메뉴 건너뛰기




Volumn 7, Issue 4, 2014, Pages 421-434

Barcoding heat shock proteins to human diseases: Looking beyond the heat shock response

Author keywords

Chaperonopathies; Heat shock protein; Protein aggregation diseases

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID PRECURSOR PROTEIN; ATAXIN 3; CHAPERONIN 60; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 22; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; PRESENILIN 1; PRESENILIN 2;

EID: 84897939278     PISSN: 17548403     EISSN: 17548411     Source Type: Journal    
DOI: 10.1242/dmm.014563     Document Type: Review
Times cited : (89)

References (210)
  • 3
    • 31144453053 scopus 로고    scopus 로고
    • A mutation in the small heat-shock protein HSPB1 leading to distal hereditary motor neuronopathy disrupts neurofilament assembly and the axonal transport of specific cellular cargoes
    • DOI 10.1093/hmg/ddi452
    • Ackerley, S., James, P. A., Kalli, A., French, S., Davies, K. E. and Talbot, K. (2006). A mutation in the small heat-shock protein HSPB1 leading to distal hereditary motor neuronopathy disrupts neurofilament assembly and the axonal transport of specific cellular cargoes. Hum. Mol. Genet. 15, 347-354. (Pubitemid 43125988)
    • (2006) Human Molecular Genetics , vol.15 , Issue.2 , pp. 347-354
    • Ackerley, S.1    James, P.A.2    Kalli, A.3    French, S.4    Davies, K.E.5    Talbot, K.6
  • 4
    • 0037444446 scopus 로고    scopus 로고
    • Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein
    • Adachi, H., Katsuno, M., Minamiyama, M., Sang, C., Pagoulatos, G., Angelidis, C., Kusakabe, M., Yoshiki, A., Kobayashi, Y., Doyu, M. et al. (2003). Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein. J. Neurosci. 23, 2203-2211. (Pubitemid 36368908)
    • (2003) Journal of Neuroscience , vol.23 , Issue.6 , pp. 2203-2211
    • Adachi, H.1    Katsuno, M.2    Minamiyama, M.3    Sang, C.4    Pagoulatos, G.5    Angelidis, C.6    Kusakabe, M.7    Yoshiki, A.8    Kobayashi, Y.9    Doyu, M.10    Sobue, G.11
  • 7
    • 30344462410 scopus 로고    scopus 로고
    • Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
    • DOI 10.1016/j.cell.2005.11.039, PII S0092867405014091
    • Albanèse, V., Yam, A. Y., Baughman, J., Parnot, C. and Frydman, J. (2006). Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells. Cell 124, 75-88. (Pubitemid 43069311)
    • (2006) Cell , vol.124 , Issue.1 , pp. 75-88
    • Albanese, V.1    Yam, A.Y.-W.2    Baughman, J.3    Parnot, C.4    Frydman, J.5
  • 9
    • 80755133370 scopus 로고    scopus 로고
    • Clinical genetics of amyotrophic lateral sclerosis: What do we really know?
    • Andersen, P. M. and Al-Chalabi, A. (2011). Clinical genetics of amyotrophic lateral sclerosis: what do we really know? Nat. Rev. Neurol. 7, 603-615.
    • (2011) Nat. Rev. Neurol. , vol.7 , pp. 603-615
    • Andersen, P.M.1    Al-Chalabi, A.2
  • 10
    • 0037155819 scopus 로고    scopus 로고
    • The R116C mutation in αA-crystallin diminishes its protective ability against stress-induced lens epithelial cell apoptosis
    • DOI 10.1074/jbc.M109211200
    • Andley, U. P., Patel, H. C. and Xi, J. H. (2002). The R116C mutation in α A-crystallin diminishes its protective ability against stress-induced lens epithelial cell apoptosis. J. Biol. Chem. 277, 10178-10186. (Pubitemid 34968131)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 10178-10186
    • Andley, U.P.1    Patel, H.C.2    Xi, J.-H.3
  • 13
    • 0036852712 scopus 로고    scopus 로고
    • Pharmacological prevention of Parkinson disease in Drosophila [1]
    • DOI 10.1038/nm1102-1185
    • Auluck, P. K. and Bonini, N. M. (2002). Pharmacological prevention of Parkinson disease in Drosophila. Nat. Med. 8, 1185-1186. (Pubitemid 35373534)
    • (2002) Nature Medicine , vol.8 , Issue.11 , pp. 1185-1186
    • Auluck, P.K.1    Bonini, N.M.2
  • 14
    • 84897933854 scopus 로고    scopus 로고
    • First demonstration of Hsp70's neuroprotective effect in a drosophila model of Parkinson's disease
    • Auluck, P. K., Chan, H. Y. E., Trojanowsk, J. Q., Lee, V. M.-Y. and Bonini, N. M. (2002). First demonstration of Hsp70's neuroprotective effect in a drosophila model of Parkinson's disease. Drosophila. Nat. Med. 8, 1185-1186.
    • (2002) Drosophila. Nat. Med. , vol.8 , pp. 1185-1186
    • Auluck, P.K.1    Chan, H.Y.E.2    Trojanowsk, J.Q.3    Lee, V.M.-Y.4    Bonini, N.M.5
  • 15
    • 13244267202 scopus 로고    scopus 로고
    • Mechanisms of suppression of α-synuclein neurotoxicity by geldanamycin in Drosophila
    • DOI 10.1074/jbc.M412106200
    • Auluck, P. K., Meulener, M. C. and Bonini, N. M. (2005). Protein synthesis, post-translation modification, and degradation: Mechanisms of suppression of α-synuclein neurotoxicity by Geldanamycin in Drosophila. J. Biol. Chem. 280, 2873-2878. (Pubitemid 40189396)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.4 , pp. 2873-2878
    • Auluck, P.K.1    Meulener, M.C.2    Bonini, N.M.3
  • 16
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • DOI 10.1126/science.1141448
    • Balch, W. E., Morimoto, R. I., Dillin, A. and Kelly, J. W. (2008). Adapting proteostasis for disease intervention. Science 319, 916-919. (Pubitemid 351263754)
    • (2008) Science , vol.319 , Issue.5865 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 17
    • 84855478434 scopus 로고    scopus 로고
    • A screen for enhancers of clearance identifies huntingtin as a heat shock protein 90 (Hsp90) client protein
    • Baldo, B., Weiss, A., Parker, C. N., Bibel, M., Paganetti, P. and Kaupmann, K. (2012). A screen for enhancers of clearance identifies huntingtin as a heat shock protein 90 (Hsp90) client protein. J. Biol. Chem. 287, 1406-1414.
    • (2012) J. Biol. Chem. , vol.287 , pp. 1406-1414
    • Baldo, B.1    Weiss, A.2    Parker, C.N.3    Bibel, M.4    Paganetti, P.5    Kaupmann, K.6
  • 18
    • 84862764590 scopus 로고    scopus 로고
    • Pathogenesis and molecular targeted therapy of spinal and bulbar muscular atrophy (SBMA)
    • Banno, H., Katsuno, M., Suzuki, K., Tanaka, F. and Sobue, G. (2012). Pathogenesis and molecular targeted therapy of spinal and bulbar muscular atrophy (SBMA). Cell Tissue Res. 349, 313-320.
    • (2012) Cell Tissue Res. , vol.349 , pp. 313-320
    • Banno, H.1    Katsuno, M.2    Suzuki, K.3    Tanaka, F.4    Sobue, G.5
  • 19
    • 33749989045 scopus 로고    scopus 로고
    • Induction of multiple heat shock proteins and neuroprotection in a primary culture model of familial amyotrophic lateral sclerosis
    • DOI 10.1016/j.nbd.2006.06.017, PII S0969996106001525
    • Batulan, Z., Taylor, D. M., Aarons, R. J., Minotti, S., Doroudchi, M. M., Nalbantoglu, J. and Durham, H. D. (2006). Induction of multiple heat shock proteins and neuroprotection in a primary culture model of familial amyotrophic lateral sclerosis. Neurobiol. Dis. 24, 213-225. (Pubitemid 44572743)
    • (2006) Neurobiology of Disease , vol.24 , Issue.2 , pp. 213-225
    • Batulan, Z.1    Taylor, D.M.2    Aarons, R.J.3    Minotti, S.4    Doroudchi, M.M.5    Nalbantoglu, J.6    Durham, H.D.7
  • 23
    • 33749056809 scopus 로고    scopus 로고
    • ALS: A Disease of Motor Neurons and Their Nonneuronal Neighbors
    • DOI 10.1016/j.neuron.2006.09.018, PII S0896627306007252
    • Boillée, S., Vande Velde, C. and Cleveland, D. W. (2006). ALS: a disease of motor neurons and their nonneuronal neighbors. Neuron 52, 39-59. (Pubitemid 44466358)
    • (2006) Neuron , vol.52 , Issue.1 , pp. 39-59
    • Boillee, S.1    Vande, V.C.2    Cleveland, D.W.3
  • 24
    • 84864486839 scopus 로고    scopus 로고
    • The family of mammalian small heat shock proteins (HSPBs): Implications in protein deposit diseases and motor neuropathies
    • Boncoraglio, A., Minoia, M. and Carra, S. (2012). The family of mammalian small heat shock proteins (HSPBs): implications in protein deposit diseases and motor neuropathies. Int. J. Biochem. Cell Biol. 44, 1657-1669.
