메뉴 건너뛰기




Volumn 22, Issue 19, 2011, Pages 3571-3583

Heat shock factor 2 is required for maintaining proteostasis against febrile-range thermal stress and polyglutamine aggregation

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; HEAT SHOCK FACTOR 2; HEAT SHOCK PROTEIN; HEAT SHOCK TRANSCRIPTION FACTOR 1; POLYGLUTAMINE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 80053359794     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E11-04-0330     Document Type: Article
Times cited : (56)

References (75)
  • 1
    • 77957269766 scopus 로고    scopus 로고
    • Roles of heat shock factors in gametogenesis and development
    • Abane R, Mezger V (2010). Roles of heat shock factors in gametogenesis and development. FEBS J 277, 4150-4172.
    • (2010) FEBS J , vol.277 , pp. 4150-4172
    • Abane, R.1    Mezger, V.2
  • 3
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: Integrators of cell stress, development and lifespan
    • Akerfelt M, Morimoto RI, Sistonen L (2010). Heat shock factors: integrators of cell stress, development and lifespan. Nat Rev Mol Cell Biol 11, 545-555.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 545-555
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 4
    • 0041827383 scopus 로고    scopus 로고
    • Formation of nuclear stress granules involves HSF2 and coincides with the nucleolar localization of Hsp70
    • DOI 10.1242/jcs.00671
    • Alastalo TP, Hellesuo M, Sandqvist A, Hietakangas V, Kallio M, Sistonen L (2003). Formation of nuclear stress granules involves HSF2 and coincides with the nucleolar localization of Hsp70. J Cell Sci 116, 3557-3570. (Pubitemid 37063399)
    • (2003) Journal of Cell Science , vol.116 , Issue.17 , pp. 3557-3570
    • Alastalo, T.-P.1    Hellesuo, M.2    Sandqvist, A.3    Hietakangas, V.4    Kallio, M.5    Sistonen, L.6
  • 5
    • 3042559648 scopus 로고    scopus 로고
    • Mutant loxP vectors for selectable marker recycle and conditional knock-outs
    • Arakawa H, Lodygin D, Buerstedde JM (2001). Mutant loxP vectors for selectable marker recycle and conditional knock-outs. BMC Biotechnol 1, 7.
    • (2001) BMC Biotechnol , vol.1 , pp. 7
    • Arakawa, H.1    Lodygin, D.2    Buerstedde, J.M.3
  • 6
    • 0015606376 scopus 로고
    • Circadian rhythms of chicken brain temperatures
    • Aschoff C, Aschoff J, Von Saint Paul U (1973). Circadian rhythms of chicken brain temperatures. J Physiol 230, 103-113.
    • (1973) J Physiol , vol.230 , pp. 103-113
    • Aschoff, C.1    Aschoff, J.2    Von Saint Paul, U.3
  • 7
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • DOI 10.1126/science.1141448
    • Balch WE, Morimoto RI, Dillin A, Kelly JW (2008). Adapting proteostasis for disease intervention. Science 319, 916-919. (Pubitemid 351263754)
    • (2008) Science , vol.319 , Issue.5865 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 8
    • 0027474909 scopus 로고
    • Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1
    • Baler R, Dahl G, Voellmy R (1993). Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1. Mol Cell Biol 13, 2486-2496. (Pubitemid 23097727)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.4 , pp. 2486-2496
    • Baler, R.1    Dahl, G.2    Voellmy, R.3
  • 9
    • 70349266064 scopus 로고    scopus 로고
    • Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging
    • Ben-Zvi A, Miller EA, Morimoto RI (2009). Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging. Proc Natl Acad Sci USA 106, 14914-14919.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14914-14919
    • Ben-Zvi, A.1    Miller, E.A.2    Morimoto, R.I.3
  • 11
    • 35949001344 scopus 로고    scopus 로고
    • Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila
    • DOI 10.1371/journal.pgen.0030177
    • Bilen J, Bonini NM (2007). Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila. PLoS Genet 3, 1950-1964. (Pubitemid 350072059)
    • (2007) PLoS Genetics , vol.3 , Issue.10 , pp. 1950-1964
    • Bilen, J.1    Bonini, N.M.2
  • 12
    • 77957278382 scopus 로고    scopus 로고
    • Regulation of the members of the mammalian heat shock factor family
    • Björk JK, Sistonen L (2010). Regulation of the members of the mammalian heat shock factor family. FEBS J 277, 4126-4139.
