    Groettrup, M.3    Henklein, P.4    Tanaka, K.5    Kloetzel, P.-M.6
  • 255
  • 256
    • 0036384370 scopus 로고    scopus 로고
    • Physical association of the APIS complex and general transcription factors
    • Sun L., Johnston S. A., Kodadek T. 2002. Physical association of the APIS complex and general transcription factors. Biochem. Biophys. Res. Commun. 296 : 991-999.
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 991-999
    • Sun, L.1    Johnston, S.A.2    Kodadek, T.3
  • 257
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun Z. W., Allis C. D. 2002. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature. 418 : 104-108.
    • (2002) Nature , Issue.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 258
    • 0035902601 scopus 로고    scopus 로고
    • Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its antia-poptotic effect in Fas-induced cell death
    • Suzuki Y., Nakabayashi Y., Takahashi R. 2001. Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its antia-poptotic effect in Fas-induced cell death. Proc. Nat. Acad. Sci. USA. 98 : 8662-8667.
    • (2001) Proc. Nat. Acad. Sci. USA. , vol.98 , pp. 8662-8667
    • Suzuki, Y.1    Nakabayashi, Y.2    Takahashi, R.3
  • 259
    • 0041496232 scopus 로고    scopus 로고
    • Regulation of repair by the 26S proteasome
    • Sweder K., Madura K. 2002. Regulation of repair by the 26S proteasome. J. Biomed. Biotechnol. 2 : 94-105.
    • (2002) J. Biomed. Biotechnol. , vol.2 , pp. 94-105
    • Sweder, K.1    Madura, K.2
  • 260
    • 0035896601 scopus 로고    scopus 로고
    • Roles of NF-kappaB and 26 S proteasome in apoptotic cell death induced by topoisomerase i and II poisons in human nonsmall cell lung carcinoma
    • Tabata M., Tabata R., Grabowski D. R., Bukowski R. M. Ganapathi M. K., Ganapathi R. 2001. Roles of NF-kappaB and 26 S proteasome in apoptotic cell death induced by topoisomerase I and II poisons in human nonsmall cell lung carcinoma. J. Biol. Chem. 276 : 8029-8036.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8029-8036
    • Tabata, M.1    Tabata, R.2    Grabowski, D.R.3    Bukowski, R.M.4    Ganapathi, M.K.5    Ganapathi, R.6
  • 263
    • 0034745011 scopus 로고    scopus 로고
    • Control of IkappaBalpha proteolysis by the ubiquitin-protea-some pathway
    • Tanaka K., Kawakami T., Tateishi K., Yashiroda H., Chiba T. 2001. Control of IkappaBalpha proteolysis by the ubiquitin-protea-some pathway. Biochimie. 83 : 351-356.
    • (2001) Biochimie , vol.83 , pp. 351-356
    • Tanaka, K.1    Kawakami, T.2    Tateishi, K.3    Yashiroda, H.4    Chiba, T.5
  • 264
    • 0035943498 scopus 로고    scopus 로고
    • Proteasome inhibitors induce Fas-mediated apoptosis by c-Myc accumulation and subsequent induction of FasL message in human glioma cells
    • Tani E., Kitagawa H., Ikemoto H., Matsumoto T. 2001. Proteasome inhibitors induce Fas-mediated apoptosis by c-Myc accumulation and subsequent induction of FasL message in human glioma cells. FEBS Lett. 504 : 53-58.
    • (2001) FEBS Lett. , vol.504 , pp. 53-58
    • Tani, E.1    Kitagawa, H.2    Ikemoto, H.3    Matsumoto, T.4
  • 265
    • 0036217149 scopus 로고    scopus 로고
    • Proteasome inhibitors block ras/ERK signaling pathway resulting in the downregulation of Fas ligand expression during activation-induced cell death in T cells
    • Tanimoto Y., Kizaki H. 2002. Proteasome inhibitors block ras/ERK signaling pathway resulting in the downregulation of Fas ligand expression during activation-induced cell death in T cells. J. Biochem. 13 1: 319-326.
    • (2002) J. Biochem , vol.13 , Issue.1 , pp. 319-326
    • Tanimoto, Y.1    Kizaki, H.2
  • 266
    • 0030938526 scopus 로고    scopus 로고
    • Peptidyl aldehyde inhibitors of proteasome induce apoptosis rapidly in mouse lymphoma RVC cells
    • Tanimoto Y., Onishi Y., Hashimoto S., Kizaki H. 1997. Peptidyl aldehyde inhibitors of proteasome induce apoptosis rapidly in mouse lymphoma RVC cells. J. Biochem. 121 : 542-549.
