메뉴 건너뛰기




Volumn 80, Issue , 2011, Pages 1089-1115

Regulation of HSF1 function in the heat stress response: Implications in aging and disease

Author keywords

heat shock factor; longevity; posttranslational modification; proteostasis; transcription

Indexed keywords

CHAPERONE; DNA BINDING PROTEIN; HEAT SHOCK TRANSCRIPTION FACTOR 1; INSULIN;

EID: 79959463520     PISSN: 00664154     EISSN: 00664154     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-060809-095203     Document Type: Review
Times cited : (604)

References (173)
  • 1
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock andDNPin Drosophila
    • Ritossa F. 1962. A new puffing pattern induced by temperature shock andDNPin Drosophila. Experientia 18:571-573.
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.1
  • 2
    • 0030154255 scopus 로고    scopus 로고
    • Discovery of the heat shock response
    • Ritossa F. 1996. Discovery of the heat shock response. Cell Stress Chaperones 1:97-98.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 97-98
    • Ritossa, F.1
  • 4
    • 0016373748 scopus 로고
    • Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs
    • Tissìeres A, Mitchell HK, Tracy UM. 1974. Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs. J. Mol. Biol. 84:389-398.
    • (1974) J. Mol. Biol. , vol.84 , pp. 389-398
    • Tissìeres, A.1    Mitchell, H.K.2    Tracy, U.M.3
  • 5
    • 0002459499 scopus 로고
    • Parallel changes in puffing activity and patterns of protein synthesis in salivary glands of Drosophila
    • Lewis M, Helmsing PJ, AshburnerM. 1975. Parallel changes in puffing activity and patterns of protein synthesis in salivary glands of Drosophila. Proc. Natl. Acad. Sci. USA 72:3604-8.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 3604-3608
    • Lewis, M.1    Helmsing, P.J.2    Ashburner, M.3
  • 6
    • 0017595202 scopus 로고
    • Messenger RNA in heat shocked Drosophila cells
    • DOI 10.1016/S0022-2836(77)80091-0
    • Spradling A, Pardue ML, Penman S. 1977. Messenger RNA in heat shocked Drosophila cells. J. Mol. Biol. 109:559-587. (Pubitemid 8032350)
    • (1977) Journal of Molecular Biology , vol.109 , Issue.4 , pp. 559-587
    • Spradling, A.1    Pardue, M.L.2    Penman, S.3
  • 7
    • 0033229880 scopus 로고    scopus 로고
    • HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice
    • DOI 10.1093/emboj/18.21.5943
    • Xiao X, Zuo X, Davis AA, McMillanDR, Curry BB, et al. 1999.HSF1is required for extra-embryonic development, postnatal growth and protection during inflammatory responses inmice. EMBO J. 18:5943-52. (Pubitemid 29515671)
    • (1999) EMBO Journal , vol.18 , Issue.21 , pp. 5943-5952
    • Xiao, X.1    Zuo, X.2    Davis, A.A.3    McMillan, D.R.4    Curry, B.B.5    Richardson, J.A.6    Benjamin, I.J.7
  • 8
    • 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. 273:7523-528. (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
  • 9
    • 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
    • Östling P, Björk JK, Roos-Mattjus P, Mezger V, SistonenL. 2007.Heat shock factor 2HSF2 contributes to inducible expression of hsp genes through interplay with HSF1. J. Biol. Chem. 282:7077-086. (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
  • 11
    • 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
  • 12
    • 18544383003 scopus 로고    scopus 로고
    • Mutant DNA-binding domain of HSF4 is associated with autosomal dominant lamellar and Marner cataract
    • Bu L, Jin Y, Shi Y, Chu R, Ban A, et al. 2002. Mutant DNA-binding domain of HSF4 is associated with autosomal dominant lamellar and Marner cataract. Nat. Genet. 31:276-278.
    • (2002) Nat. Genet. , vol.31 , pp. 276-278
    • Bu, L.1    Jin, Y.2    Shi, Y.3    Chu, R.4    Ban, A.5
  • 14
    • 75649144450 scopus 로고    scopus 로고
    • A novel mouse HSF3 has the potential to activate nonclassical heat-shock genes during heat shock
    • Fujimoto M, Hayashida N, Katoh T, Oshima K, Shinkawa T, et al. 2010. A novel mouse HSF3 has the potential to activate nonclassical heat-shock genes during heat shock. Mol. Biol. Cell 21:106-116.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 106-116
    • Fujimoto, M.1    Hayashida, N.2    Katoh, T.3    Oshima, K.4    Shinkawa, T.5
  • 15
    • 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. (Pubitemid 26019611)
    • (1995) Annual Review of Cell and Developmental Biology , vol.11 , pp. 441-469
    • Wu, C.1
  • 16
    • 84934443868 scopus 로고    scopus 로고
    • Heat shock factor 1 as a coordinator of stress and developmental pathways
    • Anckar J, Sistonen L. 2007. Heat shock factor 1 as a coordinator of stress and developmental pathways. Adv. Exp. Med. Biol. 594:78-88.
    • (2007) Adv. Exp. Med. Biol. , vol.594 , pp. 78-88
    • Anckar, J.1    Sistonen, L.2
  • 17
    • 0032842485 scopus 로고    scopus 로고
    • Human heat shock factor 1 is predominantly a nuclear protein before and after heat stress
    • Mercier PA, Winegarden NA, Westwood JT. 1999. Human heat shock factor 1 is predominantly a nuclear protein before and after heat stress. J. Cell Sci. 112:2765-774. (Pubitemid 29429798)
    • (1999) Journal of Cell Science , vol.112 , Issue.16 , pp. 2765-2774
    • Mercier, P.A.1    Winegarden, N.A.2    Westwood, J.T.3
  • 18
    • 14544290988 scopus 로고    scopus 로고
    • Constitutive nuclear import and stress-regulated nucleocytoplasmic shuttling of mammalian heat-shock factor 1
    • DOI 10.1111/j.1600-0854.2005.00266.x
    • Vujanac M, Fenaroli A, Zimarino V. 2005. Constitutive nuclear import and stress-regulated nucleocytoplasmic shuttling of mammalian heat-shock factor 1. Traffic 6:214-229. (Pubitemid 40298156)
    • (2005) Traffic , vol.6 , Issue.3 , pp. 214-229
    • Vujanac, M.1    Fenaroli, A.2    Zimarino, V.3
  • 19
    • 2942529192 scopus 로고    scopus 로고
    • Nuclear stress bodies: A heterochromatin affair?