    • (2010) FEBS J , vol.277 , pp. 4126-4139
    • Björk, J.K.1    Sistonen, L.2
  • 13
    • 33645507078 scopus 로고    scopus 로고
    • Role of heat-shock factor 2 in cerebral cortex formation and as a regulator of p35 expression
    • Chang Y et al. (2006). Role of heat-shock factor 2 in cerebral cortex formation and as a regulator of p35 expression. Genes Dev 20, 836-847.
    • (2006) Genes Dev , vol.20 , pp. 836-847
    • Chang, Y.1
  • 14
    • 79957910655 scopus 로고    scopus 로고
    • Regulation of transcription of hypoxia-inducible factor-1α (HIF-1α) by heat shock factors HSF2 and HSF4
    • Chen R, Liliental JE, Kowalski PE, Lu Q, Cohen SN (2011). Regulation of transcription of hypoxia-inducible factor-1α (HIF-1α) by heat shock factors HSF2 and HSF4. Oncogene 30, 2570-2580.
    • (2011) Oncogene , vol.30 , pp. 2570-2580
    • Chen, R.1    Liliental, J.E.2    Kowalski, P.E.3    Lu, Q.4    Cohen, S.N.5
  • 15
    • 34548658230 scopus 로고    scopus 로고
    • Heat Shock Factor 1 Is a Powerful Multifaceted Modifier of Carcinogenesis
    • DOI 10.1016/j.cell.2007.07.020, PII S0092867407009579
    • Dai C, Whitesell L, Rogers AB, Lindquist S (2007). Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis. Cell 130, 1005-1018. (Pubitemid 47410269)
    • (2007) Cell , vol.130 , Issue.6 , pp. 1005-1018
    • Dai, C.1    Whitesell, L.2    Rogers, A.B.3    Lindquist, S.4
  • 17
    • 78650918920 scopus 로고    scopus 로고
    • FOXO/4E-BP signaling in Drosophila muscles regulates organism-wide proteostasis during aging
    • Demontis F, Perrimon N (2010). FOXO/4E-BP signaling in Drosophila muscles regulates organism-wide proteostasis during aging. Cell 143, 813-825.
    • (2010) Cell , vol.143 , pp. 813-825
    • Demontis, F.1    Perrimon, N.2
  • 18
    • 0037648469 scopus 로고    scopus 로고
    • The small heat-shock protein αB-crystallin promotes FBX4-dependent ubiquitination
    • DOI 10.1074/jbc.M211403200
    • Den Engelsman J, Keijsers V, De Jong WW, Boelens WC (2003). The small heat-shock proteinαB-crystallin promotes FBX4-dependent ubiquitination. J Biol Chem 278, 4699-4704. (Pubitemid 36800969)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.7 , pp. 4699-4704
    • Den, E.J.1    Keijsers, V.2    De Jong, W.W.3    Boelens, W.C.4
  • 19
    • 77956315999 scopus 로고    scopus 로고
    • Manipulating heat shock factor-1 in Xenopus tadpoles: Neuronal tissues are refractory to exogenous expression
    • Dirks RP, van Geel R, Hensen SM, van Genesen ST, Lubsen NH (2010). Manipulating heat shock factor-1 in Xenopus tadpoles: neuronal tissues are refractory to exogenous expression. PLoS One 5, e10158.
