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Volumn 10, Issue 7, 2015, Pages

Proteasome activity is affected by fluctuations in insulin-degrading enzyme distribution

Author keywords

[No Author keywords available]

Indexed keywords

INSULINASE; PROTEASOME; ATP DEPENDENT 26S PROTEASE; DRUG MIXTURE; PROTEIN BINDING;

EID: 84940847342     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0132455     Document Type: Article
Times cited : (29)

References (58)
  • 1
    • 84856532498 scopus 로고    scopus 로고
    • Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes
    • PMID: 22100792
    • Sbardella D, Fasciglione GF, Gioia M, Ciaccio C, Tundo GR, Marini S, et al. (2012) Human matrix metalloproteinases: An ubiquitarian class of enzymes involved in several pathological processes. Mol Aspects Med 33: 119-208. doi:10.1016/j.mam.2011.10.015 PMID: 22100792.
    • (2012) Mol Aspects Med , vol.33 , pp. 119-208
    • Sbardella, D.1    Fasciglione, G.F.2    Gioia, M.3    Ciaccio, C.4    Tundo, G.R.5    Marini, S.6
  • 2
    • 0021111565 scopus 로고
    • A high molecular weight metalloendoprotease from the cytosol of mammalian cells
    • PMID: 6401723
    • Kirschner RJ, Goldberg AL (1983) A high molecular weight metalloendoprotease from the cytosol of mammalian cells. J Biol Chem 258: 967-976. PMID: 6401723.
    • (1983) J Biol Chem , vol.258 , pp. 967-976
    • Kirschner, R.J.1    Goldberg, A.L.2
  • 3
    • 79959569095 scopus 로고    scopus 로고
    • Functional relevance of a novel SlyX motif in non-conventional secretion of insulin-degrading enzyme
    • PMID: 21576244
    • Glebov K, Schütze S, Walter J (2011) Functional Relevance of a Novel SlyX Motif in Non-conventional Secretion of Insulin-degrading Enzyme. J Biol Chem 286: 22711-22715. doi:10.1074/jbc.C110.217893 PMID: 21576244.
    • (2011) J Biol Chem , vol.286 , pp. 22711-22715
    • Glebov, K.1    Schütze, S.2    Walter, J.3
  • 4
    • 60349088206 scopus 로고    scopus 로고
    • Insulin-degrading enzyme is exported via an unconventional protein secretion pathway
    • PMID: 19144176
    • Zhao J, Li L, Leissring MA (2009) Insulin-degrading enzyme is exported via an unconventional protein secretion pathway. Mol Neurodegener 4: 1-5. doi:10.1186/1750-1326-4-4 PMID: 19144176.
    • (2009) Mol Neurodegener , vol.4 , pp. 1-5
    • Zhao, J.1    Li, L.2    Leissring, M.A.3
  • 5
    • 61849129656 scopus 로고    scopus 로고
    • Detergent resistant membrane- Associated IDE in brain tissue and cultured cells: Relevance to Aβ and insulin degradation
    • PMID: 19117523
    • Bulloj A, Leal MC, Surace E, Zhang X, Xu H, Ledesma MD, et al. (2008) Detergent resistant membrane- Associated IDE in brain tissue and cultured cells: Relevance to Aβ and insulin degradation. Mol. Neurodegener. 3: 22. doi:10.1186/1750-1326-3-22 PMID: 19117523.
    • (2008) Mol. Neurodegener , vol.3 , pp. 22
    • Bulloj, A.1    Leal, M.C.2    Surace, E.3    Zhang, X.4    Xu, H.5    Ledesma, M.D.6
  • 6
    • 54049119217 scopus 로고    scopus 로고
    • Expression of metalloprotease insulin-degrading enzyme insulysin in normal and malignant human tissues
    • Yfanti C, Mengele K, Gkazepis A, Weirich G, Giersig C, Kuo WL et al. (2008) Expression of metalloprotease insulin-degrading enzyme insulysin in normal and malignant human tissues. Int J Mol Med 4: 421-431.