    • DOI 10.1038/nrm1405
    • Biamonti G. 2004. Nuclear stress bodies: a heterochromatin affair? Nat. Rev. Mol. Cell Biol. 5:493-498. (Pubitemid 38745500)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.6 , pp. 493-498
    • Biamonti, G.1
  • 20
    • 0028500990 scopus 로고
    • Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor
    • VuisterGW, Kim SJ, Orosz A, Marquardt J, Wu C, Bax A. 1994. Solution structure of the DNA-binding domain of Drosophila heat shock transcription factor. Nat. Struct. Biol. 1:605-614.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 605-614
    • Vuister, G.W.1    Kim, S.J.2    Orosz, A.3    Marquardt, J.4    Wu, C.5    Bax, A.6
  • 21
    • 0032936785 scopus 로고    scopus 로고
    • A new use for the 'wing' of the 'winged' helix-turn-helix motif in the HSF-DNA cocrystal
    • DOI 10.1038/8269
    • Littlefield O, Nelson HCM. 1999. A new use for the 'wing' of the 'winged' helix-turn-helix motif in the HSF-DNA cocrystal. Nat. Struct. Biol. 6:464-470. (Pubitemid 29218017)
    • (1999) Nature Structural Biology , vol.6 , Issue.5 , pp. 464-470
    • Littlefield, O.1    Nelson, H.C.M.2
  • 22
    • 0035870560 scopus 로고    scopus 로고
    • The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity
    • Cicero MP, Hubl ST, Harrison CJ, Littlefield O, Hardy JA, Nelson HCM. 2001. The wing in yeast heat shock transcription factor HSF DNA-binding domain is required for full activity. Nucleic Acids Res. 29:1715-723. (Pubitemid 32427852)
    • (2001) Nucleic Acids Research , vol.29 , Issue.8 , pp. 1715-1723
    • Cicero, M.P.1    Hubl, S.T.2    Harrison, C.J.3    Littlefield, O.4    Hardy, J.A.5    Nelson, H.C.M.6
  • 23
    • 63149154055 scopus 로고    scopus 로고
    • Heterotrimerization of heatshock factors 1 and 2 provides a transcriptional switch in response to distinct stimuli
    • Sandqvist A, Björk JK, a kerfelt M, Chitikova Z, Grichine A, et al. 2009. Heterotrimerization of heatshock factors 1 and 2 provides a transcriptional switch in response to distinct stimuli. Mol. Biol. Cell 20:1340-347.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1340-1347
    • Sandqvist, A.1    Björk, J.K.2    Åkerfelt, M.3    Chitikova, Z.4    Grichine, A.5
  • 24
    • 0023694311 scopus 로고
    • Key features of heat shock regulatory elements
    • Amin J, Ananthan J, Voellmy R. 1988. Key features of heat shock regulatory elements. Mol. Cell. Biol. 8:3761-769.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3761-3769
    • Amin, J.1    Ananthan, J.2    Voellmy, R.3
  • 25
    • 0023863121 scopus 로고
    • Germline transformation used to define key features of heat-shock response elements
    • Xiao H, Lis JT. 1988. Germline transformation used to define key features of heat-shock response elements. Science 239:1139-142. (Pubitemid 18084322)
    • (1988) Science , vol.239 , Issue.4844 , pp. 1139-1142
    • Xiao, H.1    Lis, J.T.2
  • 26
    • 0028366006 scopus 로고
    • Interaction of the DNA-binding domain of Drosophila heat shock factor with its cognate DNA site: A thermodynamic analysis using analytical ultracentrifugation
    • Kim SJ, Tsukiyama T, Lewis MS, Wu C. 1994. Interaction of the DNA-binding domain of Drosophila heat shock factor with its cognate DNA site: a thermodynamic analysis using analytical ultracentrifugation. Protein Sci. 3:1040-051. (Pubitemid 24209896)
    • (1994) Protein Science , vol.3 , Issue.7 , pp. 1040-1051
    • Kim, S.-J.1    Tsukiyama, T.2    Lewis, M.S.3    Wu, C.4
  • 27
    • 0025965278 scopus 로고
    • Cooperative binding of drosophila heat shock factor to arrays of a conserved 5 bp unit
    • Xiao H, Perisic O, Lis JT. 1991. Cooperative binding of Drosophila heat shock factor to arrays of a conserved 5 bp unit. Cell 64:585-593. (Pubitemid 121002974)
    • (1991) Cell , vol.64 , Issue.3 , pp. 585-593
    • Xiao, H.1    Perisic, O.2    Lis, J.T.3
  • 28
    • 0027960541 scopus 로고
    • Selection of new HSF1 and HSF2 DNA-binding sites reveals differences in trimer cooperativity
    • Kroeger PE, Morimoto RI. 1994. Selection of new HSF1 and HSF2 DNA-binding sites reveals differences in trimer cooperativity. Mol. Cell. Biol. 14:7592-603. (Pubitemid 24326425)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.11 , pp. 7592-7603
    • Kroeger, P.E.1    Morimoto, R.I.2
  • 29
    • 1542373742 scopus 로고    scopus 로고
    • The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response
    • DOI 10.1091/mbc.E03-10-0738
    • Trinklein ND, Murray JI, Hartman SJ, Botstein D, Myers RM. 2004. The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response. Mol. Biol. Cell 15:1254-261. (Pubitemid 38316232)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.3 , pp. 1254-1261
    • Trinklein, N.D.1    Murray, J.I.2    Hartman, S.J.3    Botstein, D.4    Myers, R.M.5
  • 30
    • 0026621935 scopus 로고
    • Trimerization of the heat shock transcription factor by a triple-stranded α-helical coiled-coil
    • DOI 10.1021/bi00163a042
    • Peteranderl R, Nelson HCM. 1992. Trimerization of the heat shock transcription factor by a triplestranded alpha-helical coiled-coil. Biochemistry 31:12272-276. (Pubitemid 23011377)
    • (1992) Biochemistry , vol.31 , Issue.48 , pp. 12272-12276
    • Peteranderl, R.1    Nelson, H.C.M.2
  • 31
    • 0033596861 scopus 로고    scopus 로고
    • Biochemical and biophysical characterization of the trimerization domain from the heat shock transcription factor
    • Peteranderl R, Rabenstein M, Shin YK, LiuCW, WemmerDE, et al. 1999. Biochemical and biophysical characterization of the trimerization domain from the heat shock transcription factor. Biochemistry 38:3559-569.
    • (1999) Biochemistry , vol.38 , pp. 3559-3569
    • Peteranderl, R.1    Rabenstein, M.2    Shin, Y.K.3    Liu, C.W.4    Wemmer, D.E.5
  • 32
    • 0027452754 scopus 로고
    • Regulation of heat shock factor trimer formation: Role of a conserved leucine zipper
    • Rabindran SK, Haroun RI, Clos J, Wisniewski J, Wu C. 1993. Regulation of heat shock factor trimer formation: role of a conserved leucine zipper. Science 259:230-234. (Pubitemid 23041800)
    • (1993) Science , vol.259 , Issue.5092 , pp. 230-234
    • Rabindran, S.K.1    Haroun, R.I.2    Clos, J.3    Wisniewski, J.4    Wu, C.5
  • 33
    • 0027491654 scopus 로고
    • Identification of the C-terminal activator domain in yeast heat shock factor: Independent control of transient and sustained transcriptional activity
    • Chen Y, Barlev NA, Westergaard O, Jakobsen BK. 1993. Identification of the C-terminal activator domain in yeast heat shock factor: independent control of transient and sustained transcriptional activity. EMBO J. 12:5007-018. (Pubitemid 23358489)
    • (1993) EMBO Journal , vol.12 , Issue.13 , pp. 5007-5018
    • Chen, Y.1    Bariev, N.A.2    Westergaard, O.3    Jakobsen, B.K.4
  • 34
    • 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
  • 35
    • 0033546171 scopus 로고    scopus 로고
    • Modulation of human heat shock factor trimerization by the linker domain
    • Liu PC, Thiele DJ. 1999. Modulation of human heat shock factor trimerization by the linker domain. J. Biol. Chem. 274:17219-225.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17219-17225
    • Liu, P.C.1    Thiele, D.J.2
  • 36
    • 33947408308 scopus 로고    scopus 로고
    • The carboxy-terminal domain of heat-shock factor 1 is largely unfolded but can be induced to collapse into a compact, partially structured state
    • DOI 10.1021/bi061124c
    • Pattaramanon N, Sangha N, Gafni A. 2007. The carboxy-terminal domain of heat-shock factor 1 is largely unfolded but can be induced to collapse into a compact, partially structured state. Biochemistry 46:3405-415. (Pubitemid 46449159)
    • (2007) Biochemistry , vol.46 , Issue.11 , pp. 3405-3415
    • Pattaramanon, N.1    Sangha, N.2    Gafni, A.3
  • 37
    • 0030049318 scopus 로고    scopus 로고
    • The regulatory domain of human heat shock factor 1 is sufficient to sense heat stress
    • Newton EM, Knauf U, Green M, Kingston RE. 1996. The regulatory domain of human heat shock factor 1 is sufficient to sense heat stress. Mol. Cell. Biol. 16:839-846. (Pubitemid 26061653)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.3 , pp. 839-846
    • Newton, E.M.1    Knauf, U.2    Green, M.3    Kingston, R.E.4
  • 38
    • 0034716850 scopus 로고    scopus 로고
    • Divergent hTAF(II)31-binding motifs hidden in activation domains
    • DOI 10.1074/jbc.275.21.15912
    • Choi Y, Asada S, Uesugi M. 2000. Divergent hTAFII31-binding motifs hidden in activation domains. J. Biol. Chem. 275:15912-916. (Pubitemid 30366893)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.21 , pp. 15912-15916
    • Choi, Y.1    Asada, S.2    Uesugi, M.3
  • 39