    • (2010) PLoS One , vol.5
    • Dirks, R.P.1    Van Geel, R.2    Hensen, S.M.3    Van Genesen, S.T.4    Lubsen, N.H.5
  • 22
    • 77957252262 scopus 로고    scopus 로고
    • The heat shock factor family and adaptation to proteotoxic stress
    • Fujimoto M, Nakai A (2010). The heat shock factor family and adaptation to proteotoxic stress. FEBS J 277, 4112-4125.
    • (2010) FEBS J , vol.277 , pp. 4112-4125
    • Fujimoto, M.1    Nakai, A.2
  • 23
    • 57649155181 scopus 로고    scopus 로고
    • Analysis of HSF4 binding regions reveals its necessity for gene regulation during development and heat shock response in mouse lenses
    • Fujimoto M, Oshima I, Shinkawa T, Wang BB, Inouye S, Hayashida N, Takii R, Nakai A (2008). Analysis of HSF4 binding regions reveals its necessity for gene regulation during development and heat shock response in mouse lenses. J Biol Chem 283, 29961-29970.
    • (2008) J Biol Chem , vol.283 , pp. 29961-29970
    • Fujimoto, M.1    Oshima, I.2    Shinkawa, T.3    Wang, B.B.4    Inouye, S.5    Hayashida, N.6    Takii, R.7    Nakai, A.8
  • 24
    • 27144524290 scopus 로고    scopus 로고
    • Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models
    • DOI 10.1074/jbc.M506288200
    • Fujimoto M, Takaki E, Hayashi T, Kitaura Y, Tanaka Y, Inouye S, Nakai A (2005). Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models. J Biol Chem 280, 34908-34916. (Pubitemid 41504625)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.41 , pp. 34908-34916
    • Fujimoto, M.1    Takaki, E.2    Hayashi, T.3    Kitaura, Y.4    Tanaka, Y.5    Inouye, S.6    Nakai, A.7
  • 25
    • 79952473198 scopus 로고    scopus 로고
    • Transcription factor cooperativity with heat shock factor 1
    • Hayashida N, Fujimoto M, Nakai A (2011). Transcription factor cooperativity with heat shock factor 1. Transcription 2, 91-94.
    • (2011) Transcription , vol.2 , pp. 91-94
    • Hayashida, N.1    Fujimoto, M.2    Nakai, A.3
  • 27
  • 29
    • 0038701745 scopus 로고    scopus 로고
    • Regulation of aging and age-related disease by DAF-16 and heat-shock factor
    • DOI 10.1126/science.1083701
    • Hsu AL, Murphy CT, Kenyon C (2003). Regulation of aging and age-related disease by DAF-16 and heat-shock factor. Science 300, 1142-1145. (Pubitemid 36583098)
    • (2003) Science , vol.300 , Issue.5622 , pp. 1142-1145
    • Hsu, A.-L.1    Murphy, C.T.2    Kenyon, C.3
  • 30
    • 36349036470 scopus 로고    scopus 로고
    • Heat shock transcription factor 1 opens chromatin structure of interleukin-6 promoter to facilitate binding of an activator or a repressor
    • DOI 10.1074/jbc.M704471200
    • Inouye S, Fujimoto M, Nakamura T, Takaki E, Hayashida N, Hai T, Nakai A (2007). Heat shock transcription factor 1 opens chromatin structure of interleukin-6 promoter to facilitate binding of an activator or a repressor. J Biol Chem 282, 33210-33217. (Pubitemid 350159268)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.45 , pp. 33210-33217
    • Inouye, S.1    Fujimoto, M.2    Nakamura, T.3    Takaki, E.4    Hayashida, N.5    Hai, T.6    Nakai, A.7
  • 31
    • 0043133760 scopus 로고    scopus 로고
    • Activation of heat shock genes is not necessary for protection by heat shock transcription factor 1 against cell death due to a single exposure to high temperatures
    • DOI 10.1128/MCB.23.16.5882-5895.2003
    • Inouye S, Katsuki K, Izu H, Fujimoto M, Sugahara K, Yamada S, Shinkai Y, Oka Y, Katoh Y, Nakai A (2003). Activation of heat shock genes is not necessary for protection by heat shock transcription factor 1 against cell death due to a single exposure to high temperatures. Mol Cell Biol 23, 5882-5895. (Pubitemid 36951349)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.16 , pp. 5882-5895
    • Inouye, S.1    Katsuki, K.2    Izu, H.3    Fujimoto, M.4    Sugahara, K.5    Yamada, S.-I.6    Shinkai, Y.7    Oka, Y.8    Katoh, Y.9    Nakai, A.10
  • 33
    • 79958763020 scopus 로고    scopus 로고
    • HSFs and regulation of Hsp70.1 (Hspa1b) in oocytes and preimplantation embryos: New insights brought by transgenic and knockout mouse models
    • Le Masson F, Christians E (2011). HSFs and regulation of Hsp70.1 (Hspa1b) in oocytes and preimplantation embryos: new insights brought by transgenic and knockout mouse models. Cell Stress Chaperones 16, 275-285.
