메뉴 건너뛰기




Volumn 22, Issue 26, 2016, Pages 4050-4062

The impact of small heat shock proteins (HspBs) in Alzheimer’s and other neurological diseases

Author keywords

Alzheimers disease; Heat shock proteins; HspB; Neurodegeneration; Neuronal stress response; Neuroprotection; Protein aggregation; crystallin

Indexed keywords

AMYLOID BETA PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 22; HEAT SHOCK PROTEIN 27; HSPB2 PROTEIN; HSPB3 PROTEIN; HSPB5 PROTEIN; HSPB6 PROTEIN; SMALL HEAT SHOCK PROTEIN; UNCLASSIFIED DRUG;

EID: 84983805816     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/1381612822666160519113339     Document Type: Review
Times cited : (11)

References (229)
  • 1
    • 34250561475 scopus 로고
    • A new puffing pattern induced by a temperature shock and DNP in Drosophila
    • Ritossa FM. A new puffing pattern induced by a temperature shock and DNP in Drosophila. Experientia 1962; 18: 571-73.
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.M.1
  • 2
    • 0016373748 scopus 로고
    • Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs
    • Tissieres A, Mitchell HK, Tracy UM. Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs. J Mol Biol 1974; 84: 389-98.
    • (1974) J Mol Biol , vol.84 , pp. 389-398
    • Tissieres, A.1    Mitchell, H.K.2    Tracy, U.M.3
  • 3
    • 0037358061 scopus 로고    scopus 로고
    • The human genome encodes 10 alpha-crystallin-related small heat shock proteins: HspB1- 10
    • Kappe G, Franck E, Verschuure P, et al. The human genome encodes 10 alpha-crystallin-related small heat shock proteins: HspB1- 10. Cell Stress Chaperones 2003; 8: 53-61.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 53-61
    • Kappe, G.1    Franck, E.2    Verschuure, P.3
  • 4
    • 64549097439 scopus 로고    scopus 로고
    • Guidelines for the nomenclature of the human heat shock proteins
    • Kampinga HH, Hageman J, Vos MJ, et al. Guidelines for the nomenclature of the human heat shock proteins. Cell Stress Chaperones 2009; 14: 105-11.
    • (2009) Cell Stress Chaperones , vol.14 , pp. 105-111
    • Kampinga, H.H.1    Hageman, J.2    Vos, M.J.3
  • 5
    • 0023917935 scopus 로고
    • Lens crystallins: The evolution and expression of proteins for a highly specialized tissue
    • Wistow GJ, Piatigorsky J. Lens crystallins: the evolution and expression of proteins for a highly specialized tissue. Annu Rev Biochem 1988; 57: 479-504.
    • (1988) Annu Rev Biochem , vol.57 , pp. 479-504
    • Wistow, G.J.1    Piatigorsky, J.2
  • 7
    • 33846840602 scopus 로고    scopus 로고
    • Preventing apoptotic cell death by a novel small heat shock protein
    • Bellyei S, Szigeti A, Pozsgai E, et al. Preventing apoptotic cell death by a novel small heat shock protein. Eur J Cell Biol 2007; 86: 161-71.
    • (2007) Eur J Cell Biol , vol.86 , pp. 161-171
    • Bellyei, S.1    Szigeti, A.2    Pozsgai, E.3
  • 8
    • 77955665257 scopus 로고    scopus 로고
    • Why proteins without an alpha-crystallin domain should not be included in the human small heat shock protein family HSPB
    • Kappe G, Boelens WC, de Jong WW. Why proteins without an alpha-crystallin domain should not be included in the human small heat shock protein family HSPB. Cell Stress Chaperones 2010; 15: 457-461.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 457-461
    • Kappe, G.1    Boelens, W.C.2    De Jong, W.W.3
  • 9
    • 0026483279 scopus 로고
    • Alpha-crystallin can function as a molecular chaperone
    • Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 1992; 89: 10449-53.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 10
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob U, Gaestel M, Engel K, Buchner J. Small heat shock proteins are molecular chaperones. J Biol Chem 1993; 268: 1517-20.
    • (1993) J Biol Chem , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 11
    • 84874157611 scopus 로고    scopus 로고
    • The protective and therapeutic function of small heat shock proteins in neurological diseases
    • Brownell SE, Becker RA, Steinman L. The protective and therapeutic function of small heat shock proteins in neurological diseases. Front Immunol 2012; 3: 74.
    • (2012) Front Immunol , vol.3 , pp. 74
    • Brownell, S.E.1    Becker, R.A.2    Steinman, L.3
  • 12
    • 84951907620 scopus 로고    scopus 로고
    • HspB5/alpha-B-crystallin in the brain, in The Big Book of Small Heat Shock Proteins
    • Tanguay RM, Hightower LE, Eds
    • Golenhofen N, Bartelt-Kirbach B. HspB5/alpha-B-crystallin in the brain, in The Big Book of Small Heat Shock Proteins, In: Tanguay RM, Hightower LE, Eds. Springer International Publishing AG, 2015; pp365-81.
    • (2015) Springer International Publishing AG , pp. 365-381
    • Golenhofen, N.1    Bartelt-Kirbach, B.2
  • 13
    • 84883852928 scopus 로고    scopus 로고
    • Different anti-aggregation and pro-degradative functions of the members of the mammalian sHSP family in neurological disorders
    • Carra S, Rusmini P, Crippa V, et al. Different anti-aggregation and pro-degradative functions of the members of the mammalian sHSP family in neurological disorders. Philos Trans R Soc Lond B Biol Sci 2013; 368: 20110409.
    • (2013) Philos Trans R Soc Lond B Biol Sci , vol.368
    • Carra, S.1    Rusmini, P.2    Crippa, V.3
  • 14
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot: The structure and function of small heat-shock proteins
    • Haslbeck M, Franzmann T, Weinfurtner D, Buchner J. Some like it hot: the structure and function of small heat-shock proteins. Nat Struct Mol Biol 2005; 12: 842-6.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3    Buchner, J.4
  • 15
    • 80054747192 scopus 로고    scopus 로고
    • Large potentials of small heat shock proteins
    • Mymrikov EV, Seit-Nebi AS, Gusev NB. Large potentials of small heat shock proteins. Physiol Rev 2011; 91: 1123-59.
    • (2011) Physiol Rev , vol.91 , pp. 1123-1159
    • Mymrikov, E.V.1    Seit-Nebi, A.S.2    Gusev, N.B.3
  • 17
    • 1342292267 scopus 로고    scopus 로고
    • Crystal structure of a small heat-shock protein
    • Kim KK, Kim R, Kim SH. Crystal structure of a small heat-shock protein. Nature 1998; 394: 595-9.
    • (1998) Nature , vol.394 , pp. 595-599
    • Kim, K.K.1    Kim, R.2    Kim, S.H.3
  • 18
    • 69449107325 scopus 로고    scopus 로고
    • The eye lens chaperone alpha-crystallin forms defined globular assemblies
    • Peschek J, Braun N, Franzmann TM, et al. The eye lens chaperone alpha-crystallin forms defined globular assemblies. Proc Natl Acad Sci USA 2009; 106: 13272-7.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13272-13277
    • Peschek, J.1    Braun, N.2    Franzmann, T.M.3
  • 19
    • 84885081139 scopus 로고    scopus 로고
    • Regulated structural transitions unleash the chaperone activity of alphaB-crystallin
    • Peschek J, Braun N, Rohrberg J, et al. Regulated structural transitions unleash the chaperone activity of alphaB-crystallin. Proc Natl Acad Sci USA 2013; 110: E3780-9.
    • (2013) Proc Natl Acad Sci USA , vol.110
    • Peschek, J.1    Braun, N.2    Rohrberg, J.3
  • 21
    • 84871015004 scopus 로고    scopus 로고
    • Binding determinants of the small heat shock protein, alphaB-crystallin: Recognition of the 'IxI' motif
    • Delbecq SP, Jehle S, Klevit R. Binding determinants of the small heat shock protein, alphaB-crystallin: recognition of the 'IxI' motif. EMBO J 2012; 31: 4587-94.
    • (2012) EMBO J , vol.31 , pp. 4587-4594
    • Delbecq, S.P.1    Jehle, S.2    Klevit, R.3
  • 23
    • 0026342759 scopus 로고
    • Identification of the phosphorylation sites of the murine small heat shock protein hsp25
    • Gaestel M, Schroder W, Benndorf R, et al. Identification of the phosphorylation sites of the murine small heat shock protein hsp25. J Biol Chem 1991; 266: 14721-4.
    • (1991) J Biol Chem , vol.266 , pp. 14721-14724
    • Gaestel, M.1    Schroder, W.2    Benndorf, R.3
  • 24
    • 0020063988 scopus 로고
    • Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin
    • Ingolia TD, Craig EA. Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin. Proc Natl Acad Sci USA 1982; 79: 2360-4.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 2360-2364
    • Ingolia, T.D.1    Craig, E.A.2
  • 26
    • 0031946770 scopus 로고    scopus 로고
    • How chaperones fold proteins
    • Beissinger M, Buchner J. How chaperones fold proteins. Biol Chem 1998; 379: 245-59.
    • (1998) Biol Chem , vol.379 , pp. 245-259
    • Beissinger, M.1    Buchner, J.2
  • 27
    • 0033927557 scopus 로고    scopus 로고
    • Structure and function of small heat shock/alphacrystallin proteins: Established concepts and emerging ideas
    • MacRae TH. Structure and function of small heat shock/alphacrystallin proteins: established concepts and emerging ideas. Cell Mol Life Sci 2000; 57: 899-913.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 899-913
    • Macrae, T.H.1
  • 28
    • 15844414479 scopus 로고    scopus 로고
    • Conformational properties of substrate proteins bound to a molecular chaperone alpha-crystallin
    • Das KP, Petrash JM, Surewicz WK. Conformational properties of substrate proteins bound to a molecular chaperone alpha-crystallin. J Biol Chem 1996; 271: 10449-52.
    • (1996) J Biol Chem , vol.271 , pp. 10449-10452
    • Das, K.P.1    Petrash, J.M.2    Surewicz, W.K.3
  • 29
    • 0029910017 scopus 로고    scopus 로고
    • Molten-globule state of carbonic anhydrase binds to the chaperone-like alpha-crystallin
    • Rajaraman K, Raman B, Rao CM. Molten-globule state of carbonic anhydrase binds to the chaperone-like alpha-crystallin. J Biol Chem 1996; 271: 27595-600.
    • (1996) J Biol Chem , vol.271 , pp. 27595-27600
    • Rajaraman, K.1    Raman, B.2    Rao, C.M.3
  • 30
    • 0033765314 scopus 로고    scopus 로고
    • A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein
    • Lee GJ, Vierling E. A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein. Plant Physiol 2000; 122: 189-98.
    • (2000) Plant Physiol , vol.122 , pp. 189-198
    • Lee, G.J.1    Vierling, E.2
  • 31
    • 0035895908 scopus 로고    scopus 로고
    • Phosphorylation-induced change of the oligomerization state of alpha B-crystallin
    • Ito H, Kamei K, Iwamoto I, et al. Phosphorylation-induced change of the oligomerization state of alpha B-crystallin. J Biol Chem 2001; 276: 5346-52.
    • (2001) J Biol Chem , vol.276 , pp. 5346-5352
    • Ito, H.1    Kamei, K.2    Iwamoto, I.3
  • 32
    • 37349032463 scopus 로고    scopus 로고
    • Effect of phosphorylation on alpha B-crystallin: Differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant
    • Ahmad MF, Raman B, Ramakrishna T, Rao Ch M. Effect of phosphorylation on alpha B-crystallin: differences in stability, subunit exchange and chaperone activity of homo and mixed oligomers of alpha B-crystallin and its phosphorylation-mimicking mutant. J Mol Biol 2008; 375: 1040-51.
    • (2008) J Mol Biol , vol.375 , pp. 1040-1051
    • Ahmad, M.F.1    Raman, B.2    Ramakrishna, T.3    Rao Ch, M.4
  • 33
    • 33846278382 scopus 로고    scopus 로고
    • Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity
    • Ecroyd H, Meehan S, Horwitz J, et al. Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity. Biochem J 2007; 401: 129-41.
    • (2007) Biochem J , vol.401 , pp. 129-141
    • Ecroyd, H.1    Meehan, S.2    Horwitz, J.3
  • 34
    • 0036558366 scopus 로고    scopus 로고
    • Structure and properties of small heat shock proteins (SHsp) and their interaction with cytoskeleton proteins
    • Gusev NB, Bogatcheva NV, Marston SB. Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins. Biochemistry (Mosc) 2002; 67: 511-9.
    • (2002) Biochemistry (Mosc) , vol.67 , pp. 511-519
    • Gusev, N.B.1    Bogatcheva, N.V.2    Marston, S.B.3
  • 35
    • 84864488251 scopus 로고    scopus 로고
    • Small heat shock proteins and the cytoskeleton: An essential interplay for cell integrity?