    • 0032101064 scopus 로고    scopus 로고
    • Transcriptional activation domains stimulate initiation and elongation at different times and via different residues
    • DOI 10.1093/emboj/17.11.3146
    • Brown SA, Weirich CS, Newton EM, Kingston RE. 1998. Transcriptional activation domains stimulate initiation and elongation at different times and via different residues. EMBO J. 17:3146-154. (Pubitemid 28254386)
    • (1998) EMBO Journal , vol.17 , Issue.11 , pp. 3146-3154
    • Brown, S.A.1    Weirich, C.S.2    Newton, E.M.3    Kingston, R.E.4
  • 40
    • 0034897667 scopus 로고    scopus 로고
    • Transcriptional activation domains of human heat shock factor 1 recruit human SWI/SNF
    • DOI 10.1128/MCB.21.17.5826-5837.2001
    • Sullivan EK, Weirich CS, Guyon JR, Sif S, Kingston RE. 2001. Transcriptional activation domains of human heat shock factor 1 recruit human SWI/SNF. Mol. Cell. Biol. 21:5826-837. (Pubitemid 32737800)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.17 , pp. 5826-5837
    • Sullivan, E.K.1    Weirich, C.S.2    Guyon, J.R.3    Sif, S.4    Kingston, R.E.5
  • 41
    • 0038623298 scopus 로고    scopus 로고
    • Localized recruitment of a chromatin-remodeling activity by an activator in vivo drives transcriptional elongation
    • Corey LL, Weirich CS, Benjamin IJ, Kingston RE. 2003. Localized recruitment of a chromatinremodeling activity by an activator in vivo drives transcriptional elongation. Genes Dev. 17:1392-401. (Pubitemid 36666008)
    • (2003) Genes and Development , vol.17 , Issue.11 , pp. 1392-1401
    • Corey, L.L.1    Weirich, C.S.2    Benjamin, I.J.3    Kingston, R.E.4
  • 42
    • 0029039963 scopus 로고
    • A heat shock-responsive domain of human HSF1 that regulates transcription activation domain function
    • Green M, Schuetz TJ, Sullivan EK, Kingston RE. 1995. A heat shock-responsive domain of human HSF1 that regulates transcription activation domain function. Mol. Cell. Biol. 15:3354-362.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3354-3362
    • Green, M.1    Schuetz, T.J.2    Sullivan, E.K.3    Kingston, R.E.4
  • 43
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto RI. 1998. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev. 12:3788-796. (Pubitemid 29024840)
    • (1998) Genes and Development , vol.12 , Issue.24 , pp. 3788-3796
    • Morimoto, R.I.1
  • 44
    • 0022455603 scopus 로고
    • Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes
    • Ananthan J, Goldberg AL, Voellmy R. 1986. Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes. Science 232:522-524. (Pubitemid 16052371)
    • (1986) Science , vol.232 , Issue.4749 , pp. 522-524
    • Ananthan, J.1    Goldberg, A.L.2    Voellmy, R.3
  • 45
    • 0020409205 scopus 로고
    • The heat shock response is self-regulated at both the transcriptional and posttranscriptional levels
    • DiDomenico BJ, Bugaisky GE, Lindquist S. 1982. The heat shock response is self-regulated at both the transcriptional and posttranscriptional levels. Cell 31:593-603. (Pubitemid 13223944)
    • (1982) Cell , vol.31 , Issue.3 , pp. 593-603
    • DiDomenico, B.J.1    Bugaisky, G.E.2    Lindquist, S.3
  • 46
    • 0027475243 scopus 로고
    • Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases
    • Nadeau K, Das A, Walsh CT. 1993. Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases. J. Biol. Chem. 268:1479-487. (Pubitemid 23019801)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.2 , pp. 1479-1487
    • Nadeau, K.1    Das, A.2    Walsh, C.T.3
  • 47
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R. 1998. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94:471-480. (Pubitemid 28391863)
    • (1998) Cell , vol.94 , Issue.4 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 48
    • 0035824621 scopus 로고    scopus 로고
    • Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex
    • Guo Y, Guettouche T, Fenna M, Boellmann F, Pratt WB, et al. 2001. Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. J. Biol. Chem. 276:45791-799.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45791-45799
    • Guo, Y.1    Guettouche, T.2    Fenna, M.3    Boellmann, F.4    Pratt, W.B.5
  • 50
    • 0031866191 scopus 로고    scopus 로고
    • HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes
    • Ali A, Bharadwaj S, O'Carroll R, Ovsenek N. 1998. HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes. Mol. Cell. Biol. 18:4949-960. (Pubitemid 28388077)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.9 , pp. 4949-4960
    • Ali, A.1    Bharadwaj, S.2    O'Carroll, R.3    Ovsenek, N.4
  • 51
    • 0033499798 scopus 로고    scopus 로고
    • Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 in vivo
    • Bharadwaj S, Ali A, OvsenekN. 1999. Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 in vivo. Mol. Cell. Biol. 19:8033-041. (Pubitemid 30413998)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.12 , pp. 8033-8041
    • Bharadwaj, S.1    Ali, A.2    Ovsenek, N.3
  • 52
    • 0037047429 scopus 로고    scopus 로고
    • Dynamic remodeling of transcription complexes by molecular chaperones
    • Morimoto RI. 2002. Dynamic remodeling of transcription complexes by molecular chaperones. Cell 110:281-284.
    • (2002) Cell , vol.110 , pp. 281-284
    • Morimoto, R.I.1
  • 53
    • 3542991477 scopus 로고    scopus 로고
    • On mechanisms that control heat shock transcription factor activity in metazoan cells
    • DOI 10.1379/CSC-14R.1
    • Voellmy R. 2004. On mechanisms that control heat shock transcription factor activity inmetazoan cells. Cell Stress Chaperones 9:122-133. (Pubitemid 39013809)
    • (2004) Cell Stress and Chaperones , vol.9 , Issue.2 , pp. 122-133
    • Voellmy, R.1
  • 54
    • 0026665975 scopus 로고
    • The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression
    • Abravaya K, Myers MP, Murphy SP, MorimotoRI. 1992. The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev. 6:1153-164.
    • (1992) Genes Dev. , vol.6 , pp. 1153-1164
    • Abravaya, K.1    Myers, M.P.2    Murphy, S.P.3    Morimoto, R.I.4
  • 55
    • 0026750001 scopus 로고
    • Heat shock gene regulation by nascent polypeptides and denatured proteins: Hsp70 as a potential autoregulatory factor
    • Baler R, Welch WJ, Voellmy R. 1992. Heat shock gene regulation by nascent polypeptides and denatured proteins: hsp70 as a potential autoregulatory factor. J. Cell Biol. 117:1151-159.
    • (1992) J. Cell Biol. , vol.117 , pp. 1151-1159
    • Baler, R.1    Welch, W.J.2    Voellmy, R.3
  • 56
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-specific transcriptional repressors
    • Shi Y, Mosser DD, Morimoto RI. 1998. Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev. 12:654-666. (Pubitemid 28134298)
    • (1998) Genes and Development , vol.12 , Issue.5 , pp. 654-666
    • Shi, Y.1    Mosser, D.D.2    Morimoto, R.I.3
  • 57
    • 0028025643 scopus 로고
    • Interaction between heat shock factor and hsp70 is insufficient to suppress induction of DNA-binding activity in vivo
    • Rabindran SK, Wisniewski J, Li L, Li GC, Wu C. 1994. Interaction between heat shock factor and hsp70 is insufficient to suppress induction of DNA-binding activity in vivo. Mol. Cell. Biol. 14:6552-560. (Pubitemid 24299724)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.10 , pp. 6552-6560
    • Rabindran, S.K.1    Wisniewski, J.2    Li, L.3    Li, G.C.4    Wu, C.5
  • 59
    • 0025024265 scopus 로고
    • Discordant expression of heat shock protein mRNAs in tissues of heat-stressed rats
    • Blake MJ, Gershon D, Fargnoli J, Holbrook NJ. 1990. Discordant expression of heat shock protein mRNAs in tissues of heat-stressed rats. J. Biol. Chem. 265:15275-279.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15275-15279
    • Blake, M.J.1    Gershon, D.2    Fargnoli, J.3    Holbrook, N.J.4
  • 62
    • 0142123203 scopus 로고    scopus 로고
    • Transcription Factor and Polymerase Recruitment, Modification, and Movement on dhsp70 In Vivo in the Minutes following Heat Shock
    • DOI 10.1128/MCB.23.21.7628-7637.2003
    • Boehm AK, Saunders A, Werner J, Lis JT. 2003. Transcription factor and polymerase recruitment, modification, and movement on dhsp70 in vivo in the minutes following heat shock. Mol. Cell. Biol. 23:7628-637. (Pubitemid 37271461)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.21 , pp. 7628-7637
    • Boehm, A.K.1    Saunders, A.2    Werner, J.3    Lis, J.T.4
  • 64
    • 33646466965 scopus 로고    scopus 로고
    • Beating the heat: A translation factor and an RNA mobilize the heat shock transcription factor HSF1
    • Kugel JF, Goodrich JA. 2006. Beating the heat: A translation factor and an RNA mobilize the heat shock transcription factor HSF1. Mol. Cell 22:153-154.
