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Volumn 7, Issue November, 2014, Pages 1-17

Divergent tissue and sex effects of rapamycin on the proteasome-chaperone network of old mice

Author keywords

Heat shock proteins; Longevity; mTOR; Proteasome; Rapamycin; Sexual dimorphic effects

Indexed keywords

CHAPERONE; CHYMOTRYPSIN; HEAT SHOCK TRANSCRIPTION FACTOR 1; PROTEASOME; PROTEASOME INHIBITOR; RAPAMYCIN; TRYPTASE;

EID: 84908622526     PISSN: 16625099     EISSN: None     Source Type: Journal    
DOI: 10.3389/fnmol.2014.00083     Document Type: Article
Times cited : (17)

References (61)
  • 1
    • 21144450049 scopus 로고    scopus 로고
    • ATP hydrolysis-dependent disassembly of the 26S proteasome is part of the catalytic cycle
    • Babbitt, S. E., Kiss, A., Deffenbaugh, A. E., Chang, Y. H., Bailly, E., Erdjument-Bromage, H., et al. (2005). ATP hydrolysis-dependent disassembly of the 26S proteasome is part of the catalytic cycle. Cell 121, 553-565. doi: 10.1016/j.cell.2005.03.028
    • (2005) Cell , vol.121 , pp. 553-565
    • Babbitt, S.E.1    Kiss, A.2    Deffenbaugh, A.E.3    Chang, Y.H.4    Bailly, E.5    Erdjument-Bromage, H.6
  • 2
    • 84867818118 scopus 로고    scopus 로고
    • A proteasome inhibitor-stimulated Nrf1 protein-dependent compensatory increase in proteasome subunit gene expression reduces polycomb group protein level
    • Balasubramanian, S., Kanade, S., Han, B., and Eckert, R. L. (2012). A proteasome inhibitor-stimulated Nrf1 protein-dependent compensatory increase in proteasome subunit gene expression reduces polycomb group protein level.J. Biol. Chem. 287, 36179-36189. doi: 10.1074/jbc.M112.359281
    • (2012) J. Biol. Chem , vol.287 , pp. 36179-36189
    • Balasubramanian, S.1    Kanade, S.2    Han, B.3    Eckert, R.L.4
  • 3
    • 38049016914 scopus 로고    scopus 로고
    • Low-level caloric restriction rescues proteasome activity and Hsc70 level in liver of aged rats
    • Bonelli, M. A., Desenzani, S., Cavallini, G., Donati, A., Romani, A. A., Bergamini, E., et al. (2008). Low-level caloric restriction rescues proteasome activity and Hsc70 level in liver of aged rats. Biogerontology 9, 1-10. doi: 10.1007/s10522-007-9111-9
    • (2008) Biogerontology , vol.9 , pp. 1-10
    • Bonelli, M.A.1    Desenzani, S.2    Cavallini, G.3    Donati, A.4    Romani, A.A.5    Bergamini, E.6
  • 4
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., et al. (2002). Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416, 507-511. doi: 10.1038/416507a
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Chiti, F.3    Baroni, F.4    Formigli, L.5    Zurdo, J.6
  • 5
    • 70449719261 scopus 로고    scopus 로고
    • The roles of ubiquitin and 26S proteasome in human obesity
    • Chang, T. L., Chang, C. J., Lee, W. Y., Lin, M. N., Huang, Y. W., and Fan, K. (2009). The roles of ubiquitin and 26S proteasome in human obesity. Metabolism 58, 1643-1648. doi: 10.1016/j.metabol.2009.05.020
    • (2009) Metabolism , vol.58 , pp. 1643-1648
    • Chang, T.L.1    Chang, C.J.2    Lee, W.Y.3    Lin, M.N.4    Huang, Y.W.5    Fan, K.6
  • 6
    • 0033792614 scopus 로고    scopus 로고
    • Fibroblast cultures from healthy centenarians have an active proteasome
    • Chondrogianni, N., Petropoulos, I., Franceschi, C., Friguet, B., and Gonos, E. S. (2000). Fibroblast cultures from healthy centenarians have an active proteasome. Exp. Gerontol. 35, 721-728. doi: 10.1016/S0531-5565(00)00137-6
    • (2000) Exp. Gerontol , vol.35 , pp. 721-728
    • Chondrogianni, N.1    Petropoulos, I.2    Franceschi, C.3    Friguet, B.4    Gonos, E.S.5
  • 7
    • 84871750894 scopus 로고    scopus 로고