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 1657-1669
    • Boncoraglio, A.1    Minoia, M.2    Carra, S.3
  • 30
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 and Co. - A holding for folding
    • Buchner, J. (1999). Hsp90 and Co. - a holding for folding. Trends Biochem. Sci. 24, 136-141.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 136-141
    • Buchner, J.1
  • 31
    • 0034646515 scopus 로고    scopus 로고
    • Getting newly synthesized proteins into shape
    • DOI 10.1016/S0092-8674(00)80806-5
    • Bukau, B., Deuerling, E., Pfund, C. and Craig, E. A. (2000). Getting newly synthesized proteins into shape. Cell 101, 119-122. (Pubitemid 32004743)
    • (2000) Cell , vol.101 , Issue.2 , pp. 119-122
    • Bukau, B.1    Deuerling, E.2    Pfund, C.3    Craig, E.A.4
  • 34
    • 43549123996 scopus 로고    scopus 로고
    • Small heat shock proteins in neurodegenerative diseases
    • ed. J. Radons and G. Multhoff Kerala, India: Research Signpost
    • Carra, S. and Landry, J. (2006). Small heat shock proteins in neurodegenerative diseases. In Heat Shock Proteins in Biology and Medicine, (ed. J. Radons and G. Multhoff), pp. 331-351. Kerala, India: Research Signpost.
    • (2006) Heat Shock Proteins in Biology and Medicine , pp. 331-351
    • Carra, S.1    Landry, J.2
  • 35
    • 38349105324 scopus 로고    scopus 로고
    • HspB8 chaperone activity toward poly(Q)-containing proteins depends on its association with Bag3, a stimulator of macroautophagy
    • Carra, S., Seguin, S. J., Lambert, H. and Landry, J. (2008). HspB8 chaperone activity toward poly(Q)-containing proteins depends on its association with Bag3, a stimulator of macroautophagy. J. Biol. Chem. 283, 1437-1444.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1437-1444
    • Carra, S.1    Seguin, S.J.2    Lambert, H.3    Landry, J.4
  • 37
    • 0033499931 scopus 로고    scopus 로고
    • Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease
    • Chai, Y., Koppenhafer, S. L., Bonini, N. M. and Paulson, H. L. (1999). Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J. Neurosci. 19, 10338-10347. (Pubitemid 30228041)
    • (1999) Journal of Neuroscience , vol.19 , Issue.23 , pp. 10338-10347
    • Chai, Y.1    Koppenhafer, S.L.2    Bonini, N.M.3    Paulson, H.L.4
  • 38
    • 0034703863 scopus 로고    scopus 로고
    • Mechanisms of chaperone suppression of polyglutamine disease: Selectivity, synergy and modulation of protein solubility in Drosophila
    • Chan, H. Y. E., Warrick, J. M., Gray-Board, G. L., Paulson, H. L. and Bonini, N. M. (2000). Mechanisms of chaperone suppression of polyglutamine disease: selectivity, synergy and modulation of protein solubility in Drosophila. Hum. Mol. Genet. 9, 2811-2820.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2811-2820
    • Chan, H.Y.E.1    Warrick, J.M.2    Gray-Board, G.L.3    Paulson, H.L.4    Bonini, N.M.5
  • 39
    • 0036850456 scopus 로고    scopus 로고
    • Genetic modulation of polyglutamine toxicity by protein conjugation pathways in Drosophila
    • Chan, H. Y. E., Warrick, J. M., Andriola, I., Merry, D. and Bonini, N. M. (2002). Genetic modulation of polyglutamine toxicity by protein conjugation pathways in Drosophila. Hum. Mol. Genet. 11, 2895-2904.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2895-2904
    • Chan, H.Y.E.1    Warrick, J.M.2    Andriola, I.3    Merry, D.4    Bonini, N.M.5
  • 40
    • 84866180204 scopus 로고    scopus 로고
    • Molecular chaperones as targets to circumvent the CFTR defect in cystic fibrosis
    • Chanoux, R. A. and Rubenstein, R. C. (2012). Molecular chaperones as targets to circumvent the CFTR defect in cystic fibrosis. Front Pharmacol. 3, 137.
    • (2012) Front Pharmacol. , vol.3 , pp. 137
    • Chanoux, R.A.1    Rubenstein, R.C.2
  • 41
    • 4344684215 scopus 로고    scopus 로고
    • Neuronal DnaJ proteins HSJ1a and HSJ1b: A role in linking the Hsp70 chaperone machine to the ubiquitin-proteasome system?
    • DOI 10.1042/BST0320640
    • Chapple, J. P., van der Spuy, J., Poopalasundaram, S. and Cheetham, M. E. (2004). Neuronal DnaJ proteins HSJ1a and HSJ1b: a role in linking the Hsp70 chaperone machine to the ubiquitin-proteasome system? Biochem. Soc. Trans. 32, 640-642. (Pubitemid 39120404)
    • (2004) Biochemical Society Transactions , vol.32 , Issue.4 , pp. 640-642
    • Chapple, J.P.1    Van Der, S.J.2    Poopalasundaram, S.3    Cheetham, M.E.4
  • 42
    • 0038104369 scopus 로고    scopus 로고
    • Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G αB-crystallin mutant
    • DOI 10.1093/hmg/ddg173
    • Chávez Zobel, A. T. C., Loranger, A., Marceau, N., Thériault, J. R., Lambert, H. and Landry, J. (2003). Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G alphaB-crystallin mutant. Hum. Mol. Genet. 12, 1609-1620. (Pubitemid 36857307)
    • (2003) Human Molecular Genetics , vol.12 , Issue.13 , pp. 1609-1620
    • Zobel, A.T.C.1    Loranger, A.2    Marceau, N.3    Theriault, J.R.4    Lambert, H.5    Landry, J.6
  • 43
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti, F. and Dobson, C. M. (2006). Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366. (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 44
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti, F. and Dobson, C. M. (2009). Amyloid formation by globular proteins under native conditions. Nat. Chem. Biol. 5, 15-22.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 45
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • DOI 10.1016/S0896-6273(03)00606-8
    • Ciechanover, A. and Brundin, P. (2003). The ubiquitin proteasome system: Sometimes the chicken, sometimes the egg. Neuron 40, 427-446. (Pubitemid 37244106)
    • (2003) Neuron , vol.40 , Issue.2 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 46
    • 0035394668 scopus 로고    scopus 로고
    • Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
    • Cummings, C. J., Sun, Y., Opal, P., Antalffy, B., Mestril, R., Orr, H. T., Dillmann, W. H. and Zoghbi, H. Y. (2001). Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum. Mol. Genet. 10, 1511-1518. (Pubitemid 32684893)
    • (2001) Human Molecular Genetics , vol.10 , Issue.14 , pp. 1511-1518
    • Cummings, C.J.1    Sun, Y.2    Opal, P.3    Antalffy, B.4    Mestril, R.5    Orr, H.T.6    Dillmann, W.H.7    Zoghbi, H.Y.8
  • 47
    • 79251565507 scopus 로고    scopus 로고
    • Heat-shock protein 70 modulates toxic extracellular α-synuclein oligomers and rescues trans-synaptic toxicity
    • Danzer, K. M., Ruf, W. P., Putcha, P., Joyner, D., Hashimoto, T., Glabe, C., Hyman, B. T. and McLean, P. J. (2011). Heat-shock protein 70 modulates toxic extracellular α-synuclein oligomers and rescues trans-synaptic toxicity. FASEB J. 25, 326-336.
    • (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    Hyman, B.T.7    McLean, P.J.8
  • 48
    • 84878935108 scopus 로고    scopus 로고
    • Mutations of small heat shock proteins and human congenital diseases
    • Datskevich, P. N., Nefedova, V. V., Sudnitsyna, M. V. and Gusev, N. B. (2012). Mutations of small heat shock proteins and human congenital diseases. Biochemistry 77, 1500-1514.
    • (2012) Biochemistry , vol.77 , pp. 1500-1514
    • Datskevich, P.N.1    Nefedova, V.V.2    Sudnitsyna, M.V.3    Gusev, N.B.4
  • 49
    • 33646427709 scopus 로고    scopus 로고
    • Mutation of DNAJC19, a human homologue of yeast inner mitochondrial membrane co-chaperones, causes DCMA syndrome, a novel autosomal recessive Barth syndrome-like condition
    • Davey, K. M., Parboosingh, J. S., McLeod, D. R., Chan, A., Casey, R., Ferreira, P., Snyder, F. F., Bridge, P. J. and Bernier, F. P. (2006). Mutation of DNAJC19, a human homologue of yeast inner mitochondrial membrane co-chaperones, causes DCMA syndrome, a novel autosomal recessive Barth syndrome-like condition. J. Med. Genet. 43, 385-393.
    • (2006) J. Med. Genet. , vol.43 , pp. 385-393
    • Davey, K.M.1    Parboosingh, J.S.2    McLeod, D.R.3    Chan, A.4    Casey, R.5    Ferreira, P.6    Snyder, F.F.7    Bridge, P.J.8    Bernier, F.P.9
  • 50
    • 33646246733 scopus 로고    scopus 로고
    • HSP induction mediates selective clearance of tau phosphorylated at proline-directed Ser/Thr sites but not KXGS (MARK) sites
    • DOI 10.1096/fj.05-5343fje
    • Dickey, C. A., Dunmore, J., Lu, B., Wang, J. W., Lee, W. C., Kamal, A., Burrows, F., Eckman, C., Hutton, M. and Petrucelli, L. (2006). HSP induction mediates selective clearance of tau phosphorylated at proline-directed Ser/Thr sites but not KXGS (MARK) sites. FASEB J. 20, 753-755. (Pubitemid 46671204)
    • (2006) FASEB Journal , vol.20 , Issue.6 , pp. 753-755
    • Dickey, C.A.1    Dunmore, J.2    Lu, B.3    Wang, J.-W.4    Lee, W.C.5    Kamal, A.6    Burrows, F.7    Eckman, C.8    Hutton, M.9    Petrucelli, L.10
  • 52
    • 84860487766 scopus 로고    scopus 로고
    • A deleterious mutation in DNAJC6 encoding the neuronal-specific clathrin-uncoating co-chaperone auxilin, is associated with juvenile parkinsonism
    • Edvardson, S., Cinnamon, Y., Ta-Shma, A., Shaag, A., Yim, Y. I., Zenvirt, S., Jalas, C., Lesage, S., Brice, A., Taraboulos, A. et al. (2012). A deleterious mutation in DNAJC6 encoding the neuronal-specific clathrin-uncoating co-chaperone auxilin, is associated with juvenile parkinsonism. PLoS ONE 7, e36458.
