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Volumn 316, Issue 15, 2010, Pages 2424-2433

Hsp105 reduces the protein aggregation and cytotoxicity by expanded-polyglutamine proteins through the induction of Hsp70

Author keywords

Hsp105 ; Hsp105 ; Hsp70; Polyglutamine diseases; Protein aggregation

Indexed keywords

GREEN FLUORESCENT PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 105ALPHA; HEAT SHOCK PROTEIN 105BETA; HEAT SHOCK PROTEIN 70; POLYGLUTAMINE; UNCLASSIFIED DRUG;

EID: 77955053465     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2010.06.003     Document Type: Article
Times cited : (18)

References (59)
  • 1
    • 0035871295 scopus 로고    scopus 로고
    • Beyond the Qs in the polyglutamine diseases
    • Orr H.T. Beyond the Qs in the polyglutamine diseases. Genes Dev. 2001, 15:925-932.
    • (2001) Genes Dev. , vol.15 , pp. 925-932
    • Orr, H.T.1
  • 2
    • 0033080367 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases: molecular aspects
    • Perutz M.F. Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem. Sci. 1999, 24:58-63.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 58-63
    • Perutz, M.F.1
  • 4
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of Huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M., Sapp E., Chase K.O., Davies S.W., Bates G.P., Vonsattel J.P., Aronin N. Aggregation of Huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 1997, 277:1990-1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 6
    • 0034426013 scopus 로고    scopus 로고
    • Amino-terminal fragments of mutant huntingtin show selective accumulation in striatal neurons and synaptic toxicity
    • Li H., Li S.H., Johnston H., Shelbourne P.E., Li X.J. Amino-terminal fragments of mutant huntingtin show selective accumulation in striatal neurons and synaptic toxicity. Nat. Genet. 2000, 25:385-389.
    • (2000) Nat. Genet. , vol.25 , pp. 385-389
    • Li, H.1    Li, S.H.2    Johnston, H.3    Shelbourne, P.E.4    Li, X.J.5
  • 7
    • 0034737299 scopus 로고    scopus 로고
    • Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease
    • Yamamoto A., Lucas J.J., Hen R. Reversal of neuropathology and motor dysfunction in a conditional model of Huntington's disease. Cell 2000, 101:57-66.
    • (2000) Cell , vol.101 , pp. 57-66
    • Yamamoto, A.1    Lucas, J.J.2    Hen, R.3
  • 9
    • 0034662915 scopus 로고    scopus 로고
    • Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease
    • Carmichael J., Chatellier J., Woolfson A., Milstein C., Fersht A.R., Rubinsztein D.C. Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease. Proc. Natl Acad. Sci. USA 2000, 97:9701-9705.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9701-9705
    • Carmichael, J.1    Chatellier, J.2    Woolfson, A.3    Milstein, C.4    Fersht, A.R.5    Rubinsztein, D.C.6
  • 10
    • 0034646426 scopus 로고    scopus 로고
    • Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease
    • Wyttenbach A., Carmichael J., Swartz J., Furlong R.A., Narain Y., Rankin J., Rubinsztein D.C. Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease. Proc. Natl Acad. Sci. USA 2000, 97:2898-2903.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 2898-2903
    • Wyttenbach, A.1    Carmichael, J.2    Swartz, J.3    Furlong, R.A.4    Narain, Y.5    Rankin, J.6    Rubinsztein, D.C.7
  • 11
    • 0034652127 scopus 로고    scopus 로고
    • Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins
    • Krobitsch S., Lindquist S. Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc. Natl Acad. Sci. USA 2000, 97:1589-1594.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 1589-1594
    • Krobitsch, S.1    Lindquist, S.2
  • 13
    • 34347258879 scopus 로고    scopus 로고
    • Small molecule inducers of heat-shock response reduce polyQ-mediated huntingtin aggregation.A possible therapeutic strategy
    • Herbst M., Wanker E.E. Small molecule inducers of heat-shock response reduce polyQ-mediated huntingtin aggregation.A possible therapeutic strategy. Neurodegener. Dis. 2007, 4:254-260.