    • mTOR is essential for the proteotoxic stress response, HSF1 activation and heat shock protein synthesis
    • Chou, S. D., Prince, T., Gong, J., and Calderwood, S. K. (2012). mTOR is essential for the proteotoxic stress response, HSF1 activation and heat shock protein synthesis. PLoS ONE 7:e39679. doi: 10.1371/journal.pone.0039679
    • (2012) PLoS ONE , vol.7
    • Chou, S.D.1    Prince, T.2    Gong, J.3    Calderwood, S.K.4
  • 8
    • 0034659505 scopus 로고    scopus 로고
    • Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes
    • Cuesta, R., Laroia, G., and Schneider, R. J. (2000). Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes. Genes Dev. 14, 1460-1470. doi: 10.1101/gad.14.12.1460
    • (2000) Genes Dev , vol.14 , pp. 1460-1470
    • Cuesta, R.1    Laroia, G.2    Schneider, R.J.3
  • 9
    • 80053578494 scopus 로고    scopus 로고
    • Proteasome alterations during adipose differentiation and aging: Links to impaired adipocyte differentiation and development of oxidative stress
    • Dasuri, K., Zhang, L., Ebenezer, P., Fernandez-Kim, S. O., Bruce-Keller, A. J., Szweda, L. I., et al. (2011). Proteasome alterations during adipose differentiation and aging: links to impaired adipocyte differentiation and development of oxidative stress. Free Radic. Biol. Med. 51, 1727-1735. doi: 10.1016/j.freeradbiomed.2011.08.001
    • (2011) Free Radic. Biol. Med , vol.51 , pp. 1727-1735
    • Dasuri, K.1    Zhang, L.2    Ebenezer, P.3    Fernandez-Kim, S.O.4    Bruce-Keller, A.J.5    Szweda, L.I.6
  • 10
    • 77956795163 scopus 로고    scopus 로고
    • Widespread protein aggregation as an inherent part of aging in C. Elegans
    • David, D. C., Ollikainen, N., Trinidad, J. C., Cary, M. P., Burlingame, A. L., and Kenyon, C. (2010). Widespread protein aggregation as an inherent part of aging in C. elegans. PLoS Biol. 8:e1000450. doi: 10.1371/journal.pbio.1000450
    • (2010) PLoS Biol , vol.8
    • David, D.C.1    Ollikainen, N.2    Trinidad, J.C.3    Cary, M.P.4    Burlingame, A.L.5    Kenyon, C.6
  • 11
    • 84857628620 scopus 로고    scopus 로고
    • Univeristy of Tokyo (Accessed November 5, 2002)
    • De Hoon, M. (2002). Cluster 3.0 Manual. Available Online at:http://bonsai.hgc.jp/~mdehoon/software/cluster/manual/Contents.html#Contents: Univeristy of Tokyo (Accessed November 5, 2002).
    • (2002) Cluster 3.0 Manual
    • De Hoon, M.1
  • 12
    • 34249085552 scopus 로고    scopus 로고
    • Proteasomes: Machines for all reasons
    • Demartino, G. N., and Gillette, T. G. (2007). Proteasomes: machines for all reasons. Cell 129, 659-662. doi: 10.1016/j.cell.2007.05.007
    • (2007) Cell , vol.129 , pp. 659-662
    • Demartino, G.N.1    Gillette, T.G.2
  • 13
    • 33845874433 scopus 로고    scopus 로고
    • Brain CHIP: Removing the culprits in neurodegenerative disease
    • Dickey, C. A., Patterson, C., Dickson, D., and Petrucelli, L. (2007). Brain CHIP: removing the culprits in neurodegenerative disease. Trends Mol. Med. 13, 32-38. doi: 10.1016/j.molmed.2006.11.003
    • (2007) Trends Mol. Med , vol.13 , pp. 32-38
    • Dickey, C.A.1    Patterson, C.2    Dickson, D.3    Petrucelli, L.4
  • 14
    • 84890100345 scopus 로고    scopus 로고
    • Oxidative damage and amyloid-beta metabolism in brain regions of the longest-lived rodents
    • Edrey, Y. H., Oddo, S., Cornelius, C., Caccamo, A., Calabrese, V., and Buffenstein, R. (2014). Oxidative damage and amyloid-beta metabolism in brain regions of the longest-lived rodents. J. Neurosci. Res. 92, 195-205. doi: 10.1002/jnr.23320
    • (2014) J. Neurosci. Res , vol.92 , pp. 195-205
    • Edrey, Y.H.1    Oddo, S.2    Cornelius, C.3    Caccamo, A.4    Calabrese, V.5    Buffenstein, R.6