    • (2011) Cell Stress Chaperones , vol.16 , pp. 275-285
    • Le Masson, F.1    Christians, E.2
  • 34
  • 35
    • 0036084675 scopus 로고    scopus 로고
    • Invited review: Cytokine regulation of fever: studies using gene knockout mice
    • Leon LR (2002). Invited review: cytokine regulation of fever: studies using gene knockout mice. J Appl Physiol 92, 2648-2655.
    • (2002) J Appl Physiol , vol.92 , pp. 2648-2655
    • Leon, L.R.1
  • 37
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist S (1986). The heat-shock response. Annu Rev Biochem 55, 1151-1191.
    • (1986) Annu Rev Biochem , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 38
    • 0032575904 scopus 로고    scopus 로고
    • Concepts of fever
    • Mackowiak PA (1998). Concepts of fever. Arch Intern Med 158, 1870-1881.
    • (1998) Arch Intern Med , vol.158 , pp. 1870-1881
    • Mackowiak, P.A.1
  • 41
    • 0031841818 scopus 로고    scopus 로고
    • Heat shock response and protein degradation: Regulation of HSF2 by the ubiquitin-proteasome pathway
    • Mathew A, Mathur SK, Morimoto RI (1998). Heat shock response and protein degradation: regulation of HSF2 by the ubiquitin-proteasome pathway. Mol Cell Biol 18, 5091-5098. (Pubitemid 28388092)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.9 , pp. 5091-5098
    • Mathew, A.1    Mathur, S.K.2    Morimoto, R.I.3
  • 43
    • 0032571397 scopus 로고    scopus 로고
    • Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis
    • DOI 10.1074/jbc.273.13.7523
    • McMillan DR, Xiao X, Shao L, Graves K, Benjamin IJ (1998). Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis. J Biol Chem 273, 7523-7528. (Pubitemid 28152777)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.13 , pp. 7523-7528
    • McMillan, D.R.1    Xiao, X.2    Shao, L.3    Graves, K.4    Benjamin, I.J.5
  • 44
    • 0014958493 scopus 로고
    • Thermoresponsiveness of the preoptic region of the brain in house sparrows
    • Mills SH, Heath JE (1970). Thermoresponsiveness of the preoptic region of the brain in house sparrows. Science 168, 1008-1009.
    • (1970) Science , vol.168 , pp. 1008-1009
    • Mills, S.H.1    Heath, J.E.2
  • 45
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto RI (2008). Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev 22, 1427-1438.