    • Wettstein G, Bellaye PS, Micheau O, Bonniaud P. Small heat shock proteins and the cytoskeleton: an essential interplay for cell integrity? Int J Biochem Cell Biol 2012; 44: 1680-6.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 1680-1686
    • Wettstein, G.1    Bellaye, P.S.2    Micheau, O.3    Bonniaud, P.4
  • 36
    • 0025813543 scopus 로고
    • A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein
    • Miron T, Vancompernolle K, Vandekerckhove J, Wilchek M, Geiger B. A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein. J Cell Biol 1991; 114: 255-61.
    • (1991) J Cell Biol , vol.114 , pp. 255-261
    • Miron, T.1    Vancompernolle, K.2    Vandekerckhove, J.3    Wilchek, M.4    Geiger, B.5
  • 37
    • 0027417852 scopus 로고
    • Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization
    • Lavoie JN, Gingras-Breton G, Tanguay RM, Landry J. Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization. J Biol Chem 1993; 268: 3420-9.
    • (1993) J Biol Chem , vol.268 , pp. 3420-3429
    • Lavoie, J.N.1    Gingras-Breton, G.2    Tanguay, R.M.3    Landry, J.4
  • 38
    • 0028365799 scopus 로고
    • Sense and antisense modification of glial alpha B-crystallin production results in alterations of stress fiber formation and thermoresistance
    • Iwaki T, Iwaki A, Tateishi J, Goldman JE. Sense and antisense modification of glial alpha B-crystallin production results in alterations of stress fiber formation and thermoresistance. J Cell Biol 1994; 125: 1385-93.
    • (1994) J Cell Biol , vol.125 , pp. 1385-1393
    • Iwaki, T.1    Iwaki, A.2    Tateishi, J.3    Goldman, J.E.4
  • 39
    • 33846618592 scopus 로고    scopus 로고
    • Association of alphaB-crystallin, a small heat shock protein, with actin: Role in modulating actin filament dynamics in vivo
    • Singh BN, Rao KS, Ramakrishna T, Rangaraj N, Rao Ch M. Association of alphaB-crystallin, a small heat shock protein, with actin: role in modulating actin filament dynamics in vivo. J Mol Biol 2007; 366: 756-67.
    • (2007) J Mol Biol , vol.366 , pp. 756-767
    • Singh, B.N.1    Rao, K.S.2    Ramakrishna, T.3    Rangaraj, N.4    Rao Ch, M.5
  • 40
    • 0029658123 scopus 로고    scopus 로고
    • Spector A. Alpha-crystallin stabilizes actin filaments and prevents cytochalasin-induced depolymerization in a phosphorylation- dependent manner
    • Wang K, Spector A. alpha-crystallin stabilizes actin filaments and prevents cytochalasin-induced depolymerization in a phosphorylation- dependent manner. Eur J Biochem 1996; 242: 56-66.
    • (1996) Eur J Biochem , vol.242 , pp. 56-66
    • Wang, K.1
  • 41
    • 0032818827 scopus 로고    scopus 로고
    • Intermediate filament interactions can be altered by HSP27 and alphaB-crystallin
    • Perng MD, Cairns L, van den IP, et al. Intermediate filament interactions can be altered by HSP27 and alphaB-crystallin. J Cell Sci 1999; 112: 2099-112.
    • (1999) J Cell Sci , vol.112 , pp. 2099-2112
    • Perng, M.D.1    Cairns, L.2    Van Den, I.P.3
  • 42
    • 0028176579 scopus 로고
    • Chaperone activity of alpha-crystallins modulates intermediate filament assembly
    • Nicholl ID, Quinlan RA. Chaperone activity of alpha-crystallins modulates intermediate filament assembly. EMBO J 1994; 13: 945-53.
    • (1994) EMBO J , vol.13 , pp. 945-953
    • Nicholl, I.D.1    Quinlan, R.A.2
  • 43
    • 17344361902 scopus 로고    scopus 로고
    • A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy
    • Vicart P, Caron A, Guicheney P, et al. A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat Genet 1998; 20: 92-5.
    • (1998) Nat Genet , vol.20 , pp. 92-95
    • Vicart, P.1    Caron, A.2    Guicheney, P.3
  • 44
    • 0344664368 scopus 로고    scopus 로고
    • Myofibrillar myopathy caused by novel dominant negative alpha B-crystallin mutations
    • Selcen D, Engel AG. Myofibrillar myopathy caused by novel dominant negative alpha B-crystallin mutations. Ann Neurol 2003; 54: 804-10.
    • (2003) Ann Neurol , vol.54 , pp. 804-810
    • Selcen, D.1    Engel, A.G.2
  • 45
    • 84856014037 scopus 로고    scopus 로고
    • A novel CRYAB mutation resulting in multisystemic disease
    • Sacconi S, Feasson L, Antoine JC, et al. A novel CRYAB mutation resulting in multisystemic disease. Neuromuscul Disord 2012; 22: 66-72.
    • (2012) Neuromuscul Disord , vol.22 , pp. 66-72
    • Sacconi, S.1    Feasson, L.2    Antoine, J.C.3
  • 46
    • 0031457379 scopus 로고    scopus 로고
    • Chaperone activity of alpha B-crystallin suppresses tubulin aggregation through complex formation
    • Arai H, Atomi Y. Chaperone activity of alpha B-crystallin suppresses tubulin aggregation through complex formation. Cell Struct Funct 1997; 22: 539-44.
    • (1997) Cell Struct Funct , vol.22 , pp. 539-544
    • Arai, H.1    Atomi, Y.2
  • 47
    • 2342439076 scopus 로고    scopus 로고
    • AlphaB-Crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassembly
    • Fujita Y, Ohto E, Katayama E, Atomi Y. alphaB-Crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassembly. J Cell Sci 2004; 117: 1719-26.
    • (2004) J Cell Sci , vol.117 , pp. 1719-1726
    • Fujita, Y.1    Ohto, E.2    Katayama, E.3    Atomi, Y.4
  • 48
    • 33744475377 scopus 로고    scopus 로고
    • Alpha-crystallin expression affects microtubule assembly and prevents their aggregation
    • Xi JH, Bai F, McGaha R, Andley UP. Alpha-crystallin expression affects microtubule assembly and prevents their aggregation. Faseb J 2006; 20: 846-57.
    • (2006) Faseb J , vol.20 , pp. 846-857
    • Xi, J.H.1    Bai, F.2    McGaha, R.3    Ley, U.P.4
  • 49
    • 77955621867 scopus 로고    scopus 로고
    • Dynamic subunit exchange and the regulation of microtubule assembly by the stress response protein human alphaB crystallin
    • Houck SA, Clark JI. Dynamic subunit exchange and the regulation of microtubule assembly by the stress response protein human alphaB crystallin. PLoS One 2010; 5: e11795.
    • (2010) Plos One , vol.5
    • Houck, S.A.1    Clark, J.I.2
  • 50
    • 31644431943 scopus 로고    scopus 로고
    • Molecular chaperone alpha-crystallin prevents detrimental effects of neuroinflammation
    • Masilamoni JG, Jesudason EP, Baben B, et al. Molecular chaperone alpha-crystallin prevents detrimental effects of neuroinflammation. Biochim Biophys Acta 2006; 1762: 284-93.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 284-293
    • Masilamoni, J.G.1    Jesudason, E.P.2    Baben, B.3
  • 51
    • 84874677592 scopus 로고    scopus 로고
    • Suppression of neuroinflammation by astrocytic dopamine D2 receptors via alphaB-crystallin
    • Shao W, Zhang SZ, Tang M, et al. Suppression of neuroinflammation by astrocytic dopamine D2 receptors via alphaB-crystallin. Nature 2013; 494: 90-4.
    • (2013) Nature , vol.494 , pp. 90-94
    • Shao, W.1    Zhang, S.Z.2    Tang, M.3
  • 53
    • 34547152612 scopus 로고    scopus 로고
    • Protective and therapeutic role for alphaB-crystallin in autoimmune demyelination
    • Ousman SS, Tomooka BH, van Noort JM, et al. Protective and therapeutic role for alphaB-crystallin in autoimmune demyelination. Nature 2007; 448: 474-9.
    • (2007) Nature , vol.448 , pp. 474-479
    • Ousman, S.S.1    Tomooka, B.H.2    Van Noort, J.M.3
  • 54
    • 0032722324 scopus 로고    scopus 로고
    • HSP27 inhibits cytochrome c-dependent activation of procaspase-9
    • Garrido C, Bruey JM, Fromentin A, et al. HSP27 inhibits cytochrome c-dependent activation of procaspase-9. FASEB J 1999; 13: 2061-70.
    • (1999) FASEB J , vol.13 , pp. 2061-2070
    • Garrido, C.1    Bruey, J.M.2    Fromentin, A.3
  • 56
    • 0034282104 scopus 로고    scopus 로고
    • Hsp27 negatively regulates cell death by interacting with cytochrome c
    • Bruey JM, Ducasse C, Bonniaud P, et al. Hsp27 negatively regulates cell death by interacting with cytochrome c. Nat Cell Biol 2000; 2: 645-52.
    • (2000) Nat Cell Biol , vol.2 , pp. 645-652
    • Bruey, J.M.1    Ducasse, C.2    Bonniaud, P.3
  • 57
    • 0034643424 scopus 로고    scopus 로고
    • Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase- 3
    • Pandey P, Farber R, Nakazawa A, et al. Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase- 3. Oncogene 2000; 19: 1975-81.
    • (2000) Oncogene , vol.19 , pp. 1975-1981
    • Pandey, P.1    Farber, R.2    Nakazawa, A.3
  • 58
    • 0037064065 scopus 로고    scopus 로고
    • The small heat shock protein alpha B-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation
    • Kamradt MC, Chen F, Sam S, Cryns VL. The small heat shock protein alpha B-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation. J Biol Chem 2002; 277: 38731-36.
    • (2002) J Biol Chem , vol.277 , pp. 38731-38736
    • Kamradt, M.C.1    Chen, F.2    Sam, S.3    Cryns, V.L.4
  • 59
    • 49449083377 scopus 로고    scopus 로고
    • Bcl2L12-mediated inhibition of effector caspase-3 and caspase-7 via distinct mechanisms in glioblastoma
    • Stegh AH, Kesari S, Mahoney JE, et al. Bcl2L12-mediated inhibition of effector caspase-3 and caspase-7 via distinct mechanisms in glioblastoma. Proc Natl Acad Sci USA 2008; 105: 10703-8.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10703-10708
    • Stegh, A.H.1    Kesari, S.2    Mahoney, J.E.3
  • 60
    • 78649322648 scopus 로고    scopus 로고
    • The small heat shock protein HspB2 is a novel anti-apoptotic protein that inhibits apical caspase activation in the extrinsic apoptotic pathway
    • Oshita SE, Chen F, Kwan T, Yehiely F, Cryns VL. The small heat shock protein HspB2 is a novel anti-apoptotic protein that inhibits apical caspase activation in the extrinsic apoptotic pathway. Breast Cancer Res Treat 2010; 124: 307-15.
    • (2010) Breast Cancer Res Treat , vol.124 , pp. 307-315
    • Oshita, S.E.1    Chen, F.2    Kwan, T.3    Yehiely, F.4    Cryns, V.L.5
  • 61
    • 0002527685 scopus 로고
    • Untersuchung der Proteinsubstanzen in den lichtbrechenden Medien des Auges
    • Mörner CT. Untersuchung der Proteinsubstanzen in den lichtbrechenden Medien des Auges. Hoppe Seyler`s Z Physiol Chem 1894; 18: 61-106.
    • (1894) Hoppe Seyler`S Z Physiol Chem , vol.18 , pp. 61-106
    • Mörner, C.T.1
  • 62
    • 0028293240 scopus 로고
    • Characterization of the alpha-gamma and alpha-beta complex: Evidence for an in vivo functional role of alpha- crystallin as a molecular chaperone
    • Boyle D, Takemoto L. Characterization of the alpha-gamma and alpha-beta complex: evidence for an in vivo functional role of alpha- crystallin as a molecular chaperone. Exp Eye Res 1994; 58: 9-15.
    • (1994) Exp Eye Res , vol.58 , pp. 9-15
    • Boyle, D.1    Takemoto, L.2
  • 63
    • 0034486034 scopus 로고    scopus 로고
    • The function of alpha-crystallin in vision
    • Horwitz J. The function of alpha-crystallin in vision. Semin Cell Dev Biol 2000; 11: 53-60.
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 53-60
    • Horwitz, J.1
  • 64
    • 0024578954 scopus 로고
    • Alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues
    • Bhat SP, Nagineni CN. alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues. Biochem Biophys Res Commun 1989; 158: 319-25.
    • (1989) Biochem Biophys Res Commun , vol.158 , pp. 319-325
    • Bhat, S.P.1    Nagineni, C.N.2
  • 65
    • 0025101570 scopus 로고
    • Cellular distribution of alpha B-crystallin in non-lenticular tissues
    • Iwaki T, Kume-Iwaki A, Goldman JE. Cellular distribution of alpha B-crystallin in non-lenticular tissues. J Histochem Cytochem 1990; 38: 31-9.