  • 15
    • 27644576445 scopus 로고    scopus 로고
    • Characterization of the proteasome using native gel electrophoresis
    • Elasser, S., Schmidt, M., and Finley, D. (2005). Characterization of the proteasome using native gel electrophoresis.Meth. Enzymol. 398, 353-363. doi: 10.1016/S0076-6879(05)98029-4
    • (2005) Meth. Enzymol , vol.398 , pp. 353-363
    • Elasser, S.1    Schmidt, M.2    Finley, D.3
  • 16
    • 16344363800 scopus 로고    scopus 로고
    • Altered proteasome structure, function, and oxidation in aged muscle
    • Ferrington, D. A., Husom, A. D., and Thompson, L. V. (2005). Altered proteasome structure, function, and oxidation in aged muscle. FASEB J. 19, 644-646. doi: 10.1096/fj.04-2578fje
    • (2005) FASEB J , vol.19 , pp. 644-646
    • Ferrington, D.A.1    Husom, A.D.2    Thompson, L.V.3
  • 17
    • 84896834460 scopus 로고    scopus 로고
    • Mice fed rapamycin have an increase in lifespan associated with major changes in the liver transcriptome
    • Fok, W. C., Chen, Y., Bokov, A., Zhang, Y., Salmon, A. B., Diaz, V., et al. (2014). Mice fed rapamycin have an increase in lifespan associated with major changes in the liver transcriptome. PLoS ONE 9:e83988. doi: 10.1371/journal.pone.0083988
    • (2014) PLoS ONE , vol.9
    • Fok, W.C.1    Chen, Y.2    Bokov, A.3    Zhang, Y.4    Salmon, A.B.5    Diaz, V.6
  • 18
    • 70450220221 scopus 로고    scopus 로고
    • The small heat shock protein HSP25 protects astrocytes against stress induced by proteasomal inhibition
    • Goldbaum, O., Riedel, M., Stahnke, T., and Richter-Landsberg, C. (2009). The small heat shock protein HSP25 protects astrocytes against stress induced by proteasomal inhibition. Glia 57, 1566-1577. doi: 10.1002/glia.20870
    • (2009) Glia , vol.57 , pp. 1566-1577
    • Goldbaum, O.1    Riedel, M.2    Stahnke, T.3    Richter-Landsberg, C.4
  • 19
    • 33646512636 scopus 로고    scopus 로고
    • Proteasome inhibition by MG-132 induces apoptotic cell death and mitochondrial dysfunction in cultured rat brain oligodendrocytes but not in astrocytes
    • Goldbaum, O., Vollmer, G., and Richter-Landsberg, C. (2006). Proteasome inhibition by MG-132 induces apoptotic cell death and mitochondrial dysfunction in cultured rat brain oligodendrocytes but not in astrocytes. Glia 53, 891-901. doi: 10.1002/glia.20348
    • (2006) Glia , vol.53 , pp. 891-901
    • Goldbaum, O.1    Vollmer, G.2    Richter-Landsberg, C.3
  • 20
    • 79959534486 scopus 로고    scopus 로고
    • Oxidative protein damage and the proteasome
    • Grimm, S., Hohn, A., and Grune, T. (2012). Oxidative protein damage and the proteasome. Amino Acids 42, 23-38. doi: 10.1007/s00726-010-0646-8
    • (2012) Amino Acids , vol.42 , pp. 23-38
    • Grimm, S.1    Hohn, A.2    Grune, T.3
  • 21
    • 80052265819 scopus 로고    scopus 로고
    • HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress
    • Grune, T., Catalgol, B., Licht, A., Ermak, G., Pickering, A. M., Ngo, J. K., 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
    • (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
  • 22
    • 67650944993 scopus 로고    scopus 로고
    • Rapamycin fed late in life extends lifespan in genetically heterogeneous mice
    • Harrison, D. E., Strong, R., Sharp, Z. D., Nelson, J. F., Astle, C. M., Flurkey, K., et al. (2009). Rapamycin fed late in life extends lifespan in genetically heterogeneous mice. Nature 460, 392-395. doi: 10.1038/nature08221
    • (2009) Nature , vol.460 , pp. 392-395
    • Harrison, D.E.1    Strong, R.2    Sharp, Z.D.3    Nelson, J.F.4    Astle, C.M.5    Flurkey, K.6
  • 23
    • 84892421283 scopus 로고    scopus 로고
    • eRapa restores a normal life span in a FAP mouse model