    • (2008) Int J Mol Med , vol.4 , pp. 421-431
    • Yfanti, C.1    Mengele, K.2    Gkazepis, A.3    Weirich, G.4    Giersig, C.5    Kuo, W.L.6
  • 7
    • 0031550507 scopus 로고    scopus 로고
    • Overexpression of insulin degrading enzyme: Cellular localization and effects on insulin signaling
    • PMID: 9070242
    • Seta KA, Roth RA (1997) Overexpression of insulin degrading enzyme: cellular localization and effects on insulin signaling. Biochem Biophys Res Commun 231: 167-171. PMID: 9070242.
    • (1997) Biochem Biophys Res Commun , vol.231 , pp. 167-171
    • Seta, K.A.1    Roth, R.A.2
  • 8
    • 0032496368 scopus 로고    scopus 로고
    • Amyloidogenic determinant as a substrate recognition motif of insulin-degrading enzyme
    • PMID: 9607302
    • Kurochkin IV (1998)Amyloidogenic determinant as a substrate recognition motif of insulin-degrading enzyme. FEBS Lett 427: 153-156. PMID: 9607302.
    • (1998) FEBS Lett , vol.427 , pp. 153-156
    • Kurochkin, I.V.1
  • 9
    • 58549093250 scopus 로고    scopus 로고
    • Somatostatin: A novel substrate and a modulator of insulin-degrading enzyme activity
    • PMID: 19073193
    • Ciaccio C, Tundo GR, Grasso G, Spoto G, Marasco D, Ruvo M et al. (2009) Somatostatin: A novel substrate and a modulator of insulin-degrading enzyme activity. J Mol Biol 385: 1556-1567. doi:10.1016/j.jmb.2008.11.025 PMID: 19073193.
    • (2009) J Mol Biol , vol.385 , pp. 1556-1567
    • Ciaccio, C.1    Tundo, G.R.2    Grasso, G.3    Spoto, G.4    Marasco, D.5    Ruvo, M.6
  • 10
    • 84859241651 scopus 로고    scopus 로고
    • Somatostatin modulates insulin-degrading-enzyme metabolism: Implications for the regulation of microglia activity in AD
    • PMID: 22509294
    • Tundo G, Ciaccio C, Sbardella D, Boraso M, Viviani B, Coletta M, et al. (2012) Somatostatin modulates insulin-degrading-enzyme metabolism: implications for the regulation of microglia activity in AD. PLoS One 7: E34376. doi:10.1371/journal.pone.0034376 PMID: 22509294.
    • (2012) PLoS One , vol.7 , pp. e34376
    • Tundo, G.1    Ciaccio, C.2    Sbardella, D.3    Boraso, M.4    Viviani, B.5    Coletta, M.6
  • 11
    • 79951786420 scopus 로고    scopus 로고
    • Copper(I) and copper(II) inhibit Aβ peptides proteolysis by insulin-degrading enzyme differently: Implications for metallostasis alteration in Alzheimer's disease
    • PMID: 21274957
    • Grasso G, Pietropaolo A, Spoto G, Pappalardo G, Tundo GR, Ciaccio C, et al.(2011) Copper(I) and copper(II) inhibit Aβ peptides proteolysis by insulin-degrading enzyme differently: implications for metallostasis alteration in Alzheimer's disease. Chemistry 17: 2752-2762. doi:10.1002/chem.201002809 PMID: 21274957.
    • (2011) Chemistry , vol.17 , pp. 2752-2762
    • Grasso, G.1    Pietropaolo, A.2    Spoto, G.3    Pappalardo, G.4    Tundo, G.R.5    Ciaccio, C.6
  • 12
    • 70449564488 scopus 로고    scopus 로고
    • Insulin-degrading enzyme: Structurefunction relationship and its possible roles in health and disease
    • PMID: 19925417
    • Fernández-Gamba A, Leal MC, Morelli L, Castaño EM (2009) Insulin-degrading enzyme: structurefunction relationship and its possible roles in health and disease. Curr Pharm Des 15: 3644-3655. PMID: 19925417.