    • (1997) J. Biochem , vol.121 , pp. 542-549
    • Tanimoto, Y.1    Onishi, Y.2    Hashimoto, S.3    Kizaki, H.4
  • 267
    • 0035336896 scopus 로고    scopus 로고
    • Transcriptional activation: Risky business
    • Tansey W. P. 2001. Transcriptional activation: risky business. Genes Develop. 15 : 1045-1050.
    • (2001) Genes Develop. , vol.15 , pp. 1045-1050
    • Tansey, W.P.1
  • 268
    • 0034616885 scopus 로고    scopus 로고
    • 2+-free calmodulin and calmodulin damaged by in vitro aging are selectively degraded by 26 S proteasomes without ubiquitination
    • 2+-free calmodulin and calmodulin damaged by in vitro aging are selectively degraded by 26 S proteasomes without ubiquitination. J. Biol. Chem. 275 : 20 295 - 20 301.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20295-20301
    • Tarcsa, E.1    Szymanska, G.2    Lecker, S.3    O'Connor, C.M.4    Goldberg, A.L.5
  • 269
    • 14944368609 scopus 로고    scopus 로고
    • A cytosolic pathway for MHC class II-restricted antigen processing that is proteasome and TAP dependent
    • Tewari M. K., Sinnathamby G., Rajagopal D., Eisenlohr L. C. 2005. A cytosolic pathway for MHC class II-restricted antigen processing that is proteasome and TAP dependent. Nat. Immunol. 6 : 287-294.
    • (2005) Nat. Immunol. , Issue.6 , pp. 287-294
    • Tewari, M.K.1    Sinnathamby, G.2    Rajagopal, D.3    Eisenlohr, L.C.4
  • 270
    • 0031058531 scopus 로고    scopus 로고
    • Identification and characterization of an activated 20S proteasome in Trypanosoma brucei
    • To W. Y., Wang C. C. 1997. Identification and characterization of an activated 20S proteasome in Trypanosoma brucei. FEBS Lett. 404 : 253-262.
    • (1997) FEBS Lett , Issue.404 , pp. 253-262
    • To, W.Y.1    Wang, C.C.2
  • 271
    • 0033976984 scopus 로고    scopus 로고
    • Two proteins, a goldfish 20S proteasome subunit and the protein interacting with 26S proteasome, change in the meiotic cell cycle
    • Tokumoto M., Horiguchi R., Nagahama Y., Ishikawa K., Tokumoto T. 2000. Two proteins, a goldfish 20S proteasome subunit and the protein interacting with 26S proteasome, change in the meiotic cell cycle. Eur. J. Biochem. 267 : 97-103.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 97-103
    • Tokumoto, M.1    Horiguchi, R.2    Nagahama, Y.3    Ishikawa, K.4    Tokumoto, T.5
  • 272
    • 0032740651 scopus 로고    scopus 로고
    • Identification of the Xenopus 20S proteasome alpha4 subunit which is modified in the meiotic cell cycle
    • Tokumoto M., Horiguchi R., Nagahama Y., Tokumoto T. 1999. Identification of the Xenopus 20S proteasome alpha4 subunit which is modified in the meiotic cell cycle. Gene. 239 : 301-308.
    • (1999) Gene , vol.239 , pp. 301-308
    • Tokumoto, M.1    Horiguchi, R.2    Nagahama, Y.3    Tokumoto, T.4
  • 273
    • 0025195135 scopus 로고
    • The NH2-terminal residues of rat liver proteasome (multicatalytic proteinase complex) subunits, C2, C3 and C8, are Nα-acetylated
    • Tokunaga F., Aruga R., Iwanaga S., Tanaka K., Ichihara A., Takao T., Shimonishi Y. 1990. The NH2-terminal residues of rat liver proteasome (multicatalytic proteinase complex) subunits, C2, C3 and C8, are Nα-acetylated. FEBS Lett. 263 : 373-375.
    • (1990) FEBS Lett. , Issue.263 , pp. 373-375
    • Tokunaga, F.1    Aruga, R.2    Iwanaga, S.3    Tanaka, K.4    Ichihara, A.5    Takao, T.6    Shimonishi, Y.7
  • 274
    • 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., Al- lday M. J. 2001. 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. 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
  • 275
    • 0028148227 scopus 로고
    • A proteasome inhibitor prevents activation of NFkB and stabilizes a newly phosphorylated form of i kappa B-alpha that is still bound to NFκB.