    • Hasty, P., Livi, C. B., Dodds, S. G., Jones, D., Strong, R., Javors, M., et al. (2014). eRapa restores a normal life span in a FAP mouse model. Cancer Prev. Res. 7, 169-178. doi: 10.1158/1940-6207.CAPR-13-0299
    • (2014) Cancer Prev. Res , vol.7 , pp. 169-178
    • Hasty, P.1    Livi, C.B.2    Dodds, S.G.3    Jones, D.4    Strong, R.5    Javors, M.6
  • 24
    • 0034644608 scopus 로고    scopus 로고
    • Membrane estrogen receptor engagement activates endothelial nitric oxide synthase via the PI3-kinase-Akt pathway in human endothelial cells
    • Haynes, M. P., Sinha, D., Russell, K. S., Collinge, M., Fulton, D., Morales-Ruiz, M., et al. (2000). Membrane estrogen receptor engagement activates endothelial nitric oxide synthase via the PI3-kinase-Akt pathway in human endothelial cells. Circ. Res. 87, 677-682. doi: 10.1161/01.RES.87.8.677
    • (2000) Circ. Res , vol.87 , pp. 677-682
    • Haynes, M.P.1    Sinha, D.2    Russell, K.S.3    Collinge, M.4    Fulton, D.5    Morales-Ruiz, M.6
  • 25
    • 80053445278 scopus 로고    scopus 로고
    • Elevated proteasome capacity extends replicative lifespan in Saccharomyces cerevisiae
    • Kruegel, U., Robison, B., Dange, T., Kahlert, G., Delaney, J. R., Kotireddy, S., et al. (2011). Elevated proteasome capacity extends replicative lifespan in Saccharomyces cerevisiae. PLoS Genet. 7:e1002253. doi: 10.1371/journal.pgen.1002253
    • (2011) PLoS Genet , vol.7
    • Kruegel, U.1    Robison, B.2    Dange, T.3    Kahlert, G.4    Delaney, J.R.5    Kotireddy, S.6
  • 26
    • 84894225988 scopus 로고    scopus 로고
    • Hepatic signaling by the mechanistic target of rapamycin complex 2 (mTORC2)
    • Lamming, D. W., Demirkan, G., Boylan, J. M., Mihaylova, M. M., Peng, T., Ferreira, J., et al. (2014). Hepatic signaling by the mechanistic target of rapamycin complex 2 (mTORC2). FASEB J. 28, 300-315. doi: 10.1096/fj.13-237743
    • (2014) FASEB J , vol.28 , pp. 300-315
    • Lamming, D.W.1    Demirkan, G.2    Boylan, J.M.3    Mihaylova, M.M.4    Peng, T.5    Ferreira, J.6
  • 27
    • 84880507764 scopus 로고    scopus 로고
    • Young and old genetically heterogeneous HET3 mice on a rapamycin diet are glucose intolerant but insulin sensitive
    • Lamming, D. W., Ye, L., Astle, C. M., Baur, J. A., Sabatini, D. M., and Harrison, D. E. (2013). Young and old genetically heterogeneous HET3 mice on a rapamycin diet are glucose intolerant but insulin sensitive. Aging Cell12, 712-718. doi: 10.1111/acel.12097
    • (2013) Aging Cell , vol.12 , pp. 712-718
    • Lamming, D.W.1    Ye, L.2    Astle, C.M.3    Baur, J.A.4    Sabatini, D.M.5    Harrison, D.E.6
  • 28
    • 33749069075 scopus 로고    scopus 로고
    • ATP Binding and ATP hydrolysis play distinct roles in the function of 26S Proteasome
    • Liu, C.-W., Li, X., Thompson, D., Wooding, K., Chang, T.-I., Tang, Z., et al. (2006). ATP Binding and ATP hydrolysis play distinct roles in the function of 26S Proteasome. Mol. Cell 24, 39-50. doi: 10.1016/j.molcel.2006.08.025
    • (2006) Mol. Cell , vol.24 , pp. 39-50
    • Liu, C.-W.1    Li, X.2    Thompson, D.3    Wooding, K.4    Chang, T.-I.5    Tang, Z.6
  • 29
    • 77952393003 scopus 로고    scopus 로고
    • Mechanisms governing the control of mRNA translation
    • Livingstone, M., Atas, E., Meller, A., and Sonenberg, N. (2010). Mechanisms governing the control of mRNA translation. Phys. Biol. 7:021001. doi: 10.1088/1478-3975/7/2/021001
    • (2010) Phys. Biol , vol.7
    • Livingstone, M.1    Atas, E.2    Meller, A.3    Sonenberg, N.4
  • 30
    • 33745154534 scopus 로고    scopus 로고
    • Autophagic defects in aging - Looking for an emergency exit?
