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Volumn 288, Issue 17, 2013, Pages 12161-12174

Negative regulation of 26S proteasome stability via calpain-mediated cleavage of Rpn10 subunit upon mitochondrial dysfunction in neurons

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN ACTIVATION; CELL-DEATH PATHWAYS; ELECTRON TRANSPORT CHAIN; MICROTUBULE ASSOCIATED PROTEIN; MITOCHONDRIAL DYSFUNCTION; NEUROFIBRILLARY TANGLES; PROTEIN DEGRADATION; PROTEIN TURNOVERS;

EID: 84876903554     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.464552     Document Type: Article
Times cited : (54)

References (68)
  • 1
    • 79151480727 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system and mitochondria - Reciprocity
    • Livnat-Levanon, N., and Glickman, M. H. (2011) Ubiquitin-proteasome system and mitochondria - reciprocity. Biochim. Biophys. Acta 1809, 80-87
    • (2011) Biochim. Biophys. Acta , vol.1809 , pp. 80-87
    • Livnat-Levanon, N.1    Glickman, M.H.2
  • 2
    • 33644652951 scopus 로고    scopus 로고
    • Proteasome regulation of oxidative stress in aging and age-related diseases of the CNS
    • Ding, Q., Dimayuga, E., and Keller, J. N. (2006) Proteasome regulation of oxidative stress in aging and age-related diseases of the CNS. Antioxid. Redox Signal. 8, 163-172
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 163-172
    • Ding, Q.1    Dimayuga, E.2    Keller, J.N.3
  • 3
    • 84857369951 scopus 로고    scopus 로고
    • Recruiting adaptive cellular stress responses for successful brain ageing
    • Stranahan, A. M., and Mattson, M. P. (2012) Recruiting adaptive cellular stress responses for successful brain ageing. Nat. Rev. Neurosci. 13, 209-216
    • (2012) Nat. Rev. Neurosci. , vol.13 , pp. 209-216
    • Stranahan, A.M.1    Mattson, M.P.2
  • 4
    • 34648834538 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in aging and Alzheimer's disease: Strategies to protect neurons
    • Reddy, P. H. (2007) Mitochondrial dysfunction in aging and Alzheimer's disease: strategies to protect neurons. Antioxid. Redox Signal. 9, 1647-1658
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 1647-1658
    • Reddy, P.H.1
  • 5
    • 25444474703 scopus 로고    scopus 로고
    • Mitochondria take center stage in aging and neurodegeneration
    • Beal, M. F. (2005) Mitochondria take center stage in aging and neurodegeneration. Ann. Neurol. 58, 495-505
    • (2005) Ann. Neurol. , vol.58 , pp. 495-505
    • Beal, M.F.1
  • 6
    • 61649121516 scopus 로고    scopus 로고
    • The UPS and autophagy in chronic neurodegenerative disease: Six of one and half a dozen of the other-or not?