    • (2006) Mol. Cell , vol.22 , pp. 153-154
    • Kugel, J.F.1    Goodrich, J.A.2
  • 66
    • 0025935407 scopus 로고
    • Attenuation of the heat shock response in HeLa cells is mediated by the release of bound heat shock transcription factor and is modulated by changes in growth and in heat shock temperatures
    • Abravaya K, Phillips B, Morimoto RI. 1991. Attenuation of the heat shock response in HeLa cells is mediated by the release of bound heat shock transcription factor and ismodulated by changes in growth and in heat shock temperatures. Genes Dev. 5:2117-127. (Pubitemid 21905903)
    • (1991) Genes and Development , vol.5 , Issue.11 , pp. 2117-2127
    • Abravaya, K.1    Phillips, B.2    Morimoto, R.I.3
  • 67
    • 0027220057 scopus 로고
    • Induction temperature of human heat shock factor is reprogrammed in a Drosophila cell environment
    • DOI 10.1038/364252a0
    • Clos J, Rabindran S, Wisniewski J, Wu C. 1993. Induction temperature of human heat shock factor is reprogrammed in a Drosophila cell environment. Nature 364:252-255. (Pubitemid 23257086)
    • (1993) Nature , vol.364 , Issue.6434 , pp. 252-255
    • Clos, J.1    Rabindran, S.2    Wisniewski, J.3    Wu, C.4
  • 68
    • 0029154777 scopus 로고
    • Male germ cell-specific alteration in temperature set point of the cellular stress response
    • Sarge KD. 1995. Male germ cell-specific alteration in temperature set point of the cellular stress response. J. Biol. Chem. 270:18745-748.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18745-18748
    • Sarge, K.D.1
  • 69
  • 70
    • 0025300038 scopus 로고
    • In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation
    • Mosser DD, Kotzbauer PT, Sarge KD, Morimoto RI. 1990. In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation. Proc. Natl. Acad. Sci. USA 87:3748-752.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3748-3752
    • Mosser, D.D.1    Kotzbauer, P.T.2    Sarge, K.D.3    Morimoto, R.I.4
  • 71
    • 0028896839 scopus 로고
    • Heat-inducibleDNAbinding of purified heat shock transcription factor
    • Goodson ML, Sarge KD. 1995. Heat-inducibleDNAbinding of purified heat shock transcription factor. J. Biol. Chem. 270:2447-450.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2447-2450
    • Goodson, M.L.1    Sarge, K.D.2
  • 73
    • 0032112367 scopus 로고    scopus 로고
    • Direct sensing of heat and oxidation by Drosophila heat shock transcription factor
    • Zhong M, Orosz A, Wu C. 1998. Direct sensing of heat and oxidation by Drosophila heat shock transcription factor. Mol. Cell 2:101-8. (Pubitemid 128378971)
    • (1998) Molecular Cell , vol.2 , Issue.1 , pp. 101-108
    • Zhong, M.1    Orosz, A.2    Wu, C.3
  • 74
    • 0037442768 scopus 로고    scopus 로고
    • Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress
    • DOI 10.1101/gad.1044503
    • Ahn SG, Thiele DJ. 2003. Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress. Genes Dev. 17:516-528. (Pubitemid 36258765)
    • (2003) Genes and Development , vol.17 , Issue.4 , pp. 516-528
    • Ahn, S.-G.1    Thiele, D.J.2
  • 75
    • 66149138815 scopus 로고    scopus 로고
    • Aromatic-participant interactions are essential for disulfide-bond-based trimerization in human heat shock transcription factor 1
    • Lu M, Lee YJ, Park SM, KangHS, Kang SW, et al. 2009. Aromatic-participant interactions are essential for disulfide-bond-based trimerization in human heat shock transcription factor 1. Biochemistry 48:3795-97.
    • (2009) Biochemistry , vol.48 , pp. 3795-3797
    • Lu, M.1    Lee, Y.J.2    Park, S.M.3    Kang, H.S.4    Kang, S.W.5
  • 76
    • 44049095652 scopus 로고    scopus 로고
    • Regulation of the cellular heat shock response in Caenorhabditis elegans by thermosensory neurons
    • DOI 10.1126/science.1156093
    • Prahlad V, Cornelius T, Morimoto RI. 2008. Regulation of the cellular heat shock response in Caenorhabditis elegans by thermosensory neurons. Science 320:811-814. (Pubitemid 351929633)
    • (2008) Science , vol.320 , Issue.5877 , pp. 811-814
    • Prahlad, V.1    Cornelius, T.2    Morimoto, R.I.3
  • 77
    • 34250020179 scopus 로고    scopus 로고
    • Temporal activity patterns in thermosensory neurons of freely moving Caenorhabditis elegans encode spatial thermal gradients
    • DOI 10.1523/JNEUROSCI.1032-07.2007
    • Clark DA, Gabel CV, Gabel H, Samuel AD. 2007. Temporal activity patterns in thermosensory neurons of freely moving Caenorhabditis elegans encode spatial thermal gradients. J. Neurosci. 27:6083-090. (Pubitemid 46890022)
    • (2007) Journal of Neuroscience , vol.27 , Issue.23 , pp. 6083-6090
    • Clark, D.A.1    Gabel, C.V.2    Gabel, H.3    Samuel, A.D.T.4
  • 78
    • 0027113344 scopus 로고
    • Effect of sodium salicylate on the human heat shock response
    • Jurivich DA, Sistonen L, Kroes RA, Morimoto RI. 1992. Effect of sodium salicylate on the human heat shock response. Science 255:1243-245.
    • (1992) Science , vol.255 , pp. 1243-1245
    • Jurivich, D.A.1    Sistonen, L.2    Kroes, R.A.3    Morimoto, R.I.4
  • 79
    • 0028846894 scopus 로고
    • Salicylate triggers heat shock factor differently than heat
    • Jurivich DA, Pachetti C, Qiu L, Welk JF. 1995. Salicylate triggers heat shock factor differently than heat. J. Biol. Chem. 270:24489-495.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24489-24495
    • Jurivich, D.A.1    Pachetti, C.2    Qiu, L.3    Welk, J.F.4
  • 80
    • 0030043401 scopus 로고    scopus 로고
    • Activation of heat shock factor 1 DNA binding precedes stress-induced serine phosphorylation. Evidence for a multistep pathway of regulation
    • Cotto JJ, Kline M, Morimoto RI. 1996. Activation of heat shock factor 1 DNA binding precedes stress-induced serine phosphorylation. Evidence for a multistep pathway of regulation. J. Biol. Chem. 271:3355-358.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3355-3358
    • Cotto, J.J.1    Kline, M.2    Morimoto, R.I.3
  • 81
    • 46149108345 scopus 로고    scopus 로고
    • Rapid, Transcription-Independent Loss of Nucleosomes over a Large Chromatin Domain at Hsp70 Loci
    • DOI 10.1016/j.cell.2008.05.029, PII S0092867408006892
    • Petesch SJ, Lis JT. 2008. Rapid, transcription-independent loss of nucleosomes over a large chromatin domain at Hsp70 loci. Cell 134:74-84. (Pubitemid 351905736)
    • (2008) Cell , vol.134 , Issue.1 , pp. 74-84
    • Petesch, S.J.1    Lis, J.T.2
  • 82
    • 0030988941 scopus 로고    scopus 로고
    • Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation
    • Kline MP, Morimoto RI. 1997. Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation. Mol. Cell. Biol. 17:2107-115. (Pubitemid 27133296)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.4 , pp. 2107-2115
    • Kline, M.P.1    Morimoto, R.I.2
  • 83
    • 18244384703 scopus 로고    scopus 로고
    • Analysis of phosphorylation of human heat shock factor 1 in cells experiencing a stress
    • Guettouche T, Boellmann F, Lane WS, Voellmy R. 2005. Analysis of phosphorylation of human heat shock factor 1 in cells experiencing a stress. BMC Biochem. 6:4.
