메뉴 건너뛰기




Volumn 11, Issue APR, 2017, Pages

Protein quality control by molecular chaperones in neurodegeneration

Author keywords

Autophagy lysosome system; Chaperon mediated autophagy; Macroautophagy; Protein aggregation; Protein quality control; Proteolysis; Ubiquitin proteasome system

Indexed keywords

CELASTROL; CHAPERONE; CHAPERONIN 60; DEUBIQUITINASE; GELDANAMYCIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HUNTINGTIN; POLYGLUTAMINE; PROTEIN DNAJ; SEQUESTOSOME 1; TANESPIMYCIN; UBIQUITIN PROTEIN LIGASE;

EID: 85018401049     PISSN: 16624548     EISSN: 1662453X     Source Type: Journal    
DOI: 10.3389/fnins.2017.00185     Document Type: Review
Times cited : (237)

References (262)
  • 1
    • 0034914206 scopus 로고    scopus 로고
    • A molecular chaperone complex at the lysosomal membrane is required for protein translocation
    • Agarraberes, F. A., and Dice, J. F. (2001). A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J. Cell Sci. 114(Pt 13), 2491-2499
    • (2001) J. Cell Sci , vol.114 , pp. 2491-2499
    • Agarraberes, F.A.1    Dice, J.F.2
  • 2
    • 0030923854 scopus 로고    scopus 로고
    • An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation
    • Agarraberes, F. A., Terlecky, S. R., and Dice, J. F. (1997). An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. J. Cell Biol. 137, 825-834
    • (1997) J. Cell Biol , vol.137 , pp. 825-834
    • Agarraberes, F.A.1    Terlecky, S.R.2    Dice, J.F.3
  • 3
    • 0344443774 scopus 로고    scopus 로고
    • BAG-1-a nucleotide exchange factor of Hsc70 with multiple cellular functions
    • Alberti, S., Esser, C., and Hohfeld, J. (2003). BAG-1-a nucleotide exchange factor of Hsc70 with multiple cellular functions. Cell Stress Chaperones 8, 225-231
    • (2003) Cell Stress Chaperones , vol.8 , pp. 225-231
    • Alberti, S.1    Esser, C.2    Hohfeld, J.3
  • 4
    • 33748741301 scopus 로고    scopus 로고
    • CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation
    • Al-Ramahi, I., Lam, Y. C., Chen, H. K., de Gouyon, B., Zhang, M., Perez, A. M., et al. (2006). CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation. J. Biol. Chem. 281, 26714-26724. doi: 10.1074/jbc.M601603200
    • (2006) J. Biol. Chem , vol.281 , pp. 26714-26724
    • Al-Ramahi, I.1    Lam, Y.C.2    Chen, H.K.3    de Gouyon, B.4    Zhang, M.5    Perez, A.M.6
  • 5
    • 39149083699 scopus 로고    scopus 로고
    • The activity of hsp90a promoter is regulated by NF-ß B transcription factors
    • Ammirante, M., Rosati, A., Gentilella, A., Festa, M., Petrella, A., Marzullo, L., et al. (2008). The activity of hsp90a promoter is regulated by NF-ß B transcription factors. Oncogene 27, 1175-1178. doi: 10.1038/sj.onc.1210716
    • (2008) Oncogene , vol.27 , pp. 1175-1178
    • Ammirante, M.1    Rosati, A.2    Gentilella, A.3    Festa, M.4    Petrella, A.5    Marzullo, L.6
  • 6
    • 33646573377 scopus 로고    scopus 로고
    • Impaired neurogenesis and cardiovascular development in mice lacking the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway
    • An, J. Y., Seo, J. W., Tasaki, T., Lee, M. J., Varshavsky, A., and Kwon, Y. T. (2006). Impaired neurogenesis and cardiovascular development in mice lacking the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway. Proc. Natl. Acad. Sci. U.S.A. 103, 6212-6217. doi: 10.1073/pnas.0601700103
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 6212-6217
    • An, J.Y.1    Seo, J.W.2    Tasaki, T.3    Lee, M.J.4    Varshavsky, A.5    Kwon, Y.T.6
  • 7
    • 84857213897 scopus 로고    scopus 로고
    • Misfolded PrP and a novel mechanism of proteasome inhibition
    • Andre, R., and Tabrizi, S. J. (2012). Misfolded PrP and a novel mechanism of proteasome inhibition. Prion 6, 32-36. doi: 10.4161/pri.6.1.18272
    • (2012) Prion , vol.6 , pp. 32-36
    • Andre, R.1    Tabrizi, S.J.2
  • 8
    • 56949083650 scopus 로고    scopus 로고
    • Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Aß fibrils and protofibrils
    • Arimon, M., Grimminger, V., Sanz, F., and Lashuel, H. A. (2008). Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Aß fibrils and protofibrils. J. Mol. Biol. 384, 1157-1173. doi: 10.1016/j.jmb.2008.09.063
    • (2008) J. Mol. Biol , vol.384 , pp. 1157-1173
    • Arimon, M.1    Grimminger, V.2    Sanz, F.3    Lashuel, H.A.4
  • 10
    • 0036852712 scopus 로고    scopus 로고
    • Pharmacological prevention of Parkinson disease in Drosophila
    • Auluck, P. K., and Bonini, N. M. (2002). Pharmacological prevention of Parkinson disease in Drosophila. Nat. Med. 8, 1185-1186. doi: 10.1038/nm1102-1185
    • (2002) Nat. Med , vol.8 , pp. 1185-1186
    • Auluck, P.K.1    Bonini, N.M.2
  • 11
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., Finley, D., and Varshavsky, A. (1986). In vivo half-life of a protein is a function of its amino-terminal residue. Science 234, 179-186
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 12
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger, C. A., Connell, P., Wu, Y., Hu, Z., Thompson, L. J., Yin, L. Y., et al. (1999). Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol. Cell. Biol. 19, 4535-4545
    • (1999) Mol. Cell. Biol , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6
  • 13
    • 0033793995 scopus 로고    scopus 로고
    • Varying intertrial interval reveals temporally defined memory deficits and enhancements in NTAN1-deficient mice
    • Balogh, S. A., Kwon, Y. T., and Denenberg, V. H. (2000). Varying intertrial interval reveals temporally defined memory deficits and enhancements in NTAN1-deficient mice. Learn. Mem. 7, 279-286. doi: 10.1101/lm.33500
    • (2000) Learn. Mem , vol.7 , pp. 279-286
    • Balogh, S.A.1    Kwon, Y.T.2    Denenberg, V.H.3
  • 14
    • 0035936959 scopus 로고    scopus 로고
    • Facilitated stimulus-response associative learning and long-term memory in mice lacking the NTAN1 amidase of the N-end rule pathway
    • Balogh, S. A., McDowell, C. S., Kwon, Y. T., and Denenberg, V. H. (2001). Facilitated stimulus-response associative learning and long-term memory in mice lacking the NTAN1 amidase of the N-end rule pathway. Brain Res. 892, 336-343. doi: 10.1016/S0006-8993(00)03268-6
    • (2001) Brain Res , vol.892 , pp. 336-343
    • Balogh, S.A.1    McDowell, C.S.2    Kwon, Y.T.3    Denenberg, V.H.4
  • 15
    • 51349130544 scopus 로고    scopus 로고
    • The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane
    • Bandyopadhyay, U., Kaushik, S., Varticovski, L., and Cuervo, A. M. (2008). The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol. Cell. Biol. 28, 5747-5763. doi: 10.1128/MCB.02070-07
    • (2008) Mol. Cell. Biol , vol.28 , pp. 5747-5763
    • Bandyopadhyay, U.1    Kaushik, S.2    Varticovski, L.3    Cuervo, A.M.4
  • 16
    • 33749989045 scopus 로고    scopus 로고
    • Induction of multiple heat shock proteins and neuroprotection in a primary culture model of familial amyotrophic lateral sclerosis
    • Batulan, Z., Taylor, D. M., Aarons, R. J., Minotti, S., Doroudchi, M. M., Nalbantoglu, J., et al. (2006). Induction of multiple heat shock proteins and neuroprotection in a primary culture model of familial amyotrophic lateral sclerosis. Neurobiol. Dis. 24, 213-225. doi: 10.1016/j.nbd.2006.06.017
    • (2006) Neurobiol. Dis , vol.24 , pp. 213-225
    • Batulan, Z.1    Taylor, D.M.2    Aarons, R.J.3    Minotti, S.4    Doroudchi, M.M.5    Nalbantoglu, J.6
  • 17
    • 77749319356 scopus 로고    scopus 로고
    • Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein
    • Bauer, P. O., Goswami, A., Wong, H. K., Okuno, M., Kurosawa, M., Yamada, M., et al. (2010). Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein. Nat. Biotechnol. 28, 256-263. doi: 10.1038/nbt.1608
    • (2010) Nat. Biotechnol , vol.28 , pp. 256-263
    • Bauer, P.O.1    Goswami, A.2    Wong, H.K.3    Okuno, M.4    Kurosawa, M.5    Yamada, M.6
  • 18
    • 33748561495 scopus 로고    scopus 로고
    • Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers
    • Behrends, C., Langer, C. A., Boteva, R., Bottcher, U. M., Stemp, M. J., Schaffar, G., et al. (2006). Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers. Mol. Cell 23, 887-897. doi: 10.1016/j.molcel.2006.08.017
    • (2006) Mol. Cell , vol.23 , pp. 887-897
    • Behrends, C.1    Langer, C.A.2    Boteva, R.3    Bottcher, U.M.4    Stemp, M.J.5    Schaffar, G.6
  • 19
    • 77957169824 scopus 로고    scopus 로고
    • Role of a ribosome-associated E3 ubiquitin ligase in protein quality control
    • Bengtson, M. H., and Joazeiro, C. A. (2010). Role of a ribosome-associated E3 ubiquitin ligase in protein quality control. Nature 467, 470-473. doi: 10.1038/nature09371
    • (2010) Nature , vol.467 , pp. 470-473
    • Bengtson, M.H.1    Joazeiro, C.A.2
  • 20
    • 0031004769 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70
    • Bercovich, B., Stancovski, I., Mayer, A., Blumenfeld, N., Laszlo, A., Schwartz, A. L., et al. (1997). Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70. J. Biol. Chem. 272, 9002-9010
    • (1997) J. Biol. Chem , vol.272 , pp. 9002-9010
    • Bercovich, B.1    Stancovski, I.2    Mayer, A.3    Blumenfeld, N.4    Laszlo, A.5    Schwartz, A.L.6
  • 21
    • 49049096562 scopus 로고    scopus 로고
    • Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease
    • Boland, B., Kumar, A., Lee, S., Platt, F. M., Wegiel, J., Yu, W. H., et al. (2008). Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease. J. Neurosci. 28, 6926-6937. doi: 10.1523/JNEUROSCI.0800-08.2008
    • (2008) J. Neurosci , vol.28 , pp. 6926-6937
    • Boland, B.1    Kumar, A.2    Lee, S.3    Platt, F.M.4    Wegiel, J.5    Yu, W.H.6
  • 22
    • 79951761390 scopus 로고    scopus 로고
    • The culprit behind amyloid ß peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation?
    • Broersen, K., Rousseau, F., and Schymkowitz, J. (2010). The culprit behind amyloid ß peptide related neurotoxicity in Alzheimer's disease: oligomer size or conformation? Alzheimers. Res. Ther. 2:12. doi: 10.1186/alzrt36
    • (2010) Alzheimers. Res. Ther , vol.2 , pp. 12
    • Broersen, K.1    Rousseau, F.2    Schymkowitz, J.3
  • 23
    • 84876832401 scopus 로고    scopus 로고
    • Neurodegeneration-associated protein fragments as short-lived substrates of the N-end rule pathway
    • Brower, C. S., Piatkov, K. I., and Varshavsky, A. (2013). Neurodegeneration-associated protein fragments as short-lived substrates of the N-end rule pathway. Mol. Cell 50, 161-171. doi: 10.1016/j.molcel.2013.02.009
    • (2013) Mol. Cell , vol.50 , pp. 161-171
    • Brower, C.S.1    Piatkov, K.I.2    Varshavsky, A.3
  • 25
    • 0030027968 scopus 로고    scopus 로고
    • Supervising the fold: functional principles of molecular chaperones
    • Buchner, J. (1996). Supervising the fold: functional principles of molecular chaperones. FASEB J. 10, 10-19
    • (1996) FASEB J , vol.10 , pp. 10-19
    • Buchner, J.1
  • 26
    • 84944622121 scopus 로고    scopus 로고
    • Chaperone-dependent Neurodegeneration: a Molecular Perspective on Therapeutic Intervention
    • Carman, A., Kishinevsky, S., Koren, J. III., Lou, W., and Chiosis, G. (2013). Chaperone-dependent Neurodegeneration: a Molecular Perspective on Therapeutic Intervention. J. Alzheimers Dis. Parkinson. 2013(Suppl 10):007. doi: 10.4172/2161-0460.S10-007
    • (2013) J. Alzheimers Dis. Parkinson , vol.2013 , pp. 007
    • Carman, A.1    Kishinevsky, S.2    Koren, J.3    Lou, W.4    Chiosis, G.5
  • 27
    • 84860668972 scopus 로고    scopus 로고
    • Alteration of protein folding and degradation in motor neuron diseases: implications and protective functions of small heat shock proteins
    • Carra, S., Crippa, V., Rusmini, P., Boncoraglio, A., Minoia, M., Giorgetti, E., et al. (2012). Alteration of protein folding and degradation in motor neuron diseases: implications and protective functions of small heat shock proteins. Prog. Neurobiol. 97, 83-100. doi: 10.1016/j.pneurobio.2011.09.009
    • (2012) Prog. Neurobiol , vol.97 , pp. 83-100
    • Carra, S.1    Crippa, V.2    Rusmini, P.3    Boncoraglio, A.4    Minoia, M.5    Giorgetti, E.6
  • 28
    • 84899854286 scopus 로고    scopus 로고
    • Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation
    • Carroni, M., Kummer, E., Oguchi, Y., Wendler, P., Clare, D. K., Sinning, I., et al. (2014). Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. Elife 3:e02481. doi: 10.7554/eLife.02481
    • (2014) Elife , vol.3
    • Carroni, M.1    Kummer, E.2    Oguchi, Y.3    Wendler, P.4    Clare, D.K.5    Sinning, I.6
  • 29
    • 84934298725 scopus 로고    scopus 로고
    • Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding
    • Cha-Molstad, H., Sung, K. S., Hwang, J., Kim, K. A., Yu, J. E., Yoo, Y. D., et al. (2015). Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding. Nat. Cell Biol. 17, 917-929. doi: 10.1038/ncb3177
    • (2015) Nat. Cell Biol , vol.17 , pp. 917-929
    • Cha-Molstad, H.1    Sung, K.S.2    Hwang, J.3    Kim, K.A.4    Yu, J.E.5    Yoo, Y.D.6
  • 30
    • 0026696593 scopus 로고
    • Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons
    • Cheetham, M. E., Brion, J. P., and Anderton, B. H. (1992). Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons. Biochem. J. 284(Pt 2), 469-476
    • (1992) Biochem. J , vol.284 , pp. 469-476
    • Cheetham, M.E.1    Brion, J.P.2    Anderton, B.H.3
  • 31
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function
    • Cheetham, M. E., and Caplan, A. J. (1998). Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones 3, 28-36
    • (1998) Cell Stress Chaperones , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 32
    • 84893639934 scopus 로고    scopus 로고
    • Hsp90 chaperone inhibitor 17-AAG attenuates Aß-induced synaptic toxicity and memory impairment
    • Chen, Y., Wang, B., Liu, D., Li, J. J., Xue, Y., Sakata, K., et al. (2014). Hsp90 chaperone inhibitor 17-AAG attenuates Aß-induced synaptic toxicity and memory impairment. J. Neurosci. 34, 2464-2470. doi: 10.1523/JNEUROSCI.0151-13.2014
    • (2014) J. Neurosci , vol.34 , pp. 2464-2470
    • Chen, Y.1    Wang, B.2    Liu, D.3    Li, J.J.4    Xue, Y.5    Sakata, K.6
  • 33
    • 0023891846 scopus 로고
    • Peptide sequences that target proteins for enhanced degradation during serum withdrawal