    • Traenckner E. B., Wilk S. Baeuerle P. A. 1994. A proteasome inhibitor prevents activation of NFkB and stabilizes a newly phosphorylated form of I kappa B-alpha that is still bound to NFκB. EMBO J. 13 : 5433-5441.
    • (1994) EMBO J. , vol.13 , pp. 5433-5441
    • Traenckner, E.B.1    Wilk, S.2    Baeuerle, P.A.3
  • 276
    • 33947595988 scopus 로고    scopus 로고
    • Changes in composition and activities of 26S proteasomes under the action of doxorubicin - Apoptosis inductor of erythroleukemic K562 cells
    • Tsimokha A. S., Mittenberg A. G., Kulichkova V. A., Kozhu- kharova I. V., Gause L. N., Konstantinova I. M. 2007. Changes in composition and activities of 26S proteasomes under the action of doxorubicin - apoptosis inductor of erythroleukemic K562 cells. Cell Biol. Int. 31 : 338-348.
    • (2007) Cell Biol. Int. , vol.31 , pp. 338-348
    • Tsimokha, A.S.1    Mittenberg, A.G.2    Kulichkova, V.A.3    Kozhukharova, I.V.4    Gause, L.N.5    Konstantinova, I.M.6
  • 277
    • 0031041162 scopus 로고    scopus 로고
    • Phosphorylation of the C2 subunit of the proteasome in rice (Oryza sativa L.)
    • Umeda M., Manabe Y., Uchimiya H. 1997. Phosphorylation of the C2 subunit of the proteasome in rice (Oryza sativa L.). FEBS Lett. 403 : 303-307.
    • (1997) FEBS Lett , vol.403 , pp. 303-307
    • Umeda, M.1    Manabe, Y.2    Uchimiya, H.3
  • 278
    • 0036646488 scopus 로고    scopus 로고
    • PA200, a nuclear proteasome activator involved in DNA repair
    • Ustrell V., Hoffman L., Pratt G., Rechsteiner M. 2002. PA200, a nuclear proteasome activator involved in DNA repair. EMBO J. 21 : 3516-3525.
    • (2002) EMBO J. , vol.21 , pp. 3516-3525
    • Ustrell, V.1    Hoffman, L.2    Pratt, G.3    Rechsteiner, M.4
  • 280
    • 33745621044 scopus 로고    scopus 로고
    • Proteasome inhibition as novel treatment strategy in leukaemia
    • Vink J., Cloos J., Kaspers G. J. 2006. Proteasome inhibition as novel treatment strategy in leukaemia. Br. J. Haematol. 134 : 253-262.
    • (2006) Br. J. Haematol. , vol.134 , pp. 253-262
    • Vink, J.1    Cloos, J.2    Kaspers, G.J.3
  • 281
  • 283
    • 33745192054 scopus 로고    scopus 로고
    • The nuclear ubiquitin-proteasome system
    • Von Mikecz A. 2006. The nuclear ubiquitin-proteasome system. J. Cell Sci. 119 : 1977-1984.
    • (2006) J. Cell Sci. , vol.119 , pp. 1977-1984
    • Von Mikecz, A.1
  • 284
    • 34248649848 scopus 로고    scopus 로고
    • Identification of alpha-type subunits of the Xenopus 20S proteasome and analysis of their changes during the meiotic cell cycle
    • Wakata Y., Tokumoto M., Horiguchi R., Ishikawa K., Nagaha- ma Y., Tokumoto T. 2004. Identification of alpha-type subunits of the Xenopus 20S proteasome and analysis of their changes during the meiotic cell cycle. BMC Biochem. 5 : 18.
    • (2004) BMC Biochem. , vol.5 , pp. 18
    • Wakata, Y.1    Tokumoto, M.2    Horiguchi, R.3    Ishikawa, K.4    Nagahama, Y.5    Tokumoto, T.6
  • 285
    • 0035900780 scopus 로고    scopus 로고
    • Proteasomemediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids
    • Wallace A. D., Cidlowski J. A. 2001. Proteasomemediated glucocorticoid receptor degradation restricts transcriptional signaling by glucocorticoids. J. Biol. Chem. 276 : 42 714 - 42 721.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42714-42721
    • Wallace, A.D.1    Cidlowski, J.A.2
  • 287
    • 0029858387 scopus 로고    scopus 로고
    • TNF and cancer therapy-induced apoptosis: Potentiation by inhibition of NFκB
    • Wang C. Y., Mayo M.W., Baldwin A. S. Jr. 1996. TNF and cancer therapy-induced apoptosis: potentiation by inhibition of NFkB. Science. 274 : 787-789.
