메뉴 건너뛰기




Volumn 8, Issue 2, 1996, Pages 95-158

The stress gene response in brain

Author keywords

Excitotoxicity; Glucose transporter; Glucose regulated protein; Heat shock protein; Heme oxygenase; Ischemia; Ubiquitin

Indexed keywords

ANIMAL; BRAIN ISCHEMIA; BRAIN LEVEL; GENE EXPRESSION REGULATION; GENETICS; HUMAN; METABOLISM; PHYSIOLOGY; REVIEW; STRESS;

EID: 0030170852     PISSN: 10408827     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (152)

References (402)
  • 1
    • 33845197236 scopus 로고    scopus 로고
    • Nowak TS. Stress protein induction is not required to express ischémie tolerance in the gerbil. 1994;20:423.4.
    • Abe H, Nowak TS. Stress protein induction is not required to express ischémie tolerance in the gerbil. Soc NeurosdAbstr 1994;20:423.4.
    • Soc NeurosdAbstr
    • Abe, H.1
  • 2
    • 0026633664 scopus 로고    scopus 로고
    • Araki T, Kawagoe J, Aoki M, Kogure K. Phospholipid metabolism and second messenger system after brain ischemia. 1992;318:183-95.
    • Abe K, Araki T, Kawagoe J, Aoki M, Kogure K. Phospholipid metabolism and second messenger system after brain ischemia. Adv Exp Med Biol 1992;318:183-95.
    • Adv Exp Med Biol
    • Abe, K.1
  • 3
    • 0027391065 scopus 로고    scopus 로고
    • Kawagoe J, Aoki M, Kogure K. Dissociation of HSP70 and HSC70 heat shock mRNA inductions as an early biochemical marker of ischémie neuronal death. 1993; 149:165-8.
    • Abe K, Kawagoe J, Aoki M, Kogure K. Dissociation of HSP70 and HSC70 heat shock mRNA inductions as an early biochemical marker of ischémie neuronal death. Neurosci Lett 1993; 149:165-8.
    • Neurosci Lett
    • Abe, K.1
  • 4
    • 0027051392 scopus 로고    scopus 로고
    • Kawagoe J, Araki T, Aoki M, Kogure K. Differential expression of heat shock protein 70 gene between the cortex and caudate after transient focal cerebral ischaemia in rats. 1992;14:381- 5.
    • Abe K, Kawagoe J, Araki T, Aoki M, Kogure K. Differential expression of heat shock protein 70 gene between the cortex and caudate after transient focal cerebral ischaemia in rats. Neural Res 1992;14:381- 5.
    • Neural Res
    • Abe, K.1
  • 5
    • 0027436970 scopus 로고    scopus 로고
    • Lee TH, Aoki M, Nitta Y, Isoyama S. Preferential expression of HSC70 heat shock mRNA in gerbil heart after transient brain ischemia. 1993;25:1131-5.
    • Abe K, Lee TH, Aoki M, Nitta Y, Isoyama S. Preferential expression of HSC70 heat shock mRNA in gerbil heart after transient brain ischemia. J Mol Cell Cardiol 1993;25:1131-5.
    • J Mol Cell Cardiol
    • Abe, K.1
  • 6
    • 0025762448 scopus 로고    scopus 로고
    • Tanzi RE, Kogure K. Induction of HSP70 mRNA after transient ischemia in gerbil brain. 1991;125:166-8.
    • Abe K, Tanzi RE, Kogure K. Induction of HSP70 mRNA after transient ischemia in gerbil brain. Neurosci Lett 1991;125:166-8.
    • Neurosci Lett
    • Abe, K.1
  • 7
    • 0026665975 scopus 로고    scopus 로고
    • Myers MP, Murphy SP, Morimoto RI. The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. 1992;6:1153-64.
    • Abravaya K, Myers MP, Murphy SP, Morimoto RI. The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev 1992;6:1153-64.
    • Genes Dev
    • Abravaya, K.1
  • 8
    • 0025935407 scopus 로고    scopus 로고
    • Phillips B, Morimoto RJ. 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. 1991;5:2117-27.