    • (2009) Curr Pharm des , vol.15 , pp. 3644-3655
    • Fernández-Gamba, A.1    Leal, M.C.2    Morelli, L.3    Castaño, E.M.4
  • 13
    • 0000398342 scopus 로고    scopus 로고
    • Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation
    • PMID: 9830016
    • Qiu WQ, Walsh DM, Ye Z, Vekrellis K, Zhang J (1998) Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation. J Biol Chem 273: 32730-32738. PMID: 9830016.
    • (1998) J Biol Chem , vol.273 , pp. 32730-32738
    • Qiu, W.Q.1    Walsh, D.M.2    Ye, Z.3    Vekrellis, K.4    Zhang, J.5
  • 14
    • 33750870063 scopus 로고    scopus 로고
    • The insulysin (insulin degrading enzyme) enigma
    • PMID: 16952049
    • Hersh LB (2006) The insulysin (insulin degrading enzyme) enigma. Cell Mol Life Sci 63:2432-2434. PMID: 16952049.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2432-2434
    • Hersh, L.B.1
  • 15
    • 84879468695 scopus 로고    scopus 로고
    • Deletion of the fission yeast homologue of human insulinase reveals a TORC1-dependent pathway mediating resistance to proteotoxic stress
    • PMID: 23826334
    • Beuzelin C, Evnouchidou I, Rigolet P, Cauvet-Burgevin A, Girard PM, Dardalhon D, et al.(2013) Deletion of the Fission Yeast Homologue of Human Insulinase Reveals a TORC1-Dependent Pathway Mediating Resistance to Proteotoxic Stress. PLoS One 8: E67705. doi:10.1371/journal.pone.0067705 PMID: 23826334.
    • (2013) PLoS One , vol.8 , pp. e67705
    • Beuzelin, C.1    Evnouchidou, I.2    Rigolet, P.3    Cauvet-Burgevin, A.4    Girard, P.M.5    Dardalhon, D.6
  • 16
    • 84855286354 scopus 로고    scopus 로고
    • Anion activation site of insulin-degrading enzyme
    • PMID: 22049080
    • Noinaj N, Song ES, Bhasin S, Alper BJ, Schmidt WK, Hersh LB, et al. (2012) Anion activation site of insulin-degrading enzyme. J Biol Chem 287: 48-57. doi:10.1074/jbc.M111.264614 PMID: 22049080.
    • (2012) J Biol Chem , vol.287 , pp. 48-57
    • Noinaj, N.1    Song, E.S.2    Bhasin, S.3    Alper, B.J.4    Schmidt, W.K.5    Hersh, L.B.6
  • 17
    • 77951298520 scopus 로고    scopus 로고
    • Production of an antigenic peptide by insulin-degrading enzyme
    • PMID: 20364150
    • Parmentier N, Stroobant V, Colau D, de Diesbach P, Morel S, Chapiro J, et al. (2010) Production of an antigenic peptide by insulin-degrading enzyme. Nat Immunol 11: 449-454. doi:10.1038/ni.1862 PMID: 20364150.
    • (2010) Nat Immunol , vol.11 , pp. 449-454
    • Parmentier, N.1    Stroobant, V.2    Colau, D.3    De Diesbach, P.4    Morel, S.5    Chapiro, J.6
  • 18
    • 77951620280 scopus 로고    scopus 로고
    • Retinoblastoma protein co-purifies with proteasomal insulin-degrading enzyme: Implications for cell proliferation control
    • PMID: 20362553
    • Radulescu RT, Duckworth WC, Levy JL, Fawcett J (2010) Retinoblastoma protein co-purifies with proteasomal insulin-degrading enzyme: implications for cell proliferation control. Biochem Biophys Res Commun 395: 196-199. doi:10.1016/j.bbrc.2010.03.157 PMID: 20362553.