    • (2005) BMC Biochem. , vol.6 , pp. 4
    • Guettouche, T.1    Boellmann, F.2    Lane, W.S.3    Voellmy, R.4
  • 85
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • DOI 10.1016/j.cell.2006.09.026, PII S0092867406012748
    • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, et al. 2006. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127:635-648. (Pubitemid 44647421)
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 86
    • 54749092118 scopus 로고    scopus 로고
    • HSF1 as a mitotic regulator: Phosphorylation of HSF1 by Plk1 is essential for mitotic progression
    • Lee YJ, Kim EH, Lee JS, Jeoung D, Bae S, et al. 2008. HSF1 as a mitotic regulator: Phosphorylation of HSF1 by Plk1 is essential for mitotic progression. Cancer Res. 68:7550-560.
    • (2008) Cancer Res. , vol.68 , pp. 7550-7560
    • Lee, Y.J.1    Kim, E.H.2    Lee, J.S.3    Jeoung, D.4    Bae, S.5
  • 87
    • 70350462371 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions
    • Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, et al. 2009. Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci. Signal. 2:ra46.
    • (2009) Sci. Signal. , vol.2
    • Mayya, V.1    Lundgren, D.H.2    Hwang, S.I.3    Rezaul, K.4    Wu, L.5
  • 88
    • 77951644400 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis
    • Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, et al. 2010. Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci. Signal. 3:ra3.
    • (2010) Sci. Signal. , vol.3
    • Olsen, J.V.1    Vermeulen, M.2    Santamaria, A.3    Kumar, C.4    Miller, M.L.5
  • 91
    • 0029804194 scopus 로고    scopus 로고
    • Repression of human heat shock factor 1 activity at control temperature by phosphorylation
    • Knauf U, Newton EM, Kyriakis J, Kingston RE. 1996. Repression of human heat shock factor 1 activity at control temperature by phosphorylation. Genes Dev. 10:2782-793. (Pubitemid 26384497)
    • (1996) Genes and Development , vol.10 , Issue.21 , pp. 2782-2793
    • Knauf, U.1    Newton, E.M.2    Kyriakis, J.3    Kingston, R.E.4
  • 92
    • 0041468990 scopus 로고    scopus 로고
    • Regulation of molecular chaperone gene transcription involves the serine phosphorylation, 14-3-3ε binding, and cytoplasmic sequestration of heat shock factor 1
    • DOI 10.1128/MCB.23.17.6013-6026.2003
    • Wang X, Grammatikakis N, Siganou A, Calderwood SK. 2003. Regulation ofmolecular chaperone gene transcription involves the serine phosphorylation, 14-3-3 epsilon binding, and cytoplasmic sequestration of heat shock factor 1. Mol. Cell. Biol. 23:6013-026. (Pubitemid 37013082)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.17 , pp. 6013-6026
    • Wang, X.Z.1    Grammatikakis, N.2    Siganou, A.3    Calderwood, S.K.4
  • 93
    • 10344252829 scopus 로고    scopus 로고
    • Interactions between extracellular signal-regulated protein kinase 1, 14-3-3ε, and heat shock factor 1 during stress
    • DOI 10.1074/jbc.M406059200
    • Wang X, Grammatikakis N, Siganou A, Stevenson MA, Calderwood SK. 2004. Interactions between extracellular signal-regulated protein kinase 1, 14-3-3epsilon, and heat shock factor 1 during stress. J. Biol. Chem. 279:49460-469. (Pubitemid 39625833)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.47 , pp. 49460-49469
    • Wang, X.1    Grammatikakis, N.2    Siganou, A.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 99
    • 0024282827 scopus 로고
    • The RNA polymerase II molecule at the 5′ end of the uninduced hsp70 gene of D. melanogaster is transcriptionally engaged
    • Rougvie AE, Lis JT. 1988. The RNA polymerase II molecule at the 5′ end of the uninduced hsp70 gene of D. melanogaster is transcriptionally engaged. Cell 54:795-804.
    • (1988) Cell , vol.54 , pp. 795-804
    • Rougvie, A.E.1    Lis, J.T.2
  • 100
    • 41349094797 scopus 로고    scopus 로고
    • Transcription regulation through promoter-proximal pausing of RNA polymerase II
    • DOI 10.1126/science.1150843
    • Core LJ, Lis JT. 2008. Transcription regulation through promoter-proximal pausing of RNA polymerase II. Science 319:1791-792. (Pubitemid 351451556)
    • (2008) Science , vol.319 , Issue.5871 , pp. 1791-1792
    • Core, L.J.1    Lis, J.T.2
  • 101
    • 0033515521 scopus 로고    scopus 로고
    • NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation
    • Yamaguchi Y, Takagi T, Wada T, Yano K, Furuya A, et al. 1999. NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation. Cell 97:41-51. (Pubitemid 29165888)
    • (1999) Cell , vol.97 , Issue.1 , pp. 41-51
    • Yamaguchi, Y.1    Takagi, T.2    Wada, T.3    Yano, K.4    Furuya, A.5    Sugimoto, S.6    Hasegawa, J.7    Handa, H.8
  • 102
    • 0034667949 scopus 로고    scopus 로고
    • High-resolution localization of Drosophila Spt5 and Spt6 at heat shock genes in vivo: Roles in promoter proximal pausing and transcription elongation
    • Andrulis ED, Guzḿan E, D̈oring P, Werner J, Lis JT. 2000. High-resolution localization of Drosophila Spt5 and Spt6 at heat shock genes in vivo: roles in promoter proximal pausing and transcription elongation. Genes Dev. 14:2635-649.
    • (2000) Genes Dev. , vol.14 , pp. 2635-2649
    • Andrulis, E.D.1    Guzḿan, E.2    D̈oring, P.3    Werner, J.4    Lis, J.T.5
  • 104
    • 0029959881 scopus 로고    scopus 로고
    • Control of RNA polymerase II elongation potential by a novel carboxyl- terminal domain kinase
    • DOI 10.1074/jbc.271.43.27176
    • Marshall NF, Peng J, Xie Z, Price DH. 1996. Control of RNA polymerase II elongation potential by a novel carboxyl-terminal domain kinase. J. Biol. Chem. 271:27176-183. (Pubitemid 26359140)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.43 , pp. 27176-27183
    • Marshall, N.F.1    Peng, J.2    Xie, Z.3    Price, D.H.4
  • 106
    • 1642441939 scopus 로고    scopus 로고
    • Coordination of transcription, RNA processing, and surveillance by P-TEFb kinase on heat shock genes
    • DOI 10.1016/S1097-2765(03)00526-4
    • Ni Z, Schwartz BE, Werner J, Suarez JR, Lis JT. 2004. Coordination of transcription, RNA processing, and surveillance by P-TEFb kinase on heat shock genes. Mol. Cell 13:55-65. (Pubitemid 38117115)
    • (2004) Molecular Cell , vol.13 , Issue.1 , pp. 55-65
    • Ni, Z.1    Schwartz, B.E.2    Werner, J.3    Suarez, J.-R.4    Lis, J.T.5
  • 108
  • 109
    • 0029759928 scopus 로고    scopus 로고
    • Activator-dependent regulation of transcriptional pausing on nucleosomal templates
    • Brown SA, Imbalzano AN, Kingston RE. 1996. Activator-dependent regulation of transcriptional pausing on nucleosomal templates. Genes Dev. 10:1479-490. (Pubitemid 26260705)
    • (1996) Genes and Development , vol.10 , Issue.12 , pp. 1479-1490
    • Brown, S.A.1    Imbalzano, A.N.2    Kingston, R.E.3
  • 110
    • 0036790591 scopus 로고    scopus 로고
    • The DrosophilaBRMcomplex facilitates global transcription by RNA polymerase II
    • Armstrong JA, Papoulas O, Daubresse G, Sperling AS, Lis JT, et al. 2002. The DrosophilaBRMcomplex facilitates global transcription by RNA polymerase II. EMBO J. 21:5245-254.