    • (2012) PLoS ONE , vol.7
    • Edvardson, S.1    Cinnamon, Y.2    Ta-Shma, A.3    Shaag, A.4    Yim, Y.I.5    Zenvirt, S.6    Jalas, C.7    Lesage, S.8    Brice, A.9    Taraboulos, A.10
  • 53
    • 0032822103 scopus 로고    scopus 로고
    • Principles of protein folding in the cellular environment
    • DOI 10.1016/S0959-440X(99)80013-X
    • Ellis, R. J. and Hartl, F. U. (1999). Principles of protein folding in the cellular environment. Curr. Opin. Struct. Biol. 9, 102-110. (Pubitemid 29471981)
    • (1999) Current Opinion in Structural Biology , vol.9 , Issue.1 , pp. 102-110
    • Ellis, R.J.1    Hartl, F.U.2
  • 55
    • 79957488875 scopus 로고    scopus 로고
    • Wild-type and A315T mutant TDP-43 exert differential neurotoxicity in a Drosophila model of ALS
    • Estes, P. S., Boehringer, A., Zwick, R., Tang, J. E., Grigsby, B. and Zarnescu, D. C. (2011). Wild-type and A315T mutant TDP-43 exert differential neurotoxicity in a Drosophila model of ALS. Hum. Mol. Genet. 20, 2308-2321.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2308-2321
    • Estes, P.S.1    Boehringer, A.2    Zwick, R.3    Tang, J.E.4    Grigsby, B.5    Zarnescu, D.C.6
  • 56
    • 33845918172 scopus 로고    scopus 로고
    • Heat shock proteins 70 and 90 inhibit early stages of amyloid β-(1-42) aggregation in vitro
    • DOI 10.1074/jbc.M606192200
    • Evans, C. G., Wisén, S. and Gestwicki, J. E. (2006). Heat shock proteins 70 and 90 inhibit early stages of amyloid β-(1-42) aggregation in vitro. J. Biol. Chem. 281, 33182-33191. (Pubitemid 46036699)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.44 , pp. 33182-33191
    • Evans, C.G.1    Wisen, S.2    Gestwicki, J.E.3
  • 57
    • 0033018496 scopus 로고    scopus 로고
    • Accelerated transport and maturation of lysosomal α-galactosidase A in fabry lymphoblasts by an enzyme inhibitor
    • DOI 10.1038/4801
    • Fan, J. Q., Ishii, S., Asano, N. and Suzuki, Y. (1999). Accelerated transport and maturation of lysosomal alpha-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor. Nat. Med. 5, 112-115. (Pubitemid 29051008)
    • (1999) Nature Medicine , vol.5 , Issue.1 , pp. 112-115
    • Fan, J.-Q.1    Ishii, S.2    Asano, N.3    Suzuki, Y.4
  • 58
    • 0033607770 scopus 로고    scopus 로고
    • Domain requirements of DnaJ-like (Hsp40) molecular chaperones in the activation of a steroid hormone receptor
    • Fliss, A. E., Rao, J., Melville, M. W., Cheetham, M. E. and Caplan, A. J. (1999). Domain requirements of DnaJ-like (Hsp40) molecular chaperones in the activation of a steroid hormone receptor. J. Biol. Chem. 274, 34045-34052. (Pubitemid 129511737)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.48 , pp. 34045-34052
    • Fliss, A.E.1    Rao, J.2    Melvillell, M.W.3    Cheetham, M.E.4    Caplan, A.J.5
  • 59
    • 33845600705 scopus 로고    scopus 로고
    • Abnormal small heat shock protein interactions involving neuropathy-associated HSP22 (HSPB8) mutants
    • Fontaine, J.-M., Sun, X., Hoppe, A. D., Simon, S., Vicart, P., Welsh, M. J. and Benndorf, R. (2006). Abnormal small heat shock protein interactions involving neuropathy-associated HSP22 (HSPB8) mutants. FASEB J. 20, 2168-2170.
    • (2006) FASEB J. , vol.20 , pp. 2168-2170
    • Fontaine, J.-M.1    Sun, X.2    Hoppe, A.D.3    Simon, S.4    Vicart, P.5    Welsh, M.J.6    Benndorf, R.7
  • 60
    • 0037040277 scopus 로고    scopus 로고
    • Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay
    • DOI 10.1074/jbc.M110027200
    • Fu, L. and Liang, J. J. (2002). Detection of protein-protein interactions among lens crystalings in a mammalian two-hybrid system assay. J. Biol. Chem. 277, 4255-4260. (Pubitemid 34968689)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.6 , pp. 4255-4260
    • Fu, L.1    Liang, J.J.-N.2
  • 61
    • 0037336078 scopus 로고    scopus 로고
    • Alteration of protein-protein interactions of congenital cataract crystallin mutants
    • DOI 10.1167/iovs.02-0950
    • Fu, L. and Liang, J. J. (2003). Alteration of protein-protein interactions of congenital cataract crystallin mutants. Invest. Ophthalmol. Vis. Sci. 44, 1155-1159. (Pubitemid 36297835)
    • (2003) Investigative Ophthalmology and Visual Science , vol.44 , Issue.3 , pp. 1155-1159
    • Fu, L.1    Liang, J.J.-N.2
  • 62
    • 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.
    • (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
  • 63
    • 27144524290 scopus 로고    scopus 로고
    • Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models
    • DOI 10.1074/jbc.M506288200
    • Fujimoto, M., Takaki, E., Hayashi, T., Kitaura, Y., Tanaka, Y., Inouye, S. and Nakai, A. (2005). Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models. J. Biol. Chem. 280, 34908-34916. (Pubitemid 41504625)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.41 , pp. 34908-34916
    • Fujimoto, M.1    Takaki, E.2    Hayashi, T.3    Kitaura, Y.4    Tanaka, Y.5    Inouye, S.6    Nakai, A.7
  • 72
    • 84857477831 scopus 로고    scopus 로고
    • The aggregation and neurotoxicity of TDP-43 and its ALS-associated 25 kDa fragment are differentially affected by molecular chaperones in Drosophila
    • Gregory, J. M., Barros, T. P., Meehan, S., Dobson, C. M. and Luheshi, L. M. (2012). The aggregation and neurotoxicity of TDP-43 and its ALS-associated 25 kDa fragment are differentially affected by molecular chaperones in Drosophila. PLoS ONE 7, e31899.
    • (2012) PLoS ONE , vol.7
    • Gregory, J.M.1    Barros, T.P.2    Meehan, S.3    Dobson, C.M.4    Luheshi, L.M.5
  • 73
    • 84855819016 scopus 로고    scopus 로고
    • The genetic architecture of Alzheimer's disease: Beyond APP, PSENs and APOE
    • Guerreiro, R. J., Gustafson, D. R. and Hardy, J. (2012). The genetic architecture of Alzheimer's disease: beyond APP, PSENs and APOE. Neurobiol. Aging 33, 437-456.
    • (2012) Neurobiol. Aging , vol.33 , pp. 437-456
    • Guerreiro, R.J.1    Gustafson, D.R.2    Hardy, J.3
  • 74
    • 0141750470 scopus 로고    scopus 로고
    • Disruption of axonal transport by loss of huntingtin or expression of pathogenic polyQ proteins in Drosophila
    • DOI 10.1016/S0896-6273(03)00594-4
    • Gunawardena, S., Her, L.-S., Brusch, R. G., Laymon, R. A., Niesman, I. R., Gordesky-Gold, B., Sintasath, L., Bonini, N. M. and Goldstein, L. S. B. (2003). Disruption of axonal transport by loss of huntingtin or expression of pathogenic polyQ proteins in Drosophila. Neuron 40, 25-40. (Pubitemid 37222462)
    • (2003) Neuron , vol.40 , Issue.1 , 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    Sintasath, L.7    Bonini, N.M.8    Goldstein, L.S.B.9
  • 75
    • 0034329159 scopus 로고    scopus 로고
    • Molecular genetics: Unmasking polyglutamine triggers in neurodegenerative disease
    • Gusella, J. F. and MacDonald, M. E. (2000). Molecular genetics: unmasking polyglutamine triggers in neurodegenerative disease. Nat. Rev. Neurosci. 1, 109-115.
    • (2000) Nat. Rev. Neurosci. , vol.1 , pp. 109-115
    • Gusella, J.F.1    MacDonald, M.E.2
  • 77
    • 79952833763 scopus 로고    scopus 로고
    • The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities
    • Hageman, J., van Waarde, M. A. W. H., Zylicz, A., Walerych, D. and Kampinga, H. H. (2011). The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities. Biochem. J. 435, 127-142.