    • Abravaya K, Phillips B, Morimoto RJ. 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. Genes Dev 1991;5:2117-27.
    • Genes Dev
    • Abravaya, K.1
  • 10
    • 0026788471 scopus 로고    scopus 로고
    • DenZ. Distal AP-1 binding sites mediate basal level enhancement and TPA induction of the mouse heme oxygenase-1 gene. 1992;267:21894-900.
    • Alam J, DenZ. Distal AP-1 binding sites mediate basal level enhancement and TPA induction of the mouse heme oxygenase-1 gene. J Biol Chem 1992;267:21894-900.
    • J Biol Chem
    • Alam, J.1
  • 11
    • 0027938515 scopus 로고    scopus 로고
    • Fernandez M, Ananthan J, Lis JT, Voellmy R. Cooperative binding of heat shock transcription factor to the Hsp70 promoter in vivo and in vitro. 1994;269:4804-11.
    • Amin J, Fernandez M, Ananthan J, Lis JT, Voellmy R. Cooperative binding of heat shock transcription factor to the Hsp70 promoter in vivo and in vitro. J Biol Chem 1994;269:4804-11.
    • J Biol Chem
    • Amin, J.1
  • 12
    • 0022633852 scopus 로고    scopus 로고
    • Tao TW, Betten DA, Hahn GM. Heat shock protein levels are not elevated in heat-resistant B16 melanoma cells. 1986; 105:240-6.
    • Anderson RL, Tao TW, Betten DA, Hahn GM. Heat shock protein levels are not elevated in heat-resistant B16 melanoma cells. Radiât Res 1986; 105:240-6.
    • Radiât Res
    • Anderson, R.L.1
  • 13
    • 0025821926 scopus 로고    scopus 로고
    • Lazaridis I, Pagoulatos GN. Constitutive expression of heat shock protein 70 in mammalian cells confers thermoresistance. 1991; 199:35-9.
    • Angelidis CE, Lazaridis I, Pagoulatos GN. Constitutive expression of heat shock protein 70 in mammalian cells confers thermoresistance. Eur J Biochem 1991; 199:35-9.
    • Eur J Biochem
    • Angelidis, C.E.1
  • 14
    • 0027164673 scopus 로고    scopus 로고
    • Abe K, Kawagoe J, Nakamura S, Kogure K. Acceleration of HSP70 and HSC70 heat shock gene expression following transient ischemia in the preconditioned gerbil hippocampus. 1993;13:781-8.
    • Aoki M, Abe K, Kawagoe J, Nakamura S, Kogure K. Acceleration of HSP70 and HSC70 heat shock gene expression following transient ischemia in the preconditioned gerbil hippocampus. J Cereb Blood Flow Metab 1993;13:781-8.
    • J Cereb Blood Flow Metab
    • Aoki, M.1
  • 15
    • 0027479403 scopus 로고    scopus 로고
    • Abe K, Kawagoe J, Sato S, Nakamura S, Kogure K. Temporal profile of the induction of heat shock protein 70 and heat shock cognate protein 70 mRNAs after transient ischemia in gerbil brain. 1993;601:185-92.
    • Aoki M, Abe K, Kawagoe J, Sato S, Nakamura S, Kogure K. Temporal profile of the induction of heat shock protein 70 and heat shock cognate protein 70 mRNAs after transient ischemia in gerbil brain. Brain Res 1993;601:185-92.
    • Brain Res
    • Aoki, M.1
  • 16
    • 0027300914 scopus 로고    scopus 로고
    • Abe K, Liu XH, Lee TH, Kato H, Kogure K. Reduction of HSP70 and HSC70 mRNA inductions by bifemelane hydrochloride after transient ischemia in gerbil brain. 1993;154:69-72.
    • Aoki M, Abe K, Liu XH, Lee TH, Kato H, Kogure K. Reduction of HSP70 and HSC70 mRNA inductions by bifemelane hydrochloride after transient ischemia in gerbil brain. Neurosci Lett 1993;154:69-72.