    • (2002) EMBO J. , vol.21 , pp. 5245-5254
    • Armstrong, J.A.1    Papoulas, O.2    Daubresse, G.3    Sperling, A.S.4    Lis, J.T.5
  • 111
    • 0042830962 scopus 로고    scopus 로고
    • Tracking FACT and the RNA polymerase II elongation complex through chromatin in vivo
    • DOI 10.1126/science.1085712
    • Saunders A, Werner J, Andrulis ED, Nakayama T, Hirose S, et al. 2003. Tracking FACT and the RNA polymerase II elongation complex through chromatin in vivo. Science 301:1094-096. (Pubitemid 37022310)
    • (2003) Science , vol.301 , Issue.5636 , pp. 1094-1096
    • Saunders, A.1    Werner, J.2    Andrulis, E.D.3    Nakayama, T.4    Hirose, S.5    Reinberg, D.6    Lis, J.T.7
  • 112
    • 67349153355 scopus 로고    scopus 로고
    • Spt6 enhances the elongation rate of RNA polymerase II in vivo
    • Ardehali MB, Yao J, Adelman K, Fuda NJ, Petesch SJ, et al. 2009. Spt6 enhances the elongation rate of RNA polymerase II in vivo. EMBO J. 28:1067-077.
    • (2009) EMBO J. , vol.28 , pp. 1067-1077
    • Ardehali, M.B.1    Yao, J.2    Adelman, K.3    Fuda, N.J.4    Petesch, S.J.5
  • 113
  • 114
    • 46349088661 scopus 로고    scopus 로고
    • Clearing the way for unpaused polymerases
    • DOI 10.1016/j.cell.2008.06.031, PII S0092867408008180
    • Weake VM, Workman JL. 2008. Clearing the way for unpaused polymerases. Cell 134:16-18. (Pubitemid 351916709)
    • (2008) Cell , vol.134 , Issue.1 , pp. 16-18
    • Weake, V.M.1    Workman, J.L.2
  • 115
    • 0037462597 scopus 로고    scopus 로고
    • Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci
    • DOI 10.1126/science.1078764
    • Tulin A, Spradling A. 2003. Chromatin loosening by polyADP-ribose polymerase PARP at Drosophila puff loci. Science 299:560-562. (Pubitemid 36135152)
    • (2003) Science , vol.299 , Issue.5606 , pp. 560-562
    • Tulin, A.1    Spradling, A.2
  • 117
    • 70450255284 scopus 로고    scopus 로고
    • PARP-1 transcriptional activity is regulated by sumoylation upon heat shock
    • Martin N, Schwamborn K, Schreiber V, Werner A, Guillier C, et al. 2009. PARP-1 transcriptional activity is regulated by sumoylation upon heat shock. EMBO J. 28:3534-548.
    • (2009) EMBO J. , vol.28 , pp. 3534-3548
    • Martin, N.1    Schwamborn, K.2    Schreiber, V.3    Werner, A.4    Guillier, C.5
  • 118
    • 0024282785 scopus 로고
    • Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation
    • Sorger PK, Pelham HRB. 1988. Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation. Cell 54:855-864.
    • (1988) Cell , vol.54 , pp. 855-864
    • Sorger, P.K.1    Pelham, H.R.B.2
  • 119
    • 0027439593 scopus 로고
    • Heat shock factor is required for growth at normal temperatures in the fission yeast Schizosaccharomyces pombe
    • Gallo GJ, Prentice H, Kingston RE. 1993. Heat shock factor is required for growth at normal temperatures in the fission yeast Schizosaccharomyces pombe. Mol. Cell. Biol. 13:749-761. (Pubitemid 23040239)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.2 , pp. 749-761
    • Gallo, G.J.1    Prentice, H.2    Kingston, R.E.3
  • 120
    • 0032931842 scopus 로고    scopus 로고
    • A trans-activation domain in yeast heat shock transcription factor is essential for cell cycle progression during stress
    • Morano KA, Santoro N, Koch KA, Thiele DJ. 1999. A trans-activation domain in yeast heat shock transcription factor is essential for cell cycle progression during stress. Mol. Cell. Biol. 19:402-411. (Pubitemid 29018442)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.1 , pp. 402-411
    • Morano, K.A.1    Santoro, N.2    Koch, K.A.3    Thiele, D.J.4
  • 121
    • 20444480988 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae heat shock transcription factor regulates cell wall remodeling in response to heat shock
    • DOI 10.1128/EC.4.6.1050-1056.2005
    • Imazu H, Sakurai H. 2005. Saccharomyces cerevisiae heat shock transcription factor regulates cell wall remodeling in response to heat shock. Eukaryot. Cell 4:1050-056. (Pubitemid 40817464)
    • (2005) Eukaryotic Cell , vol.4 , Issue.6 , pp. 1050-1056
    • Imazu, H.1    Sakurai, H.2
  • 122
    • 2942598422 scopus 로고    scopus 로고
    • Genome-wide analysis of the biology of stress responses through heat shock transcription factor
    • DOI 10.1128/MCB.24.12.5249-5256.2004
    • Hahn JS, Hu Z, Thiele DJ, Iyer VR. 2004. Genome-wide analysis of the biology of stress responses through heat shock transcription factor. Mol. Cell. Biol. 24:5249-256. (Pubitemid 38738160)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.12 , pp. 5249-5256
    • Hahn, J.-S.1    Hu, Z.2    Thiele, D.J.3    Iyer, V.R.4
  • 123
    • 0030985251 scopus 로고    scopus 로고
    • Multiple functions of Drosophila heat shock transcription factor in vivo
    • DOI 10.1093/emboj/16.9.2452
    • Jedlicka P, Mortin MA, Wu C. 1997. Multiple functions of Drosophila heat shock transcription factor in vivo. EMBO J. 16:2452-462. (Pubitemid 27258642)
    • (1997) EMBO Journal , vol.16 , Issue.9 , pp. 2452-2462
    • Jedlicka, P.1    Mortin, M.A.2    Wu, C.3
  • 126
    • 76249095293 scopus 로고    scopus 로고
    • Heat shock transcription factor 1 inhibits expression of IL-6 through activating transcription factor 3
    • Takii R, Inouye S, Fujimoto M, Nakamura T, Shinkawa T, et al. 2010. Heat shock transcription factor 1 inhibits expression of IL-6 through activating transcription factor 3. J. Immunol. 184:1041-048.
    • (2010) J. Immunol. , vol.184 , pp. 1041-1048
    • Takii, R.1    Inouye, S.2    Fujimoto, M.3    Nakamura, T.4    Shinkawa, T.5
  • 127
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: Integrators of cell stress, development and lifespan
    • ÅkerfeltM, 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
    • Åkerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 128
    • 33751092252 scopus 로고    scopus 로고
    • Genome-wide analysis of human HSF1 signaling reveals a transcriptional program linked to cellular adaptation and survival
    • DOI 10.1039/b606129j
    • Page TJ, Sikder D, Yang L, Pluta L, Wolfinger RD, et al. 2006. Genome-wide analysis of human HSF1 signaling reveals a transcriptional program linked to cellular adaptation and survival. Mol. Biosyst. 2:627-639. (Pubitemid 44772306)
    • (2006) Molecular BioSystems , vol.2 , Issue.12 , pp. 627-639
    • Page, T.J.1    Sikder, D.2    Yang, L.3    Pluta, L.4    Wolfinger, R.D.5    Kodadek, T.6    Thomas, R.S.7
  • 129
    • 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 130:1005-018. (Pubitemid 47410269)
    • (2007) Cell , vol.130 , Issue.6 , pp. 1005-1018
    • Dai, C.1    Whitesell, L.2    Rogers, A.B.3    Lindquist, S.4
  • 130
    • 34547616810 scopus 로고    scopus 로고
    • Selective suppression of lymphomas by functional loss of Hsf1 in a p53-deficient mouse model for spontaneous tumors
    • DOI 10.1038/sj.onc.1210317, PII 1210317
    • Min JN, Huang L, Zimonjic DB, Moskophidis D, Mivechi NF. 2007. Selective suppression of lymphomas by functional loss of Hsf1 in a p53-deficient mouse model for spontaneous tumors. Oncogene 26:5086-097. (Pubitemid 47206948)
    • (2007) Oncogene , vol.26 , Issue.35 , pp. 5086-5097
    • Min, J.-N.1    Huang, L.2    Zimonjic, D.B.3    Moskophidis, D.4    Mivechi, N.F.5
  • 131
    • 73649142444 scopus 로고    scopus 로고
    • Heat shock factor 1-mediated aneuploidy requires a defective function of p53
    • Kim EH, Lee YJ, Bae S, Lee JS, Kim J, Lee YS. 2009. Heat shock factor 1-mediated aneuploidy requires a defective function of p53. Cancer Res. 69:9404-412.