    • (2011) Biochem. J. , vol.435 , pp. 127-142
    • Hageman, J.1    Van Waarde, M.A.W.H.2    Zylicz, A.3    Walerych, D.4    Kampinga, H.H.5
  • 80
    • 0347928859 scopus 로고    scopus 로고
    • Overexpression of heat shock protein 70 in R6/2 Huntington's disease mice has only modest effects on disease progression
    • DOI 10.1016/S0006-8993(02)04275-0
    • Hansson, O., Nylandsted, J., Castilho, R. F., Leist, M., Jäättelä, M. and Brundin, P. (2003). Overexpression of heat shock protein 70 in R6/2 Huntington's disease mice has only modest effects on disease progression. Brain Res. 970, 47-57. (Pubitemid 36423181)
    • (2003) Brain Research , vol.970 , Issue.1-2 , pp. 47-57
    • Hansson, O.1    Nylandsted, J.2    Castilho, R.F.3    Leist, M.4    Jaattela, M.5    Brundin, P.6
  • 82
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • DOI 10.1093/hmg/ddh144
    • Hay, D. G., Sathasivam, K., Tobaben, S., Stahl, B., Marber, M., Mestril, R., Mahal, A., Smith, D. L., Woodman, B. and Bates, G. P. (2004). Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach. Hum. Mol. Genet. 13, 1389-1405. (Pubitemid 38961645)
    • (2004) Human Molecular Genetics , vol.13 , Issue.13 , pp. 1389-1405
    • Hay, D.G.1    Sathasivam, K.2    Tobaben, S.3    Stahl, B.4    Marber, M.5    Mestril, R.6    Mahal, A.7    Smith, D.L.8    Woodman, B.9    Bates, G.P.10
  • 83
    • 44849103123 scopus 로고    scopus 로고
    • Truncation of alphaB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells
    • Hayes, V. H., Devlin, G. and Quinlan, R. A. (2008). Truncation of alphaB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells. J. Biol. Chem. 283, 10500-10512.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10500-10512
    • Hayes, V.H.1    Devlin, G.2    Quinlan, R.A.3
  • 84
    • 78649728763 scopus 로고    scopus 로고
    • The mitochondrial UPR - Protecting organelle protein homeostasis
    • Haynes, C. M. and Ron, D. (2010). The mitochondrial UPR - protecting organelle protein homeostasis. J. Cell Sci. 123, 3849-3855.
    • (2010) J. Cell Sci. , vol.123 , pp. 3849-3855
    • Haynes, C.M.1    Ron, D.2
  • 85
    • 34347258879 scopus 로고    scopus 로고
    • Small molecule inducers of heat-shock response reduce polyQ-mediated huntingtin aggregation: A possible therapeutic strategy
    • DOI 10.1159/000101849
    • Herbst, M. and Wanker, E. E. (2007). Small molecule inducers of heat-shock response reduce polyQ-mediated huntingtin aggregation. A possible therapeutic strategy. Neurodegener. Dis. 4, 254-260. (Pubitemid 47000417)
    • (2007) Neurodegenerative Diseases , vol.4 , Issue.2-3 , pp. 254-260
    • Herbst, M.1    Wanker, E.E.2
  • 86
    • 79952635812 scopus 로고    scopus 로고
    • BAG3 directly interacts with mutated alphaB-crystallin to suppress its aggregation and toxicity
    • Hishiya, A., Salman, M. N., Carra, S., Kampinga, H. H. and Takayama, S. (2011). BAG3 directly interacts with mutated alphaB-crystallin to suppress its aggregation and toxicity. PLoS ONE 6, e16828.
    • (2011) PLoS ONE , vol.6
    • Hishiya, A.1    Salman, M.N.2    Carra, S.3    Kampinga, H.H.4    Takayama, S.5
  • 88
    • 34249286265 scopus 로고    scopus 로고
    • Hsp40 molecules that target to the ubiquitin-proteasome system decrease inclusion formation in models of polyglutamine disease
    • DOI 10.1038/sj.mt.6300163, PII 6300163
    • Howarth, J. L., Kelly, S., Keasey, M. P., Glover, C. P. J., Lee, Y. B., Mitrophanous, K., Chapple, J. P., Gallo, J. M., Cheetham, M. E. and Uney, J. B. (2007). Hsp40 molecules that target to the ubiquitin-proteasome system decrease inclusion formation in models of polyglutamine disease. Mol. Ther. 15, 1100-1105. (Pubitemid 46813612)
    • (2007) Molecular Therapy , vol.15 , Issue.6 , pp. 1100-1105
    • Howarth, J.L.1    Kelly, S.2    Keasey, M.P.3    Glover, C.P.J.4    Lee, Y.-B.5    Mitrophanous, K.6    Chapple, J.P.7    Gallo, J.M.8    Cheetham, M.E.9    Uney, J.B.10
  • 89
    • 73949089674 scopus 로고    scopus 로고
    • Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-β peptide
    • Hu, X., Crick, S. L., Bu, G., Frieden, C., Pappu, R. V. and Lee, J.-M. (2009). Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-β peptide. Proc. Natl. Acad. Sci. USA 106, 20324-20329.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20324-20329
    • Hu, X.1    Crick, S.L.2    Bu, G.3    Frieden, C.4    Pappu, R.V.5    Lee, J.-M.6
  • 91
    • 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. (Pubitemid 30642666)
    • (2000) Human Molecular Genetics , vol.9 , Issue.13 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.-H.3    Nukina, N.4
  • 92
    • 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., Peng, T., Zhang, Y. and Li, H. (2012). GRP78 counteracts cell death and protein aggregation caused by mutant huntingtin proteins. Neurosci. Lett. 516, 182-187.
    • (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    Peng, T.7    Zhang, Y.8    Li, H.9
  • 93
    • 84878752125 scopus 로고    scopus 로고
    • Increased heat shock transcription factor 1 in the cerebellum reverses the deficiency of Purkinje cells in Alzheimer's disease
    • Jiang, Y.-Q., Wang, X.-L., Cao, X. H., Ye, Z. Y., Li, L. and Cai, W.-Q. (2013). Increased heat shock transcription factor 1 in the cerebellum reverses the deficiency of Purkinje cells in Alzheimer's disease. Brain Res. 1519, 105-111.
    • (2013) Brain Res. , vol.1519 , pp. 105-111
    • Jiang, Y.-Q.1    Wang, X.-L.2    Cao, X.H.3    Ye, Z.Y.4    Li, L.5    Cai, W.-Q.6
  • 95
    • 84874833124 scopus 로고    scopus 로고
    • DNAJ proteins and protein aggregation diseases
    • Kakkar, V., Prins, L. C. and Kampinga, H. H. (2013). DNAJ proteins and protein aggregation diseases. Curr. Top. Med. Chem. 12, 2479-2490.
    • (2013) Curr. Top. Med. Chem. , vol.12 , pp. 2479-2490
    • Kakkar, V.1    Prins, L.C.2    Kampinga, H.H.3
  • 96
    • 53149114499 scopus 로고    scopus 로고
    • Late stage treatment with arimoclomol delays disease progression and prevents protein aggregation in the SOD1 mouse model of ALS
    • Kalmar, B., Novoselov, S., Gray, A., Cheetham, M. E., Margulis, B. and Greensmith, L. (2008). Late stage treatment with arimoclomol delays disease progression and prevents protein aggregation in the SOD1 mouse model of ALS. J. Neurochem. 107, 339-350.
    • (2008) J. Neurochem. , vol.107 , pp. 339-350
    • Kalmar, B.1    Novoselov, S.2    Gray, A.3    Cheetham, M.E.4    Margulis, B.5    Greensmith, L.6
  • 97
    • 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.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 98
    • 84864456309 scopus 로고    scopus 로고
    • HSPBs: Small proteins with big implications in human disease
    • Kampinga, H. H. and Garrido, C. (2012). HSPBs: small proteins with big implications in human disease. Int. J. Biochem. Cell Biol. 44, 1706-1710.
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 1706-1710
    • Kampinga, H.H.1    Garrido, C.2
  • 102
    • 33744486642 scopus 로고    scopus 로고
    • Celastrol blocks neuronal cell death and extends life in transgenic mouse model of amyotrophic lateral sclerosis
    • DOI 10.1159/000090364
    • Kiaei, M., Kipiani, K., Petri, S., Chen, J., Calingasan, N. Y. and Beal, M. F. (2005). Celastrol blocks neuronal cell death and extends life in transgenic mouse model of amyotrophic lateral sclerosis. Neurodegener. Dis. 2, 246-254. (Pubitemid 43805908)
    • (2005) Neurodegenerative Diseases , vol.2 , Issue.5 , pp. 246-254
    • Kiaei, M.1    Kipiani, K.2    Petri, S.3    Chen, J.4    Calingasan, N.Y.5    Beal, M.F.6
  • 103
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • DOI 10.1038/nm1021
    • Kieran, D., Kalmar, B., Dick, J. R. T., 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. (Pubitemid 38508519)
    • (2004) Nature Medicine , vol.10 , Issue.4 , pp. 402-405
    • Kieran, D.1    Kalmar, B.2    Dick, J.R.T.3    Riddoch-Contreras, J.4    Burnstock, G.5    Greensmith, L.6
  • 110
    • 49549120206 scopus 로고    scopus 로고
    • Over-expression of Hsp27 does not influence disease in the mutant SOD1(G93A) mouse model of amyotrophic lateral sclerosis
    • Krishnan, J., Vannuvel, K., Andries, M., Waelkens, E., Robberecht, W. and Van Den Bosch, L. (2008). Over-expression of Hsp27 does not influence disease in the mutant SOD1(G93A) mouse model of amyotrophic lateral sclerosis. J. Neurochem. 106, 2170-2183.