    • Bedford, L., Paine, S., Rezvani, N., Mee, M., Lowe, J., and Mayer, R. J. (2009) The UPS and autophagy in chronic neurodegenerative disease: six of one and half a dozen of the other-or not? Autophagy. 5, 224-227
    • (2009) Autophagy. , vol.5 , pp. 224-227
    • Bedford, L.1    Paine, S.2    Rezvani, N.3    Mee, M.4    Lowe, J.5    Mayer, R.J.6
  • 7
    • 57649178442 scopus 로고    scopus 로고
    • Oxidative stress and energy crises in neuronal dysfunction
    • Nicholls, D. G. (2008) Oxidative stress and energy crises in neuronal dysfunction. Ann. N. Y. Acad. Sci. 1147, 53-60
    • (2008) Ann. N. Y. Acad. Sci. , vol.1147 , pp. 53-60
    • Nicholls, D.G.1
  • 8
    • 57649187117 scopus 로고    scopus 로고
    • Brain glucose hypome-tabolism and oxidative stress in preclinical Alzheimer's disease
    • Mosconi, L., Pupi, A., and De Leon, M. J. (2008) Brain glucose hypome-tabolism and oxidative stress in preclinical Alzheimer's disease. Ann. N. Y. Acad. Sci. 1147, 180-195
    • (2008) Ann. N. Y. Acad. Sci. , vol.1147 , pp. 180-195
    • Mosconi, L.1    Pupi, A.2    De Leon, M.J.3
  • 9
    • 0026781603 scopus 로고
    • Oxidative energy metabolism in Alzheimer brain. Studies in early-onset and late-onset cases
    • Hoyer, S. (1992) Oxidative energy metabolism in Alzheimer brain. Studies in early-onset and late-onset cases. Mol. Chem. Neuropathol. 16, 207-224
    • (1992) Mol. Chem. Neuropathol. , vol.16 , pp. 207-224
    • Hoyer, S.1
  • 11
    • 84872532360 scopus 로고    scopus 로고
    • Abnormal mitochondrial dynamics in the pathogenesis of Alzheimer's disease
    • Zhu, X., Perry, G., Smith, M. A., and Wang, X. (2013) Abnormal mitochondrial dynamics in the pathogenesis of Alzheimer's disease. J. Alzheimers Dis. 33, Suppl. 1, S253-S262
    • (2013) J. Alzheimers Dis. , vol.33 , Issue.SUPPL. 1
    • Zhu, X.1    Perry, G.2    Smith, M.A.3    Wang, X.4
  • 12
    • 0031831270 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman, E. R., and Berlett, B. S. (1998) Reactive oxygen-mediated protein oxidation in aging and disease. Drug Metab. Rev. 30, 225-243
    • (1998) Drug Metab. Rev. , vol.30 , pp. 225-243
    • Stadtman, E.R.1    Berlett, B.S.2
  • 13
    • 79957933700 scopus 로고    scopus 로고
    • Ubiquitin-proteasome pathway and cellular responses to oxidative stress
    • Shang, F., and Taylor, A. (2011) Ubiquitin-proteasome pathway and cellular responses to oxidative stress. Free Radic. Biol. Med. 51, 5-16
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 5-16
    • Shang, F.1    Taylor, A.2
  • 14
    • 0037414834 scopus 로고    scopus 로고
    • Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome
    • Shringarpure, R., Grune, T., Mehlhase, J., and Davies, K. J. (2003) Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome. J. Biol. Chem. 278, 311-318
    • (2003) J. Biol. Chem. , vol.278 , pp. 311-318
    • Shringarpure, R.1    Grune, T.2    Mehlhase, J.3    Davies, K.J.4
  • 15
    • 0034769477 scopus 로고    scopus 로고
    • Removal of oxidatively damaged proteins from lens cells by the ubiquitin-proteasome pathway
    • Shang, F., Nowell, T. R., Jr., and Taylor, A. (2001) Removal of oxidatively damaged proteins from lens cells by the ubiquitin-proteasome pathway. Exp. EyeRes. 73, 229-238
    • (2001) Exp. EyeRes. , vol.73 , pp. 229-238
    • Shang, F.1    Nowell Jr., T.R.2    Taylor, A.3
  • 16
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin, M. T., and Beal, M. F. (2006) Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443, 787-795
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 17
    • 79960042882 scopus 로고    scopus 로고
    • Selective vulnerability of neurons to acute toxicity after proteasome inhibitor treatment: Implications for oxidative stress and insolubility of newly synthesized proteins