    • (2007) Neurodegener. Dis. , vol.4 , pp. 254-260
    • Herbst, M.1    Wanker, E.E.2
  • 14
    • 36849044616 scopus 로고    scopus 로고
    • Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response
    • Zhang Y.Q., Sarge K.D. Celastrol inhibits polyglutamine aggregation and toxicity though induction of the heat shock response. J. Mol. Med. 2007, 85:1421-1428.
    • (2007) J. Mol. Med. , vol.85 , pp. 1421-1428
    • Zhang, Y.Q.1    Sarge, K.D.2
  • 15
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings C.J., Mancini M.A., Antalffy B., DeFranco D.B., Orr H.T., Zoghbi H.Y. Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat. Genet. 1998, 19:148-154.
    • (1998) Nat. Genet. , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 16
    • 0033499931 scopus 로고    scopus 로고
    • Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease
    • Chai Y., Koppenhafer S.L., Bonini N.M., Paulson H.L. Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J. Neurosci. 1999, 19:10338-10347.
    • (1999) J. Neurosci. , vol.19 , pp. 10338-10347
    • Chai, Y.1    Koppenhafer, S.L.2    Bonini, N.M.3    Paulson, H.L.4
  • 17
    • 0032945938 scopus 로고    scopus 로고
    • Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone
    • Stenoien D.L., Cummings C.J., Adams H.P., Mancini M.G., Patel K., DeMartino G.N., Marcelli M., Weigel N.L., Mancini M.A. Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone. Hum. Mol. Genet. 1999, 8:731-741.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 731-741
    • Stenoien, D.L.1    Cummings, C.J.2    Adams, H.P.3    Mancini, M.G.4    Patel, K.5    DeMartino, G.N.6    Marcelli, M.7    Weigel, N.L.8    Mancini, M.A.9
  • 18
    • 0034708793 scopus 로고    scopus 로고
    • Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract
    • Kobayashi Y., Kume A., Li M., Doyu M., Hata M., Ohtsuka K., Sobue G. Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract. J. Biol. Chem. 2000, 275:8772-8778.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8772-8778
    • Kobayashi, Y.1    Kume, A.2    Li, M.3    Doyu, M.4    Hata, M.5    Ohtsuka, K.6    Sobue, G.7
  • 20
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity
    • Jana N.R., Tanaka M., Wang G., Nukina N. Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Hum. Mol. Genet. 2000, 9:2009-2018.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.3    Nukina, N.4
  • 22
    • 0037444446 scopus 로고    scopus 로고
    • Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein
    • Adachi H., Katsuno M., Minamiyama M., Sang C., Pagoulatos G., Angelidis C., Kusakabe M., Yoshiki A., Kobayashi Y., Doyu M., Sobue G. Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein. J. Neurosci. 2003, 23:2203-2211.
    • (2003) J. Neurosci. , vol.23 , pp. 2203-2211
    • Adachi, H.1    Katsuno, M.2    Minamiyama, M.3    Sang, C.4    Pagoulatos, G.5    Angelidis, C.6    Kusakabe, M.7    Yoshiki, A.8    Kobayashi, Y.9    Doyu, M.10    Sobue, G.11
  • 23
    • 16544383250 scopus 로고    scopus 로고
    • Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer
    • Wacker J.L., Zareie M.H., Fong H., Sarikaya M., Muchowski P.J. Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer. Nat. Struct. Mol. Biol. 2004, 11:1215-1222.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1215-1222
    • Wacker, J.L.1    Zareie, M.H.2    Fong, H.3    Sarikaya, M.4    Muchowski, P.J.5
  • 24
    • 54449101793 scopus 로고    scopus 로고
    • Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones
    • Fujikake N., Nagai Y., Popiel H.A., Okamoto Y., Yamaguchi M., Toda T. Heat shock transcription factor 1-activating compounds suppress polyglutamine-induced neurodegeneration through induction of multiple molecular chaperones. J. Biol. Chem. 2008, 283:26188-26197.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26188-26197
    • Fujikake, N.1    Nagai, Y.2    Popiel, H.A.3    Okamoto, Y.4    Yamaguchi, M.5    Toda, T.6
  • 25
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick J.P., Hartl F.U. Molecular chaperone functions of heat-shock proteins. Ann. Rev. Biochem. 1993, 62:349-384.