    • (2008) J. Neurochem. , vol.106 , pp. 2170-2183
    • Krishnan, J.1    Vannuvel, K.2    Andries, M.3    Waelkens, E.4    Robberecht, W.5    Van Den Bosch, L.6
  • 112
    • 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. and Cheetham, M. E. (2012). Suppression of protein aggregation by chaperone modification of high molecular weight complexes. Brain 135, 1180-1196.
    • (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    Cheetham, M.E.7
  • 114
    • 63149090431 scopus 로고    scopus 로고
    • Parkinson's disease: From monogenic forms to genetic susceptibility factors
    • Lesage, S. and Brice, A. (2009). Parkinson's disease: from monogenic forms to genetic susceptibility factors. Hum. Mol. Genet. 18 R1, R48-R59.
    • (2009) Hum. Mol. Genet. , vol.18 , Issue.R1
    • Lesage, S.1    Brice, A.2
  • 116
    • 77953175438 scopus 로고    scopus 로고
    • Dominant-positive HSF1 decreases α-synuclein level and α-synuclein-induced toxicity
    • Liangliang, X., Yonghui, H., Shunmei, E., Shoufang, G., Wei, Z. and Jiangying, Z. (2010). Dominant-positive HSF1 decreases α-synuclein level and α-synuclein-induced toxicity. Mol. Biol. Rep. 37, 1875-1881.
    • (2010) Mol. Biol. Rep. , vol.37 , pp. 1875-1881
    • Liangliang, X.1    Yonghui, H.2    Shunmei, E.3    Shoufang, G.4    Wei, Z.5    Jiangying, Z.6
  • 117
    • 68649110959 scopus 로고    scopus 로고
    • Bridging the gap: From protein misfolding to protein misfolding diseases
    • Luheshi, L. M. and Dobson, C. M. (2009). Bridging the gap: from protein misfolding to protein misfolding diseases. FEBS Lett. 583, 2581-2586.
    • (2009) FEBS Lett. , vol.583 , pp. 2581-2586
    • Luheshi, L.M.1    Dobson, C.M.2
  • 118
    • 0036549108 scopus 로고    scopus 로고
    • Sick chaperones and ageing: A perspective
    • DOI 10.1016/S1568-1637(01)00005-8, PII S1568163701000058
    • Macario, A. J. L. and Conway de Macario, E. (2002). Sick chaperones and ageing: a perspective. Ageing Res. Rev. 1, 295-311. (Pubitemid 38340347)
    • (2002) Ageing Research Reviews , vol.1 , Issue.2 , pp. 295-311
    • Macario, A.J.L.1    De Macario, E.C.2
  • 119
    • 34447526219 scopus 로고    scopus 로고
    • Chaperonopathies and chaperonotherapy
    • Macario, A. J. L. and Conway de Macario, E. (2007). Chaperonopathies and chaperonotherapy. FEBS Lett. 581, 3681-3688.
    • (2007) FEBS Lett. , vol.581 , pp. 3681-3688
    • Macario, A.J.L.1    Conway De Macario, E.2
  • 120
    • 12144282296 scopus 로고    scopus 로고
    • Genetic disorders involving molecular-chaperone genes: A perspective
    • DOI 10.1097/01.GIM.0000151351.11876.C3
    • Macario, A. J. L., Grippo, T. M. and Conway de Macario, E. (2005). Genetic disorders involving molecular-chaperone genes: a perspective. Genet. Med. 7, 3-12. (Pubitemid 40111125)
    • (2005) Genetics in Medicine , vol.7 , Issue.1 , pp. 3-12
    • Macario, A.J.L.1    Grippo, T.M.2    De Macario, E.C.3
  • 121
    • 0242287938 scopus 로고    scopus 로고
    • Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q
    • DOI 10.1038/sj.ejhg.5201046
    • Mackay, D. S., Andley, U. P. and Shiels, A. (2003). Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q. Eur. J. Hum. Genet. 11, 784-793. (Pubitemid 37337062)
    • (2003) European Journal of Human Genetics , vol.11 , Issue.10 , pp. 784-793
    • Mackay, D.S.1    Andley, U.P.2    Shiels, A.3
  • 122
    • 46149097136 scopus 로고    scopus 로고
    • Mitochondrial hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy
    • Magen, D., Georgopoulos, C., Bross, P., Ang, D., Segev, Y., Goldsher, D., Nemirovski, A., Shahar, E., Ravid, S., Luder, A. et al. (2008). Mitochondrial hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy. Am. J. Hum. Genet. 83, 30-42.
    • (2008) Am. J. Hum. Genet. , vol.83 , pp. 30-42
    • Magen, D.1    Georgopoulos, C.2    Bross, P.3    Ang, D.4    Segev, Y.5    Goldsher, D.6    Nemirovski, A.7    Shahar, E.8    Ravid, S.9    Luder, A.10
  • 123
    • 84874901074 scopus 로고    scopus 로고
    • Co-induction of the heat shock response ameliorates disease progression in a mouse model of human spinal and bulbar muscular atrophy: Implications for therapy
    • Malik, B., Nirmalananthan, N., Gray, A. L., La Spada, A. R., Hanna, M. G. and Greensmith, L. (2013). Co-induction of the heat shock response ameliorates disease progression in a mouse model of human spinal and bulbar muscular atrophy: implications for therapy. Brain 136, 926-943.
    • (2013) Brain , vol.136 , pp. 926-943
    • Malik, B.1    Nirmalananthan, N.2    Gray, A.L.3    La Spada, A.R.4    Hanna, M.G.5    Greensmith, L.6
  • 124
    • 84868677556 scopus 로고    scopus 로고
    • Biochemistry and cell biology of tau protein in neurofibrillary degeneration
    • Mandelkow, E.-M. and Mandelkow, E. (2012). Biochemistry and cell biology of tau protein in neurofibrillary degeneration. Cold Spring Harb. Perspect. Med. 2, a006247.
    • (2012) Cold Spring Harb. Perspect. Med. , vol.2
    • Mandelkow, E.-M.1    Mandelkow, E.2
  • 125
    • 84896094717 scopus 로고    scopus 로고
    • DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios
    • PubMed
    • Mansson, C., Kakkar, V., Monsellier, E., Sourigues, Y., Härmark, J., Kampinga, H. H., Melki, R. and Emanuelsson, C. (2013). DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios. Cell Stress Chaperones 19, 227-239. PubMed
    • (2013) Cell Stress Chaperones , vol.19 , pp. 227-239
    • Mansson, C.1    Kakkar, V.2    Monsellier, E.3    Sourigues, Y.4    Härmark, J.5    Kampinga, H.H.6    Melki, R.7    Emanuelsson, C.8
  • 127
    • 44949240513 scopus 로고    scopus 로고
    • Combinational approach of intrabody with enhanced Hsp70 expression addresses multiple pathologies in a fly model of Huntington's disease
    • DOI 10.1096/fj.07-099689
    • McLear, J. A., Lebrecht, D., Messer, A. and Wolfgang, W. J. (2003). Combinational approach of intrabody with enhanced Hsp70 expression addresses multiple pathologies in a fly model of Huntington's disease. FASEB J. 22, 2003-2011. (Pubitemid 351811476)
    • (2008) FASEB Journal , vol.22 , Issue.6 , pp. 2003-2011
    • McLear, J.A.1    Lebrecht, D.2    Messer, A.3    Wolfgang, W.J.4
  • 129
    • 80052488572 scopus 로고    scopus 로고
    • Molecular chaperones and regulation of tau quality control: Strategies for drug discovery in tauopathies
    • Miyata, Y., Koren, J., III, Kiray, J., Dickey, C. A. and Gestwicki, J. (2011). Molecular chaperones and regulation of tau quality control: strategies for drug discovery in tauopathies. Future Med. Chem 3, 1523-1537.
    • (2011) Future Med. Chem , vol.3 , pp. 1523-1537
    • Miyata, Y.1    Koren III, J.2    Kiray, J.3    Dickey, C.A.4    Gestwicki, J.5
  • 130
    • 0141865519 scopus 로고    scopus 로고
    • Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria
    • DOI 10.1093/emboj/cdg485
    • Mokranjac, D., Sichting, M., Neupert, W. and Hell, K. (2003). Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria. EMBO J. 22, 4945-4956. (Pubitemid 37222016)
    • (2003) EMBO Journal , vol.22 , Issue.19 , pp. 4945-4956
    • Mokranjac, D.1    Sichting, M.2    Neupert, W.3    Hell, K.4
  • 131
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto, R. I. (2008). Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 22, 1427-1438.
    • (2008) Genes Dev. , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 132
    • 84866488172 scopus 로고    scopus 로고
    • The heat shock response: Systems biology of proteotoxic stress in aging and disease
    • Morimoto, R. I. (2011). The heat shock response: systems biology of proteotoxic stress in aging and disease. Cold Spring Harb. Symp. Quant. Biol. 76, 91-99.
    • (2011) Cold Spring Harb. Symp. Quant. Biol. , vol.76 , pp. 91-99
    • Morimoto, R.I.1
  • 133
    • 80054747192 scopus 로고    scopus 로고
    • Large potentials of small heat shock proteins
    • Mymrikov, E. V., Seit-Nebi, A. S. and Gusev, N. B. (2011). Large potentials of small heat shock proteins. Physiol. Rev. 91, 1123-1159.