    • Neurosci Lett
    • Aoki, M.1
  • 17
    • 0027954255 scopus 로고    scopus 로고
    • Coulter KC. The nature and time course of neuronal vacuolation induced by the W-methyl-D-aspartate antagonist MK-801. 1994;87:l-7.
    • Auer RN, Coulter KC. The nature and time course of neuronal vacuolation induced by the W-methyl-D-aspartate antagonist MK-801. Acta Neuropathol (Berl) 1994;87:l-7.
    • Acta Neuropathol (Berl)
    • Auer, R.N.1
  • 18
    • 0027474909 scopus 로고    scopus 로고
    • Dahl G, Voellmy R. Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1. 1993;13:2486-96.
    • Baler R, Dahl G, Voellmy R. Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1. Mol Cell Biol 1993;13:2486-96.
    • Mol Cell Biol
    • Baler, R.1
  • 19
    • 0026750001 scopus 로고    scopus 로고
    • Welch WJ, Voellmy R. Heat shock gene regulation by nascent polypeptides and denatured proteins: hsp70 as a potential autoregulatory factor. 1992; 117:1151-9.
    • Baler R, Welch WJ, Voellmy R. Heat shock gene regulation by nascent polypeptides and denatured proteins: hsp70 as a potential autoregulatory factor. J Cell Biol 1992; 117:1151-9.
    • J Cell Biol
    • Baler, R.1
  • 20
    • 0027358877 scopus 로고    scopus 로고
    • Jacob HS, Balla G, Nath K, Eaton JW, Vercellotti GM (1993) Endothelial-cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidant damage. 9285-9.
    • Balla J, Jacob HS, Balla G, Nath K, Eaton JW, Vercellotti GM (1993) Endothelial-cell heme uptake from heme proteins: induction of sensitization and desensitization to oxidant damage. Proc Natl AcadSei USA l993;90:9285-9.
    • Proc Natl AcadSei USA L993;90
    • Balla, J.1
  • 21
    • 0025745511 scopus 로고    scopus 로고
    • Norton PM, Latchman DS. The 90-kDa heat shock protein protects mammalian cells from thermal stress but not from viral infection. 1991 ; 195:303-6.
    • Bansal GS, Norton PM, Latchman DS. The 90-kDa heat shock protein protects mammalian cells from thermal stress but not from viral infection. Exp Cell Res 1991 ; 195:303-6.
    • Exp Cell Res
    • Bansal, G.S.1
  • 22
    • 0023732689 scopus 로고    scopus 로고
    • Tytell M, Gower DJ, Welch WJ. Hyperthermia protects against light damage in the rat retina. 1988;241:1817-20.
    • Barbe MF, Tytell M, Gower DJ, Welch WJ. Hyperthermia protects against light damage in the rat retina. Science 1988;241:1817-20.
    • Science
    • Barbe, M.F.1
  • 23
    • 0028337337 scopus 로고    scopus 로고
    • Williams ME, Benz CC, Chepenik KP. Oxidant-sensitive protein phosphorylation in endothelial cells. 1994;16:771-7.
    • Barchowsky A, Williams ME, Benz CC, Chepenik KP. Oxidant-sensitive protein phosphorylation in endothelial cells. Free Radical Biol Med 1994;16:771-7.
    • Free Radical Biol Med
    • Barchowsky, A.1
  • 24
    • 0027420589 scopus 로고    scopus 로고
    • Tyrrell RM. Singlet oxygen: a primary effector in the ultraviolet A/near-visible light induction of the human heme oxygenase gene. 1993;53:4505-10.
    • Basu MS, Tyrrell RM. Singlet oxygen: a primary effector in the ultraviolet A/near-visible light induction of the human heme oxygenase gene. Cancer Res 1993;53:4505-10.
    • Cancer Res
    • Basu, M.S.1
  • 25
    • 0026038235 scopus 로고    scopus 로고
    • Mezger V, Courgeon AM, Best BM. On the mechanism of action of H202 in the cellular stress. 1991 ; 1:455-60.