    • (1996) Science. , vol.274 , pp. 787-789
    • Wang, C.Y.1    Mayo, M.W.2    Baldwin Jr., A.S.3
  • 288
    • 0030919574 scopus 로고    scopus 로고
    • Import of human and Thermoplasma 20S proteasomes into nuclei of HeLa cells requires functional NLS sequences
    • Wang H. R., Kania M., Baumeister W., Nederlof P. M. 1997. Import of human and Thermoplasma 20S proteasomes into nuclei of HeLa cells requires functional NLS sequences. Eur. J. Cell Biol. 73 : 105-113.
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 105-113
    • Wang, H.R.1    Kania, M.2    Baumeister, W.3    Nederlof, P.M.4
  • 289
    • 34250011799 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and its role in inflammatory and autoimmune diseases
    • Wang J., Maldonado M. A. 2006. The ubiquitin-proteasome system and its role in inflammatory and autoimmune diseases. Cell Mol. Immunol. 3 : 255-261.
    • (2006) Cell Mol. Immunol. , vol.3 , pp. 255-261
    • Wang, J.1    Maldonado, M.A.2
  • 290
    • 0033375769 scopus 로고    scopus 로고
    • Role of p53 and apoptosis in carcinogenesis
    • Wang X. W. 1999. Role of p53 and apoptosis in carcinogenesis. Anticancer Res. 19 : 4759-4771.
    • (1999) Anticancer Res. , vol.19 , pp. 4759-4771
    • Wang, X.W.1
  • 291
    • 33947380146 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the affinity-purified human 26S proteasome complex
    • Wang X., Chen C., Baker P. R., Chen P., Kaiser P., Huang L. 2007. Mass spectrometric characterization of the affinity-purified human 26S proteasome complex. Biochemistry. 46 : 3553-3565.
    • (2007) Biochemistry , vol.46 , pp. 3553-3565
    • Wang, X.1    Chen, C.2    Baker, P.R.3    Chen, P.4    Kaiser, P.5    Huang, L.6
  • 293
    • 0001607910 scopus 로고    scopus 로고
    • Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications
    • Wells L., Vosseller K., Cole R. N., Cronshaw J. M., Matunis M. J., Hart G. W. 2002. Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications. Mol. Cell Proteomics. 1 : 791-804.
    • (2002) Mol. Cell Proteomics. , vol.1 , pp. 791-804
    • Wells, L.1    Vosseller, K.2    Cole, R.N.3    Cronshaw, J.M.4    Matunis, M.J.5    Hart, G.W.6
  • 294
    • 0034604384 scopus 로고    scopus 로고
    • Characterization of the newly identified human Ump1 homologue POMP and analysis of LMP7 (beta 5i) incorporation into 20S proteasomes
    • Witt E., Zantopf D., Schmidt M., Kraft R., Kloetzel P. M., Kruger E. 2000. Characterization of the newly identified human Ump1 homologue POMP and analysis of LMP7 (beta 5i) incorporation into 20S proteasomes. J. Mol. Biol. 301 : 1-9.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1-9
    • Witt, E.1    Zantopf, D.2    Schmidt, M.3    Kraft, R.4    Kloetzel, P.M.5    Kruger, E.6
  • 295
    • 0002080055 scopus 로고    scopus 로고
    • Inhibition of the proteasome as a therapeutic approach
    • Wojcik C. 1999. Inhibition of the proteasome as a therapeutic approach. Drug Discov. Today. 4 : 188-192.
    • (1999) Drug Discov. Today , vol.4 , pp. 188-192
    • Wojcik, C.1
  • 296
    • 0036355705 scopus 로고    scopus 로고
    • Regulation of apoptosis by the ubiquitin and proteasome pathway
    • Wojcik C. 2002. Regulation of apoptosis by the ubiquitin and proteasome pathway. J. Cell Mol. Med. 6 : 25-48.