    • (2008) Genes Dev , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 46
    • 0742323000 scopus 로고    scopus 로고
    • Regulation of Longevity in Caenorhabditis elegans by Heat Shock Factor and Molecular Chaperones
    • DOI 10.1091/mbc.E03-07-0532
    • Morley JF, Morimoto RI (2004). Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones. Mol Biol Cell 15, 657-664. (Pubitemid 38146482)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.2 , pp. 657-664
    • Morley, J.F.1    Morimoto, R.I.2
  • 47
    • 2342651518 scopus 로고    scopus 로고
    • Molecular chaperones and the stress of oncogenesis
    • DOI 10.1038/sj.onc.1207529
    • Mosser DD, Morimoto RI (2004). Molecular chaperones and the stress of oncogenesis. Oncogene 23, 2907-2918. (Pubitemid 38638852)
    • (2004) Oncogene , vol.23 , Issue.16 REV. ISS. 2 , pp. 2907-2918
    • Mosser, D.D.1    Morimoto, R.I.2
  • 48
    • 75649118599 scopus 로고    scopus 로고
    • Heat shock transcription factors and sensory placode development
    • Nakai A (2009). Heat shock transcription factors and sensory placode development. BMB Rep 42, 631-635.
    • (2009) BMB Rep , vol.42 , pp. 631-635
    • Nakai, A.1
  • 49
    • 0035355470 scopus 로고    scopus 로고
    • Cell cycle transition under stress conditions controlled by vertebrate heat shock factors
    • DOI 10.1093/emboj/20.11.2885
    • Nakai A, Ishikawa T (2001). Cell cycle transition under stress conditions controlled by vertebrate heat shock factors. EMBO J 20, 2885-2895. (Pubitemid 32938571)
    • (2001) EMBO Journal , vol.20 , Issue.11 , pp. 2885-2895
    • Nakai, A.1    Ishikawa, T.2
  • 50
    • 0029121347 scopus 로고
    • The DNA-binding properties of two heat shock factors, HSF1 and HSF3, are induced in the avian erythroblast cell line HD6
    • Nakai A, Kawazoe Y, Tanabe M, Nagata K, Morimoto RI (1995). The DNA-binding properties of two heat shock factors, HSF1 and HSF3, are induced in the avian erythroblast cell line HD6. Mol Cell Biol 15, 5168-5178.
    • (1995) Mol Cell Biol , vol.15 , pp. 5168-5178
    • Nakai, A.1    Kawazoe, Y.2    Tanabe, M.3    Nagata, K.4    Morimoto, R.I.5
  • 51
    • 0034599517 scopus 로고    scopus 로고
    • Arrest of spermatogenesis in mice expressing an active heat shock transcription factor 1
    • Nakai A, Suzuki M, Tanabe M (2000). Arrest of spermatogenesis in mice expressing an active heat shock transcription factor 1. EMBO J 19, 1545-1554. (Pubitemid 30182162)
    • (2000) EMBO Journal , vol.19 , Issue.7 , pp. 1545-1554
    • Nakai, A.1    Suzuki, M.2    Tanabe, M.3
  • 52
    • 0031032550 scopus 로고    scopus 로고
    • HSF4, a new member of the human heat shock factor family which lacks properties of a transcriptional activator
    • Nakai A, Tanabe M, Kawazoe Y, Inazawa J, Morimoto RI, Nagata K (1997). HSF4, a new member of the human heat shock factor family which lacks properties of a transcriptional activator. Mol Cell Biol 17, 469-481. (Pubitemid 26425637)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.1 , pp. 469-481
    • Nakai, A.1    Tanabe, M.2    Kawazoe, Y.3    Inazawa, J.4    Morimoto, R.I.5    Nagata, K.6
  • 53
    • 75749136948 scopus 로고    scopus 로고
    • Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease
    • Neef DW, Turski ML, Thiele DJ (2010). Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease. PLoS Biol 8, e1000291.