    • Becker J, Mezger V, Courgeon AM, Best BM. On the mechanism of action of H202 in the cellular stress. Free Radical Res Commun 1991 ; 1:455-60.
    • Free Radical Res Commun
    • Becker, J.1
  • 26
    • 0025303147 scopus 로고    scopus 로고
    • Mizzen LE, Welch WJ. Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. 1990:248:850-41.
    • Beckmann RP, Mizzen LE, Welch WJ. Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science 1990:248:850-41.
    • Science
    • Beckmann, R.P.1
  • 27
    • 0027166231 scopus 로고    scopus 로고
    • Burant CF, Takeda J, Gould GW Structure and function of mammalian facilitative sugar transporters. 1993:268:19161-4.
    • Bell GI, Burant CF, Takeda J, Gould GW Structure and function of mammalian facilitative sugar transporters. JBiolChem 1993:268:19161-4.
    • JBiolChem
    • Bell, G.I.1
  • 29
    • 0024999067 scopus 로고    scopus 로고
    • Kroger B, Williams RS. Activation of the heat shock transcription factor by hypoxia in mammalian cells. 1990:87:6263-7.
    • Benjamin IJ, Kroger B, Williams RS. Activation of the heat shock transcription factor by hypoxia in mammalian cells. Proc Natl Acad Sei USA 1990:87:6263-7.
    • Proc Natl Acad Sei USA
    • Benjamin, I.J.1
  • 30
    • 85177152600 scopus 로고    scopus 로고
    • Hayess K, Ryazantsev S, Wieske M, Behlke J, Lutsch G. Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity. 1994;269:20780-4.
    • Benndorf R, Hayess K, Ryazantsev S, Wieske M, Behlke J, Lutsch G. Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity. JBiolChem 1994;269:20780-4.
    • JBiolChem
    • Benndorf, R.1
  • 31
    • 0028222785 scopus 로고    scopus 로고
    • Farrel K, Sharp F, Skolnick P. Drugs acting at the strychnine-insensitive glycine receptor do not induce HSP-70 protein in the cingulate cortex. 1994:168:147-50.
    • Berger P, Farrel K, Sharp F, Skolnick P. Drugs acting at the strychnine-insensitive glycine receptor do not induce HSP-70 protein in the cingulate cortex. Neurosci Lett 1994:168:147-50.
    • Neurosci Lett
    • Berger, P.1
  • 32
    • 0015821560 scopus 로고    scopus 로고
    • Gilboe DD, Yudilevich DL, Drewes LR. Kinetics of unidirectional glucose transport into the isolated dog brain. 1973:225:586-92.
    • Betz AL, Gilboe DD, Yudilevich DL, Drewes LR. Kinetics of unidirectional glucose transport into the isolated dog brain. Am J Physiol 1973:225:586-92.
    • Am J Physiol
    • Betz, A.L.1
  • 33
    • 0023043264 scopus 로고    scopus 로고
    • Pelham HR. Heat shock regulatory elements function as an inducible enhancer in the Xenopus hsp70 gene and when linked to a heterologous promoter. 1986:45:753-60.
    • Bienz M, Pelham HR. Heat shock regulatory elements function as an inducible enhancer in the Xenopus hsp70 gene and when linked to a heterologous promoter. Cell 1986:45:753-60.
    • Cell
    • Bienz, M.1
  • 34
    • 0025821986 scopus 로고    scopus 로고
    • Fargnoli J, Gershon D, Holbrook NJ. Concomitant decline in heat-induced hyperthermia and HSP70 mRNA expression in aged rats. 1991;R663-7.
    • Blake MJ, Fargnoli J, Gershon D, Holbrook NJ. Concomitant decline in heat-induced hyperthermia and HSP70 mRNA expression in aged rats. Am J Physiol 1991;R663-7.
    • Am J Physiol
    • Blake, M.J.1
  • 35
    • 0025024265 scopus 로고    scopus 로고
    • Gershon D, Fargnoli J, Holbrook NJ. Discordant expression of heat shock protein mRNAs in tissues of heat-stressed rats. 1990:265:15275-9.