    • Dasuri, K., Ebenezer, P. J., Zhang, L., Fernandez-Kim, S. O., Uranga, R. M., Gavilan, E., Di Blasio, A., and Keller, J. N. (2010) Selective vulnerability of neurons to acute toxicity after proteasome inhibitor treatment: implications for oxidative stress and insolubility of newly synthesized proteins. Free Radic. Biol. Med. 49, 1290-1297
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 1290-1297
    • Dasuri, K.1    Ebenezer, P.J.2    Zhang, L.3    Fernandez-Kim, S.O.4    Uranga, R.M.5    Gavilan, E.6    Di Blasio, A.7    Keller, J.N.8
  • 18
    • 4344677922 scopus 로고    scopus 로고
    • Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease
    • Grune, T., Jung, T., Merker, K., and Davies, K. J. (2004) Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int. J. Biochem. Cell Biol. 36, 2519-2530
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2519-2530
    • Grune, T.1    Jung, T.2    Merker, K.3    Davies, K.J.4
  • 19
    • 79955757695 scopus 로고    scopus 로고
    • Oxidative stress-mediated regulation of proteasome complexes
    • R110.006924
    • Aiken, C. T., Kaake, R. M., Wang, X., and Huang, L. (2011) Oxidative stress-mediated regulation of proteasome complexes. Mol. Cell. Proteo-mics 10, R110.006924
    • (2011) Mol. Cell. Proteo-mics , vol.10
    • Aiken, C.T.1    Kaake, R.M.2    Wang, X.3    Huang, L.4
  • 20
    • 78650142376 scopus 로고    scopus 로고
    • Protein oxidative modifications in the ageing brain: Consequence for the onset of neurodegenerative disease
    • Grimm, S., Hoehn, A., Davies, K. J., and Grune, T. (2011) Protein oxidative modifications in the ageing brain: consequence for the onset of neurodegenerative disease. Free Radic. Res. 45, 73-88
    • (2011) Free Radic. Res. , vol.45 , pp. 73-88
    • Grimm, S.1    Hoehn, A.2    Davies, K.J.3    Grune, T.4
  • 21
    • 0027226219 scopus 로고
    • Optimized survival ofhippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination
    • Brewer, G. J., Torricelli, J. R., Evege, E. K., and Price, P. J. (1993) Optimized survival ofhippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination. J. Neurosci. Res. 35, 567-576
    • (1993) J. Neurosci. Res. , vol.35 , pp. 567-576
    • Brewer, G.J.1    Torricelli, J.R.2    Evege, E.K.3    Price, P.J.4
  • 22
    • 34548044244 scopus 로고    scopus 로고
    • Development of astroglial cells in patterned neuronal cultures
    • Nam, Y., Brewer, G. J., and Wheeler, B. C. (2007) Development of astroglial cells in patterned neuronal cultures. J Biomater. Sci. Polym. Ed. 18, 1091-1100
    • (2007) J Biomater. Sci. Polym. Ed. , vol.18 , pp. 1091-1100
    • Nam, Y.1    Brewer, G.J.2    Wheeler, B.C.3
  • 23
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann, T. (1983) Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65, 55-63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 24
    • 0036329641 scopus 로고    scopus 로고
    • Glutathione decreases in dopaminergic PC12 cells interfere with the ubiquitin protein degradation pathway: Relevance for Parkinson's disease?
    • Jha, N., Kumar, M. J., Boonplueang, R., and Andersen, J. K. (2002) Glutathione decreases in dopaminergic PC12 cells interfere with the ubiquitin protein degradation pathway: relevance for Parkinson's disease? J. Neuro-chem. 80, 555-561
    • (2002) J. Neuro-chem. , vol.80 , pp. 555-561
    • Jha, N.1    Kumar, M.J.2    Boonplueang, R.3    Andersen, J.K.4
  • 25
    • 80054723117 scopus 로고    scopus 로고
    • Assessment of proteasome impairment and accumulation/aggregation of ubiquitinated proteins in neuronal cultures. Methods