    • (1993) Ann. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 26
    • 0028061311 scopus 로고
    • Heat shock proteins and molecular chaperones: mediators of protein conformation and turnover in the cell
    • Craig E.A., Weissman J.S., Horwich A.L. Heat shock proteins and molecular chaperones: mediators of protein conformation and turnover in the cell. Cell 1994, 78:365-372.
    • (1994) Cell , vol.78 , pp. 365-372
    • Craig, E.A.1    Weissman, J.S.2    Horwich, A.L.3
  • 27
    • 0035930598 scopus 로고    scopus 로고
    • Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation
    • Zhou H., Li S.H., Li X.J. Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation. J. Biol. Chem. 2001, 276:48417-48424.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48417-48424
    • Zhou, H.1    Li, S.H.2    Li, X.J.3
  • 28
    • 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., Diaz-Latoud C., Arrigo A.P., Rubinsztein D.C. Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum. Mol. Genet. 2002, 11:1137-1151.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1137-1151
    • Wyttenbach, A.1    Sauvageot, O.2    Carmichael, J.3    Diaz-Latoud, C.4    Arrigo, A.P.5    Rubinsztein, D.C.6
  • 29
    • 0028139086 scopus 로고
    • Characterization of high-molecular-mass heat shock proteins and 42 degrees C-specific heat shock proteins of murine cells
    • Hatayama T., Yasuda K., Nishiyama E. Characterization of high-molecular-mass heat shock proteins and 42 degrees C-specific heat shock proteins of murine cells. Biochem. Biophys. Res. Commun. 1994, 204:357-365.
    • (1994) Biochem. Biophys. Res. Commun. , vol.204 , pp. 357-365
    • Hatayama, T.1    Yasuda, K.2    Nishiyama, E.3
  • 30
    • 0029564092 scopus 로고
    • Cloning and expression of murine high molecular mass heat shock proteins, HSP105
    • Yasuda K., Nakai A., Hatayama T., Nagata K. Cloning and expression of murine high molecular mass heat shock proteins, HSP105. J. Biol. Chem. 1995, 270:29718-29723.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29718-29723
    • Yasuda, K.1    Nakai, A.2    Hatayama, T.3    Nagata, K.4
  • 31
    • 0033579961 scopus 로고    scopus 로고
    • Molecular cloning, expression and localization of human 105kDa heat shock protein, hsp105
    • Ishihara K., Yasuda K., Hatayama T. Molecular cloning, expression and localization of human 105kDa heat shock protein, hsp105. Biochim. Biophys. Acta 1999, 1444:138-142.
    • (1999) Biochim. Biophys. Acta , vol.1444 , pp. 138-142
    • Ishihara, K.1    Yasuda, K.2    Hatayama, T.3
  • 33
    • 0038245297 scopus 로고    scopus 로고
    • Protein kinase CK2 phosphorylates Hsp105 alpha at Ser509 and modulates its function
    • Ishihara K., Yamagishi N., Hatayama T. Protein kinase CK2 phosphorylates Hsp105 alpha at Ser509 and modulates its function. Biochem. J. 2003, 371:917-925.
    • (2003) Biochem. J. , vol.371 , pp. 917-925
    • Ishihara, K.1    Yamagishi, N.2    Hatayama, T.3
  • 34
    • 0344009436 scopus 로고    scopus 로고
    • Hsp105 but not Hsp70 family proteins suppress the aggregation of heat-denatured protein in the presence of ADP
    • Yamagishi N., Ishihara K., Saito Y., Hatayama T. Hsp105 but not Hsp70 family proteins suppress the aggregation of heat-denatured protein in the presence of ADP. FEBS Lett. 2003, 555:390-396.
    • (2003) FEBS Lett. , vol.555 , pp. 390-396
    • Yamagishi, N.1    Ishihara, K.2    Saito, Y.3    Hatayama, T.4
  • 35
    • 34648857577 scopus 로고    scopus 로고
    • Different localization of Hsp105 family proteins in mammalian cells
    • Saito Y., Yamagishi N., Hatayama T. Different localization of Hsp105 family proteins in mammalian cells. Exp. Cell Res. 2007, 313:3707-3717.