    • (2009) Cancer Res. , vol.69 , pp. 9404-9412
    • Kim, E.H.1    Lee, Y.J.2    Bae, S.3    Lee, J.S.4    Kim, J.5    Lee, Y.S.6
  • 132
    • 67649217159 scopus 로고    scopus 로고
    • Inhibiting the transcription factor HSF1 as an anticancer strategy
    • Whitesell L, Lindquist S. 2009. Inhibiting the transcription factor HSF1 as an anticancer strategy. Expert Opin. Ther. Targets 13:469-478.
    • (2009) Expert Opin. Ther. Targets , vol.13 , pp. 469-478
    • Whitesell, L.1    Lindquist, S.2
  • 133
  • 134
    • 33846225133 scopus 로고    scopus 로고
    • Huntington's disease
    • DOI 10.1016/S0140-6736(07)60111-1, PII S0140673607601111
    • Walker FO. 2007. Huntington's disease. Lancet 369:218-228. (Pubitemid 46107685)
    • (2007) Lancet , vol.369 , Issue.9557 , pp. 218-228
    • Walker, F.O.1
  • 135
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • Morley JF, Brignull HR, Weyers JJ, Morimoto RI. 2002. The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 99:10417-422.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10417-10422
    • Morley, J.F.1    Brignull, H.R.2    Weyers, J.J.3    Morimoto, R.I.4
  • 138
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • DOI 10.1126/science.1124514
    • Gidalevitz T, Ben-Zvi A, Ho KH, Brignull HR, Morimoto RI. 2006. Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311:1471-474. (Pubitemid 43376703)
    • (2006) Science , vol.311 , Issue.5766 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 140
    • 70349266064 scopus 로고    scopus 로고
    • Collapse of proteostasis represents an earlymolecular event in Caenorhabditis elegans aging
    • Ben-Zvi A, Miller EA, Morimoto RI. 2009. Collapse of proteostasis represents an earlymolecular event in Caenorhabditis elegans aging. Proc. Natl. Acad. Sci. USA 106:14914-19
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 14914-19
    • Ben-Zvi, A.1    Miller, E.A.2    Morimoto, R.I.3
  • 142
    • 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 300:1142-145. (Pubitemid 36583098)
    • (2003) Science , vol.300 , Issue.5622 , pp. 1142-1145
    • Hsu, A.-L.1    Murphy, C.T.2    Kenyon, C.3
  • 143
    • 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
  • 144
    • 0027771804 scopus 로고
    • A C. elegans mutant that lives twice as long as wild type
    • DOI 10.1038/366461a0
    • Kenyon C, Chang J, Gensch E, Rudner A, Tabtiang R. 1993. A C. elegans mutant that lives twice as long as wild type. Nature 366:461-464. (Pubitemid 24013878)
    • (1993) Nature , vol.366 , Issue.6454 , pp. 461-464
    • Kenyon, C.1    Chang, J.2    Gensch, E.3    Rudner, A.4    Tabtiang, R.5
  • 145
    • 52449086907 scopus 로고    scopus 로고
    • The insulin paradox: Aging, proteotoxicity and neurodegeneration
    • Cohen E, Dillin A. 2008. The insulin paradox: aging, proteotoxicity and neurodegeneration. Nat. Rev. Neurosci. 9:759-767.
    • (2008) Nat. Rev. Neurosci. , vol.9 , pp. 759-767
    • Cohen, E.1    Dillin, A.2
  • 146
    • 0029123058 scopus 로고
    • Thermotolerance and extended life-span conferred by single-gene mutations and induced by thermal stress
    • Lithgow GJ, White TM, Melov S, Johnson TE. 1995. Thermotolerance and extended life-span conferred by single-gene mutations and induced by thermal stress. Proc. Natl. Acad. Sci. USA 92:7540-544.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7540-7544
    • Lithgow, G.J.1    White, T.M.2    Melov, S.3    Johnson, T.E.4
  • 147
    • 13944269223 scopus 로고    scopus 로고
    • The plasticity of aging: Insights from long-lived mutants
    • DOI 10.1016/j.cell.2005.02.002
    • Kenyon C. 2005. The plasticity of aging: insights from long-lived mutants. Cell 120:449-460. (Pubitemid 40269760)
    • (2005) Cell , vol.120 , Issue.4 , pp. 449-460
    • Kenyon, C.1
  • 149
    • 71449108913 scopus 로고    scopus 로고
    • Reduced IGF-1 signaling delays age-associated proteotoxicity in mice
    • Cohen E, Paulsson JF, Blinder P, Burstyn-Cohen T, Du D, et al. 2009. Reduced IGF-1 signaling delays age-associated proteotoxicity in mice. Cell 139:1157-169.
    • (2009) Cell , vol.139 , pp. 1157-1169
    • Cohen, E.1    Paulsson, J.F.2    Blinder, P.3    Burstyn-Cohen, T.4    Du, D.5
  • 151
    • 33748792821 scopus 로고    scopus 로고
    • Opposing activities protect against age-onset proteotoxicity
    • DOI 10.1126/science.1124646
    • Cohen E, Bieschke J, Perciavalle RM, Kelly JW, Dillin A. 2006. Opposing activities protect against age-onset proteotoxicity. Science 313:1604-610. (Pubitemid 44414028)
    • (2006) Science , vol.313 , Issue.5793 , pp. 1604-1610
    • Cohen, E.1    Bieschke, J.2    Perciavalle, R.M.3    Kelly, J.W.4    Dillin, A.5
  • 152
    • 77953247518 scopus 로고    scopus 로고
    • Temporal requirements of insulin/ IGF-1 signaling for proteotoxicity protection
    • Cohen E, Du D, Joyce D, Kapernick EA, Volovik Y, et al. 2010. Temporal requirements of insulin/ IGF-1 signaling for proteotoxicity protection. Aging Cell 9:126-134.
    • (2010) Aging Cell , vol.9 , pp. 126-134
    • Cohen, E.1    Du, D.2    Joyce, D.3    Kapernick, E.A.4    Volovik, Y.5
  • 153
    • 35348972430 scopus 로고    scopus 로고
    • Genetic links between diet and lifespan: Shared mechanisms from yeast to humans
    • DOI 10.1038/nrg2188, PII NRG2188
    • Bishop NA, Guarente L. 2007. Genetic links between diet and lifespan: shared mechanisms from yeast to humans. Nat. Rev. Genet. 8:835-844. (Pubitemid 47609089)
    • (2007) Nature Reviews Genetics , vol.8 , Issue.11 , pp. 835-844
    • Bishop, N.A.1    Guarente, L.2
  • 154
    • 33746228121 scopus 로고    scopus 로고
    • Sirtuins in aging and age-related disease
    • DOI 10.1016/j.cell.2006.07.002, PII S0092867406008920
    • Longo VD, Kennedy BK. 2006. Sirtuins in aging and age-related disease. Cell 126:257-268. (Pubitemid 44092970)
    • (2006) Cell , vol.126 , Issue.2 , pp. 257-268
    • Longo, V.D.1    Kennedy, B.K.2
  • 155
    • 77953257025 scopus 로고    scopus 로고
    • Aging and disease: Connections to sirtuins
    • Donmez G, Guarente L. 2010. Aging and disease: connections to sirtuins. Aging Cell 9:285-290.