    • Chiang, H. L., and Dice, J. F. (1988). Peptide sequences that target proteins for enhanced degradation during serum withdrawal. J. Biol. Chem. 263, 6797-6805
    • (1988) J. Biol. Chem , vol.263 , pp. 6797-6805
    • Chiang, H.L.1    Dice, J.F.2
  • 34
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang, H. L., Terlecky, S. R., Plant, C. P., and Dice, J. F. (1989). A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 246, 382-385
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.L.1    Terlecky, S.R.2    Plant, C.P.3    Dice, J.F.4
  • 35
    • 3543141113 scopus 로고    scopus 로고
    • Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release
    • Choo, Y. S., Johnson, G. V., MacDonald, M., Detloff, P. J., and Lesort, M. (2004). Mutant huntingtin directly increases susceptibility of mitochondria to the calcium-induced permeability transition and cytochrome c release. Hum. Mol. Genet. 13, 1407-1420. doi: 10.1093/hmg/ddh162
    • (2004) Hum. Mol. Genet , vol.13 , pp. 1407-1420
    • Choo, Y.S.1    Johnson, G.V.2    MacDonald, M.3    Detloff, P.J.4    Lesort, M.5
  • 36
    • 84908463972 scopus 로고    scopus 로고
    • Genetics of Alzheimer's disease
    • Chouraki, V., and Seshadri, S. (2014). Genetics of Alzheimer's disease. Adv. Genet. 87, 245-294. doi: 10.1016/B978-0-12-800149-3.00005-6
    • (2014) Adv. Genet , vol.87 , pp. 245-294
    • Chouraki, V.1    Seshadri, S.2
  • 37
    • 84878231850 scopus 로고    scopus 로고
    • Intracellular protein degradation: from a vague idea through the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting
    • Ciechanover, A. (2013). Intracellular protein degradation: from a vague idea through the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Bioorg. Med. Chem. 21, 3400-3410. doi: 10.1016/j.bmc.2013.01.056
    • (2013) Bioorg. Med. Chem , vol.21 , pp. 3400-3410
    • Ciechanover, A.1
  • 38
    • 84989284335 scopus 로고    scopus 로고
    • Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies
    • Ciechanover, A., and Kwon, Y. T. (2015). Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies. Exp. Mol. Med. 47:e147. doi: 10.1038/emm.2014.117
    • (2015) Exp. Mol. Med , vol.47
    • Ciechanover, A.1    Kwon, Y.T.2
  • 39
    • 0029551271 scopus 로고
    • The ubiquitin-mediated proteolytic system: involvement of molecular chaperones, degradation of oncoproteins, and activation of transcriptional regulators
    • Ciechanover, A., Laszlo, A., Bercovich, B., Stancovski, I., Alkalay, I., Ben-Neriah, Y., et al. (1995). The ubiquitin-mediated proteolytic system: involvement of molecular chaperones, degradation of oncoproteins, and activation of transcriptional regulators. Cold Spring Harb. Symp. Quant. Biol. 60, 491-501
    • (1995) Cold Spring Harb. Symp. Quant. Biol , vol.60 , pp. 491-501
    • Ciechanover, A.1    Laszlo, A.2    Bercovich, B.3    Stancovski, I.4    Alkalay, I.5    Ben-Neriah, Y.6
  • 40
    • 23844529468 scopus 로고    scopus 로고
    • Celastrol protects against MPTP-and 3-nitropropionic acid-induced neurotoxicity
    • Cleren, C., Calingasan, N. Y., Chen, J., and Beal, M. F. (2005). Celastrol protects against MPTP-and 3-nitropropionic acid-induced neurotoxicity. J. Neurochem. 94, 995-1004. doi: 10.1111/j.1471-4159.2005.03253.x
    • (2005) J. Neurochem , vol.94 , pp. 995-1004
    • Cleren, C.1    Calingasan, N.Y.2    Chen, J.3    Beal, M.F.4
  • 41
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • Connell, P., Ballinger, C. A., Jiang, J., Wu, Y., Thompson, L. J., Hohfeld, J., et al. (2001). The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat. Cell Biol. 3, 93-96. doi: 10.1038/35050618
    • (2001) Nat. Cell Biol , vol.3 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Jiang, J.3    Wu, Y.4    Thompson, L.J.5    Hohfeld, J.6
  • 42
    • 33845600006 scopus 로고    scopus 로고
    • Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities
    • Crosas, B., Hanna, J., Kirkpatrick, D. S., Zhang, D. P., Tone, Y., Hathaway, N. A., et al. (2006). Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Cell 127, 1401-1413. doi: 10.1016/j.cell.2006.09.051
    • (2006) Cell , vol.127 , pp. 1401-1413
    • Crosas, B.1    Hanna, J.2    Kirkpatrick, D.S.3    Zhang, D.P.4    Tone, Y.5    Hathaway, N.A.6
  • 43
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo, A. M., and Dice, J. F. (1996). A receptor for the selective uptake and degradation of proteins by lysosomes. Science 273, 501-503
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 44
    • 0034232418 scopus 로고    scopus 로고
    • Regulation of lamp2a levels in the lysosomal membrane
    • Cuervo, A. M., and Dice, J. F. (2000). Regulation of lamp2a levels in the lysosomal membrane. Traffic 1, 570-583. doi: 10.1034/j.1600-0854.2000.010707.x
    • (2000) Traffic , vol.1 , pp. 570-583
    • Cuervo, A.M.1    Dice, J.F.2
  • 45
    • 0031041902 scopus 로고    scopus 로고
    • A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins
    • Cuervo, A. M., Dice, J. F., and Knecht, E. (1997). A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins. J. Biol. Chem. 272, 5606-5615
    • (1997) J. Biol. Chem , vol.272 , pp. 5606-5615
    • Cuervo, A.M.1    Dice, J.F.2    Knecht, E.3
  • 46
    • 0028848119 scopus 로고
    • Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation
    • Cuervo, A. M., Knecht, E., Terlecky, S. R., and Dice, J. F. (1995). Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation. Am. J. Physiol. 269(5 Pt 1), C1200-C1208
    • (1995) Am. J. Physiol , vol.269 , Issue.5 , pp. C1200-C1208
    • Cuervo, A.M.1    Knecht, E.2    Terlecky, S.R.3    Dice, J.F.4
  • 47
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant a-synuclein by chaperone-mediated autophagy
    • Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., and Sulzer, D. (2004). Impaired degradation of mutant a-synuclein by chaperone-mediated autophagy. Science 305, 1292-1295. doi: 10.1126/science.1101738
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 48
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • Cyr, D. M., Hohfeld, J., and Patterson, C. (2002). Protein quality control: U-box-containing E3 ubiquitin ligases join the fold. Trends Biochem. Sci. 27, 368-375. doi: 10.1016/S0968-0004(02)02125-4
    • (2002) Trends Biochem. Sci , vol.27 , pp. 368-375
    • Cyr, D.M.1    Hohfeld, J.2    Patterson, C.3
  • 49
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: the versatile helix
    • D'Andrea, L. D., and Regan, L. (2003). TPR proteins: the versatile helix. Trends Biochem. Sci. 28, 655-662. doi: 10.1016/j.tibs.2003.10.007
    • (2003) Trends Biochem. Sci , vol.28 , pp. 655-662
    • D'Andrea, L.D.1    Regan, L.2
  • 50
    • 72949105329 scopus 로고    scopus 로고
    • Stressing the ubiquitin-proteasome system
    • Dantuma, N. P., and Lindsten, K. (2010). Stressing the ubiquitin-proteasome system. Cardiovasc. Res. 85, 263-271. doi: 10.1093/cvr/cvp255
    • (2010) Cardiovasc. Res , vol.85 , pp. 263-271
    • Dantuma, N.P.1    Lindsten, K.2
  • 51
    • 79251565507 scopus 로고    scopus 로고
    • Heat-shock protein 70 modulates toxic extracellular a-synuclein oligomers and rescues trans-synaptic toxicity
    • Danzer, K. M., Ruf, W. P., Putcha, P., Joyner, D., Hashimoto, T., Glabe, C., et al. (2011). Heat-shock protein 70 modulates toxic extracellular a-synuclein oligomers and rescues trans-synaptic toxicity. FASEB J. 25, 326-336. doi: 10.1096/fj.10-164624
    • (2011) FASEB J , vol.25 , pp. 326-336
    • Danzer, K.M.1    Ruf, W.P.2    Putcha, P.3    Joyner, D.4    Hashimoto, T.5    Glabe, C.6
  • 52
    • 17644383748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits a-synuclein fibril formation via preferential binding to prefibrillar species
    • Dedmon, M. M., Christodoulou, J., Wilson, M. R., and Dobson, C. M. (2005). Heat shock protein 70 inhibits a-synuclein fibril formation via preferential binding to prefibrillar species. J. Biol. Chem. 280, 14733-14740. doi: 10.1074/jbc.M413024200
    • (2005) J. Biol. Chem , vol.280 , pp. 14733-14740
    • Dedmon, M.M.1    Christodoulou, J.2    Wilson, M.R.3    Dobson, C.M.4
  • 53
    • 80054832080 scopus 로고    scopus 로고
    • Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS
    • DeJesus-Hernandez, M., Mackenzie, I. R., Boeve, B. F., Boxer, A. L., Baker, M., Rutherford, N. J., et al. (2011). Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS. Neuron 72, 245-256. doi: 10.1016/j.neuron.2011.09.011
    • (2011) Neuron , vol.72 , pp. 245-256
    • DeJesus-Hernandez, M.1    Mackenzie, I.R.2    Boeve, B.F.3    Boxer, A.L.4    Baker, M.5    Rutherford, N.J.6
  • 54
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
    • Demand, J., Alberti, S., Patterson, C., and Hohfeld, J. (2001). Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr. Biol. 11, 1569-1577. doi: 10.1016/S0960-9822(01)00487-0
    • (2001) Curr. Biol , vol.11 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 55
    • 84869017593 scopus 로고    scopus 로고
    • Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients
    • DeSantis, M. E., Leung, E. H., Sweeny, E. A., Jackrel, M. E., Cushman-Nick, M., Neuhaus-Follini, A., et al. (2012). Operational plasticity enables hsp104 to disaggregate diverse amyloid and nonamyloid clients. Cell 151, 778-793. doi: 10.1016/j.cell.2012.09.038
    • (2012) Cell , vol.151 , pp. 778-793
    • DeSantis, M.E.1    Leung, E.H.2    Sweeny, E.A.3    Jackrel, M.E.4    Cushman-Nick, M.5    Neuhaus-Follini, A.6
  • 56
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice, J. F. (1990). Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem. Sci. 15, 305-309
    • (1990) Trends Biochem. Sci , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 57
    • 36749002683 scopus 로고    scopus 로고
    • Anti-cancer therapeutic approaches based on intracellular and extracellular heat shock proteins
    • Didelot, C., Lanneau, D., Brunet, M., Joly, A. L., De Thonel, A., Chiosis, G., et al. (2007). Anti-cancer therapeutic approaches based on intracellular and extracellular heat shock proteins. Curr. Med. Chem. 14, 2839-2847. doi: 10.2174/092986707782360079
    • (2007) Curr. Med. Chem , vol.14 , pp. 2839-2847
    • Didelot, C.1    Lanneau, D.2    Brunet, M.3    Joly, A.L.4    De Thonel, A.5    Chiosis, G.6
  • 58
    • 34047175919 scopus 로고    scopus 로고
    • Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
    • Dompierre, J. P., Godin, J. D., Charrin, B. C., Cordelieres, F. P., King, S. J., Humbert, S., et al. (2007). Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. J. Neurosci. 27, 3571-3583. doi: 10.1523/JNEUROSCI.0037-07.2007
    • (2007) J. Neurosci , vol.27 , pp. 3571-3583
    • Dompierre, J.P.1    Godin, J.D.2    Charrin, B.C.3    Cordelieres, F.P.4    King, S.J.5    Humbert, S.6
  • 59
    • 67649306771 scopus 로고    scopus 로고
    • Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways
    • Douglas, P. M., Summers, D. W., and Cyr, D. M. (2009). Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways. Prion 3, 51-58
    • (2009) Prion , vol.3 , pp. 51-58
    • Douglas, P.M.1    Summers, D.W.2    Cyr, D.M.3
  • 60
    • 84886446627 scopus 로고    scopus 로고
    • Protein rescue from aggregates by powerful molecular chaperone machines
    • Doyle, S. M., Genest, O., and Wickner, S. (2013). Protein rescue from aggregates by powerful molecular chaperone machines. Nat. Rev. Mol. Cell Biol. 14, 617-629. doi: 10.1038/nrm3660
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 617-629
    • Doyle, S.M.1    Genest, O.2    Wickner, S.3
  • 61
    • 58149181486 scopus 로고    scopus 로고
    • Hsp104 and ClpB: protein disaggregating machines
    • Doyle, S. M., and Wickner, S. (2009). Hsp104 and ClpB: protein disaggregating machines. Trends Biochem. Sci. 34, 40-48. doi: 10.1016/j.tibs.2008.09.010
    • (2009) Trends Biochem. Sci , vol.34 , pp. 40-48
    • Doyle, S.M.1    Wickner, S.2
  • 62
    • 84858263923 scopus 로고    scopus 로고
    • Molecular chaperones in Parkinson's disease-present and future
    • Ebrahimi-Fakhari, D., Wahlster, L., and McLean, P. J. (2011). Molecular chaperones in Parkinson's disease-present and future. J. Parkinsons. Dis. 1, 299-320
    • (2011) J. Parkinsons. Dis , vol.1 , pp. 299-320
    • Ebrahimi-Fakhari, D.1    Wahlster, L.2    McLean, P.J.3
  • 63
    • 57049182407 scopus 로고    scopus 로고
    • Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1
    • Eisele, F., and Wolf, D. H. (2008). Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1. FEBS Lett. 582, 4143-4146. doi: 10.1016/j.febslet.2008.11.015
    • (2008) FEBS Lett , vol.582 , pp. 4143-4146
    • Eisele, F.1    Wolf, D.H.2
  • 64
    • 77449103325 scopus 로고    scopus 로고
    • Therapeutic strategies within the ubiquitin proteasome system
    • Eldridge, A. G., and O'Brien, T. (2010). Therapeutic strategies within the ubiquitin proteasome system. Cell Death Differ. 17, 4-13. doi: 10.1038/cdd.2009.82
    • (2010) Cell Death Differ , vol.17 , pp. 4-13
    • Eldridge, A.G.1    O'Brien, T.2
  • 65
    • 65649110502 scopus 로고    scopus 로고
    • BAG-1M is up-regulated in hippocampus of Alzheimer's disease patients and associates with tau and APP proteins
    • Elliott, E., Laufer, O., and Ginzburg, I. (2009). BAG-1M is up-regulated in hippocampus of Alzheimer's disease patients and associates with tau and APP proteins. J. Neurochem. 109, 1168-1178. doi: 10.1111/j.1471-4159.2009.06047.x
    • (2009) J. Neurochem , vol.109 , pp. 1168-1178
    • Elliott, E.1    Laufer, O.2    Ginzburg, I.3
  • 66
    • 37549025063 scopus 로고    scopus 로고
    • BAG-1 associates with Hsc70.Tau complex and regulates the proteasomal degradation of Tau protein
    • Elliott, E., Tsvetkov, P., and Ginzburg, I. (2007). BAG-1 associates with Hsc70.Tau complex and regulates the proteasomal degradation of Tau protein. J. Biol. Chem. 282, 37276-37284. doi: 10.1074/jbc.M706379200
    • (2007) J. Biol. Chem , vol.282 , pp. 37276-37284
    • Elliott, E.1    Tsvetkov, P.2    Ginzburg, I.3
  • 67
    • 33745829795 scopus 로고    scopus 로고
    • Molecular chaperones: assisting assembly in addition to folding
    • Ellis, R. J. (2006). Molecular chaperones: assisting assembly in addition to folding. Trends Biochem. Sci. 31, 395-401. doi: 10.1016/j.tibs.2006.05.001
    • (2006) Trends Biochem. Sci , vol.31 , pp. 395-401
    • Ellis, R.J.1
  • 68