    • (2011) Physiol. Rev. , vol.91 , pp. 1123-1159
    • Mymrikov, E.V.1    Seit-Nebi, A.S.2    Gusev, N.B.3
  • 134
    • 84880940762 scopus 로고    scopus 로고
    • A novel Lys141Thr mutation in small heat shock protein 22 (HSPB8) gene in Charcot-Marie-Tooth disease type 2L
    • Nakhro, K., Park, J. M., Kim, Y. J., Yoon, B. R., Yoo, J. H., Koo, H., Choi, B. O. and Chung, K. W. (2013). A novel Lys141Thr mutation in small heat shock protein 22 (HSPB8) gene in Charcot-Marie-Tooth disease type 2L. Neuromuscul. Disord. 23, 656-663.
    • (2013) Neuromuscul. Disord. , vol.23 , pp. 656-663
    • Nakhro, K.1    Park, J.M.2    Kim, Y.J.3    Yoon, B.R.4    Yoo, J.H.5    Koo, H.6    Choi, B.O.7    Chung, K.W.8
  • 135
    • 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.
    • (2010) PLoS Biol. , vol.8
    • Neef, D.W.1    Turski, M.L.2    Thiele, D.J.3
  • 136
    • 82455210670 scopus 로고    scopus 로고
    • Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases
    • Neef, D. W., Jaeger, A. M. and Thiele, D. J. (2011). Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases. Nat. Rev. Drug Discov. 10, 930-944.
    • (2011) Nat. Rev. Drug Discov. , vol.10 , pp. 930-944
    • Neef, D.W.1    Jaeger, A.M.2    Thiele, D.J.3
  • 139
    • 84872482226 scopus 로고    scopus 로고
    • Intracellular degradation of misfolded tau protein induced by geldanamycin is associated with activation of proteasome
    • Opattova, A., Filipcik, P., Cente, M. and Novak, M. (2013). Intracellular degradation of misfolded tau protein induced by geldanamycin is associated with activation of proteasome. J. Alzheimers Dis. 33, 339-348.
    • (2013) J. Alzheimers Dis. , vol.33 , pp. 339-348
    • Opattova, A.1    Filipcik, P.2    Cente, M.3    Novak, M.4
  • 143
    • 84879920420 scopus 로고    scopus 로고
    • PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone
    • Park, S. H., Kukushkin, Y., Gupta, R., Chen, T., Konagai, A., Hipp, M. S., Hayer-Hartl, M. and Hartl, F. U. (2013). PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone. Cell 154, 134-145.
    • (2013) Cell , vol.154 , pp. 134-145
    • Park, S.H.1    Kukushkin, Y.2    Gupta, R.3    Chen, T.4    Konagai, A.5    Hipp, M.S.6    Hayer-Hartl, M.7    Hartl, F.U.8
  • 144
    • 70350502104 scopus 로고    scopus 로고
    • The MitCHAP-60 disease is due to entropic destabilization of the human mitochondrial Hsp60 oligomer
    • Parnas, A., Nadler, M., Nisemblat, S., Horovitz, A., Mandel, H. and Azem, A. (2009). The MitCHAP-60 disease is due to entropic destabilization of the human mitochondrial Hsp60 oligomer. J. Biol. Chem. 284, 28198-28203.
    • (2009) J. Biol. Chem. , vol.284 , pp. 28198-28203
    • Parnas, A.1    Nadler, M.2    Nisemblat, S.3    Horovitz, A.4    Mandel, H.5    Azem, A.6
  • 145
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell, D. A. and Lindquist, S. (1993). The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu. Rev. Genet. 27, 437-496. (Pubitemid 24011359)
    • (1993) Annual Review of Genetics , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 147
    • 2342455798 scopus 로고    scopus 로고
    • Desmin Aggregate Formation by R120G αB-Crystallin Is Caused by Altered Filament Interactions and Is Dependent upon Network Status in Cells
    • DOI 10.1091/mbc.E03-12-0893
    • Perng, M. D., Wen, S. F., van den IJssel, P., Prescott, A. R. and Quinlan, R. A. (2004). Desmin aggregate formation by R120G alphaB-crystallin is caused by altered filament interactions and is dependent upon network status in cells. Mol. Biol. Cell 15, 2335-2346. (Pubitemid 38580650)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.5 , pp. 2335-2346
    • Perng, M.D.1    Wen, S.F.2    Van Den, I.P.3    Prescott, A.R.4    Quinlan, R.A.5
  • 149
    • 74249109889 scopus 로고    scopus 로고
    • To fold or not to fold: Modulation and consequences of Hsp90 inhibition
    • Peterson, L. B. and Blagg, B. S. J. (2009). To fold or not to fold: modulation and consequences of Hsp90 inhibition. Future Med. Chem. 1, 267-283.
    • (2009) Future Med. Chem. , vol.1 , pp. 267-283
    • Peterson, L.B.1    Blagg, B.S.J.2
  • 151
    • 78049280231 scopus 로고    scopus 로고
    • A Novel mouse model of enhanced proteostasis: Full-length human heat shock factor 1 transgenic mice
    • Pierce, A., Wei, R., Halade, D., Yoo, S.-E., Ran, Q. and Richardson, A. (2010). A Novel mouse model of enhanced proteostasis: Full-length human heat shock factor 1 transgenic mice. Biochem. Biophys. Res. Commun. 402, 59-65.
    • (2010) Biochem. Biophys. Res. Commun. , vol.402 , pp. 59-65
    • Pierce, A.1    Wei, R.2    Halade, D.3    Yoo, S.-E.4    Ran, Q.5    Richardson, A.6
  • 152
    • 84874678862 scopus 로고    scopus 로고
    • Over-expression of heat shock factor 1 phenocopies the effect of chronic inhibition of TOR by rapamycin and is sufficient to ameliorate Alzheimer's-like deficits in mice modeling the disease
    • Pierce, A., Podlutskaya, N., Halloran, J. J., Hussong, S. A., Lin, P. Y., Burbank, R., Hart, M. J. and Galvan, V. (2013). Over-expression of heat shock factor 1 phenocopies the effect of chronic inhibition of TOR by rapamycin and is sufficient to ameliorate Alzheimer's-like deficits in mice modeling the disease. J. Neurochem. 124, 880-893.
    • (2013) J. Neurochem. , vol.124 , pp. 880-893
    • Pierce, A.1    Podlutskaya, N.2    Halloran, J.J.3    Hussong, S.A.4    Lin, P.Y.5    Burbank, R.6    Hart, M.J.7    Galvan, V.8
  • 153
    • 84872403035 scopus 로고    scopus 로고
    • Mutants of human αB-crystallin cause enhanced protein aggregation and apoptosis in mammalian cells: Influence of co-expression of HspB1
    • Raju, I. and Abraham, E. C. (2013). Mutants of human αB-crystallin cause enhanced protein aggregation and apoptosis in mammalian cells: influence of co-expression of HspB1. Biochem. Biophys. Res. Commun. 430, 107-112.
    • (2013) Biochem. Biophys. Res. Commun. , vol.430 , pp. 107-112
    • Raju, I.1    Abraham, E.C.2
  • 154
    • 84866556269 scopus 로고    scopus 로고
    • Identification of protein interfaces between α-synuclein, the principal component of Lewy bodies in Parkinson disease, and the molecular chaperones human Hsc70 and the yeast Ssa1p
    • Redeker, V., Pemberton, S., Bienvenut, W., Bousset, L. and Melki, R. (2012). Identification of protein interfaces between α-synuclein, the principal component of Lewy bodies in Parkinson disease, and the molecular chaperones human Hsc70 and the yeast Ssa1p. J. Biol. Chem. 287, 32630-32639.
    • (2012) J. Biol. Chem. , vol.287 , pp. 32630-32639
    • Redeker, V.1    Pemberton, S.2    Bienvenut, W.3    Bousset, L.4    Melki, R.5
  • 155
    • 77649305375 scopus 로고    scopus 로고
    • 17-AAG induces cytoplasmic α-synuclein aggregate clearance by induction of autophagy
    • Riedel, M., Goldbaum, O., Schwarz, L., Schmitt, S. and Richter-Landsberg, C. (2010). 17-AAG induces cytoplasmic α-synuclein aggregate clearance by induction of autophagy. PLoS ONE 5, e8753.
    • (2010) PLoS ONE , vol.5
    • Riedel, M.1    Goldbaum, O.2    Schwarz, L.3    Schmitt, S.4    Richter-Landsberg, C.5
  • 156
    • 0035503470 scopus 로고    scopus 로고
    • Analysis of heat shock transcription factor for suppression of polyglutamine toxicity
    • DOI 10.1016/S0361-9230(01)00602-5, PII S0361923001006025
    • Rimoldi, M., Servadio, A. and Zimarino, V. (2001). Analysis of heat shock transcription factor for suppression of polyglutamine toxicity. Brain Res. Bull. 56, 353-362. (Pubitemid 33062361)
    • (2001) Brain Research Bulletin , vol.56 , Issue.3-4 , pp. 353-362
    • Rimoldi, M.1    Servadio, A.2    Zimarino, V.3
  • 157
    • 84872458771 scopus 로고    scopus 로고
    • Aggregation and neurotoxicity of recombinant α-synuclein aggregates initiated by dimerization
    • Roostaee, A., Beaudoin, S., Staskevicius, A. and Roucou, X. (2013). Aggregation and neurotoxicity of recombinant α-synuclein aggregates initiated by dimerization. Mol. Neurodegener. 8, 5.