    • (2010) Biochem Biophys Res Commun , vol.395 , pp. 196-199
    • Radulescu, R.T.1    Duckworth, W.C.2    Levy, J.L.3    Fawcett, J.4
  • 19
    • 79551684420 scopus 로고    scopus 로고
    • Ubiquitin is a novel substrate for human insulin-degrading enzyme
    • PMID: 21185309
    • Ralat LA, Kalas V, Zheng Z, Goldman RD, Sosnick TR, Tang WJ (2010) Ubiquitin is a novel substrate for human insulin-degrading enzyme. J Mol Biol 406: 454-466. doi:10.1016/j.jmb.2010.12.026 PMID: 21185309.
    • (2010) J Mol Biol , vol.406 , pp. 454-466
    • Ralat, L.A.1    Kalas, V.2    Zheng, Z.3    Goldman, R.D.4    Sosnick, T.R.5    Tang, W.J.6
  • 20
    • 52449135535 scopus 로고    scopus 로고
    • How the binding and degrading capabilities of insulin degrading enzyme are affected by ubiquitin
    • PMID: 18489915
    • Grasso G, Rizzarelli E, Spoto G (2008) How the binding and degrading capabilities of insulin degrading enzyme are affected by ubiquitin. Biochim Biophys Acta 1784: 1122-1126. doi:10.1016/j.bbapap.2008.04.011 PMID: 18489915.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1122-1126
    • Grasso, G.1    Rizzarelli, E.2    Spoto, G.3
  • 21
    • 0038377693 scopus 로고    scopus 로고
    • Insulin inhibition of the proteasome is dependent on degradation of insulin by insulin-degrading enzyme
    • PMID: 12773120
    • Bennett RG, Fawcett J, Kruer MC, Duckworth WC, Hamel FG (2003) Insulin inhibition of the proteasome is dependent on degradation of insulin by insulin-degrading enzyme. J Endocrinol 177: 399-405. PMID: 12773120.
    • (2003) J Endocrinol , vol.177 , pp. 399-405
    • Bennett, R.G.1    Fawcett, J.2    Kruer, M.C.3    Duckworth, W.C.4    Hamel, F.G.5
  • 22
    • 84873817119 scopus 로고    scopus 로고
    • Insulin-degrading enzyme (IDE): A novel heat shock-like protein
    • PMID: 23188819
    • Tundo GR, Sbardella D, Ciaccio C, Bianculli A, Orlandi A, Desimio MG, et al. (2013) Insulin-degrading enzyme (IDE): A novel heat shock-like protein. J Biol Chem 288: 2281-2289. doi:10.1074/jbc.M112.393108PMID: 23188819.
    • (2013) J Biol Chem , vol.288 , pp. 2281-2289
    • Tundo, G.R.1    Sbardella, D.2    Ciaccio, C.3    Bianculli, A.4    Orlandi, A.5    Desimio, M.G.6
  • 23
    • 84925491046 scopus 로고    scopus 로고
    • Novel Platinum (II) compounds modulate insulin-degrading enzyme activity and induce cell death in neuroblastoma cells
    • PMID: 25450414
    • Tundo GR, Sbardella D, De Pascali SA, Ciaccio C, Coletta M, Fanizzi FP, et al. (2015) Novel Platinum (II) compounds modulate insulin-degrading enzyme activity and induce cell death in neuroblastoma cells. J Biol Inorg Chem 20:101-8. doi:10.1007/s00775-014-1217-3 PMID: 25450414.
    • (2015) J Biol Inorg Chem , vol.20 , pp. 101-108
    • Tundo, G.R.1    Sbardella, D.2    De Pascali, S.A.3    Ciaccio, C.4    Coletta, M.5    Fanizzi, F.P.6
  • 24
    • 84875666140 scopus 로고    scopus 로고
    • The proteasome: From basic mechanisms to emerging roles
    • PMID: 23563787
    • Tanaka K (2013) The proteasome: from basic mechanisms to emerging roles. Keio J Med 62: 1-12. PMID: 23563787.