    • (2010) Aging Cell , vol.9 , pp. 285-290
    • Donmez, G.1    Guarente, L.2
  • 156
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2α promotes cell survival under stress
    • DOI 10.1016/S0092-8674(01)00524-4
    • Luo J, Nikolaev AY, Imai S, Chen D, Su F, et al. 2001. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 107:137-148. (Pubitemid 33035941)
    • (2001) Cell , vol.107 , Issue.2 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.-I.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 158
    • 0036084783 scopus 로고    scopus 로고
    • Invited review: Heat shock proteins: Modifying factors in physiological stress responses and acquired thermotolerance
    • Kregel KC. 2002. Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance. J. Appl. Physiol. 92:2177-186. (Pubitemid 34666449)
    • (2002) Journal of Applied Physiology , vol.92 , Issue.5 , pp. 2177-2186
    • Kregel, K.C.1
  • 159
    • 0028586833 scopus 로고
    • Effects of neurohormonal stress and aging on the activation of mammalian heat shock factor 1
    • Fawcett TW, Sylvester SL, Sarge KD, Morimoto RI, Holbrook NJ. 1994. Effects of neurohormonal stress and aging on the activation of mammalian heat shock factor 1. J. Biol. Chem. 269:32272-278.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32272-32278
    • Fawcett, T.W.1    Sylvester, S.L.2    Sarge, K.D.3    Morimoto, R.I.4    Holbrook, N.J.5
  • 160
    • 0030322758 scopus 로고    scopus 로고
    • Diminished heat shock response in the aged myocardium
    • Locke M, Tanguay RM. 1996. Diminished heat shock response in the aged myocardium. Cell Stress Chaperones 1:251-260.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 251-260
    • Locke, M.1    Tanguay, R.M.2
  • 161
    • 0031008913 scopus 로고    scopus 로고
    • Attenuated stress responses in young and old human lymphocytes
    • DOI 10.1016/S0047-6374(96)01856-8, PII S0047637496018568
    • Jurivich DA, Qiu L, Welk JF. 1997. Attenuated stress responses in young and old human lymphocytes. Mech. Ageing Dev. 94:233-249. (Pubitemid 27216111)
    • (1997) Mechanisms of Ageing and Development , vol.94 , Issue.1-3 , pp. 233-249
    • Jurivich, D.A.1    Qiu, L.2    Welk, J.F.3
  • 162
    • 0032527007 scopus 로고    scopus 로고
    • The expression of heat shock protein 70 decreases with cellular senescence in vitro and in cells derived from young and old human subjects
    • DOI 10.1006/excr.1998.4069
    • Gutsmann-Conrad A, Heydari AR, You S, Richardson A. 1998. The expression of heat shock protein 70 decreases with cellular senescence in vitro and in cells derived from young and old human subjects. Exp. Cell Res. 241:404-413. (Pubitemid 28366566)
    • (1998) Experimental Cell Research , vol.241 , Issue.2 , pp. 404-413
    • Gutsmann-Conrad, A.1    Heydari, A.R.2    You, S.3    Richardson, A.4
  • 163
    • 0029870841 scopus 로고    scopus 로고
    • Effect of caloric restriction on the expression of heat shock protein 70 and the activation of heat shock transcription factor 1
    • Heydari AR, You S, Takahashi R, Gutsmann A, Sarge KD, Richardson A. 1996. Effect of caloric restriction on the expression of heat shock protein 70 and the activation of heat shock transcription factor 1. Dev. Genet. 18:114-124.
    • (1996) Dev. Genet. , vol.18 , pp. 114-124
    • Heydari, A.R.1    You, S.2    Takahashi, R.3    Gutsmann, A.4    Sarge, K.D.5    Richardson, A.6
  • 164
    • 44649170501 scopus 로고    scopus 로고
    • Age- and calorie-independent life span extension from dietary restriction by bacterial deprivation in Caenorhabditis elegans
    • Smith ED, Kaeberlein TL, Lydum BT, Sager J, Welton KL, et al. 2008. Age- and calorie-independent life span extension from dietary restriction by bacterial deprivation in Caenorhabditis elegans. BMC Dev. Biol. 8:49.
    • (2008) BMC Dev. Biol. , vol.8 , pp. 49
    • Smith, E.D.1    Kaeberlein, T.L.2    Lydum, B.T.3    Sager, J.4    Welton, K.L.5
  • 165
    • 43449138491 scopus 로고    scopus 로고
    • Dietary restriction suppresses proteotoxicity and enhances longevity by an hsf-1-dependent mechanism in Caenorhabditis elegans
    • DOI 10.1111/j.1474-9726.2008.00385.x
    • Steinkraus KA, Smith ED, Davis C, Carr D, Pendergrass WR, et al. 2008. Dietary restriction suppresses proteotoxicity and enhances longevity by an hsf-1-dependent mechanism in Caenorhabditis elegans. Aging Cell 7:394-404. (Pubitemid 351663908)
    • (2008) Aging Cell , vol.7 , Issue.3 , pp. 394-404
    • Steinkraus, K.A.1    Smith, E.D.2    Davis, C.3    Carr, D.4    Pendergrass, W.R.5    Sutphin, G.L.6    Kennedy, B.K.7    Kaeberlein, M.8
  • 166
    • 33644872354 scopus 로고    scopus 로고
    • Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding
    • Wang X, Khaleque MA, Zhao MJ, Zhong R, Gaestel M, Calderwood SK. 2006. Phosphorylation of HSF1 by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding. J. Biol. Chem. 281:782-791.
    • (2006) J. Biol. Chem. , vol.281 , pp. 782-791
    • Wang, X.1    Khaleque, M.A.2    Zhao, M.J.3    Zhong, R.4    Gaestel, M.5    Calderwood, S.K.6
  • 167
    • 0035955662 scopus 로고    scopus 로고
    • Regulation of heat shock transcription factor 1 by stress-induced SUMO-1 modification
    • Hong Y, Rogers R, Matunis MJ, Mayhew CN, Goodson ML, et al. 2001. Regulation of heat shock transcription factor 1 by stress-induced SUMO-1 modification. J. Biol. Chem. 276:40263-267.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40263-40267
    • Hong, Y.1    Rogers, R.2    Matunis, M.J.3    Mayhew, C.N.4    Goodson, M.L.5
  • 168
    • 0029846433 scopus 로고    scopus 로고
    • Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor-1
    • DOI 10.1074/jbc.271.48.30847
    • Chu B, Soncin F, Price BD, Stevenson MA, Calderwood SK. 1996. Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor-1. J. Biol. Chem. 271:30847-857. (Pubitemid 26404108)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.48 , pp. 30847-30857
    • Chu, B.1    Soncin, F.2    Price, B.D.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 169
    • 0032541032 scopus 로고    scopus 로고
    • Transcriptional activity of heat shock factor 1 at 37 °c is repressed through phosphorylation on two distinct serine residues by glycogen synthase kinase 3α and protein kinases cα and cζ
    • DOI 10.1074/jbc.273.29.18640
    • Chu B, Zhong R, Soncin F, Stevenson MA, Calderwood SK. 1998. Transcriptional activity of heat shock factor 1 at 37?C is repressed through phosphorylation on two distinct serine residues by glycogen synthase kinase 3 and protein kinases Calpha and Czeta. J. Biol. Chem. 273:18640-646. (Pubitemid 28334797)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.29 , pp. 18640-18646
    • Chu, B.1    Zhong, R.2    Soncin, F.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 170
    • 0032502705 scopus 로고    scopus 로고
    • 32P-labeled in vivo
    • DOI 10.1074/jbc.273.15.8749
    • Xia W, Guo Y, Vilaboa N, Zuo J, Voellmy R. 1998. Transcriptional activation of heat shock factor HSF1 probed by phosphopeptide analysis of factor 32P-labeled in vivo. J. Biol. Chem. 273:8749-755. (Pubitemid 28176153)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.15 , pp. 8749-8755
    • Xia, W.1    Guo, Y.2    Vilaboa, N.3    Zuo, J.4    Voellmy, R.5
  • 171
    • 0034674061 scopus 로고    scopus 로고
    • 2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity
    • DOI 10.1074/jbc.M000958200
    • Dai R, Frejtag W, He B, Zhang Y, Mivechi NF. 2000. c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity. J. Biol. Chem. 275:18210-18. (Pubitemid 30414773)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.24 , pp. 18210-18218
    • Dai, R.1    Frejtag, W.2    He, B.3    Zhang, Y.4    Mivechi, N.F.5
  • 172
    • 16844366162 scopus 로고    scopus 로고
    • Polo-like kinase 1 phosphorylates heat shock transcription factor 1 and mediates its nuclear translocation during heat stress
    • Kim SA, Yoon JH, Lee SH, Ahn SG. 2005. Polo-like kinase 1 phosphorylates heat shock transcription factor 1 and mediates its nuclear translocation during heat stress. J. Biol. Chem. 280:12653-657.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12653-12657
    • Kim, S.A.1    Yoon, J.H.2    Lee, S.H.3    Ahn, S.G.4
  • 173
    • 73449137269 scopus 로고    scopus 로고
    • Glutamine enhances heat shock protein 70 expression via increased hexosamine biosynthetic pathway activity
    • Hamiel CR, Pinto S, Hau A, Wischmeyer PE. 2009. Glutamine enhances heat shock protein 70 expression via increased hexosamine biosynthetic pathway activity. Am. J. Physiol. Cell Physiol. 297:1509-19
    • (2009) Am. J. Physiol. Cell Physiol. , vol.297 , pp. 1509-1519
    • Hamiel, C.R.1    Pinto, S.2    Hau, A.3    Wischmeyer, P.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.