    • (2007) Exp. Cell Res. , vol.313 , pp. 3707-3717
    • Saito, Y.1    Yamagishi, N.2    Hatayama, T.3
  • 36
    • 59449103206 scopus 로고    scopus 로고
    • Nuclear localization mechanism of Hsp105β and its possible function in mammalian cells
    • Saito Y., Yamagishi N., Hatayama T. Nuclear localization mechanism of Hsp105β and its possible function in mammalian cells. J. Biochem. 2009, 145:185-191.
    • (2009) J. Biochem. , vol.145 , pp. 185-191
    • Saito, Y.1    Yamagishi, N.2    Hatayama, T.3
  • 37
    • 70349522006 scopus 로고    scopus 로고
    • Hsp105β up-regulates hsp70 gene expression through signal transducer and activator of transcription-3
    • Yamagishi N., Fujii H., Saito Y., Hatayama T. Hsp105β up-regulates hsp70 gene expression through signal transducer and activator of transcription-3. FEBS J. 2009, 276:5870-5880.
    • (2009) FEBS J. , vol.276 , pp. 5870-5880
    • Yamagishi, N.1    Fujii, H.2    Saito, Y.3    Hatayama, T.4
  • 38
    • 0042591262 scopus 로고    scopus 로고
    • Hsp105alpha suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity
    • Ishihara K., Yamagishi N., Saito Y., Adachi H., Kobayashi Y., Sobue G., Ohtsuka K., Hatayama T. Hsp105alpha suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity. J. Biol. Chem. 2003, 278:25143-25150.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25143-25150
    • Ishihara, K.1    Yamagishi, N.2    Saito, Y.3    Adachi, H.4    Kobayashi, Y.5    Sobue, G.6    Ohtsuka, K.7    Hatayama, T.8
  • 39
    • 0023797306 scopus 로고
    • Common antigenicity of mouse 42 degrees C-specific heat-shock protein with mouse HSP 105
    • Honda K., Hatayama T., Yukioka M. Common antigenicity of mouse 42 degrees C-specific heat-shock protein with mouse HSP 105. J. Biochem. 1988, 103:81-85.
    • (1988) J. Biochem. , vol.103 , pp. 81-85
    • Honda, K.1    Hatayama, T.2    Yukioka, M.3
  • 40
  • 41
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B., Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell 1998, 92:351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 42
    • 33745749328 scopus 로고    scopus 로고
    • Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor
    • Raviol H., Sadlish H., Rodriguez F., Mayer M.P., Bukau B. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J. 2006, 25:2510-2018.
    • (2006) EMBO J. , vol.25 , pp. 2510-2018
    • Raviol, H.1    Sadlish, H.2    Rodriguez, F.3    Mayer, M.P.4    Bukau, B.5
  • 43
    • 33745762927 scopus 로고    scopus 로고
    • Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
    • Dragovic Z., Broadley S.A., Shomura Y., Bracher A., Hartl F.U. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J. 2006, 25:2519-2028.
    • (2006) EMBO J. , vol.25 , pp. 2519-2028
    • Dragovic, Z.1    Broadley, S.A.2    Shomura, Y.3    Bracher, A.4    Hartl, F.U.5
  • 44
    • 33845587149 scopus 로고    scopus 로고
    • Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1
    • Shaner L., Sousa R., Morano K.A. Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1. Biochemistry 2006, 45:15075-15084.
    • (2006) Biochemistry , vol.45 , pp. 15075-15084
    • Shaner, L.1    Sousa, R.2    Morano, K.A.3
  • 47
    • 0030716768 scopus 로고    scopus 로고
    • The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1
    • Matilla A., Koshy B.T., Cummings C.J., Isobe T., Orr H.T., Zoghbi H.Y. The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1. Nature 1997, 389:974-978.