    • (1990) J Histochem Cytochem , vol.38 , pp. 31-39
    • Iwaki, T.1    Kume-Iwaki, A.2    Goldman, J.E.3
  • 66
    • 0024580908 scopus 로고
    • Expression of the murine alpha B-crystallin gene is not restricted to the lens
    • Dubin RA, Wawrousek EF, Piatigorsky J. Expression of the murine alpha B-crystallin gene is not restricted to the lens. Mol Cell Biol 1989; 9: 1083-91.
    • (1989) Mol Cell Biol , vol.9 , pp. 1083-1091
    • Dubin, R.A.1    Wawrousek, E.F.2    Piatigorsky, J.3
  • 67
    • 0033984092 scopus 로고    scopus 로고
    • Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation
    • Sugiyama Y, Suzuki A, Kishikawa M, et al. Muscle develops a specific form of small heat shock protein complex composed of MKBP/HSPB2 and HSPB3 during myogenic differentiation. J Biol Chem 2000; 275: 1095-104.
    • (2000) J Biol Chem , vol.275 , pp. 1095-1104
    • Sugiyama, Y.1    Suzuki, A.2    Kishikawa, M.3
  • 68
    • 0033579508 scopus 로고    scopus 로고
    • Identification and characterization of cvHsp. A novel human small stress protein selectively expressed in cardiovascular and insulin- sensitive tissues
    • Krief S, Faivre JF, Robert P, et al. Identification and characterization of cvHsp. A novel human small stress protein selectively expressed in cardiovascular and insulin- sensitive tissues. J Biol Chem 1999; 274: 36592-600.
    • (1999) J Biol Chem , vol.274 , pp. 36592-36600
    • Krief, S.1    Faivre, J.F.2    Robert, P.3
  • 69
    • 0035920143 scopus 로고    scopus 로고
    • HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 ((3D)HSP27)
    • Benndorf R, Sun X, Gilmont RR, et al. HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 ((3D)HSP27). J Biol Chem 2001; 276: 26753-61.
    • (2001) J Biol Chem , vol.276 , pp. 26753-26761
    • Benndorf, R.1    Sun, X.2    Gilmont, R.R.3
  • 70
    • 84864437102 scopus 로고    scopus 로고
    • Small heat shock proteins in redox metabolism: Implications for cardiovascular diseases
    • Christians ES, Ishiwata T, Benjamin IJ. Small heat shock proteins in redox metabolism: implications for cardiovascular diseases. Int J Biochem Cell Biol 2012; 44: 1632-45.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 1632-1645
    • Christians, E.S.1    Ishiwata, T.2    Benjamin, I.J.3
  • 71
    • 0033104818 scopus 로고    scopus 로고
    • Binding of the stress protein alpha B-crystallin to cardiac myofibrils correlates with the degree of myocardial damage during ischemia/reperfusion in vivo
    • Golenhofen N, Htun P, Ness W, et al. Binding of the stress protein alpha B-crystallin to cardiac myofibrils correlates with the degree of myocardial damage during ischemia/reperfusion in vivo. J Mol Cell Cardiol 1999; 31: 569-80.
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 569-580
    • Golenhofen, N.1    Htun, P.2    Ness, W.3
  • 73
    • 0035124724 scopus 로고    scopus 로고
    • Transgene overexpression of aB crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion
    • Ray PS, Martin JL, Swanson EA, et al. Transgene overexpression of aB crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion. FASEB J 2001; 15: 393-402.
    • (2001) FASEB J , vol.15 , pp. 393-402
    • Ray, P.S.1    Martin, J.L.2    Swanson, E.A.3
  • 74
    • 33344474711 scopus 로고    scopus 로고
    • Alpha B-crystallin mutation in dilated cardiomyopathy
    • Inagaki N, Hayashi T, Arimura T, et al. Alpha B-crystallin mutation in dilated cardiomyopathy. Biochem Biophys Res Commun 2006; 342: 379-86.
    • (2006) Biochem Biophys Res Commun , vol.342 , pp. 379-386
    • Inagaki, N.1    Hayashi, T.2    Arimura, T.3
  • 75
    • 0026694490 scopus 로고
    • Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments
    • Bennardini F, Wrzosek A, Chiesi M. Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments. Circ Res 1992; 71: 288-94.
    • (1992) Circ Res , vol.71 , pp. 288-294
    • Bennardini, F.1    Wrzosek, A.2    Chiesi, M.3
  • 76
    • 1542349941 scopus 로고    scopus 로고
    • Association of the chaperone alphaB-crystallin with titin in heart muscle
    • Bullard B, Ferguson C, Minajeva A, et al. Association of the chaperone alphaB-crystallin with titin in heart muscle. J Biol Chem 2004; 279: 7917-24.
    • (2004) J Biol Chem , vol.279 , pp. 7917-7924
    • Bullard, B.1    Ferguson, C.2    Minajeva, A.3
  • 77
    • 0036517816 scopus 로고    scopus 로고
    • Ischemiainduced association of the stress protein alpha B-crystallin with Iband portion of cardiac titin
    • Golenhofen N, Arbeiter A, Koob R, Drenckhahn D. Ischemiainduced association of the stress protein alpha B-crystallin with Iband portion of cardiac titin. J Mol Cell Cardiol 2002; 34: 309-19.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 309-319
    • Golenhofen, N.1    Arbeiter, A.2    Koob, R.3    Drenckhahn, D.4
  • 78
    • 29044442697 scopus 로고    scopus 로고
    • Ischemiainduced increase of stiffness of alphaB-crystallin/HSPB2-deficient myocardium
    • Golenhofen N, Redel A, Wawrousek EF, Drenckhahn D. Ischemiainduced increase of stiffness of alphaB-crystallin/HSPB2-deficient myocardium. Pflugers Arch 2006; 451: 518-25.
    • (2006) Pflugers Arch , vol.451 , pp. 518-525
    • Golenhofen, N.1    Redel, A.2    Wawrousek, E.F.3    Drenckhahn, D.4
  • 79
    • 38049170987 scopus 로고    scopus 로고
    • Unmasking different mechanical and energetic roles for the small heat shock proteins CryAB and HSPB2 using genetically modified mouse hearts
    • Pinz I, Robbins J, Rajasekaran NS, Benjamin IJ, Ingwall JS. Unmasking different mechanical and energetic roles for the small heat shock proteins CryAB and HSPB2 using genetically modified mouse hearts. FASEB J 2008; 22: 84-92.
    • (2008) FASEB J , vol.22 , pp. 84-92
    • Pinz, I.1    Robbins, J.2    Rajasekaran, N.S.3    Benjamin, I.J.4    Ingwall, J.S.5
  • 80
    • 0027490757 scopus 로고
    • Sequence, expression, and chromosomal assignment of a human sperm outer dense fiber gene
    • Gastmann O, Burfeind P, Gunther E, et al. Sequence, expression, and chromosomal assignment of a human sperm outer dense fiber gene. Mol Reprod Dev 1993; 36: 407-18.
    • (1993) Mol Reprod Dev , vol.36 , pp. 407-418
    • Gastmann, O.1    Burfeind, P.2    Gunther, E.3
  • 81
    • 0035973873 scopus 로고    scopus 로고
    • Characterization of two novel human small heat shock proteins: Protein kinase-related HspB8 and testis-specific HspB9
    • Kappe G, Verschuure P, Philipsen RL, et al. Characterization of two novel human small heat shock proteins: protein kinase-related HspB8 and testis-specific HspB9. Biochim Biophys Acta 2001; 1520: 1-6.
    • (2001) Biochim Biophys Acta , vol.1520 , pp. 1-6
    • Kappe, G.1    Verschuure, P.2    Philipsen, R.L.3
  • 82
    • 78650187121 scopus 로고    scopus 로고
    • Differential expression and induction of small heat shock proteins in rat brain and cultured hippocampal neurons
    • Kirbach BB, Golenhofen N. Differential expression and induction of small heat shock proteins in rat brain and cultured hippocampal neurons. J Neurosci Res 2011; 89: 162-75.
    • (2011) J Neurosci Res , vol.89 , pp. 162-175
    • Kirbach, B.B.1    Golenhofen, N.2
  • 83
    • 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 WC, O'Connor V, Wyttenbach A. Expression of the small heat shock protein family in the mouse CNS: Differential anatomical and biochemical compartmentalization. Neuroscience 2008; 153: 483-91.
    • (2008) Neuroscience , vol.153 , pp. 483-491
    • Quraishe, S.1    Asuni, A.2    Boelens, W.C.3    O'connor, V.4    Wyttenbach, A.5
  • 84
    • 0025877859 scopus 로고
    • Tissue distribution and developmental profiles of immunoreactive alpha B crystallin in the rat determined with a sensitive immunoassay system
    • Kato K, Shinohara H, Kurobe N, et al. Tissue distribution and developmental profiles of immunoreactive alpha B crystallin in the rat determined with a sensitive immunoassay system. Biochim Biophys Acta 1991; 1074: 201-8.
    • (1991) Biochim Biophys Acta , vol.1074 , pp. 201-208
    • Kato, K.1    Shinohara, H.2    Kurobe, N.3
  • 85
    • 34250899962 scopus 로고    scopus 로고
    • Neuronal expression of constitutive heat shock proteins: Implications for neurodegenerative diseases
    • Chen S, Brown IR. Neuronal expression of constitutive heat shock proteins: implications for neurodegenerative diseases. Cell Stress Chaperones 2007; 12: 51-8.
    • (2007) Cell Stress Chaperones , vol.12 , pp. 51-58
    • Chen, S.1    Brown, I.R.2
  • 86
    • 0030760798 scopus 로고    scopus 로고
    • Constitutive expression of the 27-kDa heat shock protein (Hsp27) in sensory and motor neurons of the rat nervous system
    • Plumier JC, Hopkins DA, Robertson HA, Currie RW. Constitutive expression of the 27-kDa heat shock protein (Hsp27) in sensory and motor neurons of the rat nervous system. J Comp Neurol 1997; 384: 409-28.
    • (1997) J Comp Neurol , vol.384 , pp. 409-428
    • Plumier, J.C.1    Hopkins, D.A.2    Robertson, H.A.3    Currie, R.W.4
  • 87
    • 0034677093 scopus 로고    scopus 로고
    • Constitutive expression of the 25-kDa heat shock protein Hsp25 reveals novel parasagittal bands of purkinje cells in the adult mouse cerebellar cortex
    • Armstrong CL, Krueger-Naug AM, Currie RW, Hawkes R. Constitutive expression of the 25-kDa heat shock protein Hsp25 reveals novel parasagittal bands of purkinje cells in the adult mouse cerebellar cortex. J Comp Neurol 2000; 416: 383-97.
    • (2000) J Comp Neurol , vol.416 , pp. 383-397
    • Armstrong, C.L.1    Krueger-Naug, A.M.2    Currie, R.W.3    Hawkes, R.4
  • 88
    • 33644960735 scopus 로고    scopus 로고
    • Specific association of small heat shock proteins with the pathological hallmarks of Alzheimer's disease brains
    • Wilhelmus MM, Otte-Holler I, Wesseling P, et al. Specific association of small heat shock proteins with the pathological hallmarks of Alzheimer's disease brains. Neuropathol Appl Neurobiol 2006; 32: 119-30.
    • (2006) Neuropathol Appl Neurobiol , vol.32 , pp. 119-130
    • Wilhelmus, M.M.1    Otte-Holler, I.2    Wesseling, P.3
  • 89
    • 0037179756 scopus 로고    scopus 로고
    • Hsp27 upregulation and phosphorylation is required for injured sensory and motor neuron survival
    • Benn SC, Perrelet D, Kato AC, et al. Hsp27 upregulation and phosphorylation is required for injured sensory and motor neuron survival. Neuron 2002; 36: 45-56.
    • (2002) Neuron , vol.36 , pp. 45-56
    • Benn, S.C.1    Perrelet, D.2    Kato, A.C.3
  • 90
    • 31344457455 scopus 로고    scopus 로고
    • Stress-induced heat shock protein 27 expression and its role in dorsal root ganglion neuronal survival
    • Dodge ME, Wang J, Guy C, et al. Stress-induced heat shock protein 27 expression and its role in dorsal root ganglion neuronal survival. Brain Res 2006; 1068: 34-48.
    • (2006) Brain Res , vol.1068 , pp. 34-48
    • Dodge, M.E.1    Wang, J.2    Guy, C.3
  • 91
    • 2642563501 scopus 로고    scopus 로고
    • Mutant small heatshock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy
    • Evgrafov OV, Mersiyanova I, Irobi J, et al. Mutant small heatshock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy. Nat Genet 2004; 36: 602-6.