    • (2013) Keio J Med , vol.62 , pp. 1-12
    • Tanaka, K.1
  • 25
    • 61449156563 scopus 로고    scopus 로고
    • Targeting proteins for destruction by the ubiquitin system: Implications for human pathobiology
    • PMID: 18834306
    • Schwartz AL, Ciechanover A (2009) Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology. Annu Rev Pharmacol Toxicol 49: 73-96. doi:10.1146/annurev.pharmtox.051208.165340 PMID: 18834306.
    • (2009) Annu Rev Pharmacol Toxicol , vol.49 , pp. 73-96
    • Schwartz, A.L.1    Ciechanover, A.2
  • 26
    • 50149086108 scopus 로고    scopus 로고
    • Diversity of degradation signals in the ubiquitin-proteasome system
    • PMID: 18698327
    • Ravid T, Hochstrasser M (2008) Diversity of degradation signals in the ubiquitin-proteasome system. Nat Rev Mol Cell Biol 9: 679-690. doi:10.1038/nrm2468 PMID: 18698327.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 679-690
    • Ravid, T.1    Hochstrasser, M.2
  • 27
    • 0036678959 scopus 로고    scopus 로고
    • Role and function of the 26S proteasome in proliferation and apoptosis
    • PMID: 12177235
    • Naujokat C, Hoffmann S (2002) Role and function of the 26S proteasome in proliferation and apoptosis. Lab Invest 82: 965-980. PMID: 12177235.
    • (2002) Lab Invest , vol.82 , pp. 965-980
    • Naujokat, C.1    Hoffmann, S.2
  • 28
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • PMID: 9759494
    • Hershko A, Ciechanover A (1998) The ubiquitin system. Annu Rev Biochem 67: 425-479. PMID: 9759494.
    • (1998) Annu Rev Biochem , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 29
    • 84856976866 scopus 로고    scopus 로고
    • Complete subunit architecture of the proteasome regulatory particle
    • PMID: 22237024
    • Lander GC, Estrin E, Matyskiela ME, Bashore C, Nogales E, Martin A (2012) Complete subunit architecture of the proteasome regulatory particle. Nature 482: 186-191. doi:10.1038/nature10774 PMID: 22237024.
    • (2012) Nature , vol.482 , pp. 186-191
    • Lander, G.C.1    Estrin, E.2    Matyskiela, M.E.3    Bashore, C.4    Nogales, E.5    Martin, A.6
  • 30
    • 34249864120 scopus 로고    scopus 로고
    • A proteasome for all occasions
    • PMID: 17418826
    • Hanna J, Finley D (2007) A proteasome for all occasions. FEBS Lett 581: 2854-2861. PMID: 17418826.
    • (2007) FEBS Lett , vol.581 , pp. 2854-2861
    • Hanna, J.1    Finley, D.2
  • 31
    • 65849109465 scopus 로고    scopus 로고
    • Assembly pathway of the Mammalian proteasome base subcomplex is mediated by multiple specific chaperones
    • PMID: 19490896
    • Kaneko T, Hamazaki J, Iemura S, Sasaki K, Furuyama K, Natsume T, et al. (2009) Assembly pathway of the Mammalian proteasome base subcomplex is mediated by multiple specific chaperones. Cell 137: 914-925. doi:10.1016/j.cell.2009.05.008 PMID: 19490896.
    • (2009) Cell , vol.137 , pp. 914-925
    • Kaneko, T.1    Hamazaki, J.2    Iemura, S.3    Sasaki, K.4    Furuyama, K.5    Natsume, T.6
  • 32
    • 84878942836 scopus 로고    scopus 로고
    • Molecular architecture and assembly of the eukaryotic proteasome
    • PMID: 23495936
    • Tomko RJ Jr, Hochstrasser M (2013) Molecular Architecture and Assembly of the Eukaryotic Proteasome. Annu. Rev. Biochem. 82: 415-445. doi:10.1146/annurev-biochem-060410-150257 PMID: 23495936.