    • Blake MJ, Gershon D, Fargnoli J, Holbrook NJ. Discordant expression of heat shock protein mRNAs in tissues of heat-stressed rats. J Biol Chem 1990:265:15275-9.
    • J Biol Chem
    • Blake, M.J.1
  • 36
    • 0025293892 scopus 로고    scopus 로고
    • Nowak TJ, Holbrook NJ. In vivo hyperthermia induces expression of HSP70 mRNA in brain regions controlling the neuroendocrine response to stress. 1990;8:89-92.
    • Blake MJ, Nowak TJ, Holbrook NJ. In vivo hyperthermia induces expression of HSP70 mRNA in brain regions controlling the neuroendocrine response to stress. Brain Res Mol Brain Res 1990;8:89-92.
    • Brain Res Mol Brain Res
    • Blake, M.J.1
  • 37
    • 0028233372 scopus 로고    scopus 로고
    • Gonen H, Mayer A, Smith CE, Siegel NR, Schwartz AL, Ciechanover A. Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non"N-end rule" protein substrates. 1994;269:9574-81.
    • Blumenfeld N, Gonen H, Mayer A, Smith CE, Siegel NR, Schwartz AL, Ciechanover A. Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non"N-end rule" protein substrates. J Biol Chem 1994;269:9574-81.
    • J Biol Chem
    • Blumenfeld, N.1
  • 38
    • 0028215225 scopus 로고    scopus 로고
    • Deloche O, Click BS, Georgopoulos C, Jeno P, Kronidou N, Horst M, Morishima N, Schatz G. A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viability. 1994:13:1998-2006.
    • Bolliger L, Deloche O, Click BS, Georgopoulos C, Jeno P, Kronidou N, Horst M, Morishima N, Schatz G. A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viability. EMBOJ 1994:13:1998-2006.
    • EMBOJ
    • Bolliger, L.1
  • 39
    • 0022000263 scopus 로고    scopus 로고
    • Schlesinger MJ. Ubiquitin is a heat shock protein in chicken embryo fibroblasts. 1985:5:949-56.
    • Bond U, Schlesinger MJ. Ubiquitin is a heat shock protein in chicken embryo fibroblasts. Mot Cell Biol 1985:5:949-56.
    • Mot Cell Biol
    • Bond, U.1
  • 40
    • 0022999212 scopus 로고    scopus 로고
    • Schlesinger MJ. The chicken ubiquitin gene contains a heat shock promoter and expresses an unstable mRNA in heat shocked cells. 1986;6:4602-10.
    • Bond U, Schlesinger MJ. The chicken ubiquitin gene contains a heat shock promoter and expresses an unstable mRNA in heat shocked cells. Mol Cell Biol 1986;6:4602-10.
    • Mol Cell Biol
    • Bond, U.1
  • 41
    • 0027321678 scopus 로고    scopus 로고
    • JessTJ, Milligan G, Brown CM, Gould GW. Immunological analysis of glucose transporters expressed in different regions of the rat brain and central nervous system. 1993:192:1297-302.
    • Brant AM, JessTJ, Milligan G, Brown CM, Gould GW. Immunological analysis of glucose transporters expressed in different regions of the rat brain and central nervous system. Biochem Biophvs Res Commun 1993:192:1297-302.
    • Biochem Biophvs Res Commun
    • Brant, A.M.1
  • 42
    • 0025252477 scopus 로고    scopus 로고
    • Cade C, Prostko CR, Gmitter YD, Brostrom CO. Accommodation of protein synthesis to chronic deprivation of intracellular sequestered calcium. 1990:265:20539-416.
    • Brostrom MA, Cade C, Prostko CR, Gmitter YD, Brostrom CO. Accommodation of protein synthesis to chronic deprivation of intracellular sequestered calcium. A putative role for GRP78. J Biol Chem 1990:265:20539-416.