    • (2004) Nat Genet , vol.36 , pp. 602-606
    • Evgrafov, O.V.1    Mersiyanova, I.2    Irobi, J.3
  • 92
    • 58149243285 scopus 로고    scopus 로고
    • Mutations in the HSP27 (HSPB1) gene cause dominant, recessive, and sporadic distal HMN/CMT type 2
    • Houlden H, Laura M, Wavrant-De Vrieze F, et al. Mutations in the HSP27 (HSPB1) gene cause dominant, recessive, and sporadic distal HMN/CMT type 2. Neurology 2008; 71: 1660-8.
    • (2008) Neurology , vol.71 , pp. 1660-1668
    • Houlden, H.1    Laura, M.2    Wavrant-De Vrieze, F.3
  • 93
    • 80051711544 scopus 로고    scopus 로고
    • Small heat shock proteins induce a cerebral inflammatory reaction
    • Bruinsma IB, de Jager M, Carrano A, et al. Small heat shock proteins induce a cerebral inflammatory reaction. J Neurosci 2011; 31: 11992-2000.
    • (2011) J Neurosci , vol.31 , pp. 11992-12000
    • Bruinsma, I.B.1    De Jager, M.2    Carrano, A.3
  • 94
    • 70350018303 scopus 로고    scopus 로고
    • The small heat-shock proteins HSPB2 and HSPB3 form well-defined heterooligomers in a unique 3 to 1 subunit ratio
    • den Engelsman J, Boros S, Dankers PY, et al. The small heat-shock proteins HSPB2 and HSPB3 form well-defined heterooligomers in a unique 3 to 1 subunit ratio. J Mol Biol 2009; 393: 1022-32.
    • (2009) J Mol Biol , vol.393 , pp. 1022-1032
    • Den Engelsman, J.1    Boros, S.2    Dankers, P.Y.3
  • 95
    • 0026539546 scopus 로고
    • Accumulation of alpha Bcrystallin in central nervous system glia and neurons in pathologic conditions
    • Iwaki T, Wisniewski T, Iwaki A, et al. Accumulation of alpha Bcrystallin in central nervous system glia and neurons in pathologic conditions. Am J Pathol 1992; 140: 345-56.
    • (1992) Am J Pathol , vol.140 , pp. 345-356
    • Iwaki, T.1    Wisniewski, T.2    Iwaki, A.3
  • 96
    • 0026775476 scopus 로고
    • Ultrastructural and immunohistochemical studies on ballooned cortical neurons in Creutzfeldt- Jakob disease: Expression of alpha B-crystallin, ubiquitin and stress-response protein 27
    • Kato S, Hirano A, Umahara T, et al. Ultrastructural and immunohistochemical studies on ballooned cortical neurons in Creutzfeldt- Jakob disease: expression of alpha B-crystallin, ubiquitin and stress-response protein 27. Acta Neuropathol 1992; 84: 443-8.
    • (1992) Acta Neuropathol , vol.84 , pp. 443-448
    • Kato, S.1    Hirano, A.2    Umahara, T.3
  • 97
    • 0026782217 scopus 로고
    • Ballooned neurons in several neurodegenerative diseases and stroke contain alpha B crystallin
    • Lowe J, Errington DR, Lennox G, et al. Ballooned neurons in several neurodegenerative diseases and stroke contain alpha B crystallin. Neuropathol Appl Neurobiol 1992; 18: 341-50.
    • (1992) Neuropathol Appl Neurobiol , vol.18 , pp. 341-350
    • Lowe, J.1    Errington, D.R.2    Lennox, G.3
  • 98
    • 33646745737 scopus 로고    scopus 로고
    • Increased neuronal expression of alpha B-crystallin in human olivary hypertrophy
    • Fukushima K, Mizuno Y, Takatama M, Okamoto K. Increased neuronal expression of alpha B-crystallin in human olivary hypertrophy. Neuropathology 2006; 26: 196-200.
    • (2006) Neuropathology , vol.26 , pp. 196-200
    • Fukushima, K.1    Mizuno, Y.2    Takatama, M.3    Okamoto, K.4
  • 100
    • 84867331182 scopus 로고    scopus 로고
    • Phosphorylationdependent subcellular localization of the small heat shock proteins HspB1/Hsp25 and HspB5/alphaB-crystallin in cultured hippocampal neurons
    • Schmidt T, Bartelt-Kirbach B, Golenhofen N. Phosphorylationdependent subcellular localization of the small heat shock proteins HspB1/Hsp25 and HspB5/alphaB-crystallin in cultured hippocampal neurons. Histochem Cell Biol 2012; 138: 407-18.
    • (2012) Histochem Cell Biol , vol.138 , pp. 407-418
    • Schmidt, T.1    Bartelt-Kirbach, B.2    Golenhofen, N.3
  • 101
    • 0027968222 scopus 로고
    • Coordinate and independent regulation of alpha B-crystallin and hsp27 expression in response to physiological stress
    • Head MW, Corbin E, Goldman JE. Coordinate and independent regulation of alpha B-crystallin and hsp27 expression in response to physiological stress. J Cell Physiol 1994; 159: 41-50.
    • (1994) J Cell Physiol , vol.159 , pp. 41-50
    • Head, M.W.1    Corbin, E.2    Goldman, J.E.3
  • 102
    • 0029937530 scopus 로고    scopus 로고
    • Transcription regulation of alpha B-crystallin in astrocytes: Analysis of HSF and AP1 activation by different types of physiological stress
    • Head MW, Hurwitz L, Goldman JE. Transcription regulation of alpha B-crystallin in astrocytes: analysis of HSF and AP1 activation by different types of physiological stress. J Cell Sci 1996; 109 (Pt 5): 1029-39.
    • (1996) J Cell Sci , vol.109 , pp. 1029-1039
    • Head, M.W.1    Hurwitz, L.2    Goldman, J.E.3
  • 103
    • 0027495153 scopus 로고
    • Coinduction of two lowmolecular- weight stress proteins, alpha B crystallin and HSP28, by heat or arsenite stress in human glioma cells
    • Kato K, Goto S, Hasegawa K, Inaguma Y. Coinduction of two lowmolecular- weight stress proteins, alpha B crystallin and HSP28, by heat or arsenite stress in human glioma cells. J Biochem 1993; 114: 640-7.
    • (1993) J Biochem , vol.114 , pp. 640-647
    • Kato, K.1    Goto, S.2    Hasegawa, K.3    Inaguma, Y.4
  • 104
    • 0027742866 scopus 로고
    • Alpha Bcrystallin and 27-kd heat shock protein are regulated by stress conditions in the central nervous system and accumulate in Rosenthal fibers
    • Iwaki T, Iwaki A, Tateishi J, Sakaki Y, Goldman JE. Alpha Bcrystallin and 27-kd heat shock protein are regulated by stress conditions in the central nervous system and accumulate in Rosenthal fibers. Am J Pathol 1993; 143: 487-95.
    • (1993) Am J Pathol , vol.143 , pp. 487-495
    • Iwaki, T.1    Iwaki, A.2    Tateishi, J.3    Sakaki, Y.4    Goldman, J.E.5
  • 105
    • 0034801245 scopus 로고    scopus 로고
    • Stress proteins in oligodendrocytes: Differential effects of heat shock and oxidative stress
    • Goldbaum O, Richter-Landsberg C. Stress proteins in oligodendrocytes: differential effects of heat shock and oxidative stress. J Neurochem 2001; 78: 1233-42.
    • (2001) J Neurochem , vol.78 , pp. 1233-1242
    • Goldbaum, O.1    Richter-Landsberg, C.2
  • 106
    • 0035449165 scopus 로고    scopus 로고
    • Delayed induction of alpha Bcrystallin in activated glia cells of hippocampus in kainic acidtreated mouse brain
    • Che Y, Piao CS, Han PL, Lee JK. Delayed induction of alpha Bcrystallin in activated glia cells of hippocampus in kainic acidtreated mouse brain. J Neurosci Res 2001; 65: 425-31.
    • (2001) J Neurosci Res , vol.65 , pp. 425-431
    • Che, Y.1    Piao, C.S.2    Han, P.L.3    Lee, J.K.4
  • 107
    • 20544451337 scopus 로고    scopus 로고
    • Co-induction of alphaBcrystallin and MAPKAPK-2 in astrocytes in the penumbra after transient focal cerebral ischemia
    • Piao CS, Kim SW, Kim JB, Lee JK. Co-induction of alphaBcrystallin and MAPKAPK-2 in astrocytes in the penumbra after transient focal cerebral ischemia. Exp Brain Res 2005; 163: 421-9.
    • (2005) Exp Brain Res , vol.163 , pp. 421-429
    • Piao, C.S.1    Kim, S.W.2    Kim, J.B.3    Lee, J.K.4
  • 108
    • 84882262621 scopus 로고    scopus 로고
    • Increased expression of small heat shock protein alphaB-crystallin after intracerebral hemorrhage in adult rats
    • Ke K, Li L, Rui Y, et al. Increased expression of small heat shock protein alphaB-crystallin after intracerebral hemorrhage in adult rats. J Mol Neurosci 2013; 51: 159-69.
    • (2013) J Mol Neurosci , vol.51 , pp. 159-169
    • Ke, K.1    Li, L.2    Rui, Y.3
  • 109
    • 0028984955 scopus 로고
    • Alpha B-crystallin in C6 glioma cells supports their survival in elevated extracellular K+: The implication of a protective role of alpha B-crystallin accumulation in reactive glia
    • Iwaki T, Iwaki A, Fukumaki Y, Tateishi J. Alpha B-crystallin in C6 glioma cells supports their survival in elevated extracellular K+: the implication of a protective role of alpha B-crystallin accumulation in reactive glia. Brain Res 1995; 673: 47-52.
    • (1995) Brain Res , vol.673 , pp. 47-52
    • Iwaki, T.1    Iwaki, A.2    Fukumaki, Y.3    Tateishi, J.4
  • 110
    • 67349215120 scopus 로고    scopus 로고
    • AlphaB-crystallin suppresses oxidative stress-induced astrocyte apoptosis by inhibiting caspase-3 activation
    • Shin JH, Kim SW, Lim CM, et al. alphaB-crystallin suppresses oxidative stress-induced astrocyte apoptosis by inhibiting caspase-3 activation. Neurosci Res 2009; 64: 355-61.
    • (2009) Neurosci Res , vol.64 , pp. 355-361
    • Shin, J.H.1    Kim, S.W.2    Lim, C.M.3
  • 111
    • 79960287784 scopus 로고    scopus 로고
    • Phosphorylation of Ser45 and Ser59 of alphaBcrystallin and p38/extracellular regulated kinase activity determine alphaB-crystallin-mediated protection of rat brain astrocytes from C2-ceramide- and staurosporine-induced cell death
    • Li R, Reiser G. Phosphorylation of Ser45 and Ser59 of alphaBcrystallin and p38/extracellular regulated kinase activity determine alphaB-crystallin-mediated protection of rat brain astrocytes from C2-ceramide- and staurosporine-induced cell death. J Neurochem 2011; 118: 354-64.
    • (2011) J Neurochem , vol.118 , pp. 354-364
    • Li, R.1    Reiser, G.2
  • 112
    • 84891148346 scopus 로고    scopus 로고
    • Reaction of small heat-shock proteins to different kinds of cellular stress in cultured rat hippocampal neurons
    • Bartelt-Kirbach B, Golenhofen N. Reaction of small heat-shock proteins to different kinds of cellular stress in cultured rat hippocampal neurons. Cell Stress Chaperones 2014; 19: 145-53.
    • (2014) Cell Stress Chaperones , vol.19 , pp. 145-153
    • Bartelt-Kirbach, B.1    Golenhofen, N.2
  • 113
    • 0028365670 scopus 로고
    • Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin
    • Kato K, Goto S, Inaguma Y, et al. Purification and characterization of a 20-kDa protein that is highly homologous to alpha B crystallin. J Biol Chem 1994; 269: 15302-9.
    • (1994) J Biol Chem , vol.269 , pp. 15302-15309
    • Kato, K.1    Goto, S.2    Inaguma, Y.3
  • 114
    • 77449132101 scopus 로고    scopus 로고
    • The small heat shock protein, HSPB6, in muscle function and disease
    • Dreiza CM, Komalavilas P, Furnish EJ, et al. The small heat shock protein, HSPB6, in muscle function and disease. Cell Stress Chaperones 2010; 15: 1-11.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 1-11
    • Dreiza, C.M.1    Komalavilas, P.2    Furnish, E.J.3
  • 115
    • 79958765896 scopus 로고    scopus 로고
    • The emerging role of HSP20 as a multifunctional protective agent
    • Edwards HV, Cameron RT, Baillie GS. The emerging role of HSP20 as a multifunctional protective agent. Cell Signal 2011; 23: 1447-54.