    • (2013) Annu. Rev. Biochem , vol.82 , pp. 415-445
    • Tomko, R.J.1    Hochstrasser, M.2
  • 33
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • PMID: 9476896
    • Baumeister W, Walz J, Zühl F, Seemüller E (1998) The proteasome: Paradigm of a self-compartmentalizing protease. Cell 92: 367-380. PMID: 9476896.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 34
    • 0034964524 scopus 로고    scopus 로고
    • The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release
    • PMID: 11430818
    • Köhler A, Cascio P, Leggett DS, Woo KM, Goldberg AL, Finley D (2001) The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release. Mol Cell 7: 1143-1152. PMID: 11430818.
    • (2001) Mol Cell , vol.7 , pp. 1143-1152
    • Köhler, A.1    Cascio, P.2    Leggett, D.S.3    Woo, K.M.4    Goldberg, A.L.5    Finley, D.6
  • 35
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • PMID: 9857172
    • Ciechanover A (1998) The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J 17: 7151-7160. PMID: 9857172.
    • (1998) EMBO J , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 37
    • 0037414834 scopus 로고    scopus 로고
    • Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome
    • PMID: 12401807
    • Shringarpure R, Grune T, Mehlhase J, Davies KJ (2003) Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome. J Biol Chem 278: 311-318. PMID: 12401807.
    • (2003) J Biol Chem , vol.278 , pp. 311-318
    • Shringarpure, R.1    Grune, T.2    Mehlhase, J.3    Davies, K.J.4
  • 38
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • PMID: 11295490
    • Davies KJ (2001) Degradation of oxidized proteins by the 20S proteasome. Biochimie 83: 301-310. PMID: 11295490.
    • (2001) Biochimie , vol.83 , pp. 301-310
    • Davies, K.J.1
  • 39
    • 84874192860 scopus 로고    scopus 로고
    • Formation of alternative proteasomes: Same lady, different cap?
    • PMID: 23333296
    • Pick E, Berman TS (2013) Formation of alternative proteasomes: same lady, different cap? FEBS Lett. 587: 389-393. doi:10.1016/j.febslet.2013.01.014 PMID: 23333296.
    • (2013) FEBS Lett , vol.587 , pp. 389-393
    • Pick, E.1    Berman, T.S.2
  • 40
    • 84857065362 scopus 로고    scopus 로고
    • Proteasome subtypes and the processing of tumor antigens: Increasing antigenic diversity
    • PMID: 22206698
    • Vigneron N, Van den Eynde BJ (2012) Proteasome subtypes and the processing of tumor antigens: increasing antigenic diversity. Curr Opin Immunol 24: 84-91. doi:10.1016/j.coi.2011.12.002 PMID: 22206698.
    • (2012) Curr Opin Immunol , vol.24 , pp. 84-91
    • Vigneron, N.1    Van Den Eynde, B.J.2
  • 42
    • 20444384416 scopus 로고    scopus 로고
    • Proteasome plasticity
    • PMID: 15890341
    • Glickman MH, Raveh D (2005) Proteasome plasticity. FEBS Lett 579: 3214-3223. PMID: 15890341.
    • (2005) FEBS Lett , vol.579 , pp. 3214-3223
    • Glickman, M.H.1    Raveh, D.2
  • 43
    • 78650720758 scopus 로고    scopus 로고
    • Proteasome activators
    • PMID: 21211719
    • Stadtmueller BM, Hill CP (2011) Proteasome activators. Mol Cell 41: 8-19. doi:10.1016/j.molcel.2010.12.020 PMID: 21211719.