    • Massey, A. C., Kiffin, R., and Cuervo, A. M. (2006). Autophagic defects in aging - Looking for an emergency exit?Cell Cycle 5, 1292-1296. doi: 10.4161/cc.5.12.2865
    • (2006) Cell Cycle , vol.5 , pp. 1292-1296
    • Massey, A.C.1    Kiffin, R.2    Cuervo, A.M.3
  • 31
    • 0031841818 scopus 로고    scopus 로고
    • Heat shock response and protein degradation: Regulation of HSF2 by the ubiquitin-proteasome pathway
    • Mathew, A., Mathur, S. K., and Morimoto, R. I. (1998). Heat shock response and protein degradation: regulation of HSF2 by the ubiquitin-proteasome pathway. Mol. Cell Biol. 18, 5091-5098.
    • (1998) Mol. Cell Biol , vol.18 , pp. 5091-5098
    • Mathew, A.1    Mathur, S.K.2    Morimoto, R.I.3
  • 32
    • 79951794971 scopus 로고    scopus 로고
    • Rapamycin, but not resveratrol or simvastatin, extends life span of genetically heterogeneous mice
    • Miller, R. A., Harrison, D. E., Astle, C. M., Baur, J. A., Boyd, A. R., De Cabo, R., et al. (2011). Rapamycin, but not resveratrol or simvastatin, extends life span of genetically heterogeneous mice. J. Gerontol. A Biol. Sci. Med. Sci. 66, 191-201. doi: 10.1093/gerona/glq178
    • (2011) J. Gerontol. A Biol. Sci. Med. Sci , vol.66 , pp. 191-201
    • Miller, R.A.1    Harrison, D.E.2    Astle, C.M.3    Baur, J.A.4    Boyd, A.R.5    De Cabo, R.6
  • 33
    • 84901403995 scopus 로고    scopus 로고
    • Rapamycin-mediated lifespan increase in mice is dose and sex dependent and metabolically distinct from dietary restriction
    • Miller, R. A., Harrison, D. E., Astle, C. M., Fernandez, E., Flurkey, K., Han, M., et al. (2014). Rapamycin-mediated lifespan increase in mice is dose and sex dependent and metabolically distinct from dietary restriction. Aging Cell13, 468-477. doi: 10.1111/acel.12194
    • (2014) Aging Cell , vol.13 , pp. 468-477
    • Miller, R.A.1    Harrison, D.E.2    Astle, C.M.3    Fernandez, E.4    Flurkey, K.5    Han, M.6
  • 34
    • 84903362402 scopus 로고    scopus 로고
    • Mammalian target of rapamycin hyperactivity mediates the detrimental effects of a high sucrose diet on Alzheimer's disease pathology
    • Orr, M. E., Salinas, A., Buffenstein, R., and Oddo, S. (2014). Mammalian target of rapamycin hyperactivity mediates the detrimental effects of a high sucrose diet on Alzheimer's disease pathology. Neurobiol. Aging 35, 1233-1242. doi: 10.1016/j.neurobiolaging.2013.12.006
    • (2014) Neurobiol. Aging , vol.35 , pp. 1233-1242
    • Orr, M.E.1    Salinas, A.2    Buffenstein, R.3    Oddo, S.4
  • 35
    • 84879105829 scopus 로고    scopus 로고
    • Rapamycin allosterically inhibits the proteasome
    • Osmulski, P. A., and Gaczynska, M. (2013). Rapamycin allosterically inhibits the proteasome. Mol. Pharmacol. 84, 104-113. doi: 10.1124/mol.112.083873
    • (2013) Mol. Pharmacol , vol.84 , pp. 104-113
    • Osmulski, P.A.1    Gaczynska, M.2
  • 36
    • 84874678862 scopus 로고    scopus 로고
    • Over-expression of heat shock factor 1 phenocopies the effect of chronic inhibition of TOR by rapamycin and is sufficient to ameliorate Alzheimer's-like deficits in mice modeling the disease
    • Pierce, A., Podlutskaya, N., Halloran, J. J., Hussong, S. A., Lin, P. Y., Burbank, R., et al. (2013). Over-expression of heat shock factor 1 phenocopies the effect of chronic inhibition of TOR by rapamycin and is sufficient to ameliorate Alzheimer's-like deficits in mice modeling the disease. J. Neurochem. 124, 880-893. doi: 10.1111/jnc.12080
    • (2013) J. Neurochem , vol.124 , pp. 880-893
    • Pierce, A.1    Podlutskaya, N.2    Halloran, J.J.3    Hussong, S.A.4    Lin, P.Y.5    Burbank, R.6
  • 37
    • 78049280231 scopus 로고    scopus 로고