    • (2011) Cell Signal , vol.23 , pp. 1447-1454
    • Edwards, H.V.1    Cameron, R.T.2    Baillie, G.S.3
  • 116
    • 68849108388 scopus 로고    scopus 로고
    • Spatiotemporal expression of Hsp20 and its phosphorylation in hippocampal CA1 pyramidal neurons after transient forebrain ischemia
    • Niwa M, Hara A, Taguchi A, et al. Spatiotemporal expression of Hsp20 and its phosphorylation in hippocampal CA1 pyramidal neurons after transient forebrain ischemia. Neurol Res 2009; 31: 721-7.
    • (2009) Neurol Res , vol.31 , pp. 721-727
    • Niwa, M.1    Hara, A.2    Taguchi, A.3
  • 117
    • 33749184049 scopus 로고    scopus 로고
    • Up-regulation of heat shock protein HSP 20 in the hippocampus as an early response to hypoxia of the newborn
    • David JC, Boelens WC, Grongnet JF. Up-regulation of heat shock protein HSP 20 in the hippocampus as an early response to hypoxia of the newborn. J Neurochem 2006; 99: 570-81.
    • (2006) J Neurochem , vol.99 , pp. 570-581
    • David, J.C.1    Boelens, W.C.2    Grongnet, J.F.3
  • 118
    • 33646190092 scopus 로고    scopus 로고
    • Small heat shock protein HspB8: Its distribution in Alzheimer's disease brains and its inhibition of amyloid-beta protein aggregation and cerebrovascular amyloid-beta toxicity
    • Wilhelmus MM, Boelens WC, Otte-Holler I, et al. Small heat shock protein HspB8: its distribution in Alzheimer's disease brains and its inhibition of amyloid-beta protein aggregation and cerebrovascular amyloid-beta toxicity. Acta Neuropathol 2006; 111: 139-49.
    • (2006) Acta Neuropathol , vol.111 , pp. 139-149
    • Wilhelmus, M.M.1    Boelens, W.C.2    Otte-Holler, I.3
  • 119
    • 84875417970 scopus 로고    scopus 로고
    • The alpha crystallin domain of small heat shock protein b8 (Hspb8) acts as survival and differentiation factor in adult hippocampal neurogenesis
    • Ramirez-Rodriguez G, Babu H, Klempin F, et al. The alpha crystallin domain of small heat shock protein b8 (Hspb8) acts as survival and differentiation factor in adult hippocampal neurogenesis. J Neurosci 2013; 33: 5785-96.
    • (2013) J Neurosci , vol.33 , pp. 5785-5796
    • Ramirez-Rodriguez, G.1    Babu, H.2    Klempin, F.3
  • 120
    • 2642539919 scopus 로고    scopus 로고
    • Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy
    • Irobi J, Van Impe K, Seeman P, et al. Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy. Nat Genet 2004; 36: 597-601.
    • (2004) Nat Genet , vol.36 , pp. 597-601
    • Irobi, J.1    Van Impe, K.2    Seeman, P.3
  • 121
    • 19944433659 scopus 로고    scopus 로고
    • Small heat-shock protein 22 mutated in autosomal dominant Charcot-Marie-Tooth disease type 2L
    • Tang BS, Zhao GH, Luo W, et al. Small heat-shock protein 22 mutated in autosomal dominant Charcot-Marie-Tooth disease type 2L. Hum Genet 2005; 116: 222-4.
    • (2005) Hum Genet , vol.116 , pp. 222-224
    • Tang, B.S.1    Zhao, G.H.2    Luo, W.3
  • 122
    • 78149266599 scopus 로고    scopus 로고
    • HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones
    • Vos MJ, Zijlstra MP, Kanon B, et al. HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones. Hum Mol Genet 2010; 19: 4677-93.
    • (2010) Hum Mol Genet , vol.19 , pp. 4677-4693
    • Vos, M.J.1    Zijlstra, M.P.2    Kanon, B.3
  • 123
    • 78549246252 scopus 로고    scopus 로고
    • Identification of the Drosophila ortholog of HSPB8: Implication of HSPB8 loss of function in protein folding diseases
    • Carra S, Boncoraglio A, Kanon B, et al. Identification of the Drosophila ortholog of HSPB8: implication of HSPB8 loss of function in protein folding diseases. J Biol Chem 2010; 285: 37811-22.
    • (2010) J Biol Chem , vol.285 , pp. 37811-37822
    • Carra, S.1    Boncoraglio, A.2    Kanon, B.3
  • 124
    • 77957665681 scopus 로고    scopus 로고
    • A role of small heat shock protein B8 (HspB8) in the autophagic removal of misfolded proteins responsible for neurodegenerative diseases
    • Crippa V, Carra S, Rusmini P, et al. A role of small heat shock protein B8 (HspB8) in the autophagic removal of misfolded proteins responsible for neurodegenerative diseases. Autophagy 2010; 6: 958-60.
    • (2010) Autophagy , vol.6 , pp. 958-960
    • Crippa, V.1    Carra, S.2    Rusmini, P.3
  • 125
    • 0141891166 scopus 로고    scopus 로고
    • Gene expression profiling in ataxin-3 expressing cell lines reveals distinct effects of normal and mutant ataxin-3
    • Evert BO, Vogt IR, Vieira-Saecker AM, et al. Gene expression profiling in ataxin-3 expressing cell lines reveals distinct effects of normal and mutant ataxin-3. J Neuropathol Exp Neurol 2003; 62: 1006-18.
    • (2003) J Neuropathol Exp Neurol , vol.62 , pp. 1006-1018
    • Evert, B.O.1    Vogt, I.R.2    Vieira-Saecker, A.M.3
  • 126
    • 0036566675 scopus 로고    scopus 로고
    • Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin
    • Wyttenbach A, Sauvageot O, Carmichael J, et al. Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum Mol Genet 2002; 11: 1137-51.
    • (2002) Hum Mol Genet , vol.11 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3
  • 127
    • 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, et al. Neuroprotection by Hsp104 and Hsp27 in lentiviral-based rat models of Huntington's disease. Mol Ther 2007; 15: 903-11.
    • (2007) Mol Ther , vol.15 , pp. 903-911
    • Perrin, V.1    Regulier, E.2    Abbas-Terki, T.3
  • 128
    • 34447331291 scopus 로고    scopus 로고
    • Hsp27 overexpression in the R6/2 mouse model of Huntington's disease: Chronic neurodegeneration does not induce Hsp27 activation
    • Zourlidou A, Gidalevitz T, Kristiansen M, et al. Hsp27 overexpression in the R6/2 mouse model of Huntington's disease: chronic neurodegeneration does not induce Hsp27 activation. Hum Mol Genet 2007; 16: 1078-90.
    • (2007) Hum Mol Genet , vol.16 , pp. 1078-1090
    • Zourlidou, A.1    Gidalevitz, T.2    Kristiansen, M.3
  • 129
    • 62949154852 scopus 로고    scopus 로고
    • Decreased protein synthesis of Hsp27 associated with cellular toxicity in a cell model of Machado-Joseph disease
    • Chang WH, Tien CL, Chen TJ, Nukina N, Hsieh M. Decreased protein synthesis of Hsp27 associated with cellular toxicity in a cell model of Machado-Joseph disease. Neurosci Lett 2009; 454: 152-6.
    • (2009) Neurosci Lett , vol.454 , pp. 152-156
    • Chang, W.H.1    Tien, C.L.2    Chen, T.J.3    Nukina, N.4    Hsieh, M.5
  • 130
    • 0037494974 scopus 로고    scopus 로고
    • Down-regulation of heat shock protein 27 in neuronal cells and non-neuronal cells expressing mutant ataxin-3
    • Wen FC, Li YH, Tsai HF, et al. Down-regulation of heat shock protein 27 in neuronal cells and non-neuronal cells expressing mutant ataxin-3. FEBS Lett 2003; 546: 307-14.
    • (2003) FEBS Lett , vol.546 , pp. 307-314
    • Wen, F.C.1    Li, Y.H.2    Tsai, H.F.3
  • 131
    • 0036582045 scopus 로고    scopus 로고
    • Alterations in the mouse and human proteome caused by Huntington's disease
    • Zabel C, Chamrad DC, Priller J, et al. Alterations in the mouse and human proteome caused by Huntington's disease. Mol Cell Proteomics 2002; 1: 366-75.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 366-375
    • Zabel, C.1    Chamrad, D.C.2    Priller, J.3
  • 132
    • 44449119580 scopus 로고    scopus 로고
    • Noninvasive measurement of protein aggregation by mutant huntingtin fragments or alpha-synuclein in the lens
    • Muchowski PJ, Ramsden R, Nguyen Q, et al. Noninvasive measurement of protein aggregation by mutant huntingtin fragments or alpha-synuclein in the lens. J Biol Chem 2008; 283: 6330-6.
    • (2008) J Biol Chem , vol.283 , pp. 6330-6336
    • Muchowski, P.J.1    Ramsden, R.2    Nguyen, Q.3
  • 133
    • 77953799932 scopus 로고    scopus 로고
    • Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation
    • Robertson AL, Headey SJ, Saunders HM, et al. Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation. Proc Natl Acad Sci USA 2010; 107: 10424-9.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 10424-10429
    • Robertson, A.L.1    Headey, S.J.2    Saunders, H.M.3
  • 134
    • 84859708231 scopus 로고    scopus 로고
    • Effect of alphaBcrystallin on protein aggregation in Drosophila
    • Tue NT, Shimaji K, Tanaka N, Yamaguchi M. Effect of alphaBcrystallin on protein aggregation in Drosophila. J Biomed Biotechnol 2012; 2012: 252049.
    • (2012) J Biomed Biotechnol , vol.2012 , pp. 252049
    • Tue, N.T.1    Shimaji, K.2    Tanaka, N.3    Yamaguchi, M.4
  • 135
    • 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 SJ, Lambert H, Landry J. HspB8 chaperone activity toward poly(Q)-containing proteins depends on its association with Bag3, a stimulator of macroautophagy. J Biol Chem 2008; 283: 1437-44.
    • (2008) J Biol Chem , vol.283 , pp. 1437-1444
    • Carra, S.1    Seguin, S.J.2    Lambert, H.3    Landry, J.4
  • 136
    • 72449141635 scopus 로고    scopus 로고
    • Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction
    • Fuchs M, Poirier DJ, Seguin SJ, et al. Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction. Biochem J 2009; 425: 245-55.
    • (2009) Biochem J , vol.425 , pp. 245-255
    • Fuchs, M.1    Poirier, D.J.2    Seguin, S.J.3
  • 137
    • 84855516743 scopus 로고    scopus 로고
    • The HSPB8-BAG3 chaperone complex is upregulated in astrocytes in the human brain affected by protein aggregation diseases
    • Seidel K, Vinet J, Dunnen WF, et al. The HSPB8-BAG3 chaperone complex is upregulated in astrocytes in the human brain affected by protein aggregation diseases. Neuropathol Appl Neurobiol 2012; 38: 39-53.
    • (2012) Neuropathol Appl Neurobiol , vol.38 , pp. 39-53
    • Seidel, K.1    Vinet, J.2    Dunnen, W.F.3
  • 138
    • 84944937332 scopus 로고    scopus 로고
    • Aberrant Autophagic Response in The Muscle of A Knock-in Mouse Model of Spinal and Bulbar Muscular Atrophy
    • Rusmini P, Polanco MJ, Cristofani R, et al. Aberrant Autophagic Response in The Muscle of A Knock-in Mouse Model of Spinal and Bulbar Muscular Atrophy. Sci Rep 2015; 5: 15174.
    • (2015) Sci Rep , vol.5 , pp. 15174
    • Rusmini, P.1    Polanco, M.J.2    Cristofani, R.3
  • 139
    • 1342334759 scopus 로고    scopus 로고
    • Interaction of human HSP22 (HSPB8) with other small heat shock proteins
    • Sun X, Fontaine JM, Rest JS, et al. Interaction of human HSP22 (HSPB8) with other small heat shock proteins. J Biol Chem 2004; 279: 2394-402.
    • (2004) J Biol Chem , vol.279 , pp. 2394-2402
    • Sun, X.1    Fontaine, J.M.2    Rest, J.S.3
  • 140
    • 41149163183 scopus 로고    scopus 로고
    • Parkinson's disease: Clinical features and diagnosis
    • Jankovic J. Parkinson's disease: clinical features and diagnosis. J Neurol Neurosurg Psychiatry 2008; 79: 368-76.
    • (2008) J Neurol Neurosurg Psychiatry , vol.79 , pp. 368-376
    • Jankovic, J.1
  • 141
    • 0344898557 scopus 로고    scopus 로고
    • Clinical and quantitative pathologic correlates of dementia with Lewy bodies
    • Gomez-Tortosa E, Newell K, Irizarry MC, et al. Clinical and quantitative pathologic correlates of dementia with Lewy bodies. Neurology 1999; 53: 1284-91.
    • (1999) Neurology , vol.53 , pp. 1284-1291
    • Gomez-Tortosa, E.1    Newell, K.2    Irizarry, M.C.3
  • 143
    • 0033955608 scopus 로고    scopus 로고
    • Cell death mechanisms in Parkinson's disease
    • Jellinger KA. Cell death mechanisms in Parkinson's disease. J Neural Transm 2000; 107: 1-29.