    • 84934438837 scopus 로고    scopus 로고
    • Protein misassembly: macromolecular crowding and molecular chaperones
    • Ellis, R. J. (2007). Protein misassembly: macromolecular crowding and molecular chaperones. Adv. Exp. Med. Biol. 594, 1-13. doi: 10.1007/978-0-387-39975-1_1
    • (2007) Adv. Exp. Med. Biol , vol.594 , pp. 1-13
    • Ellis, R.J.1
  • 69
    • 33746099650 scopus 로고    scopus 로고
    • Protein aggregation in crowded environments
    • Ellis, R. J., and Minton, A. P. (2006). Protein aggregation in crowded environments. Biol. Chem. 387, 485-497. doi: 10.1515/BC.2006.064
    • (2006) Biol. Chem , vol.387 , pp. 485-497
    • Ellis, R.J.1    Minton, A.P.2
  • 70
    • 62949091373 scopus 로고    scopus 로고
    • Autophagy: a lysosomal degradation pathway with a central role in health and disease
    • Eskelinen, E. L., and Saftig, P. (2009). Autophagy: a lysosomal degradation pathway with a central role in health and disease. Biochim. Biophys. Acta 1793, 664-673. doi: 10.1016/j.bbamcr.2008.07.014
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 664-673
    • Eskelinen, E.L.1    Saftig, P.2
  • 71
    • 33845918172 scopus 로고    scopus 로고
    • Heat shock proteins 70 and 90 inhibit early stages of amyloid ß-(1-42) aggregation in vitro
    • Evans, C. G., Wisen, S., and Gestwicki, J. E. (2006). Heat shock proteins 70 and 90 inhibit early stages of amyloid ß-(1-42) aggregation in vitro. J. Biol. Chem. 281, 33182-33191. doi: 10.1074/jbc.M606192200
    • (2006) J. Biol. Chem , vol.281 , pp. 33182-33191
    • Evans, C.G.1    Wisen, S.2    Gestwicki, J.E.3
  • 72
    • 80455122748 scopus 로고    scopus 로고
    • Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins
    • Fang, N. N., Ng, A. H., Measday, V., and Mayor, T. (2011). Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins. Nat. Cell Biol. 13, 1344-1352. doi: 10.1038/ncb2343
    • (2011) Nat. Cell Biol , vol.13 , pp. 1344-1352
    • Fang, N.N.1    Ng, A.H.2    Measday, V.3    Mayor, T.4
  • 73
    • 84866748196 scopus 로고    scopus 로고
    • Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase
    • Farg, M. A., Soo, K. Y., Walker, A. K., Pham, H., Orian, J., Horne, M. K., et al. (2012). Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase. Neurobiol. Aging 33, 2855-2868. doi: 10.1016/j.neurobiolaging.2012.02.009
    • (2012) Neurobiol. Aging , vol.33 , pp. 2855-2868
    • Farg, M.A.1    Soo, K.Y.2    Walker, A.K.3    Pham, H.4    Orian, J.5    Horne, M.K.6
  • 74
    • 33845926057 scopus 로고    scopus 로고
    • Triad3A regulates ubiquitination and proteasomal degradation of RIP1 following disruption of Hsp90 binding
    • Fearns, C., Pan, Q., Mathison, J. C., and Chuang, T. H. (2006). Triad3A regulates ubiquitination and proteasomal degradation of RIP1 following disruption of Hsp90 binding. J. Biol. Chem. 281, 34592-34600. doi: 10.1074/jbc.M604019200
    • (2006) J. Biol. Chem , vol.281 , pp. 34592-34600
    • Fearns, C.1    Pan, Q.2    Mathison, J.C.3    Chuang, T.H.4
  • 75
    • 84883049362 scopus 로고    scopus 로고
    • Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis
    • Finka, A., and Goloubinoff, P. (2013). Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis. Cell Stress Chaperones 18, 591-605. doi: 10.1007/s12192-013-0413-3
    • (2013) Cell Stress Chaperones , vol.18 , pp. 591-605
    • Finka, A.1    Goloubinoff, P.2
  • 76
    • 0142009674 scopus 로고    scopus 로고
    • Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions
    • Fuertes, G., Martin De Llano, J. J., Villarroya, A., Rivett, A. J., and Knecht, E. (2003). Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions. Biochem. J. 375(Pt 1), 75-86. doi: 10.1042/BJ20030282
    • (2003) Biochem. J , vol.375 , pp. 75-86
    • Fuertes, G.1    Martin De Llano, J.J.2    Villarroya, A.3    Rivett, A.J.4    Knecht, E.5
  • 77
    • 54449101793 scopus 로고    scopus 로고
    • Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones
    • Fujikake, N., Nagai, Y., Popiel, H. A., Okamoto, Y., Yamaguchi, M., and Toda, T. (2008). Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones. J. Biol. Chem. 283, 26188-26197. doi: 10.1074/jbc.M710521200
    • (2008) J. Biol. Chem , vol.283 , pp. 26188-26197
    • Fujikake, N.1    Nagai, Y.2    Popiel, H.A.3    Okamoto, Y.4    Yamaguchi, M.5    Toda, T.6
  • 78
    • 84940897433 scopus 로고    scopus 로고
    • Human Hsp70 Disaggregase Reverses Parkinson's-Linked a-Synuclein Amyloid Fibrils
    • Gao, X., Carroni, M., Nussbaum-Krammer, C., Mogk, A., Nillegoda, N. B., Szlachcic, A., et al. (2015). Human Hsp70 Disaggregase Reverses Parkinson's-Linked a-Synuclein Amyloid Fibrils. Mol. Cell 59, 781-793. doi: 10.1016/j.molcel.2015.07.012
    • (2015) Mol. Cell , vol.59 , pp. 781-793
    • Gao, X.1    Carroni, M.2    Nussbaum-Krammer, C.3    Mogk, A.4    Nillegoda, N.B.5    Szlachcic, A.6
  • 79
    • 17644396667 scopus 로고    scopus 로고
    • Degradation-mediated protein quality control in the nucleus
    • Gardner, R. G., Nelson, Z. W., and Gottschling, D. E. (2005). Degradation-mediated protein quality control in the nucleus. Cell 120, 803-815. doi: 10.1016/j.cell.2005.01.016
    • (2005) Cell , vol.120 , pp. 803-815
    • Gardner, R.G.1    Nelson, Z.W.2    Gottschling, D.E.3
  • 80
    • 18544386399 scopus 로고    scopus 로고
    • Binding of ATP to heat shock protein 90, evidence for an ATP-binding site in the C-terminal domain
    • Garnier, C., Lafitte, D., Tsvetkov, P. O., Barbier, P., Leclerc-Devin, J., Millot, J. M., et al. (2002). Binding of ATP to heat shock protein 90: evidence for an ATP-binding site in the C-terminal domain. J. Biol. Chem. 277, 12208-12214. doi: 10.1074/jbc.M111874200
    • (2002) J. Biol. Chem , vol.277 , pp. 12208-12214
    • Garnier, C.1    Lafitte, D.2    Tsvetkov, P.O.3    Barbier, P.4    Leclerc-Devin, J.5    Millot, J.M.6
  • 81
    • 33751203833 scopus 로고    scopus 로고
    • Heat shock proteins 27 and 70, anti-apoptotic proteins with tumorigenic properties
    • Garrido, C., Brunet, M., Didelot, C., Zermati, Y., Schmitt, E., and Kroemer, G. (2006). Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties. Cell Cycle 5, 2592-2601. doi: 10.4161/cc.5.22.3448
    • (2006) Cell Cycle , vol.5 , pp. 2592-2601
    • Garrido, C.1    Brunet, M.2    Didelot, C.3    Zermati, Y.4    Schmitt, E.5    Kroemer, G.6
  • 82
    • 0034812599 scopus 로고    scopus 로고
    • Heat shock proteins: endogenous modulators of apoptotic cell death
    • Garrido, C., Gurbuxani, S., Ravagnan, L., and Kroemer, G. (2001). Heat shock proteins: endogenous modulators of apoptotic cell death. Biochem. Biophys. Res. Commun. 286, 433-442. doi: 10.1006/bbrc.2001.5427
    • (2001) Biochem. Biophys. Res. Commun , vol.286 , pp. 433-442
    • Garrido, C.1    Gurbuxani, S.2    Ravagnan, L.3    Kroemer, G.4
  • 83
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
    • Glover, J. R., and Lindquist, S. (1998). Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94, 73-82
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 84
    • 0035409575 scopus 로고    scopus 로고
    • a-synuclein and neurodegenerative diseases
    • Goedert, M. (2001). a-synuclein and neurodegenerative diseases. Nat. Rev. Neurosci. 2, 492-501. doi: 10.1038/35081564
    • (2001) Nat. Rev. Neurosci , vol.2 , pp. 492-501
    • Goedert, M.1
  • 85
    • 77950532428 scopus 로고    scopus 로고
    • Restoration of visual function in P23H rhodopsin transgenic rats by gene delivery of BiP/Grp78
    • Gorbatyuk, M. S., Knox, T., LaVail, M. M., Gorbatyuk, O. S., Noorwez, S. M., Hauswirth, W. W., et al. (2010). Restoration of visual function in P23H rhodopsin transgenic rats by gene delivery of BiP/Grp78. Proc. Natl. Acad. Sci. U.S.A. 107, 5961-5966. doi: 10.1073/pnas.0911991107
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 5961-5966
    • Gorbatyuk, M.S.1    Knox, T.2    LaVail, M.M.3    Gorbatyuk, O.S.4    Noorwez, S.M.5    Hauswirth, W.W.6
  • 86
    • 84863498486 scopus 로고    scopus 로고
    • Glucose regulated protein 78 diminishes a-synuclein neurotoxicity in a rat model of Parkinson disease
    • Gorbatyuk, M. S., Shabashvili, A., Chen, W., Meyers, C., Sullivan, L. F., Salganik, M., et al. (2012). Glucose regulated protein 78 diminishes a-synuclein neurotoxicity in a rat model of Parkinson disease. Mol. Ther. 20, 1327-1337. doi: 10.1038/mt.2012.28
    • (2012) Mol. Ther , vol.20 , pp. 1327-1337
    • Gorbatyuk, M.S.1    Shabashvili, A.2    Chen, W.3    Meyers, C.4    Sullivan, L.F.5    Salganik, M.6
  • 88
    • 0029905594 scopus 로고    scopus 로고
    • A mouse amidase specific for N-terminal asparagine. The gene, the enzyme, and their function in the N-end rule pathway
    • Grigoryev, S., Stewart, A. E., Kwon, Y. T., Arfin, S. M., Bradshaw, R. A., Jenkins, N. A., et al. (1996). A mouse amidase specific for N-terminal asparagine. The gene, the enzyme, and their function in the N-end rule pathway. J. Biol. Chem. 271, 28521-28532
    • (1996) J. Biol. Chem , vol.271 , pp. 28521-28532
    • Grigoryev, S.1    Stewart, A.E.2    Kwon, Y.T.3    Arfin, S.M.4    Bradshaw, R.A.5    Jenkins, N.A.6
  • 89
    • 0141750470 scopus 로고    scopus 로고
    • Disruption of axonal transport by loss of huntingtin or expression of pathogenic polyQ proteins in Drosophila
    • Gunawardena, S., Her, L. S., Brusch, R. G., Laymon, R. A., Niesman, I. R., Gordesky-Gold, B., et al. (2003). Disruption of axonal transport by loss of huntingtin or expression of pathogenic polyQ proteins in Drosophila. Neuron 40, 25-40. doi: 10.1016/S0896-6273(03)00594-4
    • (2003) Neuron , vol.40 , pp. 25-40
    • Gunawardena, S.1    Her, L.S.2    Brusch, R.G.3    Laymon, R.A.4    Niesman, I.R.5    Gordesky-Gold, B.6
  • 90
    • 0032103078 scopus 로고    scopus 로고
    • Huntingtin: a single bait hooks many species
    • Gusella, J. F., and MacDonald, M. E. (1998). Huntingtin: a single bait hooks many species. Curr. Opin. Neurobiol. 8, 425-430
    • (1998) Curr. Opin. Neurobiol , vol.8 , pp. 425-430
    • Gusella, J.F.1    MacDonald, M.E.2
  • 91
    • 79960419007 scopus 로고    scopus 로고
    • NF-?B essential modulator (NEMO) interaction with linear and lys-63 ubiquitin chains contributes to NF-?B activation
    • Hadian, K., Griesbach, R. A., Dornauer, S., Wanger, T. M., Nagel, D., Metlitzky, M., et al. (2011). NF-?B essential modulator (NEMO) interaction with linear and lys-63 ubiquitin chains contributes to NF-?B activation. J. Biol. Chem. 286, 26107-26117. doi: 10.1074/jbc.M111.233163
    • (2011) J. Biol. Chem , vol.286 , pp. 26107-26117
    • Hadian, K.1    Griesbach, R.A.2    Dornauer, S.3    Wanger, T.M.4    Nagel, D.5    Metlitzky, M.6
  • 92
    • 75949094261 scopus 로고    scopus 로고
    • A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation
    • Hageman, J., Rujano, M. A., van Waarde, M. A., Kakkar, V., Dirks, R. P., Govorukhina, N., et al. (2010). A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation. Mol. Cell 37, 355-369. doi: 10.1016/j.molcel.2010.01.001
    • (2010) Mol. Cell , vol.37 , pp. 355-369
    • Hageman, J.1    Rujano, M.A.2    van Waarde, M.A.3    Kakkar, V.4    Dirks, R.P.5    Govorukhina, N.6
  • 93
    • 84884593127 scopus 로고    scopus 로고
    • Proteasomes activate aggresome disassembly and clearance by producing unanchored ubiquitin chains
    • Hao, R., Nanduri, P., Rao, Y., Panichelli, R. S., Ito, A., Yoshida, M., et al. (2013). Proteasomes activate aggresome disassembly and clearance by producing unanchored ubiquitin chains. Mol. Cell 51, 819-828. doi: 10.1016/j.molcel.2013.08.016
    • (2013) Mol. Cell , vol.51 , pp. 819-828
    • Hao, R.1    Nanduri, P.2    Rao, Y.3    Panichelli, R.S.4    Ito, A.5    Yoshida, M.6
  • 94
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A., and Hayer-Hartl, M. (2011). Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332. doi: 10.1038/nature10317
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 95
    • 2242472974 scopus 로고    scopus 로고
    • Phosphorylated a-synuclein is ubiquitinated in a-synucleinopathy lesions
    • Hasegawa, M. Fujiwara, H., Nonaka, T., Wakabayashi, K., Takahashi, H., Lee, V. M., et al. (2002). Phosphorylated a-synuclein is ubiquitinated in a-synucleinopathy lesions. J. Biol. Chem. 277, 49071-49076. doi: 10.1074/jbc.M208046200
    • (2002) J. Biol. Chem , vol.277 , pp. 49071-49076
    • Hasegawa, M.1    Fujiwara, H.2    Nonaka, T.3    Wakabayashi, K.4    Takahashi, H.5    Lee, V.M.6
  • 97
    • 75749101057 scopus 로고    scopus 로고
    • Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1
    • Heck, J. W., Cheung, S. K., and Hampton, R. Y. (2010). Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1. Proc. Natl. Acad. Sci. U.S.A. 107, 1106-1111. doi: 10.1073/pnas.0910591107
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 1106-1111
    • Heck, J.W.1    Cheung, S.K.2    Hampton, R.Y.3
  • 98
    • 77954416653 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and synaptic plasticity
    • Hegde, A. N. (2010). The ubiquitin-proteasome pathway and synaptic plasticity. Learn. Mem. 17, 314-327. doi: 10.1101/lm.1504010
    • (2010) Learn. Mem , vol.17 , pp. 314-327
    • Hegde, A.N.1
  • 99
    • 79151485014 scopus 로고    scopus 로고
    • Role of ubiquitin-proteasome-mediated proteolysis in nervous system disease
    • Hegde, A. N., and Upadhya, S. C. (2011). Role of ubiquitin-proteasome-mediated proteolysis in nervous system disease. Biochim. Biophys. Acta 1809, 128-140. doi: 10.1016/j.bbagrm.2010.07.006
    • (2011) Biochim. Biophys. Acta , vol.1809 , pp. 128-140
    • Hegde, A.N.1    Upadhya, S.C.2
  • 100
    • 0031657807 scopus 로고    scopus 로고
    • The ubiquitin system
    • Hershko, A., and Ciechanover, A. (1998). The ubiquitin system. Annu. Rev. Biochem. 67, 425-479. doi: 10.1146/annurev.biochem.67.1.425
    • (1998) Annu. Rev. Biochem , vol.67 , pp. 425-479
    • Hershko, A.1    Ciechanover, A.2
  • 101
    • 84897094564 scopus 로고    scopus 로고
    • Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
    • Hetz, C., and Mollereau, B. (2014). Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases. Nat. Rev. Neurosci. 15, 233-249. doi: 10.1038/nrn3689
    • (2014) Nat. Rev. Neurosci , vol.15 , pp. 233-249
    • Hetz, C.1    Mollereau, B.2
  • 102
    • 84864395066 scopus 로고    scopus 로고