    • (2002) J. Cell Mol. Med. , vol.6 , pp. 25-48
    • Wojcik, C.1
  • 300
    • 3242730192 scopus 로고    scopus 로고
    • From lysosome to proteasome: The power of yeast in the dissection of proteinase function in cellular regulation and waste disposal
    • Wolf D. H. 2004. From lysosome to proteasome: the power of yeast in the dissection of proteinase function in cellular regulation and waste disposal. Cell Mol. Life Sci. 61 : 1-14.
    • (2004) Cell Mol. Life Sci. , vol.61 , pp. 1-14
    • Wolf, D.H.1
  • 301
    • 9644300915 scopus 로고    scopus 로고
    • The proteasome: A proteolytic nano-machine of cell regulation and waste disposal
    • Wolf D. H., Hilt W. 2004. The proteasome: a proteolytic nano-machine of cell regulation and waste disposal. Biochim. biophys. acta. 1695 : 19-31.
    • (2004) Biochim. Biophys. Acta. , vol.1695 , pp. 19-31
    • Wolf, D.H.1    Hilt, W.2
  • 302
    • 33749243499 scopus 로고    scopus 로고
    • Proteasome inhibition induces both pro-and anti-cell death pathways in prostate cancer cells
    • Yang W., Monroe J., Zhang Y., George D., Bremer E., Li H. 2006. Proteasome inhibition induces both pro- and anti-cell death pathways in prostate cancer cells. Cancer Lett. 243 : 217-227.
    • (2006) Cancer Lett , vol.243 , pp. 217-227
    • Yang, W.1    Monroe, J.2    Zhang, Y.3    George, D.4    Bremer, E.5    Li, H.6
  • 303
    • 0034607655 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli
    • Yang Y., Fang S., Jensen J.P., Weissman A. M., Ashwell J. D. 2000. Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli. Science. 288 : 874-877.
    • (2000) Science. , vol.288 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3    Weissman, A.M.4    Ashwell, J.D.5
  • 304
    • 0038375025 scopus 로고    scopus 로고
    • Regulation of apoptosis: The ubiquitous way
    • Yang Y., Yu X. 2003. Regulation of apoptosis: the ubiquitous way. FASEB J. 17 : 790-799.
    • (2003) FASEB J. , vol.17 , pp. 790-799
    • Yang, Y.1    Yu, X.2
  • 305
    • 0033607805 scopus 로고    scopus 로고
    • Structural and functional characterizations of the proteasome-activating protein PA26 from Trypanosoma brucei
    • Yao Y., Huang L., Krutchinsky A., Wong M. L., Standing K. G., Burlingame A. L., Wang C. C. 1999. Structural and functional characterizations of the proteasome-activating protein PA26 from Trypanosoma brucei. J. Biol. Chem. 274 : 33 921 - 33 930.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33921-33930
    • Yao, Y.1    Huang, L.2    Krutchinsky, A.3    Wong, M.L.4    Standing, K.G.5    Burlingame, A.L.6    Wang, C.C.7
  • 306
    • 2342539803 scopus 로고    scopus 로고
    • O-GlcNAc modification: A nutritional sensor that modulates proteasome function
    • Zachara N. E., Hart G. W. 2004. O-GlcNAc modification: a nutritional sensor that modulates proteasome function. Trends Cell Biol. 14 : 218-221.
    • (2004) Trends Cell Biol. , vol.14 , pp. 218-221
    • Zachara, N.E.1    Hart, G.W.2
  • 307
    • 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. 2007. Proteasome function is regulated by cyclic AMP-dependent protein kinase through phosphorylation of Rpt6. J. Biol. Chem. 282 : 22 460 - 22 471.
    • (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
  • 308
    • 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. 2003. O-GlcNAc modification is an endogenous inhibitor of the proteasome. Cell. 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
  • 309
    • 33748947865 scopus 로고    scopus 로고
    • The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription
    • Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R., Sun X., Shang Y. 2006. The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription. EMBO J. 25 : 4223-4233.
    • (2006) EMBO J. , vol.25 , pp. 4223-4233
    • Zhang, H.1    Sun, L.2    Liang, J.3    Yu, W.4    Zhang, Y.5    Wang, Y.6    Chen, Y.7    Li, R.8    Sun, X.9    Shang, Y.10
  • 310
    • 13444263620 scopus 로고    scopus 로고
    • Targeted protein degradation
    • Zhou P. 2005. Targeted protein degradation. Curr. Opin. Chem. Biol. 9 : 51-55.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 51-55
    • Zhou, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.