    • (2000) J Neural Transm , vol.107 , pp. 1-29
    • Jellinger, K.A.1
  • 144
    • 0006607248 scopus 로고    scopus 로고
    • Dementia, gliosis and expression of the small heat shock proteins hsp27 and alpha B-crystallin in Parkinson's disease
    • Renkawek K, Stege GJ, Bosman GJ. Dementia, gliosis and expression of the small heat shock proteins hsp27 and alpha B-crystallin in Parkinson's disease. Neuroreport 1999; 10: 2273-6.
    • (1999) Neuroreport , vol.10 , pp. 2273-2276
    • Renkawek, K.1    Stege, G.J.2    Bosman, G.J.3
  • 145
    • 33751216491 scopus 로고    scopus 로고
    • Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation
    • Outeiro TF, Klucken J, Strathearn KE, et al. Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation. Biochem Biophys Res Commun 2006; 351: 631-8.
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 631-638
    • Outeiro, T.F.1    Klucken, J.2    Strathearn, K.E.3
  • 146
    • 0025073458 scopus 로고
    • Dementia with beta-amyloid deposition: Involvement of alpha B-crystallin supports two main diseases
    • Lowe J, Landon M, Pike I, et al. Dementia with beta-amyloid deposition: involvement of alpha B-crystallin supports two main diseases. Lancet 1990; 336: 515-6.
    • (1990) Lancet , vol.336 , pp. 515-516
    • Lowe, J.1    Landon, M.2    Pike, I.3
  • 147
    • 84855838615 scopus 로고    scopus 로고
    • HspB2/myotonic dystrophy protein kinase binding protein (MKBP) as a novel molecular chaperone: Structural and functional aspects
    • Prabhu S, Raman B, Ramakrishna T, Rao Ch M. HspB2/myotonic dystrophy protein kinase binding protein (MKBP) as a novel molecular chaperone: structural and functional aspects. PLoS One 2012; 7: e29810.
    • (2012) Plos One , vol.7
    • Prabhu, S.1    Raman, B.2    Ramakrishna, T.3    Rao Ch, M.4
  • 148
    • 3242770627 scopus 로고    scopus 로고
    • Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: Effects on amyloid fibril formation and chaperone activity
    • Rekas A, Adda CG, Andrew Aquilina J, et al. Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity. J Mol Biol 2004; 340: 1167-83.
    • (2004) J Mol Biol , vol.340 , pp. 1167-1183
    • Rekas, A.1    Adda, C.G.2    Rew Aquilina, J.3
  • 149
    • 77749240461 scopus 로고    scopus 로고
    • The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation
    • Waudby CA, Knowles TP, Devlin GL, et al. The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation. Biophys J 2010; 98: 843-51.
    • (2010) Biophys J , vol.98 , pp. 843-851
    • Waudby, C.A.1    Knowles, T.P.2    Devlin, G.L.3
  • 150
    • 80052569506 scopus 로고    scopus 로고
    • Inhibition of alphasynuclein aggregation by small heat shock proteins
    • Bruinsma IB, Bruggink KA, Kinast K, et al. Inhibition of alphasynuclein aggregation by small heat shock proteins. Proteins 2011; 79: 2956-67.
    • (2011) Proteins , vol.79 , pp. 2956-2967
    • Bruinsma, I.B.1    Bruggink, K.A.2    Kinast, K.3
  • 151
    • 1642356755 scopus 로고    scopus 로고
    • HSP27 but not HSP70 has a potent protective effect against alpha-synucleininduced cell death in mammalian neuronal cells
    • Zourlidou A, Payne Smith MD, Latchman DS. HSP27 but not HSP70 has a potent protective effect against alpha-synucleininduced cell death in mammalian neuronal cells. J Neurochem 2004; 88: 1439-48.
    • (2004) J Neurochem , vol.88 , pp. 1439-1448
    • Zourlidou, A.1    Payne Smith, M.D.2    Latchman, D.S.3
  • 152
    • 84900499674 scopus 로고    scopus 로고
    • Hsp27 suppresses the Cu(2+)-induced amyloidogenicity, redox activity, and cytotoxicity of alpha-synuclein by metal ion stripping
    • Asthana A, Bollapalli M, Tangirala R, Bakthisaran R, Mohan Rao C. Hsp27 suppresses the Cu(2+)-induced amyloidogenicity, redox activity, and cytotoxicity of alpha-synuclein by metal ion stripping. Free Radic Biol Med 2014; 72: 176-90.
    • (2014) Free Radic Biol Med , vol.72 , pp. 176-190
    • Asthana, A.1    Bollapalli, M.2    Tangirala, R.3    Bakthisaran, R.4    Mohan Rao, C.5
  • 153
    • 84861199063 scopus 로고    scopus 로고
    • PEP-1-heat shock protein 27 protects from neuronal damage in cells and in a Parkinson's disease mouse model
    • Lee YP, Kim DW, Kang HW, et al. PEP-1-heat shock protein 27 protects from neuronal damage in cells and in a Parkinson's disease mouse model. Febs J 2012; 279: 1929-42.
    • (2012) Febs J , vol.279 , pp. 1929-1942
    • Lee, Y.P.1    Kim, D.W.2    Kang, H.W.3
  • 154
    • 0035163913 scopus 로고    scopus 로고
    • Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease
    • Brenner M, Johnson AB, Boespflug-Tanguy O, et al. Mutations in GFAP, encoding glial fibrillary acidic protein, are associated with Alexander disease. Nat Genet 2001; 27: 117-20.
    • (2001) Nat Genet , vol.27 , pp. 117-120
    • Brenner, M.1    Johnson, A.B.2    Boespflug-Tanguy, O.3
  • 155
    • 20044372525 scopus 로고    scopus 로고
    • Glial fibrillary acidic protein mutations in infantile, juvenile, and adult forms of Alexander disease
    • Li R, Johnson AB, Salomons G, et al. Glial fibrillary acidic protein mutations in infantile, juvenile, and adult forms of Alexander disease. Ann Neurol 2005; 57: 310-26.
    • (2005) Ann Neurol , vol.57 , pp. 310-326
    • Li, R.1    Johnson, A.B.2    Salomons, G.3
  • 156
    • 0024521440 scopus 로고
    • Alpha Bcrystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain
    • Iwaki T, Kume-Iwaki A, Liem RK, Goldman JE. Alpha Bcrystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell 1989; 57: 71-8.
    • (1989) Cell , vol.57 , pp. 71-78
    • Iwaki, T.1    Kume-Iwaki, A.2    Liem, R.K.3    Goldman, J.E.4
  • 157
    • 0027724243 scopus 로고
    • Overexpression and abnormal modification of the stress proteins alpha B-crystallin and HSP27 in Alexander disease
    • Head MW, Corbin E, Goldman JE. Overexpression and abnormal modification of the stress proteins alpha B-crystallin and HSP27 in Alexander disease. Am J Pathol 1993; 143: 1743-53.
    • (1993) Am J Pathol , vol.143 , pp. 1743-1753
    • Head, M.W.1    Corbin, E.2    Goldman, J.E.3
  • 158
    • 33746485560 scopus 로고    scopus 로고
    • The Alexander disease-causing glial fibrillary acidic protein mutant, R416W, accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of alpha B-crystallin and HSP27
    • Der Perng M, Su M, Wen SF, et al. The Alexander disease-causing glial fibrillary acidic protein mutant, R416W, accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of alpha B-crystallin and HSP27. Am J Hum Genet 2006; 79: 197-213.
    • (2006) Am J Hum Genet , vol.79 , pp. 197-213
    • Der Perng, M.1    Su, M.2    Wen, S.F.3
  • 159
    • 63149096739 scopus 로고    scopus 로고
    • Suppression of GFAP toxicity by alphaB-crystallin in mouse models of Alexander disease
    • Hagemann TL, Boelens WC, Wawrousek EF, Messing A. Suppression of GFAP toxicity by alphaB-crystallin in mouse models of Alexander disease. Hum Mol Genet 2009; 18: 1190-9.
    • (2009) Hum Mol Genet , vol.18 , pp. 1190-1199
    • Hagemann, T.L.1    Boelens, W.C.2    Wawrousek, E.F.3    Messing, A.4
  • 160
    • 77951249600 scopus 로고    scopus 로고
    • Oligomers of mutant glial fibrillary acidic protein (GFAP) Inhibit the proteasome system in alexander disease astrocytes, and the small heat shock protein alphaB-crystallin reverses the inhibition
    • Tang G, Perng MD, Wilk S, Quinlan R, Goldman JE. Oligomers of mutant glial fibrillary acidic protein (GFAP) Inhibit the proteasome system in alexander disease astrocytes, and the small heat shock protein alphaB-crystallin reverses the inhibition. J Biol Chem 2010; 285: 10527-37.
    • (2010) J Biol Chem , vol.285 , pp. 10527-10537
    • Tang, G.1    Perng, M.D.2    Wilk, S.3    Quinlan, R.4    Goldman, J.E.5
  • 161
    • 84956878513 scopus 로고    scopus 로고
    • Genotype-phenotype correlations of amyotrophic lateral sclerosis
    • Li HF, Wu ZY. Genotype-phenotype correlations of amyotrophic lateral sclerosis. Transl Neurodegener 2016; 5: 3.
    • (2016) Transl Neurodegener , vol.5 , pp. 3
    • Li, H.F.1    Wu, Z.Y.2
  • 162
    • 0030797166 scopus 로고    scopus 로고
    • Pathological characterization of astrocytic hyaline inclusions in familial amyotrophic lateral sclerosis
    • Kato S, Hayashi H, Nakashima K, et al. Pathological characterization of astrocytic hyaline inclusions in familial amyotrophic lateral sclerosis. Am J Pathol 1997; 151: 611-20.
    • (1997) Am J Pathol , vol.151 , pp. 611-620
    • Kato, S.1    Hayashi, H.2    Nakashima, K.3
  • 163
    • 0026675039 scopus 로고
    • Comparative immunohistochemical study on the expression of alpha B crystallin, ubiquitin and stress-response protein 27 in ballooned neurons in various disorders
    • Kato S, Hirano A, Umahara T, et al. Comparative immunohistochemical study on the expression of alpha B crystallin, ubiquitin and stress-response protein 27 in ballooned neurons in various disorders. Neuropathol Appl Neurobiol 1992; 18: 335-40.
    • (1992) Neuropathol Appl Neurobiol , vol.18 , pp. 335-340
    • Kato, S.1    Hirano, A.2    Umahara, T.3
  • 164
    • 0031835184 scopus 로고    scopus 로고
    • Immunohistochemical and ultrastructural characterization of ubiquitinated eosinophilic fibrillary neuronal inclusions in sporadic amyotrophic lateral sclerosis
    • Arima K, Ogawa M, Sunohara N, et al. Immunohistochemical and ultrastructural characterization of ubiquitinated eosinophilic fibrillary neuronal inclusions in sporadic amyotrophic lateral sclerosis. Acta Neuropathol 1998; 96: 75-85.
    • (1998) Acta Neuropathol , vol.96 , pp. 75-85
    • Arima, K.1    Ogawa, M.2    Sunohara, N.3
  • 165
    • 77951975098 scopus 로고    scopus 로고
    • Vesicle associated membrane protein B (VAPB) is decreased in ALS spinal cord
    • Anagnostou G, Akbar MT, Paul P, et al. Vesicle associated membrane protein B (VAPB) is decreased in ALS spinal cord. Neurobiol Aging 2010; 31: 969-85.
    • (2010) Neurobiol Aging , vol.31 , pp. 969-985
    • Anagnostou, G.1    Akbar, M.T.2    Paul, P.3
  • 166
    • 77955365630 scopus 로고    scopus 로고
    • The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS)
    • Crippa V, Sau D, Rusmini P, et al. The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS). Hum Mol Genet 2010; 19: 3440-56.
    • (2010) Hum Mol Genet , vol.19 , pp. 3440-3456
    • Crippa, V.1    Sau, D.2    Rusmini, P.3
  • 167
    • 34447294839 scopus 로고    scopus 로고
    • Gene expression analysis of the murine model of amyotrophic lateral sclerosis: Studies of the Leu126delTT mutation in SOD1
    • Fukada Y, Yasui K, Kitayama M, et al. Gene expression analysis of the murine model of amyotrophic lateral sclerosis: studies of the Leu126delTT mutation in SOD1. Brain Res 2007; 1160: 1-10.
    • (2007) Brain Res , vol.1160 , pp. 1-10
    • Fukada, Y.1    Yasui, K.2    Kitayama, M.3
  • 169
    • 39749113234 scopus 로고    scopus 로고
    • Differential regulation of small heat shock proteins in transgenic mouse models of neurodegenerative diseases
    • Wang J, Martin E, Gonzales V, Borchelt DR, Lee MK. Differential regulation of small heat shock proteins in transgenic mouse models of neurodegenerative diseases. Neurobiol Aging 2008; 29: 586-97.