    • (2013) Mol. Neurodegener. , vol.8 , pp. 5
    • Roostaee, A.1    Beaudoin, S.2    Staskevicius, A.3    Roucou, X.4
  • 158
    • 84866122688 scopus 로고    scopus 로고
    • Autophagy modulation as a potential therapeutic target for diverse diseases
    • Rubinsztein, D. C., Codogno, P. and Levine, B. (2012). Autophagy modulation as a potential therapeutic target for diverse diseases. Nat. Rev. Drug Discov. 11, 709-730.
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 709-730
    • Rubinsztein, D.C.1    Codogno, P.2    Levine, B.3
  • 159
    • 84880956773 scopus 로고    scopus 로고
    • Is SOD1 loss of function involved in amyotrophic lateral sclerosis?
    • Saccon, R. A., Bunton-Stasyshyn, R. K., Fisher, E. M. C. and Fratta, P. (2013). Is SOD1 loss of function involved in amyotrophic lateral sclerosis? Brain 136, 2342-2358.
    • (2013) Brain , vol.136 , pp. 2342-2358
    • Saccon, R.A.1    Bunton-Stasyshyn, R.K.2    Fisher, E.M.C.3    Fratta, P.4
  • 160
    • 77749308402 scopus 로고    scopus 로고
    • Amyloid oligomers: Formation and toxicity of Abeta oligomers
    • Sakono, M. and Zako, T. (2010). Amyloid oligomers: formation and toxicity of Abeta oligomers. FEBS J. 277, 1348-1358.
    • (2010) FEBS J. , vol.277 , pp. 1348-1358
    • Sakono, M.1    Zako, T.2
  • 162
    • 77954862456 scopus 로고    scopus 로고
    • Molecular and clinical prodrome of Parkinson's disease: Implications for treatment
    • Schapira, A. H. V. and Tolosa, E. (2010). Molecular and clinical prodrome of Parkinson's disease: implications for treatment. Nat. Rev. Nephrol. 6, 309-317.
    • (2010) Nat. Rev. Nephrol. , vol.6 , pp. 309-317
    • Schapira, A.H.V.1    Tolosa, E.2
  • 167
    • 77956297983 scopus 로고    scopus 로고
    • The HSP70 molecular chaperone is not beneficial in a mouse model of alpha-synucleinopathy
    • Shimshek, D. R., Mueller, M., Wiessner, C., Schweizer, T. and van der Putten, P. H. (2010). The HSP70 molecular chaperone is not beneficial in a mouse model of alpha-synucleinopathy. PLoS ONE 5, e10014.
    • (2010) PLoS ONE , vol.5
    • Shimshek, D.R.1    Mueller, M.2    Wiessner, C.3    Schweizer, T.4    Van Der Putten, P.H.5
  • 168
    • 0029810307 scopus 로고    scopus 로고
    • Genetics of amyotrophic lateral sclerosis
    • Siddique, T. and Deng, H. X. (1996). Genetics of amyotrophic lateral sclerosis. Hum. Mol. Genet. 5, 1465-1470. (Pubitemid 26293909)
    • (1996) Human Molecular Genetics , vol.5 , Issue.REVIEW , pp. 1465-1470
    • Siddique, T.1    Deng, H.-X.2
  • 169
    • 84873665973 scopus 로고    scopus 로고
    • Low endogenous and chemical induced heat shock protein induction in a 0N3Rtau-expressing Drosophila larval model of Alzheimer's disease
    • Sinadinos, C., Quraishe, S., Sealey, M., Samson, P. B., Mudher, A. and Wyttenbach, A. (2013). Low endogenous and chemical induced heat shock protein induction in a 0N3Rtau-expressing Drosophila larval model of Alzheimer's disease. J. Alzheimers Dis. 33, 1117-1133.
    • (2013) J. Alzheimers Dis. , vol.33 , pp. 1117-1133
    • Sinadinos, C.1    Quraishe, S.2    Sealey, M.3    Samson, P.B.4    Mudher, A.5    Wyttenbach, A.6
  • 170
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease
    • Sittler, A., Lurz, R., Lueder, G., Priller, J., Lehrach, H., Hayer-Hartl, M. K., Hartl, F. U. and Wanker, E. E. (2001). Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum. Mol. Genet. 10, 1307-1315. (Pubitemid 32600484)
    • (2001) Human Molecular Genetics , vol.10 , Issue.12 , pp. 1307-1315
    • Sittler, A.1    Lurz, R.2    Lueder, G.3    Priller, J.4    Hayer-Hartl, M.K.5    Hartl, F.U.6    Lehrach, H.7    Wanker, E.E.8
  • 174
    • 0032945938 scopus 로고    scopus 로고
    • Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone
    • Stenoien, D. L., Cummings, C. J., Adams, H. P., Mancini, M. G., Patel, K., DeMartino, G. N., Marcelli, M., Weigel, N. L. and Mancini, M. A. (1999). Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone. Hum. Mol. Genet. 8, 731-741. (Pubitemid 29189040)
    • (1999) Human Molecular Genetics , vol.8 , Issue.5 , pp. 731-741
    • Stenoien, D.L.1    Cummings, C.J.2    Adams, H.P.3    Mancini, M.G.4    Patel, K.5    Demartino, G.N.6    Marcelli, M.7    Weigel, N.L.8    Mancini, M.A.9
  • 178
    • 33749177252 scopus 로고    scopus 로고
    • The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
    • DOI 10.1038/ncb1477, PII NCB1477
    • Tam, S., Geller, R., Spiess, C. and Frydman, J. (2006). The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat. Cell Biol. 8, 1155-1162. (Pubitemid 44473612)
    • (2006) Nature Cell Biology , vol.8 , Issue.10 , pp. 1155-1162
    • Tam, S.1    Geller, R.2    Spiess, C.3    Frydman, J.4
  • 181
    • 0037709152 scopus 로고    scopus 로고
    • The small heat shock protein (HSP) 20 is dynamically associated with the actin cross-linking protein actinin
    • DOI 10.1016/S0022-4804(03)00113-6
    • Tessier, D. J., Komalavilas, P., Panitch, A., Joshi, L. and Brophy, C. M. (2003). The small heat shock protein (HSP) 20 is dynamically associated with the actin cross-linking protein actinin. J. Surg. Res. 111, 152-157. (Pubitemid 36808711)
    • (2003) Journal of Surgical Research , vol.111 , Issue.1 , pp. 152-157
    • Tessier, D.J.1    Komalavilas, P.2    Panitch, A.3    Joshi, L.4    Brophy, C.M.5
  • 182
    • 33744770333 scopus 로고    scopus 로고
    • Pharmacologic and genetic inhibition of hsp90-dependent trafficking reduces aggregation and promotes degradation of the expanded glutamine androgen receptor without stress protein induction
    • DOI 10.1093/hmg/ddl110
    • Thomas, M., Harrell, J. M., Morishima, Y., Peng, H. M., Pratt, W. B. and Lieberman, A. P. (2006). Pharmacologic and genetic inhibition of hsp90-dependent trafficking reduces aggregation and promotes degradation of the expanded glutamine androgen receptor without stress protein induction. Hum. Mol. Genet. 15, 1876-1883. (Pubitemid 43821778)
    • (2006) Human Molecular Genetics , vol.15 , Issue.11 , pp. 1876-1883
    • Thomas, M.1    Harrell, J.M.2    Morishima, Y.3    Peng, H.-M.4    Pratt, W.B.5    Lieberman, A.P.6
  • 183
    • 84861187816 scopus 로고    scopus 로고
    • ER chaperone-metal interactions: Links to protein folding disorders
    • Tiffany-Castiglioni, E. and Qian, Y. (2012). ER chaperone-metal interactions: links to protein folding disorders. Neurotoxicology 33, 545-557.
    • (2012) Neurotoxicology , vol.33 , pp. 545-557
    • Tiffany-Castiglioni, E.1    Qian, Y.2
  • 185
    • 84859708231 scopus 로고    scopus 로고
    • Effect of αB-crystallin on protein aggregation in Drosophila
    • Tue, N. T., Shimaji, K., Tanaka, N. and Yamaguchi, M. (2012). Effect of αB-crystallin on protein aggregation in Drosophila. J. Biomed. Biotechnol. 2012, 252049.
    • (2012) J. Biomed. Biotechnol. , vol.2012 , pp. 252049
    • Tue, N.T.1    Shimaji, K.2    Tanaka, N.3    Yamaguchi, M.4
  • 188
    • 84879983520 scopus 로고    scopus 로고
    • Opportunities and challenges for molecular chaperone modulation to treat protein-conformational brain diseases
    • van der Putten, H. and Lotz, G. P. (2013). Opportunities and challenges for molecular chaperone modulation to treat protein-conformational brain diseases. Neurotherapeutics 10, 416-428.
    • (2013) Neurotherapeutics , vol.10 , pp. 416-428
    • Van Der Putten, H.1    Lotz, G.P.2
  • 189
    • 33749543406 scopus 로고    scopus 로고
    • Differential effects of mitochondrial heat shock protein 60 and related molecular chaperones to prevent intracellular β-amyloid-induced inhibition of complex IV and limit apoptosis
    • DOI 10.1074/jbc.M602533200
    • Veereshwarayya, V., Kumar, P., Rosen, K. M., Mestril, R. and Querfurth, H. W. (2006). Differential effects of mitochondrial heat shock protein 60 and related molecular chaperones to prevent intracellular β-amyloid-induced inhibition of complex IV and limit apoptosis. J. Biol. Chem. 281, 29468-29478. (Pubitemid 44536955)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.40 , pp. 29468-29478
    • Veereshwarayya, V.1    Kumar, P.2    Rosen, K.M.3    Mestril, R.4    Querfurth, H.W.5
  • 190
    • 84855316474 scopus 로고    scopus 로고
    • Mutations in the gene DNAJC5 cause autosomal dominant Kufs disease in a proportion of cases: Study of the Parry family and 8 other families
    • Velinov, M., Dolzhanskaya, N., Gonzalez, M., Powell, E., Konidari, I., Hulme, W., Staropoli, J. F., Xin, W., Wen, G. Y., Barone, R. et al. (2012). Mutations in the gene DNAJC5 cause autosomal dominant Kufs disease in a proportion of cases: study of the Parry family and 8 other families. PLoS ONE 7, e29729.