    • Myeku, N., Metcalfe, M. J., Huang, Q., and Figueiredo-Pereira, M. (2011) Assessment of proteasome impairment and accumulation/aggregation of ubiquitinated proteins in neuronal cultures. Methods Mol. Biol. 793, 273-296
    • (2011) Mol. Biol. , vol.793 , pp. 273-296
    • Myeku, N.1    Metcalfe, M.J.2    Huang, Q.3    Figueiredo-Pereira, M.4
  • 26
    • 0020674228 scopus 로고
    • Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex
    • Wilk, S., and Orlowski, M. (1983) Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex. J. Neurochem. 40, 842-849
    • (1983) J. Neurochem. , vol.40 , pp. 842-849
    • Wilk, S.1    Orlowski, M.2
  • 27
    • 0032490114 scopus 로고    scopus 로고
    • Inhibitors of NADH-ubiquinone reductase: An overview
    • Degli Esposti, M. (1998) Inhibitors of NADH-ubiquinone reductase: an overview. Biochim. Biophys. Acta 1364, 222-235
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 222-235
    • Degli Esposti, M.1
  • 28
    • 22544467474 scopus 로고    scopus 로고
    • Binding of the respiratory chain inhibitor antimycin to the mitochondrial bc1 complex: A new crystal structure reveals an altered intramolecular hydrogen-bonding pattern
    • Huang, L. S., Cobessi, D., Tung, E. Y., and Berry, E. A. (2005) Binding of the respiratory chain inhibitor antimycin to the mitochondrial bc1 complex: a new crystal structure reveals an altered intramolecular hydrogen-bonding pattern. J. Mol. Biol. 351, 573-597
    • (2005) J. Mol. Biol. , vol.351 , pp. 573-597
    • Huang, L.S.1    Cobessi, D.2    Tung, E.Y.3    Berry, E.A.4
  • 29
    • 73449145990 scopus 로고    scopus 로고
    • The specificity of neuroprotection by antioxidants
    • Liu, Y., and Schubert, D. R. (2009) The specificity of neuroprotection by antioxidants. J. Biomed. Sci. 16, 98
    • (2009) J. Biomed. Sci. , vol.16 , pp. 98
    • Liu, Y.1    Schubert, D.R.2
  • 30
    • 0027270211 scopus 로고
    • Characterization of the cellular reduction of 3-(4, 5-dimethylthiazol-2- yl)-2, 5-diphenyltetrazolium bromide (MTT): Subcellular localization, substrate dependence, and involvement of mitochondrial electron transport in MTT reduction
    • Berridge, M. V., and Tan, A. S. (1993) Characterization of the cellular reduction of 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide (MTT): subcellular localization, substrate dependence, and involvement of mitochondrial electron transport in MTT reduction. Arch. Biochem. Biophys. 303, 474-482
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 474-482
    • Berridge, M.V.1    Tan, A.S.2
  • 31
    • 0030852948 scopus 로고    scopus 로고
    • Mechanism of cellular 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide (MTT) reduction
    • Liu, Y., Peterson, D. A., Kimura, H., and Schubert, D. (1997) Mechanism of cellular 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide (MTT) reduction. J. Neurochem. 69, 581-593
    • (1997) J. Neurochem. , vol.69 , pp. 581-593
    • Liu, Y.1    Peterson, D.A.2    Kimura, H.3    Schubert, D.4
  • 32
    • 0034781572 scopus 로고    scopus 로고
    • The mechanism of mitochondrial membrane potential retention following release of cytochrome c in apoptotic GT1-7 neural cells
    • Rego, A. C., Vesce, S., and Nicholls, D. G. (2001) The mechanism of mitochondrial membrane potential retention following release of cytochrome c in apoptotic GT1-7 neural cells. CellDeath. Differ. 8, 995-1003
    • (2001) CellDeath. Differ. , vol.8 , pp. 995-1003
    • Rego, A.C.1    Vesce, S.2    Nicholls, D.G.3
  • 33
    • 78751486039 scopus 로고    scopus 로고
    • Diminished superoxide generation is associated with respiratory chain dysfunction and changes in the mitochondrial proteome of sensory neurons from diabetic rats