    • (2010) PLoS Biol , vol.8
    • Neef, D.W.1    Turski, M.L.2    Thiele, D.J.3
  • 55
    • 34147149523 scopus 로고    scopus 로고
    • Heat Shock Factor 2 (HSF2) contributes to inducible expression of hsp genes through interplay with HSF1
    • DOI 10.1074/jbc.M607556200
    • Ostling P, Björk JK, Roos-Mattjus P, Mezger V, Sistonen L (2007). Heat shock factor 2 (HSF2) contributes to inducible expression of hsp genes through interplay with HSF1. J Biol Chem 282, 7077-7086. (Pubitemid 47093630)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.10 , pp. 7077-7086
    • Ostling, P.1    Bjork, J.K.2    Roos-Mattjus, P.3    Mezger, V.4    Sistonen, L.5
  • 56
    • 0023087430 scopus 로고
    • Effect of heat shock on protein degradation in mammalian cells: Involvement of the ubiquitin system
    • Parag HA, Raboy B, Kulka RG (1987). Effect of heat shock on protein degradation in mammalian cells: involvement of the ubiquitin system. EMBO J 6, 55-61.
    • (1987) EMBO J , vol.6 , pp. 55-61
    • Parag, H.A.1    Raboy, B.2    Kulka, R.G.3
  • 57
    • 1842864011 scopus 로고    scopus 로고
    • Phenotypic characterization of mouse embryonic fibroblasts lacking heat shock factor 2
    • Paslaru L, Morange M, Mezger V (2003). Phenotypic characterization of mouse embryonic fibroblasts lacking heat shock factor 2. J Cell Mol Med 7, 425-435. (Pubitemid 44151693)
    • (2003) Journal of Cellular and Molecular Medicine , vol.7 , Issue.4 , pp. 425-435
    • Paslaru, L.1    Morange, M.2    Mezger, V.3
  • 58
    • 0034069656 scopus 로고    scopus 로고
    • Disruption of heat shock factor 1 reveals an essential role in the ubiquitin proteolytic pathway
    • DOI 10.1128/MCB.20.8.2670-2675.2000
    • Pirkkala L, Alastalo TP, Zuo X, Benjamin IJ, Sistonen L (2000). Disruption of heat shock factor 1 reveals an essential role in the ubiquitin proteolytic pathway. Mol Cell Biol 20, 2670-2675. (Pubitemid 30183485)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.8 , pp. 2670-2675
    • Pirkkala, L.1    Alastalo, T.-P.2    Zuo, X.3    Benjamin, I.J.4    Sistonen, L.5
  • 60
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: Life on the verge of death
    • Richter K, Haslbeck M, Buchner J (2010). The heat shock response: life on the verge of death. Mol Cell 40, 253-266.
    • (2010) Mol Cell , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 61
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • DOI 10.1038/nrm2199, PII NRM2199
    • Ron D, Walter P (2007). Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8, 519-529. (Pubitemid 46985379)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.7 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 62
    • 0034987171 scopus 로고    scopus 로고
    • Heat shock factor 2 is involved in the upregulation of αb-Crystallin by high extracellular potassium
    • Sadamitsu C, Nagano T, Fukumaki Y, Iwaki A (2001). Heat shock factor 2 is involved in the upregulation of αB-crystallin by high extracellular potassium. J Biochem 129, 813-820. (Pubitemid 32499796)
    • (2001) Journal of Biochemistry , vol.129 , Issue.5 , pp. 813-820
    • Sadamitsu, C.1    Nagano, T.2    Fukumaki, Y.3    Iwaki, A.4
  • 65
    • 0027461364 scopus 로고
    • Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress
    • Sarge KD, Murphy SP, Morimoto RI (1993). Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress. Mol Cell Biol 13, 1392-1407. (Pubitemid 23068075)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.3 , pp. 1392-1407
    • Sarge, K.D.1    Murphy, S.P.2    Morimoto, R.I.3
  • 66
    • 0027177579 scopus 로고