    • A Novel mouse model of enhanced proteostasis: Full-length human heat shock factor 1 transgenic mice
    • Pierce, A., Wei, R., Halade, D., Yoo, S. E., Ran, Q., and Richardson, A. (2010). A Novel mouse model of enhanced proteostasis: full-length human heat shock factor 1 transgenic mice. Biochem. Biophys. Res. Commun. 402, 59-65. doi: 10.1016/j.bbrc.2010.09.111
    • (2010) Biochem. Biophys. Res. Commun , vol.402 , pp. 59-65
    • Pierce, A.1    Wei, R.2    Halade, D.3    Yoo, S.E.4    Ran, Q.5    Richardson, A.6
  • 38
    • 84893092734 scopus 로고    scopus 로고
    • The pros and the cons of mTOR inhibitors in kidney transplantation
    • Ponticelli, C. (2014). The pros and the cons of mTOR inhibitors in kidney transplantation. Exp. Rev. Clin. Immunol. 10, 295-305. doi: 10.1586/1744666X.2014.872562
    • (2014) Exp. Rev. Clin. Immunol , vol.10 , pp. 295-305
    • Ponticelli, C.1
  • 39
    • 77950366349 scopus 로고    scopus 로고
    • Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells
    • Radhakrishnan, S. K., Lee, C. S., Young, P., Beskow, A., Chan, J. Y., and Deshaies, R. J. (2010). Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells. Mol. Cell 38, 17-28. doi: 10.1016/j.molcel.2010.02.029
    • (2010) Mol. Cell , vol.38 , pp. 17-28
    • Radhakrishnan, S.K.1    Lee, C.S.2    Young, P.3    Beskow, A.4    Chan, J.Y.5    Deshaies, R.J.6
  • 40
    • 84860431090 scopus 로고    scopus 로고
    • Altered composition of liver proteasome assemblies contributes to enhanced proteasome activity in the exceptionally long-lived naked mole-rat
    • Rodriguez, K. A., Edrey, Y. H., Osmulski, P., Gaczynska, M., and Buffenstein, R. (2012). Altered composition of liver proteasome assemblies contributes to enhanced proteasome activity in the exceptionally long-lived naked mole-rat. PLoS ONE 7:e35890. doi: 10.1371/journal.pone.0035890
    • (2012) PLoS ONE , vol.7
    • Rodriguez, K.A.1    Edrey, Y.H.2    Osmulski, P.3    Gaczynska, M.4    Buffenstein, R.5
  • 41
    • 77249166017 scopus 로고    scopus 로고
    • Molecular mechanisms of proteasome plasticity in aging
    • Rodriguez, K. A., Gaczynska, M., and Osmulski, P. A. (2010). Molecular mechanisms of proteasome plasticity in aging. Mech. Ageing Dev. 131, 144-155. doi: 10.1016/j.mad.2010.01.002
    • (2010) Mech. Ageing Dev , vol.131 , pp. 144-155
    • Rodriguez, K.A.1    Gaczynska, M.2    Osmulski, P.A.3
  • 42
    • 84907986019 scopus 로고    scopus 로고
    • A cytosolic protein factor from the naked mole-rat activates proteasomes of other species and protects these from inhibition
    • Rodriguez, K. A., Osmulski, P., Pierce, A., Weintraub, S. T., Gaczynska, M., and Buffenstein, R. (2014). A cytosolic protein factor from the naked mole-rat activates proteasomes of other species and protects these from inhibition.Biochim. Biophys. Acta. 1842, 2060-2072. doi: 10.1016/j.bbadis.2014.07.005
    • (2014) Biochim. Biophys. Acta , vol.1842 , pp. 2060-2072
    • Rodriguez, K.A.1    Osmulski, P.2    Pierce, A.3    Weintraub, S.T.4    Gaczynska, M.5    Buffenstein, R.6
  • 43
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C. A., and Poirier, M. A. (2004). Protein aggregation and neurodegenerative disease. Nat. Med. 10(Suppl.). S10-S17. doi: 10.1038/nm1066
    • (2004) Nat. Med , vol.10 , pp. S10-S17
    • Ross, C.A.1    Poirier, M.A.2
  • 44
    • 79957684292 scopus 로고    scopus 로고
    • CHIP E3 ligase regulates mammalian senescence by modulating the levels of oxidized proteins
    • Sisoula, C., and Gonos, E. S. (2011). CHIP E3 ligase regulates mammalian senescence by modulating the levels of oxidized proteins. Mech. Ageing Dev. 132, 269-272. doi: 10.1016/j.mad.2011.04.003