    • (2012) PLoS ONE , vol.7
    • Velinov, M.1    Dolzhanskaya, N.2    Gonzalez, M.3    Powell, E.4    Konidari, I.5    Hulme, W.6    Staropoli, J.F.7    Xin, W.8    Wen, G.Y.9    Barone, R.10
  • 192
    • 16544383250 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer
    • Wacker, J. L., Zareie, M. H., Fong, H., Sarikaya, M. and Muchowski, P. J. (2004). Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer. Nat. Struct. Mol. Biol. 11, 1215-1222.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1215-1222
    • Wacker, J.L.1    Zareie, M.H.2    Fong, H.3    Sarikaya, M.4    Muchowski, P.J.5
  • 193
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter, P. and Ron, D. (2011). The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081-1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 195
    • 27144503120 scopus 로고    scopus 로고
    • 17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration
    • DOI 10.1038/nm1298, PII N1298
    • Waza, M., Adachi, H., Katsuno, M., Minamiyama, M., Sang, C., Tanaka, F., Inukai, A., Doyu, M. and Sobue, G. (2005). 17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration. Nat. Med. 11, 1088-1095. (Pubitemid 41486831)
    • (2005) Nature Medicine , vol.11 , Issue.10 , pp. 1088-1095
    • Waza, M.1    Adachi, H.2    Katsuno, M.3    Minamiyama, M.4    Sang, C.5    Tanaka, F.6    Inukai, A.7    Doyu, M.8    Sobue, G.9
  • 196
    • 34447540087 scopus 로고    scopus 로고
    • Alleviating neurodegeneration by an anticancer agent: An Hsp90 inhibitor (17-AAG)
    • DOI 10.1196/annals.1377.012, Integrated Molecular Medicine for Neuronal and Neoplastic Disorders
    • Waza, M., Adachi, H., Katsuno, M., Minamiyama, M., Tanaka, F. and Sobue, G. (2006). Alleviating neurodegeneration by an anticancer agent: an Hsp90 inhibitor (17-AAG). Ann. N. Y. Acad. Sci. 1086, 21-34. (Pubitemid 47084380)
    • (2006) Annals of the New York Academy of Sciences , vol.1086 , pp. 21-34
    • Waza, M.1    Adachi, H.2    Katsuno, M.3    Minamiyama, M.4    Tanaka, F.5    Sobue, G.6
  • 197
    • 0033708960 scopus 로고    scopus 로고
    • Huntington disease: New insights on the role of huntingtin cleavage
    • Wellington, C. L., Leavitt, B. R. and Hayden, M. R. (2000). Huntington disease: new insights on the role of huntingtin cleavage. J. Neural Transm. Suppl. 58, 1-17.
    • (2000) J. Neural Transm. Suppl. , vol.58 , pp. 1-17
    • Wellington, C.L.1    Leavitt, B.R.2    Hayden, M.R.3
  • 198
    • 20144366969 scopus 로고    scopus 로고
    • HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome
    • DOI 10.1016/j.cub.2005.04.058, PII S0960982205004847
    • Westhoff, B., Chapple, J. P., van der Spuy, J., Höhfeld, J. and Cheetham, M. E. (2005). HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome. Curr. Biol. 15, 1058-1064. (Pubitemid 40772155)
    • (2005) Current Biology , vol.15 , Issue.11 , pp. 1058-1064
    • Westhoff, B.1    Chapple, J.P.2    Van Der, S.J.3    Hohfeld, J.4    Cheetham, M.E.5
  • 199
    • 33646857038 scopus 로고    scopus 로고
    • Small heat shock proteins inhibit amyloid-β protein aggregation and cerebrovascular amyloid-β protein toxicity
    • DOI 10.1016/j.brainres.2006.03.058, PII S0006899306007621
    • Wilhelmus, M. M. M., Boelens, W. C., Otte-Höller, I., Kamps, B., de Waal, R. M. and Verbeek, M. M. (2006). Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta protein toxicity. Brain Res. 1089, 67-78. (Pubitemid 43786300)
    • (2006) Brain Research , vol.1089 , Issue.1 , pp. 67-78
    • Wilhelmus, M.M.M.1    Boelens, W.C.2    Otte-Holler, I.3    Kamps, B.4    De Waal, R.M.W.5    Verbeek, M.M.6
  • 200
    • 36248968668 scopus 로고    scopus 로고
    • Heat shock proteins and amateur chaperones in amyloid-beta accumulation and clearance in Alzheimer's disease
    • DOI 10.1007/s12035-007-0029-7
    • Wilhelmus, M. M. M., de Waal, R. M. W. and Verbeek, M. M. (2007). Heat shock proteins and amateur chaperones in amyloid-Beta accumulation and clearance in Alzheimer's disease. Mol. Neurobiol. 35, 203-216. (Pubitemid 350129682)
    • (2007) Molecular Neurobiology , vol.35 , Issue.3 , pp. 203-216
    • Wilhelmus, M.M.M.1    De Waal, R.M.W.2    Verbeek, M.M.3
  • 201
    • 76349117689 scopus 로고    scopus 로고
    • Structure of clathrin coat with bound Hsc70 and auxilin: Mechanism of Hsc70-facilitated disassembly
    • Xing, Y., Böcking, T., Wolf, M., Grigorieff, N., Kirchhausen, T. and Harrison, S. C. (2010). Structure of clathrin coat with bound Hsc70 and auxilin: mechanism of Hsc70-facilitated disassembly. EMBO J. 29, 655-665.
    • (2010) EMBO J. , vol.29 , pp. 655-665
    • Xing, Y.1    Böcking, T.2    Wolf, M.3    Grigorieff, N.4    Kirchhausen, T.5    Harrison, S.C.6
  • 202
    • 57149098022 scopus 로고    scopus 로고
    • Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
    • Yam, A. Y., Xia, Y., Lin, H. T., Burlingame, A., Gerstein, M. and Frydman, J. (2008). Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies. Nat. Struct. Mol. Biol. 15, 1255-1262.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1255-1262
    • Yam, A.Y.1    Xia, Y.2    Lin, H.T.3    Burlingame, A.4    Gerstein, M.5    Frydman, J.6
  • 203
    • 0034737299 scopus 로고    scopus 로고
    • Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease
    • Yamamoto, A., Lucas, J. J. and Hen, R. (2000). Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease. Cell 101, 57-66.
    • (2000) Cell , vol.101 , pp. 57-66
    • Yamamoto, A.1    Lucas, J.J.2    Hen, R.3
  • 204
    • 84872541302 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors increase glucocerebrosidase activity in Gaucher disease by modulation of molecular chaperones
    • Yang, C., Rahimpour, S., Lu, J., Pacak, K., Ikejiri, B., Brady, R. O. and Zhuang, Z. (2013). Histone deacetylase inhibitors increase glucocerebrosidase activity in Gaucher disease by modulation of molecular chaperones. Proc. Natl. Acad. Sci. USA 110, 966-971.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 966-971
    • Yang, C.1    Rahimpour, S.2    Lu, J.3    Pacak, K.4    Ikejiri, B.5    Brady, R.O.6    Zhuang, Z.7
  • 205
    • 84876081004 scopus 로고    scopus 로고
    • The small heat shock proteins αB-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 αB-crystallin and Hsp27 suppress SOD1 aggregation in vitro. Cell Stress Chaperones 18, 251-257.
    • (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
  • 206
    • 84897133734 scopus 로고    scopus 로고
    • The role of the cytosolic HSP70 chaperone system in diseases caused by misfolding and aberrant trafficking of ion channels
    • Young, J. C. (2014). The role of the cytosolic HSP70 chaperone system in diseases caused by misfolding and aberrant trafficking of ion channels. Dis. Model. Mech. 7, 319-329.
    • (2014) Dis. Model. Mech. , vol.7 , pp. 319-329
    • Young, J.C.1
  • 207
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • Young, J. C., Moarefi, I. and Hartl, F. U. (2001). Hsp90: a specialized but essential protein-folding tool. J. Cell Biol. 154, 267-274.
    • (2001) J. Cell Biol. , vol.154 , pp. 267-274
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 208
    • 78149416783 scopus 로고    scopus 로고
    • Selective degradation of aggregate-prone CryAB mutants by HSPB1 is mediated by ubiquitin-proteasome pathways
    • Zhang, H., Rajasekaran, N. S., Orosz, A., Xiao, X., Rechsteiner, M. and Benjamin, I. J. (2010). Selective degradation of aggregate-prone CryAB mutants by HSPB1 is mediated by ubiquitin-proteasome pathways. J. Mol. Cell. Cardiol. 49, 918-930.
    • (2010) J. Mol. Cell. Cardiol. , vol.49 , pp. 918-930
    • Zhang, H.1    Rajasekaran, N.S.2    Orosz, A.3    Xiao, X.4    Rechsteiner, M.5    Benjamin, I.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.