    • Hydrophobic coiled-coil domains regulate the subcellular localization of human heat shock factor 2
    • Sheldon LA, Kingston RE (1993). Hydrophobic coiled-coil domains regulate the subcellular localization of human heat shock factor 2. Genes Dev 7, 1549-1558. (Pubitemid 23234348)
    • (1993) Genes and Development , vol.7 , Issue.8 , pp. 1549-1558
    • Sheldon, L.A.1    Kingston, R.E.2
  • 67
    • 0028314945 scopus 로고
    • Human heat shock factors 1 and 2 are differentially activated and can synergistically induce hsp70 gene transcription
    • Sistonen L, Sarge SD, Morimoto RI (1994). Human heat shock factors 1 and 2 are differentially activated and can synergistically induce hsp70 gene transcription. Mol Cell Biol 14, 2087-2099. (Pubitemid 24074606)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.3 , pp. 2087-2099
    • Sistonen, L.1    Sarge, K.D.2    Morimoto, R.I.3
  • 69
    • 0032536772 scopus 로고    scopus 로고
    • Disruption of the HSF3 gene results in the severe reduction of heat shock gene expression and loss of thermotolerance
    • DOI 10.1093/emboj/17.6.1750
    • Tanabe M, Kawazoe Y, Takeda S, Morimoto RI, Nagata K, Nakai A (1998). Disruption of the HSF3 gene results in the severe reduction of heat shock gene expression and loss of thermotolerance. EMBO J 17, 1750-1758. (Pubitemid 28119128)
    • (1998) EMBO Journal , vol.17 , Issue.6 , pp. 1750-1758
    • Tanabe, M.1    Kawazoe, Y.2    Takeda, S.3    Morimoto, R.I.4    Nagata, K.5    Nakai, A.6
  • 70
    • 0038320258 scopus 로고    scopus 로고
    • Targeted disruption of the heat shock transcription factor (hsf)-2 gene results in increased embryonic lethality, neuronal defects, and reduced spermatogenesis
    • DOI 10.1002/gene.10200
    • Wang G, Zhang J, Moskophidis D, Mivechi NF (2003). Targeted disruption of the heat shock transcription factor (hsf)-2 gene results in increased embryonic lethality, neuronal defects, and reduced spermatogenesis. Genesis 36, 48-61. (Pubitemid 36666238)
    • (2003) Genesis , vol.36 , Issue.1 , pp. 48-61
    • Wang, G.1    Zhang, J.2    Moskophidis, D.3    Mivechi, N.F.4
  • 72
    • 0029564954 scopus 로고
    • Heat shock transcription factors: Structure and regulation
    • Wu C (1995). Heat shock transcription factors: structure and regulation. Annu Rev Cell Dev Biol 11, 441-469.
    • (1995) Annu Rev Cell Dev Biol , vol.11 , pp. 441-469
    • Wu, C.1
  • 73
    • 77951257955 scopus 로고    scopus 로고
    • PEST sequences mediate heat shock factor 2 turnover by interacting with the Cul3 subunit of the Cul3-RING ubiquitin ligase
    • Xing H, Hong Y, Sarge KD (2010). PEST sequences mediate heat shock factor 2 turnover by interacting with the Cul3 subunit of the Cul3-RING ubiquitin ligase. Cell Stress Chaperones 15, 301-308.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 301-308
    • Xing, H.1    Hong, Y.2    Sarge, K.D.3
  • 75
    • 0035986356 scopus 로고    scopus 로고
    • Targeted disruption of hsf1 leads to lack of thermotolerance and defines tissue-specific regulation for stress-inducible hsp molecular chaperones
    • DOI 10.1002/jcb.10232
    • Zhang Y, Huang L, Zhang J, Moskophidis D, Mivechi NF (2002). Targeted disruption of hsf1 leads to lack of thermotolerance and defines tissue-specific regulation for stress-inducible Hsp molecular chaperones. J Cell Biochem 86, 376-393. (Pubitemid 34743394)
    • (2002) Journal of Cellular Biochemistry , vol.86 , Issue.2 , pp. 376-393
    • Zhang, Y.1    Huang, L.2    Zhang, J.3    Moskophidis, D.4    Mivechi, N.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.