    • (2011) Mech. Ageing Dev , vol.132 , pp. 269-272
    • Sisoula, C.1    Gonos, E.S.2
  • 45
    • 79951707743 scopus 로고    scopus 로고
    • ATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycle
    • Smith, D. M., Fraga, H., Reis, C., Kafri, G., and Goldberg, A. L. (2011). ATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycle. Cell 144, 526-538. doi: 10.1016/j.cell.2011.02.005
    • (2011) Cell , vol.144 , pp. 526-538
    • Smith, D.M.1    Fraga, H.2    Reis, C.3    Kafri, G.4    Goldberg, A.L.5
  • 46
    • 77956305343 scopus 로고    scopus 로고
    • Inhibition of mTOR by rapamycin abolishes cognitive deficits and reduces amyloid-beta levels in a mouse model of Alzheimer's disease
    • Spilman, P., Podlutskaya, N., Hart, M. J., Debnath, J., Gorostiza, O., Bredesen, D., et al. (2010). Inhibition of mTOR by rapamycin abolishes cognitive deficits and reduces amyloid-beta levels in a mouse model of Alzheimer's disease.PLoS ONE 5:e9979. doi: 10.1371/journal.pone.0009979
    • (2010) PLoS ONE , vol.5
    • Spilman, P.1    Podlutskaya, N.2    Hart, M.J.3    Debnath, J.4    Gorostiza, O.5    Bredesen, D.6
  • 47
    • 23844438209 scopus 로고    scopus 로고
    • Activation of Akt and eIF4E survival pathways by rapamycin-mediated mammalian target of rapamycin inhibition
    • Sun, S. Y., Rosenberg, L. M., Wang, X., Zhou, Z., Yue, P., Fu, H., et al. (2005). Activation of Akt and eIF4E survival pathways by rapamycin-mediated mammalian target of rapamycin inhibition. Cancer Res. 65, 7052-7058. doi: 10.1158/0008-5472.CAN-05-0917
    • (2005) Cancer Res , vol.65 , pp. 7052-7058
    • Sun, S.Y.1    Rosenberg, L.M.2    Wang, X.3    Zhou, Z.4    Yue, P.5    Fu, H.6
  • 48
    • 0000085132 scopus 로고    scopus 로고
    • Insulin-induced insulin receptor substrate-1 degradation is mediated by the proteasome degradation pathway
    • Sun, X. J., Goldberg, J. L., Qiao, L. Y., and Mitchell, J. J. (1999). Insulin-induced insulin receptor substrate-1 degradation is mediated by the proteasome degradation pathway. Diabetes 48, 1359-1364. doi: 10.2337/diabetes.48.7.1359
    • (1999) Diabetes , vol.48 , pp. 1359-1364
    • Sun, X.J.1    Goldberg, J.L.2    Qiao, L.Y.3    Mitchell, J.J.4
  • 49
    • 77953467032 scopus 로고    scopus 로고
    • Characterization of the brain 26S Proteasome and its interacting proteins
    • Tai, H. C., Besche, H., Goldberg, A. L., and Schuman, E. M. (2010). Characterization of the brain 26S Proteasome and its interacting proteins. Front. Mol. Neurosci. 3:12. doi: 10.3389/fnmol.2010.00012
    • (2010) Front. Mol. Neurosci , vol.3 , pp. 12
    • Tai, H.C.1    Besche, H.2    Goldberg, A.L.3    Schuman, E.M.4
  • 50
    • 84860527756 scopus 로고    scopus 로고
    • A unifying model for mTORC1-mediated regulation of mRNA translation
    • Thoreen, C. C., Chantranupong, L., Keys, H. R., Wang, T., Gray, N. S., and Sabatini, D. M. (2012). A unifying model for mTORC1-mediated regulation of mRNA translation. Nature 485, 109-113. doi: 10.1038/nature11083
    • (2012) Nature , vol.485 , pp. 109-113
    • Thoreen, C.C.1    Chantranupong, L.2    Keys, H.R.3    Wang, T.4    Gray, N.S.5    Sabatini, D.M.6
  • 51
    • 84903958633 scopus 로고    scopus 로고
    • Liver damage, inflammation, and enhanced tumorigenesis after persistent mTORC1 inhibition
    • Umemura, A., Park, E. J., Taniguchi, K., Lee, J. H., Shalapour, S., Valasek, M. A., et al. (2014). Liver damage, inflammation, and enhanced tumorigenesis after persistent mTORC1 inhibition. Cell Metab. 20, 133-144. doi: 10.1016/j.cmet.2014.05.001
    • (2014) Cell Metab , vol.20 , pp. 133-144
    • Umemura, A.1    Park, E.J.2    Taniguchi, K.3    Lee, J.H.4    Shalapour, S.5    Valasek, M.A.6
  • 52