    • (2011) Mol Cell , vol.41 , pp. 8-19
    • Stadtmueller, B.M.1    Hill, C.P.2
  • 44
    • 78650632460 scopus 로고    scopus 로고
    • Osmotic stress inhibits proteasome by p38 MAPK-dependent phosphorylation
    • PMID: 21044959
    • Lee SH, Park Y, Yoon SK, Yoon JB (2010) Osmotic stress inhibits proteasome by p38 MAPK-dependent phosphorylation. J Biol Chem 285: 41280-41289. doi:10.1074/jbc.M110.182188 PMID: 21044959.
    • (2010) J Biol Chem , vol.285 , pp. 41280-41289
    • Lee, S.H.1    Park, Y.2    Yoon, S.K.3    Yoon, J.B.4
  • 45
    • 34249007126 scopus 로고    scopus 로고
    • A ubiquitin stress response induces altered proteasome composition
    • PMID: 17512408
    • Hanna J, Meides A, Zhang DP, Finley D (2007) A ubiquitin stress response induces altered proteasome composition. Cell 129: 747-759. PMID: 17512408.
    • (2007) Cell , vol.129 , pp. 747-759
    • Hanna, J.1    Meides, A.2    Zhang, D.P.3    Finley, D.4
  • 46
    • 0042313977 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome
    • PMID: 12853471
    • Imai J, Maruya M, Yashiroda H, Yahara I, Tanaka K (2003) The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J 22: 3557-3567. PMID: 12853471.
    • (2003) EMBO J , vol.22 , pp. 3557-3567
    • Imai, J.1    Maruya, M.2    Yashiroda, H.3    Yahara, I.4    Tanaka, K.5
  • 47
    • 0034194227 scopus 로고    scopus 로고
    • Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress
    • PMID: 10775442
    • Reinheckel T, Ullrich O, Sitte N, Grune T (2000) Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress. Arch Biochem Biophys 377: 65- 68. PMID: 10775442.
    • (2000) Arch Biochem Biophys , vol.377 , pp. 65-68
    • Reinheckel, T.1    Ullrich, O.2    Sitte, N.3    Grune, T.4
  • 48
    • 0034457014 scopus 로고    scopus 로고
    • Insulin inhibits the ubiquitin-dependent degrading activity of the 26S proteasome
    • PMID: 10875252
    • Bennett RG, Hamel FG, Duckworth WC (2000) Insulin inhibits the ubiquitin-dependent degrading activity of the 26S proteasome. Endocrinology 141: 2508-2517. PMID: 10875252.
    • (2000) Endocrinology , vol.141 , pp. 2508-2517
    • Bennett, R.G.1    Hamel, F.G.2    Duckworth, W.C.3
  • 49
    • 0028024153 scopus 로고
    • Identification and isolation of a cytosolic proteolytic complex containing insulin degrading enzyme and the multicatalytic proteinase
    • PMID: 8048917
    • Bennett RG, Hamel FG, Duckworth WC (1994) Identification and isolation of a cytosolic proteolytic complex containing insulin degrading enzyme and the multicatalytic proteinase. Biochem Biophys Res Commun 202: 1047-1053. PMID: 8048917.
    • (1994) Biochem Biophys Res Commun , vol.202 , pp. 1047-1053
    • Bennett, R.G.1    Hamel, F.G.2    Duckworth, W.C.3
  • 50
    • 27644518292 scopus 로고    scopus 로고
    • Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates
    • PMID: 16275343
    • Kisselev AF, Goldberg AL (2005) Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates. Methods Enzymol 398: 364-378. PMID: 16275343.
    • (2005) Methods Enzymol , vol.398 , pp. 364-378
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 51
    • 40949104848 scopus 로고    scopus 로고
    • Isolation of endoplasmic reticulum, mitochondria, and mitochondria-associated membrane fractions from transfected cells and from human cytomegalovirus- infected primary fibroblasts
    • Chapter 3: Unit 3.27
    • Bozidis P, Williamson CD, Colberg-Poley AM (2007) Isolation of endoplasmic reticulum, mitochondria, and mitochondria-associated membrane fractions from transfected cells and from human cytomegalovirus- infected primary fibroblasts. Curr Protoc Cell Biol Chapter 3: Unit 3.27.