    • Akude, E., Zherebitskaya, E., Chowdhury, S. K., Smith, D. R., Dobrowsky, R. T., and Fernyhough, P. (2011) Diminished superoxide generation is associated with respiratory chain dysfunction and changes in the mitochondrial proteome of sensory neurons from diabetic rats. Diabetes 60, 288-297
    • (2011) Diabetes , vol.60 , pp. 288-297
    • Akude, E.1    Zherebitskaya, E.2    Chowdhury, S.K.3    Smith, D.R.4    Dobrowsky, R.T.5    Fernyhough, P.6
  • 34
    • 48149092833 scopus 로고    scopus 로고
    • High membrane potential promotes alkenal-induced mitochondrial uncoupling and influences adenine nucleotide translocase conformation
    • Azzu, V., Parker, N., and Brand, M. D. (2008) High membrane potential promotes alkenal-induced mitochondrial uncoupling and influences adenine nucleotide translocase conformation. Biochem. J. 413, 323-332
    • (2008) Biochem. J. , vol.413 , pp. 323-332
    • Azzu, V.1    Parker, N.2    Brand, M.D.3
  • 35
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens, J. F. (2003) Mitochondrial formation of reactive oxygen species. J. Physiol. 552, 335-344
    • (2003) J. Physiol. , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 36
    • 79955063530 scopus 로고    scopus 로고
    • Proteins bearing oxidation-induced carbonyl groups are not preferentially ubiquitinated
    • Kastle, M., and Grune, T. (2011) Proteins bearing oxidation-induced carbonyl groups are not preferentially ubiquitinated. Biochimie 93, 1076-1079
    • (2011) Biochimie , vol.93 , pp. 1076-1079
    • Kastle, M.1    Grune, T.2
  • 37
    • 42349089604 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in Alzheimer's disease
    • Oddo, S. (2008) The ubiquitin-proteasome system in Alzheimer's disease. J. Cell Mol. Med. 12, 363-373
    • (2008) J. Cell Mol. Med. , vol.12 , pp. 363-373
    • Oddo, S.1
  • 38
    • 38949126129 scopus 로고    scopus 로고
    • 12, 14-prostaglandin J2: An electrophilic trigger of cellular responses
    • 12, 14-prostaglandin J2: an electrophilic trigger of cellular responses. Chem. Res. Toxicol. 21, 138-144
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 138-144
    • Uchida, K.1    Shibata, T.2
  • 41
    • 0024413057 scopus 로고
    • ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin
    • Eytan, E., Ganoth, D., Armon, T., and Hershko, A. (1989) ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin. Proc. Natl. Acad. Sci. U. S. A. 86, 7751-7755
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 7751-7755
    • Eytan, E.1    Ganoth, D.2    Armon, T.3    Hershko, A.4
  • 42
    • 33847066706 scopus 로고    scopus 로고
    • Functions of the proteasome: From protein degradation and immune surveillance to cancer therapy
    • Goldberg, A. L. (2007) Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy. Biochem. Soc. Trans. 35, 12-17
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 12-17
    • Goldberg, A.L.1
  • 44
    • 0033956278 scopus 로고    scopus 로고
    • Calpain and caspase: Can you tell the difference?
    • Wang, K. K. (2000) Calpain and caspase: can you tell the difference? Trends Neurosci. 23, 20-26
    • (2000) Trends Neurosci. , vol.23 , pp. 20-26
    • Wang, K.K.1
  • 46
    • 0027517636 scopus 로고
    • Differential kinetics of propidium iodide uptake in apoptotic and necrotic thymocytes
    • Vitale, M., Zamai, L., Mazzotti, G., Cataldi, A., and Falcieri, E. (1993) Differential kinetics of propidium iodide uptake in apoptotic and necrotic thymocytes. Histochemistry 100, 223-229
    • (1993) Histochemistry , vol.100 , pp. 223-229
    • Vitale, M.1    Zamai, L.2    Mazzotti, G.3    Cataldi, A.4    Falcieri, E.5
  • 47
    • 0028904919 scopus 로고