    • 34548479261 scopus 로고    scopus 로고
    • Aging perturbs 26S proteasome assembly in Drosophila melanogaster
    • Vernace, V. A., Arnaud, L., Schmidt-Glenewinkel, T., and Figueiredo-Pereira, M. E. (2007). Aging perturbs 26S proteasome assembly in Drosophila melanogaster. FASEB J. 21, 2672-2682. doi: 10.1096/fj.06-6751com
    • (2007) FASEB J , vol.21 , pp. 2672-2682
    • Vernace, V.A.1    Arnaud, L.2    Schmidt-Glenewinkel, T.3    Figueiredo-Pereira, M.E.4
  • 53
    • 33947538050 scopus 로고    scopus 로고
    • Rapamycin induces feedback activation of Akt signaling through an IGF-1R-dependent mechanism
    • Wan, X., Harkavy, B., Shen, N., Grohar, P., and Helman, L. J. (2007). Rapamycin induces feedback activation of Akt signaling through an IGF-1R-dependent mechanism. Oncogene 26, 1932-1940. doi: 10.1038/sj.onc.1209990
    • (2007) Oncogene , vol.26 , pp. 1932-1940
    • Wan, X.1    Harkavy, B.2    Shen, N.3    Grohar, P.4    Helman, L.J.5
  • 55
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger, S., Loewith, R., and Hall, M. N. (2006). TOR signaling in growth and metabolism. Cell 124, 471-484. doi: 10.1016/j.cell.2006.01.016
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 56
    • 0034800371 scopus 로고    scopus 로고
    • Principal component analysis for clustering gene expression data
    • Yeung, K. Y., and Ruzzo, W. L. (2001). Principal component analysis for clustering gene expression data.Bioinformatics 17, 763-774. doi: 10.1093/bioinformatics/17.9.763
    • (2001) Bioinformatics , vol.17 , pp. 763-774
    • Yeung, K.Y.1    Ruzzo, W.L.2
  • 57
    • 33749573178 scopus 로고    scopus 로고
    • Cytotoxic synergy between the multikinase inhibitor sorafenib and the proteasome inhibitor bortezomib in vitro: Induction of apoptosis through Akt and c-Jun NH2-terminal kinase pathways
    • Yu, C., Friday, B. B., Lai, J. P., Yang, L., Sarkaria, J., Kay, N. E., et al. (2006). Cytotoxic synergy between the multikinase inhibitor sorafenib and the proteasome inhibitor bortezomib in vitro: induction of apoptosis through Akt and c-Jun NH2-terminal kinase pathways. Mol. Cancer Ther. 5, 2378-2387. doi: 10.1158/1535-7163.MCT-06-0235
    • (2006) Mol. Cancer Ther , vol.5 , pp. 2378-2387
    • Yu, C.1    Friday, B.B.2    Lai, J.P.3    Yang, L.4    Sarkaria, J.5    Kay, N.E.6
  • 58
    • 84926672210 scopus 로고    scopus 로고
    • Rapamycin and dietary restriction induce metabolically distinctive changes in mouse liver
    • [Epub ahead of print]
    • Yu, Z., Wang, R., Fok, W. C., Coles, A., Salmon, A. B., and Perez, V. I. (2014). Rapamycin and dietary restriction induce metabolically distinctive changes in mouse liver. J. Gerontol. A Biol. Sci. Med. Sci. doi: 10.1093/gerona/glu053. [Epub ahead of print].
    • (2014) J. Gerontol. A Biol. Sci. Med. Sci
    • Yu, Z.1    Wang, R.2    Fok, W.C.3    Coles, A.4    Salmon, A.B.5    Perez, V.I.6
  • 59
    • 84875539389 scopus 로고    scopus 로고
    • Proteasome inhibitor MG132 induces selective apoptosis in glioblastoma cells through inhibition of PI3K/Akt and NFkappaB pathways, mitochondrial dysfunction, and activation of p38-JNK1/2 signaling
    • Zanotto-Filho, A., Braganhol, E., Battastini, A. M., and Moreira, J. C. (2012). Proteasome inhibitor MG132 induces selective apoptosis in glioblastoma cells through inhibition of PI3K/Akt and NFkappaB pathways, mitochondrial dysfunction, and activation of p38-JNK1/2 signaling. Invest. New Drugs 30, 2252-2262. doi: 10.1007/s10637-012-9804-z
    • (2012) Invest. New Drugs , vol.30 , pp. 2252-2262
    • Zanotto-Filho, A.1    Braganhol, E.2    Battastini, A.M.3    Moreira, J.C.4
  • 61


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