    • Mapping the road to recovery: the ClpB/Hsp104 molecular chaperone
    • Hodson, S., Marshall, J. J., and Burston, S. G. (2012). Mapping the road to recovery: the ClpB/Hsp104 molecular chaperone. J. Struct. Biol. 179, 161-171. doi: 10.1016/j.jsb.2012.05.015
    • (2012) J. Struct. Biol , vol.179 , pp. 161-171
    • Hodson, S.1    Marshall, J.J.2    Burston, S.G.3
  • 103
    • 0842328576 scopus 로고    scopus 로고
    • Identification of a redox-regulated chaperone network
    • Hoffmann, J. H., Linke, K., Graf, P. C., Lilie, H., and Jakob, U. (2004). Identification of a redox-regulated chaperone network. EMBO J. 23, 160-168. doi: 10.1038/sj.emboj.7600016
    • (2004) EMBO J , vol.23 , pp. 160-168
    • Hoffmann, J.H.1    Linke, K.2    Graf, P.C.3    Lilie, H.4    Jakob, U.5
  • 104
    • 84867956994 scopus 로고    scopus 로고
    • Alzheimer's disease, cerebrovascular disease, and the ß-amyloid cascade
    • Honjo, K., Black, S. E., and Verhoeff, N. P. (2012). Alzheimer's disease, cerebrovascular disease, and the ß-amyloid cascade. Can. J. Neurol. Sci. 39, 712-728. doi: 10.1017/S0317167100015547
    • (2012) Can. J. Neurol. Sci , vol.39 , pp. 712-728
    • Honjo, K.1    Black, S.E.2    Verhoeff, N.P.3
  • 105
    • 80055031464 scopus 로고    scopus 로고
    • Protein disulfide isomerase-immunopositive inclusions in patients with amyotrophic lateral sclerosis
    • Honjo, Y., Kaneko, S., Ito, H., Horibe, T., Nagashima, M., Nakamura, M., et al. (2011). Protein disulfide isomerase-immunopositive inclusions in patients with amyotrophic lateral sclerosis. Amyotroph. Lateral Scler. 12, 444-450. doi: 10.3109/17482968.2011.594055
    • (2011) Amyotroph. Lateral Scler , vol.12 , pp. 444-450
    • Honjo, Y.1    Kaneko, S.2    Ito, H.3    Horibe, T.4    Nagashima, M.5    Nakamura, M.6
  • 106
    • 84866521976 scopus 로고    scopus 로고
    • Heat shock protein-inducing compounds as therapeutics to restore proteostasis in atrial fibrillation
    • Hoogstra-Berends, F., Meijering, R. A., Zhang, D., Heeres, A., Loen, L., Seerden, J. P., et al. (2012). Heat shock protein-inducing compounds as therapeutics to restore proteostasis in atrial fibrillation. Trends Cardiovasc. Med. 22, 62-68. doi: 10.1016/j.tcm.2012.06.013
    • (2012) Trends Cardiovasc. Med , vol.22 , pp. 62-68
    • Hoogstra-Berends, F.1    Meijering, R.A.2    Zhang, D.3    Heeres, A.4    Loen, L.5    Seerden, J.P.6
  • 107
    • 0038155122 scopus 로고    scopus 로고
    • Alzheimer's associated variant ubiquitin causes inhibition of the 26S proteasome and chaperone expression
    • Hope, A. D., de Silva, R., Fischer, D. F., Hol, E. M., van Leeuwen, F. W., and Lees, A. J. (2003). Alzheimer's associated variant ubiquitin causes inhibition of the 26S proteasome and chaperone expression. J. Neurochem. 86, 394-404. doi: 10.1046/j.1471-4159.2003.01844.x
    • (2003) J. Neurochem , vol.86 , pp. 394-404
    • Hope, A.D.1    de Silva, R.2    Fischer, D.F.3    Hol, E.M.4    van Leeuwen, F.W.5    Lees, A.J.6
  • 108
    • 34447514375 scopus 로고    scopus 로고
    • Age-associated decrease in proteasome content and activities in human dermal fibroblasts: restoration of normal level of proteasome subunits reduces aging markers in fibroblasts from elderly persons
    • Hwang, J. S., Hwang, J. S., Chang, I., and Kim, S. (2007). Age-associated decrease in proteasome content and activities in human dermal fibroblasts: restoration of normal level of proteasome subunits reduces aging markers in fibroblasts from elderly persons. J. Gerontol. A Biol. Sci. Med. Sci. 62, 490-499
    • (2007) J. Gerontol. A Biol. Sci. Med. Sci , vol.62 , pp. 490-499
    • Hwang, J.S.1    Hwang, J.S.2    Chang, I.3    Kim, S.4
  • 109
    • 0031944830 scopus 로고    scopus 로고
    • Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain a-synuclein immunoreactivity
    • Irizarry, M. C., Growdon, W., Gomez-Isla, T., Newell, K., George, J. M., Clayton, D. F., et al. (1998). Nigral and cortical Lewy bodies and dystrophic nigral neurites in Parkinson's disease and cortical Lewy body disease contain a-synuclein immunoreactivity. J. Neuropathol. Exp. Neurol. 57, 334-337
    • (1998) J. Neuropathol. Exp. Neurol , vol.57 , pp. 334-337
    • Irizarry, M.C.1    Growdon, W.2    Gomez-Isla, T.3    Newell, K.4    George, J.M.5    Clayton, D.F.6
  • 110
    • 18744402993 scopus 로고    scopus 로고
    • Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration
    • Itoh, H., Komatsuda, A., Ohtani, H., Wakui, H., Imai, H., Sawada, K., et al. (2002). Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration. Eur. J. Biochem. 269, 5931-5938. doi: 10.1046/j.1432-1033.2002.03317.x
    • (2002) Eur. J. Biochem , vol.269 , pp. 5931-5938
    • Itoh, H.1    Komatsuda, A.2    Ohtani, H.3    Wakui, H.4    Imai, H.5    Sawada, K.6
  • 111
    • 84892773641 scopus 로고    scopus 로고
    • Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding events
    • Jackrel, M. E., DeSantis, M. E., Martinez, B. A., Castellano, L. M., Stewart, R. M., Caldwell, K. A., et al. (2014). Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding events. Cell 156, 170-182. doi: 10.1016/j.cell.2013.11.047
    • (2014) Cell , vol.156 , pp. 170-182
    • Jackrel, M.E.1    DeSantis, M.E.2    Martinez, B.A.3    Castellano, L.M.4    Stewart, R.M.5    Caldwell, K.A.6
  • 112
    • 84907558479 scopus 로고    scopus 로고
    • Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins
    • Jackrel, M. E., and Shorter, J. (2014). Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins. Dis. Model. Mech. 7, 1175-1184. doi: 10.1242/dmm.016113
    • (2014) Dis. Model. Mech , vol.7 , pp. 1175-1184
    • Jackrel, M.E.1    Shorter, J.2
  • 113
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity
    • Jana, N. R., Tanaka, M., Wang, G., and Nukina, N. (2000). Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Hum. Mol. Genet. 9, 2009-2018. doi: 10.1093/hmg/9.13.2009
    • (2000) Hum. Mol. Genet , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.3    Nukina, N.4
  • 114
    • 84896498656 scopus 로고    scopus 로고
    • Potential effect of S-nitrosylated protein disulfide isomerase on mutant SOD1 aggregation and neuronal cell death in amyotrophic lateral sclerosis
    • Jeon, G. S., Nakamura, T., Lee, J. S., Choi, W. J., Ahn, S. W., Lee, K. W., et al. (2014). Potential effect of S-nitrosylated protein disulfide isomerase on mutant SOD1 aggregation and neuronal cell death in amyotrophic lateral sclerosis. Mol. Neurobiol. 49, 796-807. doi: 10.1007/s12035-013-8562-z
    • (2014) Mol. Neurobiol , vol.49 , pp. 796-807
    • Jeon, G.S.1    Nakamura, T.2    Lee, J.S.3    Choi, W.J.4    Ahn, S.W.5    Lee, K.W.6
  • 115
    • 84860443709 scopus 로고    scopus 로고
    • GRP78 counteracts cell death and protein aggregation caused by mutant huntingtin proteins
    • Jiang, Y., Lv, H., Liao, M., Xu, X., Huang, S., Tan, H., et al. (2012). GRP78 counteracts cell death and protein aggregation caused by mutant huntingtin proteins. Neurosci. Lett. 516, 182-187. doi: 10.1016/j.neulet.2012.03.074
    • (2012) Neurosci. Lett , vol.516 , pp. 182-187
    • Jiang, Y.1    Lv, H.2    Liao, M.3    Xu, X.4    Huang, S.5    Tan, H.6
  • 116
    • 84890560755 scopus 로고    scopus 로고
    • The role of heat shock proteins in Amyotrophic Lateral Sclerosis: the therapeutic potential of Arimoclomol
    • Kalmar, B., Lu, C. H., and Greensmith, L. (2014). The role of heat shock proteins in Amyotrophic Lateral Sclerosis: the therapeutic potential of Arimoclomol. Pharmacol. Ther. 141, 40-54. doi: 10.1016/j.pharmthera.2013.08.003
    • (2014) Pharmacol. Ther , vol.141 , pp. 40-54
    • Kalmar, B.1    Lu, C.H.2    Greensmith, L.3
  • 117
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: j proteins as drivers of functional specificity
    • Kampinga, H. H., and Craig, E. A. (2010). The HSP70 chaperone machinery: j proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 11, 579-592. doi: 10.1038/nrm2941
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 118
    • 84862742197 scopus 로고    scopus 로고
    • Interactions of the proteasomal system with chaperones: protein triage and protein quality control
    • Kastle, M., and Grune, T. (2012). Interactions of the proteasomal system with chaperones: protein triage and protein quality control. Prog. Mol. Biol. Transl. Sci. 109, 113-160. doi: 10.1016/B978-0-12-397863-9.00004-3
    • (2012) Prog. Mol. Biol. Transl. Sci , vol.109 , pp. 113-160
    • Kastle, M.1    Grune, T.2
  • 119
    • 84864318195 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: a unique way to enter the lysosome world
    • Kaushik, S., and Cuervo, A. M. (2012). Chaperone-mediated autophagy: a unique way to enter the lysosome world. Trends Cell Biol. 22, 407-417. doi: 10.1016/j.tcb.2012.05.006
    • (2012) Trends Cell Biol , vol.22 , pp. 407-417
    • Kaushik, S.1    Cuervo, A.M.2
  • 120
    • 0034629073 scopus 로고    scopus 로고
    • Genetic suppression of polyglutamine toxicity in Drosophila
    • Kazemi-Esfarjani, P., and Benzer, S. (2000). Genetic suppression of polyglutamine toxicity in Drosophila. Science 287, 1837-1840. doi: 10.1126/science.287.5459.1837
    • (2000) Science , vol.287 , pp. 1837-1840
    • Kazemi-Esfarjani, P.1    Benzer, S.2
  • 121
    • 0034087369 scopus 로고    scopus 로고
    • Decreased levels of proteasome activity and proteasome expression in aging spinal cord
    • Keller, J. N., Huang, F. F., and Markesbery, W. R. (2000). Decreased levels of proteasome activity and proteasome expression in aging spinal cord. Neuroscience 98, 149-156. doi: 10.1016/S0306-4522(00)00067-1
    • (2000) Neuroscience , vol.98 , pp. 149-156
    • Keller, J.N.1    Huang, F.F.2    Markesbery, W.R.3
  • 122
    • 77952851112 scopus 로고    scopus 로고
    • Chaperone-assisted degradation: multiple paths to destruction
    • Kettern, N., Dreiseidler, M., Tawo, R., and Hohfeld, J. (2010). Chaperone-assisted degradation: multiple paths to destruction. Biol. Chem. 391, 481-489. doi: 10.1515/BC.2010.058
    • (2010) Biol. Chem , vol.391 , pp. 481-489
    • Kettern, N.1    Dreiseidler, M.2    Tawo, R.3    Hohfeld, J.4
  • 123
    • 84870579566 scopus 로고    scopus 로고
    • Withaferin A induces proteasome inhibition, endoplasmic reticulum stress, the heat shock response and acquisition of thermotolerance
    • Khan, S., Rammeloo, A. W., and Heikkila, J. J. (2012). Withaferin A induces proteasome inhibition, endoplasmic reticulum stress, the heat shock response and acquisition of thermotolerance. PLoS ONE 7:e50547. doi: 10.1371/journal.pone.0050547
    • (2012) PLoS ONE , vol.7
    • Khan, S.1    Rammeloo, A.W.2    Heikkila, J.J.3
  • 124
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran, D., Kalmar, B., Dick, J. R., Riddoch-Contreras, J., Burnstock, G., and Greensmith, L. (2004). Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat. Med. 10, 402-405. doi: 10.1038/nm1021
    • (2004) Nat. Med , vol.10 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dick, J.R.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 125
    • 84878948560 scopus 로고    scopus 로고
    • Molecular chaperone functions in protein folding and proteostasis
    • Kim, Y. E., Hipp, M. S., Bracher, A., Hayer-Hartl, M., and Hartl, F. U. (2013). Molecular chaperone functions in protein folding and proteostasis. Annu. Rev. Biochem. 82, 323-355. doi: 10.1146/annurev-biochem-060208-092442
    • (2013) Annu. Rev. Biochem , vol.82 , pp. 323-355
    • Kim, Y.E.1    Hipp, M.S.2    Bracher, A.3    Hayer-Hartl, M.4    Hartl, F.U.5
  • 126
    • 33749176269 scopus 로고    scopus 로고
    • Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state
    • Kitamura, A., Kubota, H., Pack, C. G., Matsumoto, G., Hirayama, S., Takahashi, Y., et al. (2006). Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state. Nat. Cell Biol. 8, 1163-1170. doi: 10.1038/ncb1478
    • (2006) Nat. Cell Biol , vol.8 , pp. 1163-1170
    • Kitamura, A.1    Kubota, H.2    Pack, C.G.3    Matsumoto, G.4    Hirayama, S.5    Takahashi, Y.6
  • 127
    • 1042278905 scopus 로고    scopus 로고
    • Proteasome and peptidase function in MHC-class-I-mediated antigen presentation
    • Kloetzel, P. M., and Ossendorp, F. (2004). Proteasome and peptidase function in MHC-class-I-mediated antigen presentation. Curr. Opin. Immunol. 16, 76-81. doi: 10.1016/j.coi.2003.11.004
    • (2004) Curr. Opin. Immunol , vol.16 , pp. 76-81
    • Kloetzel, P.M.1    Ossendorp, F.2
  • 128
    • 2942620074 scopus 로고    scopus 로고
    • Hsp70 Reduces a-Synuclein Aggregation and Toxicity
    • Klucken, J., Shin, Y., Masliah, E., Hyman, B. T., and McLean, P. J. (2004). Hsp70 Reduces a-Synuclein Aggregation and Toxicity. J. Biol. Chem. 279, 25497-25502. doi: 10.1074/jbc.M400255200
    • (2004) J. Biol. Chem , vol.279 , pp. 25497-25502
    • Klucken, J.1    Shin, Y.2    Masliah, E.3    Hyman, B.T.4    McLean, P.J.5
  • 129
    • 34247185404 scopus 로고    scopus 로고
    • Disease-associated prion protein oligomers inhibit the 26S proteasome
    • Kristiansen, M., Deriziotis, P., Dimcheff, D. E., Jackson, G. S., Ovaa, H., Naumann, H., et al. (2007). Disease-associated prion protein oligomers inhibit the 26S proteasome. Mol. Cell 26, 175-188. doi: 10.1016/j.molcel.2007.04.001
    • (2007) Mol. Cell , vol.26 , pp. 175-188
    • Kristiansen, M.1    Deriziotis, P.2    Dimcheff, D.E.3    Jackson, G.S.4    Ovaa, H.5    Naumann, H.6
  • 130
    • 0030786120 scopus 로고    scopus 로고
    • Small heat shock proteins inhibit in vitro A ß(1-42) amyloidogenesis
    • Kudva, Y. C., Hiddinga, H. J., Butler, P. C., Mueske, C. S., and Eberhardt, N. L. (1997). Small heat shock proteins inhibit in vitro A ß(1-42) amyloidogenesis. FEBS Lett. 416, 117-121
    • (1997) FEBS Lett , vol.416 , pp. 117-121
    • Kudva, Y.C.1    Hiddinga, H.J.2    Butler, P.C.3    Mueske, C.S.4    Eberhardt, N.L.5
  • 131
    • 0023931333 scopus 로고
    • Lewy bodies are ubiquitinated. A light and electron microscopic immunocytochemical study
    • Kuzuhara, S., Mori, H., Izumiyama, N., Yoshimura, M., and Ihara, Y. (1988). Lewy bodies are ubiquitinated. A light and electron microscopic immunocytochemical study. Acta Neuropathol. 75, 345-353
    • (1988) Acta Neuropathol , vol.75 , pp. 345-353
    • Kuzuhara, S.1    Mori, H.2    Izumiyama, N.3    Yoshimura, M.4    Ihara, Y.5