    • (2007) Curr Protoc Cell Biol
    • Bozidis, P.1    Williamson, C.D.2    Colberg-Poley, A.M.3
  • 52
    • 0038080911 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: Role of ATP binding site in suppression of caspase-7 activation
    • PMID: 12665508
    • Ramachandra KR, Changhui M, Baumeister P, Austin RC, Kaufman RJ, Lee AS (2003) Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: Role of ATP binding site in suppression of caspase-7 activation. J Biol Chem 278: 20915-20924. PMID: 12665508.
    • (2003) J Biol Chem , vol.278 , pp. 20915-20924
    • Ramachandra, K.R.1    Changhui, M.2    Baumeister, P.3    Austin, R.C.4    Kaufman, R.J.5    Lee, A.S.6
  • 53
    • 0034634389 scopus 로고    scopus 로고
    • Different proteasome subtypes in a single tissue exhibit different enzymatic properties
    • PMID: 11061965
    • Dahlmann B, Ruppert T, Kuehn L, Merforth S, Kloetzel PM (2000) Different proteasome subtypes in a single tissue exhibit different enzymatic properties. J Mol Biol 303: 643-653. PMID: 11061965.
    • (2000) J Mol Biol , vol.303 , pp. 643-653
    • Dahlmann, B.1    Ruppert, T.2    Kuehn, L.3    Merforth, S.4    Kloetzel, P.M.5
  • 54
    • 80052265819 scopus 로고    scopus 로고
    • HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress
    • PMID: 21767633
    • Grune T, Catalgol B, Licht A, Ermak G, Pickering AM, Ngo JK, et al. (2011) HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress. Free Radic Biol Med 51: 1355-1364. doi:10.1016/j.freeradbiomed.2011.06.015 PMID: 21767633.
    • (2011) Free Radic Biol Med , vol.51 , pp. 1355-1364
    • Grune, T.1    Catalgol, B.2    Licht, A.3    Ermak, G.4    Pickering, A.M.5    Ngo, J.K.6
  • 55
    • 78649980437 scopus 로고    scopus 로고
    • Regulation of the 26S proteasome complex during oxidative stress
    • Wang X, Yen J, Kaiser P, Huang L (2010) Regulation of the 26S proteasome complex during oxidative stress. Sci Signal 3: Ra88.
    • (2010) Sci Signal , vol.3 , pp. ra88
    • Wang, X.1    Yen, J.2    Kaiser, P.3    Huang, L.4
  • 57
    • 62449140977 scopus 로고    scopus 로고
    • The irreversible binding of amyloid peptide substrates to insulin-degrading enzyme: A biological perspective
    • PMID: 19098445
    • de Tullio MB, Morelli L, Castaño EM (2008) The irreversible binding of amyloid peptide substrates to insulin-degrading enzyme: A biological perspective. Prion 2: 51-56. PMID: 19098445.
    • (2008) Prion , vol.2 , pp. 51-56
    • De Tullio, M.B.1    Morelli, L.2    Castaño, E.M.3
  • 58
    • 26944432044 scopus 로고    scopus 로고
    • Proteasome activity or expression is not altered by activation of the heat shock transcription factor Hsf1 in cultured fibroblasts or myoblasts
    • PMID: 16184768
    • Taylor DM, Kabashi E, Agar JN, Minotti S, Durham HD (2005) Proteasome activity or expression is not altered by activation of the heat shock transcription factor Hsf1 in cultured fibroblasts or myoblasts. Cell Stress Chaperones 10: 230-241. PMID: 16184768.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 230-241
    • Taylor, D.M.1    Kabashi, E.2    Agar, J.N.3    Minotti, S.4    Durham, H.D.5


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