    • (2008) Neurobiol Aging , vol.29 , pp. 586-597
    • Wang, J.1    Martin, E.2    Gonzales, V.3    Borchelt, D.R.4    Lee, M.K.5
  • 170
    • 0242524455 scopus 로고    scopus 로고
    • Copper-binding-site-null SOD1 causes ALS in transgenic mice: Aggregates of non-native SOD1 delineate a common feature
    • Wang J, Slunt H, Gonzales V, et al. Copper-binding-site-null SOD1 causes ALS in transgenic mice: aggregates of non-native SOD1 delineate a common feature. Hum Mol Genet 2003; 12: 2753-64.
    • (2003) Hum Mol Genet , vol.12 , pp. 2753-2764
    • Wang, J.1    Slunt, H.2    Gonzales, V.3
  • 171
    • 3142692478 scopus 로고    scopus 로고
    • Decrease of Hsp25 protein expression precedes degeneration of motoneurons in ALS-SOD1 mice
    • Maatkamp A, Vlug A, Haasdijk E, et al. Decrease of Hsp25 protein expression precedes degeneration of motoneurons in ALS-SOD1 mice. Eur J Neurosci 2004; 20: 14-28.
    • (2004) Eur J Neurosci , vol.20 , pp. 14-28
    • Maatkamp, A.1    Vlug, A.2    Haasdijk, E.3
  • 172
    • 77951889547 scopus 로고    scopus 로고
    • An examination of alpha B-crystallin as a modifier of SOD1 aggregate pathology and toxicity in models of familial amyotrophic lateral sclerosis
    • Karch CM, Borchelt DR. An examination of alpha B-crystallin as a modifier of SOD1 aggregate pathology and toxicity in models of familial amyotrophic lateral sclerosis. J Neurochem 2010; 113: 1092-100.
    • (2010) J Neurochem , vol.113 , pp. 1092-1100
    • Karch, C.M.1    Borchelt, D.R.2
  • 173
    • 84876081004 scopus 로고    scopus 로고
    • The small heat shock proteins alphaB-crystallin and Hsp27 suppress SOD1 aggregation in vitro
    • Yerbury JJ, Gower D, Vanags L, et al. The small heat shock proteins alphaB-crystallin and Hsp27 suppress SOD1 aggregation in vitro. Cell Stress Chaperones 2013; 18: 251-7.
    • (2013) Cell Stress Chaperones , vol.18 , pp. 251-257
    • Yerbury, J.J.1    Gower, D.2    Vanags, L.3
  • 174
    • 67449099354 scopus 로고    scopus 로고
    • Transduced HSP27 protein protects neuronal cell death by enhancing FALS-associated SOD1 mutant activity
    • An JJ, Lee YP, Kim DW, et al. Transduced HSP27 protein protects neuronal cell death by enhancing FALS-associated SOD1 mutant activity. BMB Rep 2009; 42: 136-41.
    • (2009) BMB Rep , vol.42 , pp. 136-141
    • An, J.J.1    Lee, Y.P.2    Kim, D.W.3
  • 175
    • 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 YJ, Payne Smith MD, de Belleroche J, Latchman DS. 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 2005; 134: 256-74.
    • (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
  • 176
    • 33746312670 scopus 로고    scopus 로고
    • Role of heat shock response and Hsp27 in mutant SOD1-dependent cell death
    • Krishnan J, Lemmens R, Robberecht W, Van Den Bosch L. Role of heat shock response and Hsp27 in mutant SOD1-dependent cell death. Exp Neurol 2006; 200: 301-10.
    • (2006) Exp Neurol , vol.200 , pp. 301-310
    • Krishnan, J.1    Lemmens, R.2    Robberecht, W.3    Van Den Bosch, L.4
  • 177
    • 40849140683 scopus 로고    scopus 로고
    • Protective effects of heat shock protein 27 in a model of ALS occur in the early stages of disease progression
    • Sharp PS, Akbar MT, Bouri S, et al. Protective effects of heat shock protein 27 in a model of ALS occur in the early stages of disease progression. Neurobiol Dis 2008; 30: 42-55.
    • (2008) Neurobiol Dis , vol.30 , pp. 42-55
    • Sharp, P.S.1    Akbar, M.T.2    Bouri, S.3
  • 178
    • 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, et al. Over-expression of Hsp27 does not influence disease in the mutant SOD1(G93A) mouse model of amyotrophic lateral sclerosis. J Neurochem 2008; 106: 2170-83.
    • (2008) J Neurochem , vol.106 , pp. 2170-2183
    • Krishnan, J.1    Vannuvel, K.2    Ries, M.3
  • 179
    • 84945340060 scopus 로고    scopus 로고
    • Frontotemporal dementia
    • Bang J, Spina S, Miller BL. Frontotemporal dementia. Lancet 2015; 386: 1672-82.
    • (2015) Lancet , vol.386 , pp. 1672-1682
    • Bang, J.1    Spina, S.2    Miller, B.L.3
  • 180
    • 84923288410 scopus 로고    scopus 로고
    • C9orf72 expansions in frontotemporal dementia and amyotrophic lateral sclerosis
    • Rohrer JD, Isaacs AM, Mizielinska S, et al. C9orf72 expansions in frontotemporal dementia and amyotrophic lateral sclerosis. Lancet Neurol 2015; 14: 291-301.
    • (2015) Lancet Neurol , vol.14 , pp. 291-301
    • Rohrer, J.D.1    Isaacs, A.M.2    Mizielinska, S.3
  • 181
    • 0037595532 scopus 로고    scopus 로고
    • Frontotemporal degeneration, Pick's disease, Pick complex, and Ravel
    • Kertesz A, Hillis A, Munoz DG. Frontotemporal degeneration, Pick's disease, Pick complex, and Ravel. Ann Neurol 2003; 54 Suppl 5: S1-2.
    • (2003) Ann Neurol , vol.54
    • Kertesz, A.1    Hillis, A.2    Munoz, D.G.3
  • 182
    • 0042027817 scopus 로고    scopus 로고
    • The neuropathological spectrum of neurodegenerative tauopathies
    • Tolnay M, Probst A. The neuropathological spectrum of neurodegenerative tauopathies. IUBMB Life 2003; 55: 299-305.
    • (2003) IUBMB Life , vol.55 , pp. 299-305
    • Tolnay, M.1    Probst, A.2
  • 184
    • 77955957517 scopus 로고    scopus 로고
    • The Small Heat Shock Protein HSP25/27 (HspB1) Is Abundant in Cultured Astrocytes and Associated with Astrocytic Pathology in Progressive Supranuclear Palsy and Corticobasal Degeneration
    • Schwarz L, Vollmer G, Richter-Landsberg C. The Small Heat Shock Protein HSP25/27 (HspB1) Is Abundant in Cultured Astrocytes and Associated with Astrocytic Pathology in Progressive Supranuclear Palsy and Corticobasal Degeneration. Int J Cell Biol 2010; 2010: 717520.
    • (2010) Int J Cell Biol , vol.2010 , pp. 717520
    • Schwarz, L.1    Vollmer, G.2    Richter-Landsberg, C.3
  • 185
    • 80052027012 scopus 로고    scopus 로고
    • Astrocytic neuroprotection through induction of cytoprotective molecules; a proteomic analysis of mutant P301S tau-transgenic mouse
    • Yata K, Oikawa S, Sasaki R, et al. Astrocytic neuroprotection through induction of cytoprotective molecules; a proteomic analysis of mutant P301S tau-transgenic mouse. Brain Res 2011; 1410: 12-23.
    • (2011) Brain Res , vol.1410 , pp. 12-23
    • Yata, K.1    Oikawa, S.2    Sasaki, R.3
  • 186
    • 1542574213 scopus 로고    scopus 로고
    • Expression of the small heat-shock protein alphaBcrystallin in tauopathies with glial pathology
    • Dabir DV, Trojanowski JQ, Richter-Landsberg C, Lee VM, Forman MS. Expression of the small heat-shock protein alphaBcrystallin in tauopathies with glial pathology. Am J Pathol 2004; 164: 155-66.
    • (2004) Am J Pathol , vol.164 , pp. 155-166
    • Dabir, D.V.1    Trojanowski, J.Q.2    Richter-Landsberg, C.3    Lee, V.M.4    Forman, M.S.5
  • 187
    • 84915767682 scopus 로고    scopus 로고
    • Ferrer I. AlphaB-crystallin and HSP27 in glial cells in tauopathies
    • Lopez-Gonzalez I, Carmona M, Arregui L, Kovacs GG, Ferrer I. alphaB-crystallin and HSP27 in glial cells in tauopathies. Neuropathology 2014; 34: 517-26.
    • (2014) Neuropathology , vol.34 , pp. 517-526
    • Lopez-Gonzalez, I.1    Carmona, M.2    Arregui, L.3    Kovacs, G.G.4
  • 188
    • 0029934176 scopus 로고    scopus 로고
    • Cortical ballooned neurons in progressive supranuclear palsy
    • Mori H, Oda M, Mizuno Y. Cortical ballooned neurons in progressive supranuclear palsy. Neurosci Lett 1996; 209: 109-12.
    • (1996) Neurosci Lett , vol.209 , pp. 109-112
    • Mori, H.1    Oda, M.2    Mizuno, Y.3
  • 189
    • 0022871177 scopus 로고
    • Ballooned neurons in select neurodegenerative diseases contain phosphorylated neurofilament epitopes
    • Dickson DW, Yen SH, Suzuki KI, et al. Ballooned neurons in select neurodegenerative diseases contain phosphorylated neurofilament epitopes. Acta Neuropathol 1986; 71: 216-223.
    • (1986) Acta Neuropathol , vol.71 , pp. 216-223
    • Dickson, D.W.1    Yen, S.H.2    Suzuki, K.I.3
  • 191
    • 0037368005 scopus 로고    scopus 로고
    • Perspectives on prion biology, prion disease pathogenesis, and pharmacologic approaches to treatment
    • DeArmond SJ, Prusiner SB. Perspectives on prion biology, prion disease pathogenesis, and pharmacologic approaches to treatment. Clin Lab Med 2003; 23: 1-41.
    • (2003) Clin Lab Med , vol.23 , pp. 1-41
    • Dearmond, S.J.1    Prusiner, S.B.2
  • 192
    • 80051999994 scopus 로고    scopus 로고
    • Changes in HSP gene and protein expression in natural scrapie with brain damage
    • Serrano C, Bolea R, Lyahyai J, et al. Changes in HSP gene and protein expression in natural scrapie with brain damage. Vet Res 2011; 42: 13.
    • (2011) Vet Res , vol.42 , pp. 13
    • Serrano, C.1    Bolea, R.2    Lyahyai, J.3
  • 193
    • 0026541340 scopus 로고
    • Alpha B-crystallin is present in reactive glia in Creutzfeldt-Jakob disease
    • Renkawek K, de Jong WW, Merck KB, et al. alpha B-crystallin is present in reactive glia in Creutzfeldt-Jakob disease. Acta Neuropathol 1992; 83: 324-7.
    • (1992) Acta Neuropathol , vol.83 , pp. 324-327
    • Renkawek, K.1    De Jong, W.W.2    Merck, K.B.3
  • 194
    • 84885957759 scopus 로고    scopus 로고
    • Abnormally upregulated alphaBcrystallin was highly coincidental with the astrogliosis in the brains of scrapie-infected hamsters and human patients with prion diseases
    • Wang K, Zhang J, Xu Y, et al. Abnormally upregulated alphaBcrystallin was highly coincidental with the astrogliosis in the brains of scrapie-infected hamsters and human patients with prion diseases. J Mol Neurosci 2013; 51: 734-48.
    • (2013) J Mol Neurosci , vol.51 , pp. 734-748
    • Wang, K.1    Zhang, J.2    Xu, Y.3
  • 195
    • 25844443482 scopus 로고    scopus 로고
    • Bovine PrPC directly interacts with alphaB-crystalline
    • Sun G, Guo M, Shen A, et al. Bovine PrPC directly interacts with alphaB-crystalline. FEBS Lett 2005; 579: 5419-24.
    • (2005) FEBS Lett , vol.579 , pp. 5419-5424
    • Sun, G.1    Guo, M.2    Shen, A.3
  • 196
    • 39049119728 scopus 로고    scopus 로고
    • Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size
    • Sun Y, Makarava N, Lee CI, et al. Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size. J Mol Biol 2008; 376: 1155-67.
    • (2008) J Mol Biol , vol.376 , pp. 1155-1167
    • Sun, Y.1    Makarava, N.2    Lee, C.I.3
  • 197
    • 0030669036 scopus 로고    scopus 로고
    • The pathogenesis of senile plaques
    • Dickson DW. The pathogenesis of senile plaques. J Neuropathol Exp Neurol 1997; 56: 321-39.