    • Characterization of uptake and hydrolysis of fluorescein diacetate and carboxyfluorescein diacetate by intracellular esterases in Saccharomyces cerevisiae, which result in accumulation of fluorescent product
    • Breeuwer, P., Drocourt, J. L., Bunschoten, N., Zwietering, M. H., Rom-bouts, F. M., and Abee, T. (1995) Characterization of uptake and hydrolysis of fluorescein diacetate and carboxyfluorescein diacetate by intracellular esterases in Saccharomyces cerevisiae, which result in accumulation of fluorescent product. Appl. Environ. Microbiol. 61, 1614-1619
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1614-1619
    • Breeuwer, P.1    Drocourt, J.L.2    Bunschoten, N.3    Zwietering, M.H.4    Rom-bouts, F.M.5    Abee, T.6
  • 48
    • 0037029053 scopus 로고    scopus 로고
    • Mitochondrial effects of the pleiotropic proteasomal mutation mpr1/rpn11\ uncoupling from cell cycle defects in extragenic revertants
    • Rinaldi, T., Ricordy, R., Bolotin-Fukuhara, M., and Frontali, L. (2002) Mitochondrial effects of the pleiotropic proteasomal mutation mpr1/rpn11\ uncoupling from cell cycle defects in extragenic revertants. Gene 286, 43-51
    • (2002) Gene , vol.286 , pp. 43-51
    • Rinaldi, T.1    Ricordy, R.2    Bolotin-Fukuhara, M.3    Frontali, L.4
  • 50
    • 41149164588 scopus 로고    scopus 로고
    • Persistent mitochondrial dysfunction and oxidative stress hinder neuronal cell recovery from reversible proteasome inhibition
    • Papa, L., and Rockwell, P. (2008) Persistent mitochondrial dysfunction and oxidative stress hinder neuronal cell recovery from reversible proteasome inhibition. Apoptosis 13, 588-599
    • (2008) Apoptosis , vol.13 , pp. 588-599
    • Papa, L.1    Rockwell, P.2
  • 52
    • 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., and 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
  • 53
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiq-uitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • Verma, R., Oania, R., Graumann, J., and Deshaies, R. J. (2004) Multiubiq-uitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell 118, 99-110
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 56
    • 84866704795 scopus 로고    scopus 로고
    • Regulation and physiological roles of the calpain system in muscular disorders
    • Sorimachi, H., and Ono, Y. (2012) Regulation and physiological roles of the calpain system in muscular disorders. Cardiovasc. Res. 96, 11-22
    • (2012) Cardiovasc. Res. , vol.96 , pp. 11-22
    • Sorimachi, H.1    Ono, Y.2
  • 57
    • 79955395083 scopus 로고    scopus 로고
    • GPS-CCD: A novel computational program for the prediction of calpain cleavage sites
    • Liu, Z., Cao, J., Gao, X., Ma, Q., Ren, J., and Xue, Y. (2011) GPS-CCD: a novel computational program for the prediction of calpain cleavage sites. PLoS One 6, e19001
    • (2011) PLoS One , vol.6
    • Liu, Z.1    Cao, J.2    Gao, X.3    Ma, Q.4    Ren, J.5    Xue, Y.6
  • 58
    • 79955780941 scopus 로고    scopus 로고
    • Calpain cleavage prediction using multiple kernel learning
    • DuVerle, D. A., Ono, Y., Sorimachi, H., and Mamitsuka, H. (2011) Calpain cleavage prediction using multiple kernel learning. PLoS One 6, e19035
    • (2011) PLoS One , vol.6
    • DuVerle, D.A.1    Ono, Y.2    Sorimachi, H.3    Mamitsuka, H.4
  • 59
    • 78649328672 scopus 로고    scopus 로고
    • Synthetic lethality of rpn11-1 rpn10A is linked to altered proteasome assembly and activity
    • Chandra, A., Chen, L., and Madura, K. (2010) Synthetic lethality of rpn11-1 rpn10A is linked to altered proteasome assembly and activity. Curr. Genet. 56, 543-557
    • (2010) Curr. Genet. , vol.56 , pp. 543-557
    • Chandra, A.1    Chen, L.2    Madura, K.3
  • 60
    • 66149140574 scopus 로고    scopus 로고