  • 132
    • 0001687306 scopus 로고    scopus 로고
    • Altered activity, social behavior, and spatial memory in mice lacking the NTAN1p amidase and the asparagine branch of the N-end rule pathway
    • Kwon, Y. T., Balogh, S. A., Davydov, I. V., Kashina, A. S., Yoon, J. K., Xie, Y., et al. (2000). Altered activity, social behavior, and spatial memory in mice lacking the NTAN1p amidase and the asparagine branch of the N-end rule pathway. Mol. Cell. Biol. 20, 4135-4148. doi: 10.1128/MCB.20.11.4135-4148.2000
    • (2000) Mol. Cell. Biol , vol.20 , pp. 4135-4148
    • Kwon, Y.T.1    Balogh, S.A.2    Davydov, I.V.3    Kashina, A.S.4    Yoon, J.K.5    Xie, Y.6
  • 133
    • 0037025163 scopus 로고    scopus 로고
    • An essential role of N-terminal arginylation in cardiovascular development
    • Kwon, Y. T., Kashina, A. S., Davydov, I. V., Hu, R. G., An, J. Y., Seo, J. W., et al. (2002). An essential role of N-terminal arginylation in cardiovascular development. Science 297, 96-99. doi: 10.1126/science.1069531
    • (2002) Science , vol.297 , pp. 96-99
    • Kwon, Y.T.1    Kashina, A.S.2    Davydov, I.V.3    Hu, R.G.4    An, J.Y.5    Seo, J.W.6
  • 134
    • 0001602527 scopus 로고    scopus 로고
    • Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway
    • Kwon, Y. T., Kashina, A. S., and Varshavsky, A. (1999a). Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway. Mol. Cell. Biol. 19, 182-193
    • (1999) Mol. Cell. Biol , vol.19 , pp. 182-193
    • Kwon, Y.T.1    Kashina, A.S.2    Varshavsky, A.3
  • 135
    • 0008531195 scopus 로고    scopus 로고
    • Bivalent inhibitor of the N-end rule pathway
    • Kwon, Y. T., Levy, F., and Varshavsky, A. (1999b). Bivalent inhibitor of the N-end rule pathway. J. Biol. Chem. 274, 18135-18139
    • (1999) J. Biol. Chem , vol.274 , pp. 18135-18139
    • Kwon, Y.T.1    Levy, F.2    Varshavsky, A.3
  • 136
    • 84860123776 scopus 로고    scopus 로고
    • Suppression of protein aggregation by chaperone modification of high molecular weight complexes
    • Labbadia, J., Novoselov, S. S., Bett, J. S., Weiss, A., Paganetti, P., Bates, G. P., et al. (2012). Suppression of protein aggregation by chaperone modification of high molecular weight complexes. Brain 135(Pt 4), 1180-1196. doi: 10.1093/brain/aws022
    • (2012) Brain , vol.135 , pp. 1180-1196
    • Labbadia, J.1    Novoselov, S.S.2    Bett, J.S.3    Weiss, A.4    Paganetti, P.5    Bates, G.P.6
  • 137
    • 67650517556 scopus 로고    scopus 로고
    • NBR1 and p62 as cargo receptors for selective autophagy of ubiquitinated targets
    • Lamark, T., Kirkin, V., Dikic, I., and Johansen, T. (2009). NBR1 and p62 as cargo receptors for selective autophagy of ubiquitinated targets. Cell Cycle 8, 1986-1990. doi: 10.4161/cc.8.13.8892
    • (2009) Cell Cycle , vol.8 , pp. 1986-1990
    • Lamark, T.1    Kirkin, V.2    Dikic, I.3    Johansen, T.4
  • 138
    • 78349273136 scopus 로고    scopus 로고
    • Heat shock proteins: cell protection through protein triage
    • Lanneau, D., Wettstein, G., Bonniaud, P., and Garrido, C. (2010). Heat shock proteins: cell protection through protein triage. ScientificWorldJournal 10, 1543-1552. doi: 10.1100/tsw.2010.152
    • (2010) ScientificWorldJournal , vol.10 , pp. 1543-1552
    • Lanneau, D.1    Wettstein, G.2    Bonniaud, P.3    Garrido, C.4
  • 139
    • 77956527159 scopus 로고    scopus 로고
    • Enhancement of proteasome activity by a small-molecule inhibitor of USP14
    • Lee, B. H., Lee, M. J., Park, S., Oh, D. C., Elsasser, S., Chen, P. C., et al. (2010). Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature 467, 179-184. doi: 10.1038/nature09299
    • (2010) Nature , vol.467 , pp. 179-184
    • Lee, B.H.1    Lee, M.J.2    Park, S.3    Oh, D.C.4    Elsasser, S.5    Chen, P.C.6
  • 140
    • 84878143436 scopus 로고    scopus 로고
    • Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor
    • Lee, J., Kim, J. H., Biter, A. B., Sielaff, B., Lee, S., and Tsai, F. T. (2013). Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor. Proc. Natl. Acad. Sci. U.S.A. 110, 8513-8518. doi: 10.1073/pnas.1217988110
    • (2013) Proc. Natl. Acad. Sci. U.S.A , vol.110 , pp. 8513-8518
    • Lee, J.1    Kim, J.H.2    Biter, A.B.3    Sielaff, B.4    Lee, S.5    Tsai, F.T.6
  • 141
    • 38349095024 scopus 로고    scopus 로고
    • Synthetic heterovalent inhibitors targeting recognition E3 components of the N-end rule pathway
    • Lee, M. J., Pal, K., Tasaki, T., Roy, S., Jiang, Y., An, J. Y., et al. (2008). Synthetic heterovalent inhibitors targeting recognition E3 components of the N-end rule pathway. Proc. Natl. Acad. Sci. U.S.A. 105, 100-105. doi: 10.1073/pnas.0708465105
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 100-105
    • Lee, M.J.1    Pal, K.2    Tasaki, T.3    Roy, S.4    Jiang, Y.5    An, J.Y.6
  • 142
    • 27244444724 scopus 로고    scopus 로고
    • RGS4 and RGS5 are in vivo substrates of the N-end rule pathway
    • Lee, M. J., Tasaki, T., Moroi, K., An, J. Y., Kimura, S., Davydov, I. V., et al. (2005). RGS4 and RGS5 are in vivo substrates of the N-end rule pathway. Proc. Natl. Acad. Sci. USA. 102, 15030-15035. doi: 10.1073/pnas.0507533102
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15030-15035
    • Lee, M.J.1    Tasaki, T.2    Moroi, K.3    An, J.Y.4    Kimura, S.5    Davydov, I.V.6
  • 143
    • 79959923467 scopus 로고    scopus 로고
    • Protein aggregate spreading in neurodegenerative diseases: problems and perspectives
    • Lee, S. J., Lim, H. S., Masliah, E., and Lee, H. J. (2011). Protein aggregate spreading in neurodegenerative diseases: problems and perspectives. Neurosci. Res. 70, 339-348. doi: 10.1016/j.neures.2011.05.008
    • (2011) Neurosci. Res , vol.70 , pp. 339-348
    • Lee, S.J.1    Lim, H.S.2    Masliah, E.3    Lee, H.J.4
  • 144
    • 1842424791 scopus 로고    scopus 로고
    • Proteasomal inhibition by a-synuclein filaments and oligomers
    • Lindersson, E., Beedholm, R., Hojrup, P., Moos, T., Gai, W., Hendil, K. B., et al. (2004). Proteasomal inhibition by a-synuclein filaments and oligomers. J. Biol. Chem. 279, 12924-12934. doi: 10.1074/jbc.M306390200
    • (2004) J. Biol. Chem , vol.279 , pp. 12924-12934
    • Lindersson, E.1    Beedholm, R.2    Hojrup, P.3    Moos, T.4    Gai, W.5    Hendil, K.B.6
  • 145
    • 77957740228 scopus 로고    scopus 로고
    • Protein folding sculpting evolutionary change
    • Lindquist, S. (2009). Protein folding sculpting evolutionary change. Cold Spring Harb. Symp. Quant. Biol. 74, 103-108. doi: 10.1101/sqb.2009.74.043
    • (2009) Cold Spring Harb. Symp. Quant. Biol , vol.74 , pp. 103-108
    • Lindquist, S.1
  • 146
    • 0029950703 scopus 로고    scopus 로고
    • Heat-shock protein 104 expression is sufficient for thermotolerance in yeast
    • Lindquist, S., and Kim, G. (1996). Heat-shock protein 104 expression is sufficient for thermotolerance in yeast. Proc. Natl. Acad. Sci. U.S.A. 93, 5301-5306
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 5301-5306
    • Lindquist, S.1    Kim, G.2
  • 147
    • 84873802635 scopus 로고    scopus 로고
    • Disruption of ionic interactions between the nucleotide binding domain 1 (NBD1) and middle (M) domain in Hsp100 disaggregase unleashes toxic hyperactivity and partial independence from Hsp70
    • Lipinska, N., Zietkiewicz, S., Sobczak, A., Jurczyk, A., Potocki, W., Morawiec, E., et al. (2013). Disruption of ionic interactions between the nucleotide binding domain 1 (NBD1) and middle (M) domain in Hsp100 disaggregase unleashes toxic hyperactivity and partial independence from Hsp70. J. Biol. Chem. 288, 2857-2869. doi: 10.1074/jbc.M112.387589
    • (2013) J. Biol. Chem , vol.288 , pp. 2857-2869
    • Lipinska, N.1    Zietkiewicz, S.2    Sobczak, A.3    Jurczyk, A.4    Potocki, W.5    Morawiec, E.6
  • 148
    • 18844444198 scopus 로고    scopus 로고
    • Elevation of the Hsp70 chaperone does not effect toxicity in mouse models of familial amyotrophic lateral sclerosis
    • Liu, J., Shinobu, L. A., Ward, C. M., Young, D., and Cleveland, D. W. (2005). Elevation of the Hsp70 chaperone does not effect toxicity in mouse models of familial amyotrophic lateral sclerosis. J. Neurochem. 93, 875-882. doi: 10.1111/j.1471-4159.2005.03054.x
    • (2005) J. Neurochem , vol.93 , pp. 875-882
    • Liu, J.1    Shinobu, L.A.2    Ward, C.M.3    Young, D.4    Cleveland, D.W.5
  • 149
    • 51349150684 scopus 로고    scopus 로고
    • Hsp104 antagonizes a-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease
    • Lo Bianco, C., Shorter, J., Regulier, E., Lashuel, H., Iwatsubo, T., Lindquist, S., et al. (2008). Hsp104 antagonizes a-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease. J. Clin. Invest. 118, 3087-3097. doi: 10.1172/JCI35781
    • (2008) J. Clin. Invest , vol.118 , pp. 3087-3097
    • Lo Bianco, C.1    Shorter, J.2    Regulier, E.3    Lashuel, H.4    Iwatsubo, T.5    Lindquist, S.6
  • 150
    • 84941173009 scopus 로고    scopus 로고
    • The mechanism and function of Group II Chaperonins
    • Lopez, T., Dalton, K., and Frydman, J. (2015). The mechanism and function of Group II Chaperonins. J. Mol. Biol. 427, 2919-2930. doi: 10.1016/j.jmb.2015.04.013
    • (2015) J. Mol. Biol , vol.427 , pp. 2919-2930
    • Lopez, T.1    Dalton, K.2    Frydman, J.3
  • 151
    • 79955737369 scopus 로고    scopus 로고
    • The role of ubiquitin-proteasome system in ageing
    • Low, P. (2011). The role of ubiquitin-proteasome system in ageing. Gen. Comp. Endocrinol. 172, 39-43. doi: 10.1016/j.ygcen.2011.02.005
    • (2011) Gen. Comp. Endocrinol , vol.172 , pp. 39-43
    • Low, P.1
  • 152
    • 56749117866 scopus 로고    scopus 로고
    • Interactions between Hsp70 and the hydrophobic core of a-synuclein inhibit fibril assembly
    • Luk, K. C., Mills, I. P., Trojanowski, J. Q., and Lee, V. M. (2008). Interactions between Hsp70 and the hydrophobic core of a-synuclein inhibit fibril assembly. Biochemistry 47, 12614-12625. doi: 10.1021/bi801475r
    • (2008) Biochemistry , vol.47 , pp. 12614-12625
    • Luk, K.C.1    Mills, I.P.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 153
    • 34547183507 scopus 로고    scopus 로고
    • Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies
    • Luo, W., Dou, F., Rodina, A., Chip, S., Kim, J., Zhao, Q., et al. (2007). Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies. Proc. Natl. Acad. Sci. U.S.A. 104, 9511-9516. doi: 10.1073/pnas.0701055104
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 9511-9516
    • Luo, W.1    Dou, F.2    Rodina, A.3    Chip, S.4    Kim, J.5    Zhao, Q.6
  • 154
    • 84909951802 scopus 로고    scopus 로고
    • Interaction of the molecular chaperone DNAJB6 with growing amyloid-ß 42 (Aß42) aggregates leads to sub-stoichiometric inhibition of amyloid formation
    • Mansson, C., Arosio, P., Hussein, R., Kampinga, H. H., Hashem, R. M., Boelens, W. C., et al. (2014). Interaction of the molecular chaperone DNAJB6 with growing amyloid-ß 42 (Aß42) aggregates leads to sub-stoichiometric inhibition of amyloid formation. J. Biol. Chem. 289, 31066-31076. doi: 10.1074/jbc.M114.595124
    • (2014) J. Biol. Chem , vol.289 , pp. 31066-31076
    • Mansson, C.1    Arosio, P.2    Hussein, R.3    Kampinga, H.H.4    Hashem, R.M.5    Boelens, W.C.6
  • 155
    • 33645829816 scopus 로고    scopus 로고
    • Consequences of the selective blockage of chaperone-mediated autophagy
    • Massey, A. C., Kaushik, S., Sovak, G., Kiffin, R., and Cuervo, A. M. (2006). Consequences of the selective blockage of chaperone-mediated autophagy. Proc. Natl. Acad. Sci. U.S.A. 103, 5805-5810. doi: 10.1073/pnas.0507436103
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 5805-5810
    • Massey, A.C.1    Kaushik, S.2    Sovak, G.3    Kiffin, R.4    Cuervo, A.M.5
  • 156
    • 77955516435 scopus 로고    scopus 로고
    • K11-linked polyubiquitination in cell cycle control revealed by a K11 linkage-specific antibody
    • Matsumoto, M. L., Wickliffe, K. E., Dong, K. C., Yu, C., Bosanac, I., Bustos, D., et al. (2010). K11-linked polyubiquitination in cell cycle control revealed by a K11 linkage-specific antibody. Mol. Cell 39, 477-484. doi: 10.1016/j.molcel.2010.07.001
    • (2010) Mol. Cell , vol.39 , pp. 477-484
    • Matsumoto, M.L.1    Wickliffe, K.E.2    Dong, K.C.3    Yu, C.4    Bosanac, I.5    Bustos, D.6
  • 157
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: a link between the chaperone and proteasome systems
    • McDonough, H., and Patterson, C. (2003). CHIP: a link between the chaperone and proteasome systems. Cell Stress Chaperones 8, 303-308
    • (2003) Cell Stress Chaperones , vol.8 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 158
    • 0036846119 scopus 로고    scopus 로고
    • TorsinA and heat shock proteins act as molecular chaperones: suppression of a-synuclein aggregation
    • McLean, P. J., Kawamata, H., Shariff, S., Hewett, J., Sharma, N., Ueda, K., et al. (2002). TorsinA and heat shock proteins act as molecular chaperones: suppression of a-synuclein aggregation. J. Neurochem. 83, 846-854. doi: 10.1046/j.1471-4159.2002.01190.x
    • (2002) J. Neurochem , vol.83 , pp. 846-854
    • McLean, P.J.1    Kawamata, H.2    Shariff, S.3    Hewett, J.4    Sharma, N.5    Ueda, K.6
  • 159
    • 4344569643 scopus 로고    scopus 로고
    • Geldanamycin induces Hsp70 and prevents a-synuclein aggregation and toxicity in vitro
    • McLean, P. J., Klucken, J., Shin, Y., and Hyman, B. T. (2004). Geldanamycin induces Hsp70 and prevents a-synuclein aggregation and toxicity in vitro. Biochem. Biophys. Res. Commun. 321, 665-669. doi: 10.1016/j.bbrc.2004.07.021
    • (2004) Biochem. Biophys. Res. Commun , vol.321 , pp. 665-669
    • McLean, P.J.1    Klucken, J.2    Shin, Y.3    Hyman, B.T.4
  • 160
    • 84855871792 scopus 로고    scopus 로고
    • Ubiquitin ligase UBR3 regulates cellular levels of the essential DNA repair protein APE1 and is required for genome stability
    • Meisenberg, C., Tait, P. S., Dianova, I. I., Wright, K., Edelmann, M. J., Ternette, N., et al. (2012). Ubiquitin ligase UBR3 regulates cellular levels of the essential DNA repair protein APE1 and is required for genome stability. Nucleic Acids Res. 40, 701-711. doi: 10.1093/nar/gkr744
    • (2012) Nucleic Acids Res , vol.40 , pp. 701-711
    • Meisenberg, C.1    Tait, P.S.2    Dianova, I.I.3    Wright, K.4    Edelmann, M.J.5    Ternette, N.6