    • A Putative Role for GRP78. J Biol Chem
    • Brostrom, M.A.1
  • 43
    • 0020530939 scopus 로고    scopus 로고
    • Hyperthermia induces the synthesis of a heat shock protein by polysomes isolated from the fetal and neonatal mammalian brain. 1983:40:1490-3.
    • Brown IR. Hyperthermia induces the synthesis of a heat shock protein by polysomes isolated from the fetal and neonatal mammalian brain. JNeurochem 1983:40:1490-3.
    • JNeurochem
    • Brown, I.R.1
  • 44
    • 0025611307 scopus 로고    scopus 로고
    • Induction of heat shock (stress) genes in the mammalian brain by hyperthermia and other traumatic events: a current perspective. 1990:27:247-55.
    • Brown IR. Induction of heat shock (stress) genes in the mammalian brain by hyperthermia and other traumatic events: a current perspective. J Neurosci Res 1990:27:247-55.
    • J Neurosci Res
    • Brown, I.R.1
  • 45
    • 0022004202 scopus 로고    scopus 로고
    • Löwe DG, Moran LA. Expression of heat shock genes in fetal and maternal rabbit brain. 1985:10:1277-84.
    • Brown IR, Löwe DG, Moran LA. Expression of heat shock genes in fetal and maternal rabbit brain. Neurochem Res 1985:10:1277-84.
    • Neurochem Res
    • Brown, I.R.1
  • 46
    • 0025017123 scopus 로고    scopus 로고
    • Rush SJ. Expression of heat shock genes (hsp70) in the mammalian brain: distinguishing constitutively expressed and hyperthermia-inducible mRNA species. 1990;25:14-9.
    • Brown IR, Rush SJ. Expression of heat shock genes (hsp70) in the mammalian brain: distinguishing constitutively expressed and hyperthermia-inducible mRNA species. J Neurosci Res 1990;25:14-9.
    • J Neurosci Res
    • Brown, I.R.1
  • 47
    • 0024677259 scopus 로고    scopus 로고
    • Rush S, Ivy GO. Induction of a heat shock gene at the site of tissue injury in the rat brain. 1989;2:1559-64.
    • Brown IR, Rush S, Ivy GO. Induction of a heat shock gene at the site of tissue injury in the rat brain. Neuron 1989;2:1559-64.
    • Neuron
    • Brown, I.R.1
  • 48
    • 0027393628 scopus 로고    scopus 로고
    • Price BD, Coleman CM, Calderwood SK. Oxidative injury rapidly activates the heat shock transcription factor but fails to increase levels of heat shock proteins. 1993;53:12-5.
    • Bruce JL, Price BD, Coleman CM, Calderwood SK. Oxidative injury rapidly activates the heat shock transcription factor but fails to increase levels of heat shock proteins. Cancer Res 1993;53:12-5.
    • Cancer Res
    • Bruce, J.L.1
  • 49
    • 0025893367 scopus 로고    scopus 로고
    • Hughes CS, Shen JW, Subjeck JR. Induction of heat shock proteins by glutamine. 1991;288:229-32.
    • Cai JW, Hughes CS, Shen JW, Subjeck JR. Induction of heat shock proteins by glutamine. The "feeding effect." FEBS Lett 1991;288:229-32.
    • The "Feeding Effect." FEBS Lett
    • Cai, J.W.1
  • 50
    • 0026739577 scopus 로고    scopus 로고
    • Crescente M. In vitro activation of heat shock transcription factor by 4-hydroxynonenal. 1992;84:97-112.
    • Cajone F, Crescente M. In vitro activation of heat shock transcription factor by 4-hydroxynonenal. Chem Biol Interact 1992;84:97-112.
    • Chem Biol Interact
    • Cajone, F.1
  • 53
    • 0026523153 scopus 로고    scopus 로고
    • Toledo H, Skaleris D, DeLisio R, Weissbach H, Brot N. Interactions of liver Grp78 and Escherichia coli recombinant Grp78 with ATP: multiple species and disaggregation. 1992;89:2081-5.