    • (1997) Nature , vol.389 , pp. 974-978
    • Matilla, A.1    Koshy, B.T.2    Cummings, C.J.3    Isobe, T.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 51
    • 0035888620 scopus 로고    scopus 로고
    • Similarities between spinocerebellar ataxia type 7 (SCA7) cell models and human brain: proteins recruited in inclusions and activation of caspase-3
    • Zander C., Takahashi J., Hachimi K.H.E., Fujigasaki H., Albanese V., Lebre A.S., Stevanin G., Duyckaerts C., Brice A. Similarities between spinocerebellar ataxia type 7 (SCA7) cell models and human brain: proteins recruited in inclusions and activation of caspase-3. Hum. Mol. Genet. 2001, 10:2569-2579.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2569-2579
    • Zander, C.1    Takahashi, J.2    Hachimi, K.H.E.3    Fujigasaki, H.4    Albanese, V.5    Lebre, A.S.6    Stevanin, G.7    Duyckaerts, C.8    Brice, A.9
  • 53
    • 0032932192 scopus 로고    scopus 로고
    • Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: a novel pathway controlled by HSP72
    • Meriin A.B., Yaglom J., Gabai V.L., Zon L., Ganiatsas S., Mosser D.D., Zon L., Sherman M.Y. Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: a novel pathway controlled by HSP72. Mol. Cell. Biol. 1999, 19:2547-2555.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2547-2555
    • Meriin, A.B.1    Yaglom, J.2    Gabai, V.L.3    Zon, L.4    Ganiatsas, S.5    Mosser, D.D.6    Zon, L.7    Sherman, M.Y.8
  • 54
    • 0034682748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3activation
    • Li C., Lee J., Ko Y., Kim J., Seo J. Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3activation. J. Biol. Chem. 2000, 275:25665-25671.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25665-25671
    • Li, C.1    Lee, J.2    Ko, Y.3    Kim, J.4    Seo, J.5
  • 56
    • 33748631305 scopus 로고    scopus 로고
    • Hsp105 family proteins suppress staurosporine-induced apoptosis by inhibiting the translocation of Bax to mitochondria in HeLa cells
    • Yamagishi N., Ishihara K., Saito Y., Hatayama T. Hsp105 family proteins suppress staurosporine-induced apoptosis by inhibiting the translocation of Bax to mitochondria in HeLa cells. Exp. Cell Res. 2006, 312:3215-3223.
    • (2006) Exp. Cell Res. , vol.312 , pp. 3215-3223
    • Yamagishi, N.1    Ishihara, K.2    Saito, Y.3    Hatayama, T.4
  • 57
    • 50849105753 scopus 로고    scopus 로고
    • Mammalian 105kDa heat shock family proteins suppress hydrogen peroxide-induced apoptosis through a p38 MAPK-dependent mitochondrial pathway in HeLa cells
    • Yamagishi N., Saito Y., Hatayama T. Mammalian 105kDa heat shock family proteins suppress hydrogen peroxide-induced apoptosis through a p38 MAPK-dependent mitochondrial pathway in HeLa cells. FEBS J. 2008, 275:4558-4570.
    • (2008) FEBS J. , vol.275 , pp. 4558-4570
    • Yamagishi, N.1    Saito, Y.2    Hatayama, T.3
  • 58
    • 0035798228 scopus 로고    scopus 로고
    • Role of hsp105 in protection against stress-induced apoptosis in neuronal PC12 cells
    • Hatayama T., Yamagishi N., Minobe E., Sakai K. Role of hsp105 in protection against stress-induced apoptosis in neuronal PC12 cells. Biochem. Biophys. Res. Commun. 2001, 288:528-534.
    • (2001) Biochem. Biophys. Res. Commun. , vol.288 , pp. 528-534
    • Hatayama, T.1    Yamagishi, N.2    Minobe, E.3    Sakai, K.4
  • 59
    • 33646190885 scopus 로고    scopus 로고
    • The ASK1-MAP kinase signaling in ER stress and neurodegenerative diseases
    • Sekine Y., Takeda K., Ichijo H. The ASK1-MAP kinase signaling in ER stress and neurodegenerative diseases. Curr. Mol. Med. 2006, 6:87-97.
    • (2006) Curr. Mol. Med. , vol.6 , pp. 87-97
    • Sekine, Y.1    Takeda, K.2    Ichijo, H.3


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