  • 161
    • 0036848793 scopus 로고    scopus 로고
    • Purification of polyglutamine aggregates and identification of elongation factor-1a and heat shock protein 84 as aggregate-interacting proteins
    • Mitsui, K., Nakayama, H., Akagi, T., Nekooki, M., Ohtawa, K., Takio, K., et al. (2002). Purification of polyglutamine aggregates and identification of elongation factor-1a and heat shock protein 84 as aggregate-interacting proteins. J. Neurosci. 22, 9267-9277
    • (2002) J. Neurosci , vol.22 , pp. 9267-9277
    • Mitsui, K.1    Nakayama, H.2    Akagi, T.3    Nekooki, M.4    Ohtawa, K.5    Takio, K.6
  • 162
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB
    • Mogk, A., Tomoyasu, T., Goloubinoff, P., Rudiger, S., Roder, D., Langen, H., et al. (1999). Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18, 6934-6949. doi: 10.1093/emboj/18.24.6934
    • (1999) EMBO J , vol.18 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rudiger, S.4    Roder, D.5    Langen, H.6
  • 163
    • 84868115008 scopus 로고    scopus 로고
    • Protein homeostasis, aging and Alzheimer's disease
    • Morawe, T., Hiebel, C., Kern, A., and Behl, C. (2012). Protein homeostasis, aging and Alzheimer's disease. Mol. Neurobiol. 46, 41-54. doi: 10.1007/s12035-012-8246-0
    • (2012) Mol. Neurobiol , vol.46 , pp. 41-54
    • Morawe, T.1    Hiebel, C.2    Kern, A.3    Behl, C.4
  • 164
    • 80053563923 scopus 로고    scopus 로고
    • Misfolded protein aggregates: mechanisms, structures and potential for disease transmission
    • Moreno-Gonzalez, I., and Soto, C. (2011). Misfolded protein aggregates: mechanisms, structures and potential for disease transmission. Semin. Cell Dev. Biol. 22, 482-487. doi: 10.1016/j.semcdb.2011.04.002
    • (2011) Semin. Cell Dev. Biol , vol.22 , pp. 482-487
    • Moreno-Gonzalez, I.1    Soto, C.2
  • 165
    • 3042561822 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Hsp104 enhances the chaperone capacity of human cells and inhibits heat stress-induced proapoptotic signaling
    • Mosser, D. D., Ho, S., and Glover, J. R. (2004). Saccharomyces cerevisiae Hsp104 enhances the chaperone capacity of human cells and inhibits heat stress-induced proapoptotic signaling. Biochemistry 43, 8107-8115. doi: 10.1021/bi0493766
    • (2004) Biochemistry , vol.43 , pp. 8107-8115
    • Mosser, D.D.1    Ho, S.2    Glover, J.R.3
  • 166
    • 84939559331 scopus 로고    scopus 로고
    • Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation
    • Nillegoda, N. B., Kirstein, J., Szlachcic, A., Berynskyy, M., Stank, A., Stengel, F., et al. (2015). Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation. Nature 524, 247-251. doi: 10.1038/nature14884
    • (2015) Nature , vol.524 , pp. 247-251
    • Nillegoda, N.B.1    Kirstein, J.2    Szlachcic, A.3    Berynskyy, M.4    Stank, A.5    Stengel, F.6
  • 167
    • 75749136948 scopus 로고    scopus 로고
    • Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease
    • Neef, D. W., Turski, M. L., and Thiele, D. J. (2010). Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease. PLoS Biol. 8:e1000291. doi: 10.1371/journal.pbio.1000291
    • (2010) PLoS Biol , vol.8
    • Neef, D.W.1    Turski, M.L.2    Thiele, D.J.3
  • 169
    • 33746045662 scopus 로고    scopus 로고
    • 17-AAG, an Hsp90 inhibitor, causes kinetochore defects: a novel mechanism by which 17-AAG inhibits cell proliferation
    • Niikura, Y., Ohta, S., Vandenbeldt, K. J., Abdulle, R., McEwen, B. F., and Kitagawa, K. (2006). 17-AAG, an Hsp90 inhibitor, causes kinetochore defects: a novel mechanism by which 17-AAG inhibits cell proliferation. Oncogene 25, 4133-4146. doi: 10.1038/sj.onc.1209461
    • (2006) Oncogene , vol.25 , pp. 4133-4146
    • Niikura, Y.1    Ohta, S.2    Vandenbeldt, K.J.3    Abdulle, R.4    McEwen, B.F.5    Kitagawa, K.6
  • 170
    • 77954196466 scopus 로고    scopus 로고
    • Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins
    • Nillegoda, N. B., Theodoraki, M. A., Mandal, A. K., Mayo, K. J., Ren, H. Y., Sultana, R., et al. (2010). Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins. Mol. Biol. Cell 21, 2102-2116. doi: 10.1091/mbc.E10-02-0098
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2102-2116
    • Nillegoda, N.B.1    Theodoraki, M.A.2    Mandal, A.K.3    Mayo, K.J.4    Ren, H.Y.5    Sultana, R.6
  • 171
    • 2342652188 scopus 로고    scopus 로고
    • Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation
    • Nollen, E. A., Garcia, S. M., van Haaften, G., Kim, S., Chavez, A., Morimoto, R. I., et al. (2004). Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation. Proc. Natl. Acad. Sci. U.S.A. 101, 6403-6408. doi: 10.1073/pnas.0307697101
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 6403-6408
    • Nollen, E.A.1    Garcia, S.M.2    van Haaften, G.3    Kim, S.4    Chavez, A.5    Morimoto, R.I.6
  • 172
    • 84883403943 scopus 로고    scopus 로고
    • Molecular chaperone mediated late-stage neuroprotection in the SOD1(G93A) mouse model of amyotrophic lateral sclerosis
    • Novoselov, S. S., Mustill, W. J., Gray, A. L., Dick, J. R., Kanuga, N., Kalmar, B., et al. (2013). Molecular chaperone mediated late-stage neuroprotection in the SOD1(G93A) mouse model of amyotrophic lateral sclerosis. PLoS ONE 8:e73944. doi: 10.1371/journal.pone.0073944
    • (2013) PLoS ONE , vol.8
    • Novoselov, S.S.1    Mustill, W.J.2    Gray, A.L.3    Dick, J.R.4    Kanuga, N.5    Kalmar, B.6
  • 173
    • 0037470073 scopus 로고    scopus 로고
    • Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity
    • Odunuga, O. O., Hornby, J. A., Bies, C., Zimmermann, R., Pugh, D. J., and Blatch, G. L. (2003). Tetratricopeptide repeat motif-mediated Hsc70-mSTI1 interaction. Molecular characterization of the critical contacts for successful binding and specificity. J. Biol. Chem. 278, 6896-6904. doi: 10.1074/jbc.M206867200
    • (2003) J. Biol. Chem , vol.278 , pp. 6896-6904
    • Odunuga, O.O.1    Hornby, J.A.2    Bies, C.3    Zimmermann, R.4    Pugh, D.J.5    Blatch, G.L.6
  • 174
    • 40349116061 scopus 로고    scopus 로고
    • Genomic evidence for independent origins of ß-like globin genes in monotremes and therian mammals
    • Opazo, J. C., Hoffmann, F. G., and Storz, J. F. (2008). Genomic evidence for independent origins of ß-like globin genes in monotremes and therian mammals. Proc. Natl. Acad. Sci. U.S.A. 105, 1590-1595. doi: 10.1073/pnas.0710531105
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 1590-1595
    • Opazo, J.C.1    Hoffmann, F.G.2    Storz, J.F.3
  • 175
    • 44849125207 scopus 로고    scopus 로고
    • Formation of toxic oligomeric a-synuclein species in living cells
    • Outeiro, T. F., Putcha, P., Tetzlaff, J. E., Spoelgen, R., Koker, M., Carvalho, F., et al. (2008). Formation of toxic oligomeric a-synuclein species in living cells. PLoS ONE 3:e1867. doi: 10.1371/journal.pone.0001867
    • (2008) PLoS ONE , vol.3
    • Outeiro, T.F.1    Putcha, P.2    Tetzlaff, J.E.3    Spoelgen, R.4    Koker, M.5    Carvalho, F.6
  • 176
    • 77950377674 scopus 로고    scopus 로고
    • Reduction of ß-amyloid pathology by celastrol in a transgenic mouse model of Alzheimer's disease
    • Paris, D., Ganey, N. J., Laporte, V., Patel, N. S., Beaulieu-Abdelahad, D., Bachmeier, C., et al. (2010). Reduction of ß-amyloid pathology by celastrol in a transgenic mouse model of Alzheimer's disease. J. Neuroinflammation 7:17. doi: 10.1186/1742-2094-7-17
    • (2010) J. Neuroinflammation , vol.7 , pp. 17
    • Paris, D.1    Ganey, N.J.2    Laporte, V.3    Patel, N.S.4    Beaulieu-Abdelahad, D.5    Bachmeier, C.6
  • 177
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell, D. A., Kowal, A. S., Singer, M. A., and Lindquist, S. (1994). Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372, 475-478. doi: 10.1038/372475a0
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 178
    • 17044403380 scopus 로고    scopus 로고
    • Hsp27 and Hsp70 administered in combination have a potent protective effect against FALS-associated SOD1-mutant-induced cell death in mammalian neuronal cells
    • Patel, Y. J., Payne Smith, M. D., de Belleroche, J., and Latchman, D. S. (2005). Hsp27 and Hsp70 administered in combination have a potent protective effect against FALS-associated SOD1-mutant-induced cell death in mammalian neuronal cells. Brain Res. Mol. Brain Res. 134, 256-274. doi: 10.1016/j.molbrainres.2004.10.028
    • (2005) Brain Res. Mol. Brain Res , vol.134 , pp. 256-274
    • Patel, Y.J.1    Payne Smith, M.D.2    de Belleroche, J.3    Latchman, D.S.4
  • 179
    • 34248366452 scopus 로고    scopus 로고
    • Chaperoning Anfinsen: the steric foldases
    • Pauwels, K., Van Molle, I., Tommassen, J., and Van Gelder, P. (2007). Chaperoning Anfinsen: the steric foldases. Mol. Microbiol. 64, 917-922. doi: 10.1111/j.1365-2958.2007.05718.x
    • (2007) Mol. Microbiol , vol.64 , pp. 917-922
    • Pauwels, K.1    Van Molle, I.2    Tommassen, J.3    Van Gelder, P.4
  • 180
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl, L. H., and Prodromou, C. (2006). Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75, 271-294. doi: 10.1146/annurev.biochem.75.103004.142738
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 182
    • 34247245632 scopus 로고    scopus 로고
    • Neuroprotection by Hsp104 and Hsp27 in lentiviral-based rat models of Huntington's disease
    • Perrin, V., Regulier, E., Abbas-Terki, T., Hassig, R., Brouillet, E., Aebischer, P., et al. (2007). Neuroprotection by Hsp104 and Hsp27 in lentiviral-based rat models of Huntington's disease. Mol. Ther. 15, 903-911. doi: 10.1038/mt.sj.6300141
    • (2007) Mol. Ther , vol.15 , pp. 903-911
    • Perrin, V.1    Regulier, E.2    Abbas-Terki, T.3    Hassig, R.4    Brouillet, E.5    Aebischer, P.6
  • 183
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • Picard, D. (2002). Heat-shock protein 90, a chaperone for folding and regulation. Cell. Mol. Life Sci. 59, 1640-1648. doi: 10.1007/PL00012491
    • (2002) Cell. Mol. Life Sci , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 184
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. (2001). Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533. doi: 10.1146/annurev.biochem.70.1.503
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 185
    • 44649110104 scopus 로고    scopus 로고
    • Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding
    • Polier, S., Dragovic, Z., Hartl, F. U., and Bracher, A. (2008). Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 133, 1068-1079. doi: 10.1016/j.cell.2008.05.022
    • (2008) Cell , vol.133 , pp. 1068-1079
    • Polier, S.1    Dragovic, Z.2    Hartl, F.U.3    Bracher, A.4
  • 186
    • 77954178073 scopus 로고    scopus 로고
    • A nucleus-based quality control mechanism for cytosolic proteins
    • Prasad, R., Kawaguchi, S., and Ng, D. T. (2010). A nucleus-based quality control mechanism for cytosolic proteins. Mol. Biol. Cell 21, 2117-2127. doi: 10.1091/mbc.E10-02-0111
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2117-2127
    • Prasad, R.1    Kawaguchi, S.2    Ng, D.T.3
  • 187
    • 77249101456 scopus 로고    scopus 로고
    • Brain-permeable small-molecule inhibitors of Hsp90 prevent a-synuclein oligomer formation and rescue a-synuclein-induced toxicity
    • Putcha, P., Danzer, K. M., Kranich, L. R., Scott, A., Silinski, M., Mabbett, S., et al. (2010). Brain-permeable small-molecule inhibitors of Hsp90 prevent a-synuclein oligomer formation and rescue a-synuclein-induced toxicity. J. Pharmacol. Exp. Ther. 332, 849-857. doi: 10.1124/jpet.109.158436
    • (2010) J. Pharmacol. Exp. Ther , vol.332 , pp. 849-857
    • Putcha, P.1    Danzer, K.M.2    Kranich, L.R.3    Scott, A.4    Silinski, M.5    Mabbett, S.6
  • 188
    • 33645293437 scopus 로고    scopus 로고
    • CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70
    • Qian, S. B., McDonough, H., Boellmann, F., Cyr, D. M., and Patterson, C. (2006). CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70. Nature 440, 551-555. doi: 10.1038/nature04600
    • (2006) Nature , vol.440 , pp. 551-555
    • Qian, S.B.1    McDonough, H.2    Boellmann, F.3    Cyr, D.M.4    Patterson, C.5
  • 189
    • 0029146852 scopus 로고
    • Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site
    • Quan, H., Fan, G., and Wang, C. C. (1995). Independence of the chaperone activity of protein disulfide isomerase from its thioredoxin-like active site. J. Biol. Chem. 270, 17078-17080
    • (1995) J. Biol. Chem , vol.270 , pp. 17078-17080
    • Quan, H.1    Fan, G.2    Wang, C.C.3
  • 190
    • 42749092501 scopus 로고    scopus 로고
    • Expression of the small heat shock protein family in the mouse CNS: differential anatomical and biochemical compartmentalization
    • Quraishe, S., Asuni, A., Boelens, W. C., O'Connor, V., and Wyttenbach, A. (2008). Expression of the small heat shock protein family in the mouse CNS: differential anatomical and biochemical compartmentalization. Neuroscience 153, 483-491. doi: 10.1016/j.neuroscience.2008.01.058
    • (2008) Neuroscience , vol.153 , pp. 483-491
    • Quraishe, S.1    Asuni, A.2    Boelens, W.C.3    O'Connor, V.4    Wyttenbach, A.5
  • 191
    • 34250659732 scopus 로고    scopus 로고
    • Huntington's disease: pathological mechanisms and therapeutic strategies
    • Ramaswamy, S., Shannon, K. M., and Kordower, J. H. (2007). Huntington's disease: pathological mechanisms and therapeutic strategies. Cell Transplant. 16, 301-312. doi: 10.3727/000000007783464687
    • (2007) Cell Transplant , vol.16 , pp. 301-312
    • Ramaswamy, S.1    Shannon, K.M.2    Kordower, J.H.3
  • 192
    • 84868525116 scopus 로고    scopus 로고
    • Metazoan Hsp70 machines use Hsp110 to power protein disaggregation
    • Rampelt, H., Kirstein-Miles, J., Nillegoda, N. B., Chi, K., Scholz, S. R., Morimoto, R. I., et al. (2012). Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. EMBO J. 31, 4221-4235. doi: 10.1038/emboj.2012.264
    • (2012) EMBO J , vol.31 , pp. 4221-4235
    • Rampelt, H.1    Kirstein-Miles, J.2    Nillegoda, N.B.3    Chi, K.4    Scholz, S.R.5    Morimoto, R.I.6
  • 193
    • 85012505857 scopus 로고    scopus 로고
    • Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones
    • Ranford, J. C., Coates, A. R., and Henderson, B. (2000). Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones. Expert Rev. Mol. Med. 2, 1-17. doi: 10.1017/S1462399400002015
    • (2000) Expert Rev. Mol. Med , vol.2 , pp. 1-17
    • Ranford, J.C.1    Coates, A.R.2    Henderson, B.3
  • 194
    • 77958005847 scopus 로고    scopus 로고
    • Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle
    • Ratzke, C., Mickler, M., Hellenkamp, B., Buchner, J., and Hugel, T. (2010). Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle. Proc. Natl. Acad. Sci. U.S.A. 107, 16101-16106. doi: 10.1073/pnas.1000916107
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 16101-16106
    • Ratzke, C.1    Mickler, M.2    Hellenkamp, B.3    Buchner, J.4    Hugel, T.5
  • 195
    • 84934444265 scopus 로고    scopus 로고
    • Clearance of mutant aggregate-prone proteins by autophagy
    • Ravikumar, B., Sarkar, S., and Rubinsztein, D. C. (2008). Clearance of mutant aggregate-prone proteins by autophagy. Methods Mol. Biol. 445, 195-211. doi: 10.1007/978-1-59745-157-4_13
    • (2008) Methods Mol. Biol , vol.445 , pp. 195-211
    • Ravikumar, B.1    Sarkar, S.2    Rubinsztein, D.C.3
  • 196
    • 0028337668 scopus 로고
    • No global neocortical nerve cell loss in brains from patients with senile dementia of Alzheimer's type
    • Regeur, L., Jensen, G. B., Pakkenberg, H., Evans, S. M., and Pakkenberg, B. (1994). No global neocortical nerve cell loss in brains from patients with senile dementia of Alzheimer's type. Neurobiol. Aging 15, 347-352
    • (1994) Neurobiol. Aging , vol.15 , pp. 347-352
    • Regeur, L.1    Jensen, G.B.2    Pakkenberg, H.3    Evans, S.M.4    Pakkenberg, B.5
  • 197
    • 3242770627 scopus 로고    scopus 로고
    • Interaction of the molecular chaperone aB-crystallin with a-synuclein: effects on amyloid fibril formation and chaperone activity
    • Rekas, A., Adda, C. G., Andrew Aquilina, J., Barnham, K. J., Sunde, M., Galatis, D., et al. (2004). Interaction of the molecular chaperone aB-crystallin with a-synuclein: effects on amyloid fibril formation and chaperone activity. J. Mol. Biol. 340, 1167-1183. doi: 10.1016/j.jmb.2004.05.054
    • (2004) J. Mol. Biol , vol.340 , pp. 1167-1183
    • Rekas, A.1    Adda, C.G.2    Andrew Aquilina, J.3    Barnham, K.J.4    Sunde, M.5    Galatis, D.6
  • 198
    • 36749037242 scopus 로고    scopus 로고
    • Monitoring the prevention of amyloid fibril formation by a-crystallin. Temperature dependence and the nature of the aggregating species
    • Rekas, A., Jankova, L., Thorn, D. C., Cappai, R., and Carver, J. A. (2007). Monitoring the prevention of amyloid fibril formation by a-crystallin. Temperature dependence and the nature of the aggregating species. FEBS J. 274, 6290-6304. doi: 10.1111/j.1742-4658.2007.06144.x
    • (2007) FEBS J , vol.274 , pp. 6290-6304
    • Rekas, A.1    Jankova, L.2    Thorn, D.C.3    Cappai, R.4    Carver, J.A.5
  • 199
    • 84875441083 scopus 로고    scopus 로고
    • The changing scene of amyotrophic lateral sclerosis
    • Robberecht, W., and Philips, T. (2013). The changing scene of amyotrophic lateral sclerosis. Nat. Rev. Neurosci. 14, 248-264. doi: 10.1038/nrn3430
    • (2013) Nat. Rev. Neurosci , vol.14 , pp. 248-264
    • Robberecht, W.1    Philips, T.2
  • 200
    • 84904567733 scopus 로고    scopus 로고
    • Cytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6
    • Rodrigo-Brenni, M. C., Gutierrez, E., and Hegde, R. S. (2014). Cytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6. Mol. Cell 55, 227-237. doi: 10.1016/j.molcel.2014.05.025
    • (2014) Mol. Cell , vol.55 , pp. 227-237
    • Rodrigo-Brenni, M.C.1    Gutierrez, E.2    Hegde, R.S.3
  • 201
    • 78650278301 scopus 로고    scopus 로고
    • Huntington's disease: a clinical review
    • Roos, R. A. (2010). Huntington's disease: a clinical review. Orphanet J. Rare Dis. 5:40. doi: 10.1186/1750-1172-5-40
    • (2010) Orphanet J. Rare Dis , vol.5 , pp. 40
    • Roos, R.A.1
  • 202
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., et al. (1993). Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362, 59-62. doi: 10.1038/362059a0
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3    Figlewicz, D.A.4    Sapp, P.5    Hentati, A.6
  • 203
    • 78650731442 scopus 로고    scopus 로고
    • Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates
    • Rosenbaum, J. C., Fredrickson, E. K., Oeser, M. L., Garrett-Engele, C. M., Locke, M. N., Richardson, L. A., et al. (2011). Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. Mol. Cell 41, 93-106. doi: 10.1016/j.molcel.2010.12.004
    • (2011) Mol. Cell , vol.41 , pp. 93-106
    • Rosenbaum, J.C.1    Fredrickson, E.K.2    Oeser, M.L.3    Garrett-Engele, C.M.4    Locke, M.N.5    Richardson, L.A.6
  • 204
    • 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
  • 205
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • Rudiger, S., Germeroth, L., Schneider-Mergener, J., and Bukau, B. (1997). Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16, 1501-1507. doi: 10.1093/emboj/16.7.1501
    • (1997) EMBO J , vol.16 , pp. 1501-1507
    • Rudiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 206
    • 0034057881 scopus 로고    scopus 로고
    • Heat shock proteins in human cancer
    • Sarto, C., Binz, P. A., and Mocarelli, P. (2000). Heat shock proteins in human cancer. Electrophoresis 21, 1218-1226. doi: 10.1002/(SICI)1522-2683(20000401)21:6<1218::AID-ELPS1218>3.0.CO;2-H
    • (2000) Electrophoresis , vol.21 , pp. 1218-1226
    • Sarto, C.1    Binz, P.A.2    Mocarelli, P.3
  • 207
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • Schulte, T. W., and Neckers, L. M. (1998). The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother. Pharmacol. 42, 273-279. doi: 10.1007/s002800050817
    • (1998) Cancer Chemother. Pharmacol , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 208
    • 84870792675 scopus 로고    scopus 로고
    • Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces
    • Seyffer, F., Kummer, E., Oguchi, Y., Winkler, J., Kumar, M., Zahn, R., et al. (2012). Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces. Nat. Struct. Mol. Biol. 19, 1347-1355. doi: 10.1038/nsmb.2442
    • (2012) Nat. Struct. Mol. Biol , vol.19 , pp. 1347-1355
    • Seyffer, F.1    Kummer, E.2    Oguchi, Y.3    Winkler, J.4    Kumar, M.5    Zahn, R.6
  • 209
    • 80053379382 scopus 로고    scopus 로고
    • Binding of the molecular chaperone aB-crystallin to Aß amyloid fibrils inhibits fibril elongation
    • Shammas, S. L., Waudby, C. A., Wang, S., Buell, A. K., Knowles, T. P., Ecroyd, H., et al. (2011). Binding of the molecular chaperone aB-crystallin to Aß amyloid fibrils inhibits fibril elongation. Biophys. J. 101, 1681-1689. doi: 10.1016/j.bpj.2011.07.056
    • (2011) Biophys. J , vol.101 , pp. 1681-1689
    • Shammas, S.L.1    Waudby, C.A.2    Wang, S.3    Buell, A.K.4    Knowles, T.P.5    Ecroyd, H.6
  • 210
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-ß protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., et al. (2008). Amyloid-ß protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat. Med. 14, 837-842. doi: 10.1038/nm1782
    • (2008) Nat. Med , vol.14 , pp. 837-842
    • Shankar, G.M.1    Li, S.2    Mehta, T.H.3    Garcia-Munoz, A.4    Shepardson, N.E.5    Smith, I.6
  • 212
    • 0037411555 scopus 로고    scopus 로고
    • Neurodegenerative disorders of protein aggregation
    • Shastry, B. S. (2003). Neurodegenerative disorders of protein aggregation. Neurochem. Int. 43, 1-7. doi: 10.1016/S0197-0186(02)00196-1
    • (2003) Neurochem. Int , vol.43 , pp. 1-7
    • Shastry, B.S.1
  • 213
    • 28844451001 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice
    • Shen, H. Y., He, J. C., Wang, Y., Huang, Q. Y., and Chen, J. F. (2005). Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice. J. Biol. Chem. 280, 39962-39969. doi: 10.1074/jbc.M505524200
    • (2005) J. Biol. Chem , vol.280 , pp. 39962-39969
    • Shen, H.Y.1    He, J.C.2    Wang, Y.3    Huang, Q.Y.4    Chen, J.F.5
  • 214
    • 80054699747 scopus 로고    scopus 로고
    • The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system
    • Shorter, J. (2011). The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS ONE 6:e26319. doi: 10.1371/journal.pone.0026319
    • (2011) PLoS ONE , vol.6
    • Shorter, J.1
  • 215
    • 2942722444 scopus 로고    scopus 로고
    • Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • Shorter, J., and Lindquist, S. (2004). Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 304, 1793-1797. doi: 10.1126/science.1098007
    • (2004) Science , vol.304 , pp. 1793-1797
    • Shorter, J.1    Lindquist, S.2
  • 216
    • 0038413759 scopus 로고    scopus 로고
    • Aggregated and monomeric a-synuclein bind to the S6' proteasomal protein and inhibit proteasomal function
    • Snyder, H., Mensah, K., Theisler, C., Lee, J., Matouschek, A., and Wolozin, B. (2003). Aggregated and monomeric a-synuclein bind to the S6' proteasomal protein and inhibit proteasomal function. J. Biol. Chem. 278, 11753-11759. doi: 10.1074/jbc.M208641200
    • (2003) J. Biol. Chem , vol.278 , pp. 11753-11759
    • Snyder, H.1    Mensah, K.2    Theisler, C.3    Lee, J.4    Matouschek, A.5    Wolozin, B.6
  • 217
    • 0032568534 scopus 로고    scopus 로고
    • a-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies
    • Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., and Goedert, M. (1998). a-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies. Proc. Natl. Acad. Sci. U.S.A. 95, 6469-6473
    • (1998) Proc. Natl. Acad. Sci. U.S.A , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 218
    • 60549087904 scopus 로고    scopus 로고
    • Multivalency-assisted control of intracellular signaling pathways: application for ubiquitin-dependent N-end rule pathway
    • Sriram, S. M., Banerjee, R., Kane, R. S., and Kwon, Y. T. (2009). Multivalency-assisted control of intracellular signaling pathways: application for ubiquitin-dependent N-end rule pathway. Chem. Biol. 16, 121-131. doi: 10.1016/j.chembiol.2009.01.012
    • (2009) Chem. Biol , vol.16 , pp. 121-131
    • Sriram, S.M.1    Banerjee, R.2    Kane, R.S.3    Kwon, Y.T.4
  • 219
    • 80054958053 scopus 로고    scopus 로고
    • The N-end rule pathway: emerging functions and molecular principles of substrate recognition
    • Sriram, S. M., Kim, B. Y., and Kwon, Y. T. (2011). The N-end rule pathway: emerging functions and molecular principles of substrate recognition. Nat. Rev. Mol. Cell Biol. 12, 735-747. doi: 10.1038/nrm3217
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 735-747
    • Sriram, S.M.1    Kim, B.Y.2    Kwon, Y.T.3
  • 220
    • 77957768979 scopus 로고    scopus 로고
    • The molecular principles of N-end rule recognition
    • Sriram, S. M., and Kwon, Y. T. (2010). The molecular principles of N-end rule recognition. Nat. Struct. Mol. Biol. 17, 1164-1165. doi: 10.1038/nsmb1010-1164
    • (2010) Nat. Struct. Mol. Biol , vol.17 , pp. 1164-1165
    • Sriram, S.M.1    Kwon, Y.T.2
  • 222
    • 84901815187 scopus 로고    scopus 로고
    • Cargo recognition and trafficking in selective autophagy
    • Stolz, A., Ernst, A., and Dikic, I. (2014). Cargo recognition and trafficking in selective autophagy. Nat. Cell Biol. 16, 495-501. doi: 10.1038/ncb2979
    • (2014) Nat. Cell Biol , vol.16 , pp. 495-501
    • Stolz, A.1    Ernst, A.2    Dikic, I.3
  • 223
    • 65549103025 scopus 로고    scopus 로고
    • Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones
    • Summers, D. W., Douglas, P. M., Ramos, C. H., and Cyr, D. M. (2009). Polypeptide transfer from Hsp40 to Hsp70 molecular chaperones. Trends Biochem. Sci. 34, 230-233. doi: 10.1016/j.tibs.2008.12.009
    • (2009) Trends Biochem. Sci , vol.34 , pp. 230-233
    • Summers, D.W.1    Douglas, P.M.2    Ramos, C.H.3    Cyr, D.M.4
  • 224
    • 20444478694 scopus 로고    scopus 로고
    • The small heat shock proteins and their role in human disease
    • Sun, Y., and MacRae, T. H. (2005). The small heat shock proteins and their role in human disease. FEBS J. 272, 2613-2627. doi: 10.1111/j.1742-4658.2005.04708.x
    • (2005) FEBS J , vol.272 , pp. 2613-2627
    • Sun, Y.1    MacRae, T.H.2
  • 225
    • 84866478442 scopus 로고    scopus 로고
    • The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system
    • Tai, H. C., Serrano-Pozo, A., Hashimoto, T., Frosch, M. P., Spires-Jones, T. L., and Hyman, B. T. (2012). The synaptic accumulation of hyperphosphorylated tau oligomers in Alzheimer disease is associated with dysfunction of the ubiquitin-proteasome system. Am. J. Pathol. 181, 1426-1435. doi: 10.1016/j.ajpath.2012.06.033
    • (2012) Am. J. Pathol , vol.181 , pp. 1426-1435
    • Tai, H.C.1    Serrano-Pozo, A.2    Hashimoto, T.3    Frosch, M.P.4    Spires-Jones, T.L.5    Hyman, B.T.6
  • 226
    • 77953916528 scopus 로고    scopus 로고
    • HSP90 at the hub of protein homeostasis: emerging mechanistic insights
    • Taipale, M., Jarosz, D. F., and Lindquist, S. (2010). HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat. Rev. Mol. Cell Biol. 11, 515-528. doi: 10.1038/nrm2918
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 515-528
    • Taipale, M.1    Jarosz, D.F.2    Lindquist, S.3
  • 227
  • 228
    • 35548974677 scopus 로고    scopus 로고
    • The mammalian N-end rule pathway: new insights into its components and physiological roles
    • Tasaki, T., and Kwon, Y. T. (2007). The mammalian N-end rule pathway: new insights into its components and physiological roles. Trends Biochem. Sci. 32, 520-528. doi: 10.1016/j.tibs.2007.08.010
    • (2007) Trends Biochem. Sci , vol.32 , pp. 520-528
    • Tasaki, T.1    Kwon, Y.T.2
  • 229
    • 23344452833 scopus 로고    scopus 로고
    • A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons
    • Tasaki, T., Mulder, L. C., Iwamatsu, A., Lee, M. J., Davydov, I. V., Varshavsky, A., et al. (2005). A family of mammalian E3 ubiquitin ligases that contain the UBR box motif and recognize N-degrons. Mol. Cell. Biol. 25, 7120-7136. doi: 10.1128/MCB.25.16.7120-7136.2005
    • (2005) Mol. Cell. Biol , vol.25 , pp. 7120-7136
    • Tasaki, T.1    Mulder, L.C.2    Iwamatsu, A.3    Lee, M.J.4    Davydov, I.V.5    Varshavsky, A.6
  • 230
    • 59449093066 scopus 로고    scopus 로고
    • The substrate recognition domains of the N-end rule pathway