    • Age-related decrease in proteasome expression contributes to defective nuclear fac-tor-KB activation during hepatic ischemia/reperfusion
    • Huber, N., Sakai, N., Eismann, T., Shin, T., Kuboki, S., Blanchard, J., Schuster, R., Edwards, M. J., Wong, H. R., and Lentsch, A. B. (2009) Age-related decrease in proteasome expression contributes to defective nuclear fac-tor-KB activation during hepatic ischemia/reperfusion. Hepatology 49, 1718-1728
    • (2009) Hepatology , vol.49 , pp. 1718-1728
    • Huber, N.1    Sakai, N.2    Eismann, T.3    Shin, T.4    Kuboki, S.5    Blanchard, J.6    Schuster, R.7    Edwards, M.J.8    Wong, H.R.9    Lentsch, A.B.10
  • 61
    • 29944438881 scopus 로고    scopus 로고
    • Necrotic death as a cell fate
    • Zong, W. X., and Thompson, C. B. (2006) Necrotic death as a cell fate. Genes Dev. 20, 1-15
    • (2006) Genes Dev. , vol.20 , pp. 1-15
    • Zong, W.X.1    Thompson, C.B.2
  • 62
    • 84858651730 scopus 로고    scopus 로고
    • Proteolytic regulation of the mitochondrial cAMP-dependent protein kinase
    • Shell, J. R., and Lawrence, D. S. (2012) Proteolytic regulation of the mitochondrial cAMP-dependent protein kinase. Biochemistry 51, 2258-2264
    • (2012) Biochemistry , vol.51 , pp. 2258-2264
    • Shell, J.R.1    Lawrence, D.S.2
  • 63
    • 79952364777 scopus 로고    scopus 로고
    • Dual vulnerability of Tau to calpains and caspase-3 proteolysis under neurotoxic and neurodegenerative conditions
    • Liu, M. C., Kobeissy, F., Zheng, W., Zhang, Z., Hayes, R. L., and Wang, K. K. (2011) Dual vulnerability of Tau to calpains and caspase-3 proteolysis under neurotoxic and neurodegenerative conditions. ASN. Neuro. 3, e00051
    • (2011) ASN. Neuro. , vol.3
    • Liu, M.C.1    Kobeissy, F.2    Zheng, W.3    Zhang, Z.4    Hayes, R.L.5    Wang, K.K.6
  • 64
    • 78449296170 scopus 로고    scopus 로고
    • Cleavage of Tau by calpain in Alzheimer's disease: The quest for the toxic 17 kD fragment
    • Garg, S., Timm, T., Mandelkow, E. M., Mandelkow, E., and Wang, Y. (2011) Cleavage of Tau by calpain in Alzheimer's disease: the quest for the toxic 17 kD fragment. Neurobiol. Aging 32, 1-14
    • (2011) Neurobiol. Aging , vol.32 , pp. 1-14
    • Garg, S.1    Timm, T.2    Mandelkow, E.M.3    Mandelkow, E.4    Wang, Y.5
  • 65
    • 79960735446 scopus 로고    scopus 로고
    • Calpain-mediated Tau cleavage: A mechanism leading to neurodegeneration shared by multiple tauopathies
    • Ferreira, A., and Bigio, E. H. (2011) Calpain-mediated Tau cleavage: a mechanism leading to neurodegeneration shared by multiple tauopathies. Mol. Med. 17, 676-685
    • (2011) Mol. Med. , vol.17 , pp. 676-685
    • Ferreira, A.1    Bigio, E.H.2
  • 66
    • 0024843661 scopus 로고
    • Macroxyproteinase (M. O. P.): A 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells
    • Pacifici, R. E., Salo, D. C., and Davies, K. J. (1989) Macroxyproteinase (M. O. P.): a 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells. FreeRadic. Biol. Med. 7, 521-536
    • (1989) FreeRadic. Biol. Med. , vol.7 , pp. 521-536
    • Pacifici, R.E.1    Salo, D.C.2    Davies, K.J.3
  • 67
    • 78649848069 scopus 로고    scopus 로고
    • The immunoproteasome, the 20S proteasome and the PA28αβ proteasome regulator are oxidative-stress-adaptive proteolytic complexes
    • Pickering, A. M., Koop, A. L., Teoh, C. Y., Ermak, G., Grune, T., and Davies, K. J. (2010) The immunoproteasome, the 20S proteasome and the PA28αβ proteasome regulator are oxidative-stress-adaptive proteolytic complexes. Biochem. J. 432, 585-594
    • (2010) Biochem. J. , vol.432 , pp. 585-594
    • Pickering, A.M.1    Koop, A.L.2    Teoh, C.Y.3    Ermak, G.4    Grune, T.5    Davies, K.J.6


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