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 321-339
    • Dickson, D.W.1
  • 198
    • 1842685948 scopus 로고
    • Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (Tau)
    • Wood JG, Mirra SS, Pollock NJ, Binder LI. Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau). Proc Natl Acad Sci USA 1986; 83: 4040-3.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4040-4043
    • Wood, J.G.1    Mirra, S.S.2    Pollock, N.J.3    Binder, L.I.4
  • 199
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (Tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik KS, Joachim CL, Selkoe DJ. Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci USA 1986; 83: 4044-8.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 200
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-associated protein tau (Tau) in Alzheimer cytoskeletal pathology
    • Grundke-Iqbal I, Iqbal K, Tung YC, et al. Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. Proc Natl Acad Sci USA 1986; 83: 4913-7.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4913-4917
    • Grundke-Iqbal, I.1    Iqbal, K.2    Tung, Y.C.3
  • 201
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001; 81: 741-66.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 202
    • 84870004031 scopus 로고    scopus 로고
    • Where, when, and in what form does sporadic Alzheimer's disease begin?
    • Braak H, Del Tredici K. Where, when, and in what form does sporadic Alzheimer's disease begin? Curr Opin Neurol 2012; 25: 708-14.
    • (2012) Curr Opin Neurol , vol.25 , pp. 708-714
    • Braak, H.1    Del Tredici, K.2
  • 203
    • 84898459097 scopus 로고    scopus 로고
    • The dendritic hypothesis for Alzheimer's disease pathophysiology
    • Cochran JN, Hall AM, Roberson ED. The dendritic hypothesis for Alzheimer's disease pathophysiology. Brain Res Bull 2014; 103: 18-28.
    • (2014) Brain Res Bull , vol.103 , pp. 18-28
    • Cochran, J.N.1    Hall, A.M.2    Roberson, E.D.3
  • 204
    • 0021572660 scopus 로고
    • The amyloid deposits in Alzheimer's disease: Their nature and pathogenesis
    • Glenner GG, Wong CW, Quaranta V, Eanes ED. The amyloid deposits in Alzheimer's disease: their nature and pathogenesis. Appl Pathol 1984; 2: 357-69.
    • (1984) Appl Pathol , vol.2 , pp. 357-369
    • Glenner, G.G.1    Wong, C.W.2    Quaranta, V.3    Eanes, E.D.4
  • 205
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy JA, Higgins GA. Alzheimer's disease: the amyloid cascade hypothesis. Science 1992; 256: 184-5.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 206
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers - A decade of discovery
    • Walsh DM, Selkoe DJ. A beta oligomers - a decade of discovery. J Neurochem 2007; 101: 1172-84.
    • (2007) J Neurochem , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 208
    • 0027330972 scopus 로고
    • Alpha B crystallin and HSP28 are enhanced in the cerebral cortex of patients with Alzheimer's disease
    • Shinohara H, Inaguma Y, Goto S, Inagaki T, Kato K. Alpha B crystallin and HSP28 are enhanced in the cerebral cortex of patients with Alzheimer's disease. J Neurol Sci 1993; 119: 203-8.
    • (1993) J Neurol Sci , vol.119 , pp. 203-208
    • Shinohara, H.1    Inaguma, Y.2    Goto, S.3    Inagaki, T.4    Kato, K.5
  • 209
    • 0028297910 scopus 로고
    • Expression of small heatshock protein hsp 27 in reactive gliosis in Alzheimer disease and other types of dementia
    • Renkawek K, Bosman GJ, de Jong WW. Expression of small heatshock protein hsp 27 in reactive gliosis in Alzheimer disease and other types of dementia. Acta Neuropathol 1994; 87: 511-9.
    • (1994) Acta Neuropathol , vol.87 , pp. 511-519
    • Renkawek, K.1    Bosman, G.J.2    De Jong, W.W.3
  • 211
    • 0034742628 scopus 로고    scopus 로고
    • The relationship between alphaB-crystallin and neurofibrillary tangles in Alzheimer's disease
    • Mao JJ, Katayama S, Watanabe C, et al. The relationship between alphaB-crystallin and neurofibrillary tangles in Alzheimer's disease. Neuropathol Appl Neurobiol 2001; 27: 180-8.
    • (2001) Neuropathol Appl Neurobiol , vol.27 , pp. 180-188
    • Mao, J.J.1    Katayama, S.2    Watanabe, C.3
  • 212
    • 9444267091 scopus 로고    scopus 로고
    • Ballooned neurones in the limbic lobe are associated with Alzheimer type pathology and lack diagnostic specificity
    • Fujino Y, Delucia MW, Davies P, Dickson DW. Ballooned neurones in the limbic lobe are associated with Alzheimer type pathology and lack diagnostic specificity. Neuropathol Appl Neurobiol 2004; 30: 676-82.
    • (2004) Neuropathol Appl Neurobiol , vol.30 , pp. 676-682
    • Fujino, Y.1    Delucia, M.W.2    Davies, P.3    Dickson, D.W.4
  • 213
    • 58149506229 scopus 로고    scopus 로고
    • Crystallin proteins and amyloid fibrils
    • Ecroyd H, Carver JA. Crystallin proteins and amyloid fibrils. Cell Mol Life Sci 2009; 66: 62-81.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 62-81
    • Ecroyd, H.1    Carver, J.A.2
  • 214
    • 0033584258 scopus 로고    scopus 로고
    • The molecular chaperone alphaB-crystallin enhances amyloid beta neurotoxicity
    • Stege GJ, Renkawek K, Overkamp PS, et al. The molecular chaperone alphaB-crystallin enhances amyloid beta neurotoxicity. Biochem Biophys Res Commun 1999; 262: 152-6.
    • (1999) Biochem Biophys Res Commun , vol.262 , pp. 152-156
    • Stege, G.J.1    Renkawek, K.2    Overkamp, P.S.3
  • 215
    • 33646857038 scopus 로고    scopus 로고
    • Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta protein toxicity
    • Wilhelmus MM, Boelens WC, Otte-Holler I, et al. Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta protein toxicity. Brain Res 2006; 1089: 67-78.
    • (2006) Brain Res , vol.1089 , pp. 67-78
    • Wilhelmus, M.M.1    Boelens, W.C.2    Otte-Holler, I.3
  • 216
    • 80053379382 scopus 로고    scopus 로고
    • Binding of the molecular chaperone alphaB-crystallin to Abeta amyloid fibrils inhibits fibril elongation
    • Shammas SL, Waudby CA, Wang S, et al. Binding of the molecular chaperone alphaB-crystallin to Abeta amyloid fibrils inhibits fibril elongation. Biophys J 2011; 101: 1681-9.
    • (2011) Biophys J , vol.101 , pp. 1681-1689
    • Shammas, S.L.1    Waudby, C.A.2    Wang, S.3
  • 217
    • 0034602513 scopus 로고    scopus 로고
    • Interaction between beta-amyloid and lens alphaBcrystallin
    • Liang JJ. Interaction between beta-amyloid and lens alphaBcrystallin. FEBS Lett 2000; 484: 98-101.
    • (2000) FEBS Lett , vol.484 , pp. 98-101
    • Liang, J.J.1
  • 218
    • 33750053608 scopus 로고    scopus 로고
    • AlphaB-crystallin competes with Alzheimer's disease beta-amyloid peptide for peptide- peptide interactions and induces oxidation of Abeta-Met35
    • Narayanan S, Kamps B, Boelens WC, Reif B. alphaB-crystallin competes with Alzheimer's disease beta-amyloid peptide for peptide- peptide interactions and induces oxidation of Abeta-Met35. FEBS Lett 2006; 580: 5941-6.
    • (2006) FEBS Lett , vol.580 , pp. 5941-5946
    • Narayanan, S.1    Kamps, B.2    Boelens, W.C.3    Reif, B.4
  • 219
    • 78149466716 scopus 로고    scopus 로고
    • AlphaB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by kappa-casein and the amyloid-beta peptide
    • Dehle FC, Ecroyd H, Musgrave IF, Carver JA. alphaB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by kappa-casein and the amyloid-beta peptide. Cell Stress Chaperones 2010; 15: 1013-26.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 1013-1026
    • Dehle, F.C.1    Ecroyd, H.2    Musgrave, I.F.3    Carver, J.A.4
  • 221
    • 14144252923 scopus 로고    scopus 로고
    • Hsp20, a novel alphacrystallin, prevents Abeta fibril formation and toxicity
    • Lee S, Carson K, Rice-Ficht A, Good T. Hsp20, a novel alphacrystallin, prevents Abeta fibril formation and toxicity. Protein Sci 2005; 14: 593-601.
    • (2005) Protein Sci , vol.14 , pp. 593-601
    • Lee, S.1    Carson, K.2    Rice-Ficht, A.3    Good, T.4
  • 222
    • 79960298697 scopus 로고    scopus 로고
    • Sequestration of toxic oligomers by HspB1 as a cytoprotective mechanism
    • Ojha J, Masilamoni G, Dunlap D, Udoff RA, Cashikar AG. Sequestration of toxic oligomers by HspB1 as a cytoprotective mechanism. Mol Cell Biol 2011; 31: 3146-57.
    • (2011) Mol Cell Biol , vol.31 , pp. 3146-3157
    • Ojha, J.1    Masilamoni, G.2    Dunlap, D.3    Udoff, R.A.4    Cashikar, A.G.5
  • 223
    • 33745874108 scopus 로고    scopus 로고
    • Small heat shock proteins differentially affect Abeta aggregation and toxicity
    • Lee S, Carson K, Rice-Ficht A, Good T. Small heat shock proteins differentially affect Abeta aggregation and toxicity. Biochem Biophys Res Commun 2006; 347: 527-33.
    • (2006) Biochem Biophys Res Commun , vol.347 , pp. 527-533
    • Lee, S.1    Carson, K.2    Rice-Ficht, A.3    Good, T.4
  • 224
    • 84902244714 scopus 로고    scopus 로고
    • The phosphorylation of Hsp20 enhances its association with amyloid-beta to increase protection against neuronal cell death
    • Cameron RT, Quinn SD, Cairns LS, et al. The phosphorylation of Hsp20 enhances its association with amyloid-beta to increase protection against neuronal cell death. Mol Cell Neurosci 2014; 61: 46-55.
    • (2014) Mol Cell Neurosci , vol.61 , pp. 46-55
    • Cameron, R.T.1    Quinn, S.D.2    Cairns, L.S.3
  • 225
    • 23044468691 scopus 로고    scopus 로고
    • The synaptic Abeta hypothesis of Alzheimer disease
    • Tanzi RE. The synaptic Abeta hypothesis of Alzheimer disease. Nat Neurosci 2005; 8: 977-9.
    • (2005) Nat Neurosci , vol.8 , pp. 977-979
    • Tanzi, R.E.1
  • 226
    • 70449461063 scopus 로고    scopus 로고
    • The small heat shock protein Hsp27 protects cortical neurons against the toxic effects of beta-amyloid peptide
    • King M, Nafar F, Clarke J, Mearow K. The small heat shock protein Hsp27 protects cortical neurons against the toxic effects of beta-amyloid peptide. J Neurosci Res 2009; 87: 3161-75.
    • (2009) J Neurosci Res , vol.87 , pp. 3161-3175
    • King, M.1    Nafar, F.2    Clarke, J.3    Mearow, K.4
  • 227
    • 84885468499 scopus 로고    scopus 로고
    • Overexpression of Hsp27 ameliorates symptoms of Alzheimer's disease in APP/PS1 mice
    • Toth ME, Szegedi V, Varga E, et al. Overexpression of Hsp27 ameliorates symptoms of Alzheimer's disease in APP/PS1 mice. Cell Stress Chaperones 2013; 18: 759-71.
    • (2013) Cell Stress Chaperones , vol.18 , pp. 759-771
    • Toth, M.E.1    Szegedi, V.2    Varga, E.3
  • 228
    • 84963748902 scopus 로고    scopus 로고
    • HspB5/alphaB-crystallin increases dendritic complexity and protects the dendritic arbor during heat shock in cultured hippocampal neurons
    • Bartelt-Kirbach B, Moron M, Glomb M, Beck CM, Weller MP, Golenhofen N. HspB5/alphaB-crystallin increases dendritic complexity and protects the dendritic arbor during heat shock in cultured hippocampal neurons. Cell Mol Life Sci 2016; DOI 10.1007/s00018-016-2219-9.
    • (2016) Cell Mol Life Sci
    • Bartelt-Kirbach, B.1    Moron, M.2    Glomb, M.3    Beck, C.M.4    Weller, M.P.5    Golenhofen, N.6
  • 229
    • 80051980871 scopus 로고    scopus 로고
    • Systemic augmentation of alphaB-crystallin provides therapeutic benefit twelve hours poststroke onset via immune modulation
    • Arac A, Brownell SE, Rothbard JB, et al. Systemic augmentation of alphaB-crystallin provides therapeutic benefit twelve hours poststroke onset via immune modulation. Proc Natl Acad Sci USA 2011; 108: 13287-92.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 13287-13292
    • Arac, A.1    Brownell, S.E.2    Rothbard, J.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.