    • Tasaki, T., Zakrzewska, A., Dudgeon, D. D., Jiang, Y., Lazo, J. S., and Kwon, Y. T. (2009). The substrate recognition domains of the N-end rule pathway. J. Biol. Chem. 284, 1884-1895. doi: 10.1074/jbc.M803641200
    • (2009) J. Biol. Chem , vol.284 , pp. 1884-1895
    • Tasaki, T.1    Zakrzewska, A.2    Dudgeon, D.D.3    Jiang, Y.4    Lazo, J.S.5    Kwon, Y.T.6
  • 231
    • 84880070798 scopus 로고    scopus 로고
    • Prefoldin protects neuronal cells from polyglutamine toxicity by preventing aggregation formation
    • Tashiro, E., Zako, T., Muto, H., Itoo, Y., Sorgjerd, K., Terada, N., et al. (2013). Prefoldin protects neuronal cells from polyglutamine toxicity by preventing aggregation formation. J. Biol. Chem. 288, 19958-19972. doi: 10.1074/jbc.M113.477984
    • (2013) J. Biol. Chem , vol.288 , pp. 19958-19972
    • Tashiro, E.1    Zako, T.2    Muto, H.3    Itoo, Y.4    Sorgjerd, K.5    Terada, N.6
  • 232
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor, J. P., Hardy, J., and Fischbeck, K. H. (2002). Toxic proteins in neurodegenerative disease. Science 296, 1991-1995. doi: 10.1126/science.1067122
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 233
    • 84893855426 scopus 로고    scopus 로고
    • The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins
    • Torrente, M. P., and Shorter, J. (2013). The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins. Prion 7, 457-463. doi: 10.4161/pri.27531
    • (2013) Prion , vol.7 , pp. 457-463
    • Torrente, M.P.1    Shorter, J.2
  • 234
    • 43449099127 scopus 로고    scopus 로고
    • The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors
    • Tsuda, H., Han, S. M., Yang, Y., Tong, C., Lin, Y. Q., Mohan, K., et al. (2008). The amyotrophic lateral sclerosis 8 protein VAPB is cleaved, secreted, and acts as a ligand for Eph receptors. Cell 133, 963-977. doi: 10.1016/j.cell.2008.04.039
    • (2008) Cell , vol.133 , pp. 963-977
    • Tsuda, H.1    Han, S.M.2    Yang, Y.3    Tong, C.4    Lin, Y.Q.5    Mohan, K.6
  • 235
    • 77949890661 scopus 로고    scopus 로고
    • Heat shock proteins; an overview
    • Tutar, L., and Tutar, Y. (2010). Heat shock proteins; an overview. Curr. Pharm. Biotechnol. 11, 216-222
    • (2010) Curr. Pharm. Biotechnol , vol.11 , pp. 216-222
    • Tutar, L.1    Tutar, Y.2
  • 236
    • 58149380769 scopus 로고    scopus 로고
    • Differential activities of the ubiquitin-proteasome system in neurons versus glia may account for the preferential accumulation of misfolded proteins in neurons
    • Tydlacka, S., Wang, C. E., Wang, X., Li, S., and Li, X. J. (2008). Differential activities of the ubiquitin-proteasome system in neurons versus glia may account for the preferential accumulation of misfolded proteins in neurons. J. Neurosci. 28, 13285-13295. doi: 10.1523/JNEUROSCI.4393-08.2008
    • (2008) J. Neurosci , vol.28 , pp. 13285-13295
    • Tydlacka, S.1    Wang, C.E.2    Wang, X.3    Li, S.4    Li, X.J.5
  • 237
    • 38449094180 scopus 로고    scopus 로고
    • Role of the ubiquitin proteasome system in Alzheimer's disease
    • Upadhya, S. C., and Hegde, A. N. (2007). Role of the ubiquitin proteasome system in Alzheimer's disease. BMC Biochem. 8 (Suppl. 1):S12. doi: 10.1186/1471-2091-8-S1-S12
    • (2007) BMC Biochem , vol.8
    • Upadhya, S.C.1    Hegde, A.N.2
  • 238
    • 27944499891 scopus 로고    scopus 로고
    • Overexpression of yeast hsp104 reduces polyglutamine aggregation and prolongs survival of a transgenic mouse model of Huntington's disease
    • Vacher, C., Garcia-Oroz, L., and Rubinsztein, D. C. (2005). Overexpression of yeast hsp104 reduces polyglutamine aggregation and prolongs survival of a transgenic mouse model of Huntington's disease. Hum. Mol. Genet. 14, 3425-3433. doi: 10.1093/hmg/ddi372
    • (2005) Hum. Mol. Genet , vol.14 , pp. 3425-3433
    • Vacher, C.1    Garcia-Oroz, L.2    Rubinsztein, D.C.3
  • 239
    • 84892408458 scopus 로고    scopus 로고
    • Mechanisms of protein-folding diseases at a glance
    • Valastyan, J. S., and Lindquist, S. (2014). Mechanisms of protein-folding diseases at a glance. Dis. Model. Mech. 7, 9-14. doi: 10.1242/dmm.013474
    • (2014) Dis. Model. Mech , vol.7 , pp. 9-14
    • Valastyan, J.S.1    Lindquist, S.2
  • 240
    • 79960683356 scopus 로고    scopus 로고
    • The N-end rule pathway and regulation by proteolysis
    • Varshavsky, A. (2011). The N-end rule pathway and regulation by proteolysis. Protein Sci. 20, 1298-1345. doi: 10.1002/pro.666
    • (2011) Protein Sci , vol.20 , pp. 1298-1345
    • Varshavsky, A.1
  • 241
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: endoplasmic reticulum-associated degradation
    • Vembar, S. S., and Brodsky, J. L. (2008). One step at a time: endoplasmic reticulum-associated degradation. Nat. Rev. Mol. Cell Biol. 9, 944-957. doi: 10.1038/nrm2546
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 242
    • 78149266599 scopus 로고    scopus 로고
    • HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones
    • Vos, M. J., Zijlstra, M. P., Kanon, B., van Waarde-Verhagen, M. A., Brunt, E. R., Oosterveld-Hut, H. M., et al. (2010). HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones. Hum. Mol. Genet. 19, 4677-4693. doi: 10.1093/hmg/ddq398
    • (2010) Hum. Mol. Genet , vol.19 , pp. 4677-4693
    • Vos, M.J.1    Zijlstra, M.P.2    Kanon, B.3    van Waarde-Verhagen, M.A.4    Brunt, E.R.5    Oosterveld-Hut, H.M.6
  • 243
    • 67650745109 scopus 로고    scopus 로고
    • Loss of Hsp70 exacerbates pathogenesis but not levels of fibrillar aggregates in a mouse model of Huntington's disease
    • Wacker, J. L., Huang, S. Y., Steele, A. D., Aron, R., Lotz, G. P., Nguyen, Q., et al. (2009). Loss of Hsp70 exacerbates pathogenesis but not levels of fibrillar aggregates in a mouse model of Huntington's disease. J. Neurosci. 29, 9104-9114. doi: 10.1523/JNEUROSCI.2250-09.2009
    • (2009) J. Neurosci , vol.29 , pp. 9104-9114
    • Wacker, J.L.1    Huang, S.Y.2    Steele, A.D.3    Aron, R.4    Lotz, G.P.5    Nguyen, Q.6
  • 244
    • 74249084267 scopus 로고    scopus 로고
    • Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis
    • Walker, A. K., Farg, M. A., Bye, C. R., McLean, C. A., Horne, M. K., and Atkin, J. D. (2010). Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis. Brain 133(Pt 1), 105-116. doi: 10.1093/brain/awp267
    • (2010) Brain , vol.133 , pp. 105-116
    • Walker, A.K.1    Farg, M.A.2    Bye, C.R.3    McLean, C.A.4    Horne, M.K.5    Atkin, J.D.6
  • 245
    • 84896710448 scopus 로고    scopus 로고
    • ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation
    • Walker, A. K., Soo, K. Y., Sundaramoorthy, V., Parakh, S., Ma, Y., Farg, M. A., et al. (2013). ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation. PLoS ONE 8:e81170. doi: 10.1371/journal.pone.0081170
    • (2013) PLoS ONE , vol.8
    • Walker, A.K.1    Soo, K.Y.2    Sundaramoorthy, V.3    Parakh, S.4    Ma, Y.5    Farg, M.A.6
  • 246
    • 34250011799 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and its role in inflammatory and autoimmune diseases
    • Wang, J., and 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
  • 247
    • 26844539619 scopus 로고    scopus 로고
    • Novel insights into the mechanism of chaperone-assisted protein disaggregation
    • Weibezahn, J., Schlieker, C., Tessarz, P., Mogk, A., and Bukau, B. (2005). Novel insights into the mechanism of chaperone-assisted protein disaggregation. Biol. Chem. 386, 739-744. doi: 10.1515/BC.2005.086
    • (2005) Biol. Chem , vol.386 , pp. 739-744
    • Weibezahn, J.1    Schlieker, C.2    Tessarz, P.3    Mogk, A.4    Bukau, B.5
  • 248
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell, L., and Lindquist, S. L. (2005). HSP90 and the chaperoning of cancer. Nat. Rev. Cancer 5, 761-772. doi: 10.1038/nrc1716
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 249
    • 0025801067 scopus 로고
    • Proteins containing peptide sequences related to Lys-Phe-Glu-Arg-Gln are selectively depleted in liver and heart, but not skeletal muscle, of fasted rats
    • Wing, S. S., Chiang, H. L., Goldberg, A. L., and Dice, J. F. (1991). Proteins containing peptide sequences related to Lys-Phe-Glu-Arg-Gln are selectively depleted in liver and heart, but not skeletal muscle, of fasted rats. Biochem. J. 275 (Pt 1), 165-169
    • (1991) Biochem. J , vol.275 , pp. 165-169
    • Wing, S.S.1    Chiang, H.L.2    Goldberg, A.L.3    Dice, J.F.4
  • 250
    • 84864387363 scopus 로고    scopus 로고
    • Chaperone networks in protein disaggregation and prion propagation
    • Winkler, J., Tyedmers, J., Bukau, B., and Mogk, A. (2012). Chaperone networks in protein disaggregation and prion propagation. J. Struct. Biol. 179, 152-160. doi: 10.1016/j.jsb.2012.05.002
    • (2012) J. Struct. Biol , vol.179 , pp. 152-160
    • Winkler, J.1    Tyedmers, J.2    Bukau, B.3    Mogk, A.4
  • 251
    • 79959728747 scopus 로고    scopus 로고
    • Epidemiology and etiology of Parkinson's disease: a review of the evidence
    • Wirdefeldt, K., Adami, H. O., Cole, P., Trichopoulos, D., and Mandel, J. (2011). Epidemiology and etiology of Parkinson's disease: a review of the evidence. Eur. J. Epidemiol. 26 (Suppl. 1), S1-S58. doi: 10.1007/s10654-011-9581-6
    • (2011) Eur. J. Epidemiol , vol.26 , pp. S1-S58
    • Wirdefeldt, K.1    Adami, H.O.2    Cole, P.3    Trichopoulos, D.4    Mandel, J.5
  • 252
    • 84894358777 scopus 로고    scopus 로고
    • Molecular chaperones, a-synuclein, and neurodegeneration
    • Witt, S. N. (2013). Molecular chaperones, a-synuclein, and neurodegeneration. Mol. Neurobiol. 47, 552-560. doi: 10.1007/s12035-012-8325-2
    • (2013) Mol. Neurobiol , vol.47 , pp. 552-560
    • Witt, S.N.1
  • 253
    • 84863986350 scopus 로고    scopus 로고
    • Roles of extracellular chaperones in amyloidosis
    • Wyatt, A. R., Yerbury, J. J., Dabbs, R. A., and Wilson, M. R. (2012). Roles of extracellular chaperones in amyloidosis. J. Mol. Biol. 421, 499-516. doi: 10.1016/j.jmb.2012.01.004
    • (2012) J. Mol. Biol , vol.421 , pp. 499-516
    • Wyatt, A.R.1    Yerbury, J.J.2    Dabbs, R.A.3    Wilson, M.R.4
  • 254
    • 4344674075 scopus 로고    scopus 로고
    • Role of heat shock proteins during polyglutamine neurodegeneration: mechanisms and hypothesis
    • Wyttenbach, A. (2004). Role of heat shock proteins during polyglutamine neurodegeneration: mechanisms and hypothesis. J. Mol. Neurosci. 23, 69-96. doi: 10.1385/JMN:23:1-2:069
    • (2004) J. Mol. Neurosci , vol.23 , pp. 69-96
    • Wyttenbach, A.1
  • 255
    • 79951483258 scopus 로고    scopus 로고
    • Structure, assembly and homeostatic regulation of the 26S proteasome
    • Xie, Y. (2010). Structure, assembly and homeostatic regulation of the 26S proteasome. J. Mol. Cell Biol. 2, 308-317. doi: 10.1093/jmcb/mjq030
    • (2010) J. Mol. Cell Biol , vol.2 , pp. 308-317
    • Xie, Y.1
  • 256
    • 77955053465 scopus 로고    scopus 로고
    • Hsp105 reduces the protein aggregation and cytotoxicity by expanded-polyglutamine proteins through the induction of Hsp70
    • Yamagishi, N., Goto, K., Nakagawa, S., Saito, Y., and Hatayama, T. (2010). Hsp105 reduces the protein aggregation and cytotoxicity by expanded-polyglutamine proteins through the induction of Hsp70. Exp. Cell Res. 316, 2424-2433. doi: 10.1016/j.yexcr.2010.06.003
    • (2010) Exp. Cell Res , vol.316 , pp. 2424-2433
    • Yamagishi, N.1    Goto, K.2    Nakagawa, S.3    Saito, Y.4    Hatayama, T.5
  • 257
    • 84939529209 scopus 로고    scopus 로고
    • Polymorphisms in protein disulfide isomerase are associated with sporadic amyotrophic lateral sclerosis in the Chinese Han population
    • Yang, Q., and Guo, Z. B. (2016). Polymorphisms in protein disulfide isomerase are associated with sporadic amyotrophic lateral sclerosis in the Chinese Han population. Int. J. Neurosci. 126, 607-611. doi: 10.3109/00207454.2015.1050098
    • (2016) Int. J. Neurosci , vol.126 , pp. 607-611
    • Yang, Q.1    Guo, Z.B.2
  • 258
    • 84876081004 scopus 로고    scopus 로고
    • The small heat shock proteins aB-crystallin and Hsp27 suppress SOD1 aggregation in vitro
    • Yerbury, J. J., Gower, D., Vanags, L., Roberts, K., Lee, J. A., and Ecroyd, H. (2013). The small heat shock proteins aB-crystallin and Hsp27 suppress SOD1 aggregation in vitro. Cell Stress Chaperones 18, 251-257. doi: 10.1007/s12192-012-0371-1
    • (2013) Cell Stress Chaperones , vol.18 , pp. 251-257
    • Yerbury, J.J.1    Gower, D.2    Vanags, L.3    Roberts, K.4    Lee, J.A.5    Ecroyd, H.6
  • 259
    • 36849044616 scopus 로고    scopus 로고
    • Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response
    • Zhang, Y. Q., and Sarge, K. D. (2007). Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response. J. Mol. Med. 85, 1421-1428. doi: 10.1007/s00109-007-0251-9
    • (2007) J. Mol. Med , vol.85 , pp. 1421-1428
    • Zhang, Y.Q.1    Sarge, K.D.2
  • 260
    • 4644291645 scopus 로고    scopus 로고
    • Analysis of a-synuclein-associated proteins by quantitative proteomics
    • Zhou, Y., Gu, G., Goodlett, D. R., Zhang, T., Pan, C., Montine, T. J., et al. (2004). Analysis of a-synuclein-associated proteins by quantitative proteomics. J. Biol. Chem. 279, 39155-39164. doi: 10.1074/jbc.M405456200
    • (2004) J. Biol. Chem , vol.279 , pp. 39155-39164
    • Zhou, Y.1    Gu, G.2    Goodlett, D.R.3    Zhang, T.4    Pan, C.5    Montine, T.J.6
  • 261
    • 33646354916 scopus 로고    scopus 로고
    • Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation
    • Zietkiewicz, S., Lewandowska, A., Stocki, P., and Liberek, K. (2006). Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation. J. Biol. Chem. 281, 7022-7029. doi: 10.1074/jbc.M507893200
    • (2006) J. Biol. Chem , vol.281 , pp. 7022-7029
    • Zietkiewicz, S.1    Lewandowska, A.2    Stocki, P.3    Liberek, K.4
  • 262
    • 84958752327 scopus 로고    scopus 로고
    • Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashion
    • Zininga, T., Achilonu, I., Hoppe, H., Prinsloo, E., Dirr, H. W., and Shonhai, A. (2016). Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashion. Cell Stress Chaperones 21, 499-513. doi: 10.1007/s12192-016-0678-4
    • (2016) Cell Stress Chaperones , vol.21 , pp. 499-513
    • Zininga, T.1    Achilonu, I.2    Hoppe, H.3    Prinsloo, E.4    Dirr, H.W.5    Shonhai, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.