    • Carlino A, Toledo H, Skaleris D, DeLisio R, Weissbach H, Brot N. Interactions of liver Grp78 and Escherichia coli recombinant Grp78 with ATP: multiple species and disaggregation. Proc Natl Acad Sei USA 1992;89:2081-5.
    • Proc Natl Acad Sei USA
    • Carlino, A.1
  • 54
    • 0027172235 scopus 로고    scopus 로고
    • Fawcett TW, Bartlett JD, Bemier M, Holbrook NJ. Regulation of the C/EBP-related gene gaddl 53 by glucose deprivation. 1993;13:4736-44.
    • Carlson SG, Fawcett TW, Bartlett JD, Bemier M, Holbrook NJ. Regulation of the C/EBP-related gene gaddl 53 by glucose deprivation. Mol Cell Biol 1993;13:4736-44.
    • Mol Cell Biol
    • Carlson, S.G.1
  • 55
    • 0020807492 scopus 로고    scopus 로고
    • Lazarides E. ADP-ribosylation of the Mv 83,000 stress-inducible and glucose-regulated protein in avian and mammalian cells: modulation by heat shock and glucose starvation. 1983;80:4664-8.
    • Carlsson L, Lazarides E. ADP-ribosylation of the Mv 83,000 stress-inducible and glucose-regulated protein in avian and mammalian cells: modulation by heat shock and glucose starvation. Proc Natl Acad Sei USA 1983;80:4664-8.
    • Proc Natl Acad Sei USA
    • Carlsson, L.1
  • 56
    • 0025166970 scopus 로고    scopus 로고
    • Yam WC, Lin CS. Coordinated induction of two unrelated glucose-regulated protein genes by a calcium ionophore: human BiP/GRP78 and GAPDH. 1990;171:431-8.
    • Chao CC, Yam WC, Lin CS. Coordinated induction of two unrelated glucose-regulated protein genes by a calcium ionophore: human BiP/GRP78 and GAPDH. Biochem Biophys Res Commun 1990;171:431-8.
    • Biochem Biophys Res Commun
    • Chao, C.C.1
  • 57
    • 0017686105 scopus 로고    scopus 로고
    • Meldrum BS, Siesjö BK. Cerebral metabolic changes during prolonged epileptic seizures in rats. 1977;28:1025-35.
    • Chapman AG, Meldrum BS, Siesjö BK. Cerebral metabolic changes during prolonged epileptic seizures in rats. JNeurochem 1977;28:1025-35.
    • JNeurochem
    • Chapman, A.G.1
  • 58
    • 0022531954 scopus 로고    scopus 로고
    • Welch WJ, Schlossman DM, Palter KB, Schlesinger MJ, Rothman JE. Uncoating ATPase is a member of the 70 kilodalton family of stress proteins. 1986;45:3-13.
    • Chappell TG, Welch WJ, Schlossman DM, Palter KB, Schlesinger MJ, Rothman JE. Uncoating ATPase is a member of the 70 kilodalton family of stress proteins. Cell 1986;45:3-13.
    • Cell
    • Chappell, T.G.1
  • 59
    • 0026696593 scopus 로고    scopus 로고
    • Brion JP, Anderton BH. Human homologues of the bacterial heat shock protein DnaJ are preferentially expressed in neurons. 1992;284:469-76.
    • Cheetham ME, Brion JP, Anderton BH. Human homologues of the bacterial heat shock protein DnaJ are preferentially expressed in neurons. Biochem J 1992;284:469-76.
    • Biochem J
    • Cheetham, M.E.1
  • 60
    • 0028099817 scopus 로고    scopus 로고
    • Jackson AP, Anderton BH. Regulation of 70-kDa heat shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJla and HSJlb. 1994;226:99-107.
    • Cheetham ME, Jackson AP, Anderton BH. Regulation of 70-kDa heat shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJla and HSJlb. EurJ Biochem 1994;226:99-107.
    • EurJ Biochem
    • Cheetham, M.E.1
  • 62
    • 0024975155 scopus 로고    scopus 로고
    • Terlecky SR, Plant CP, Dice JF. A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. 1989;246:382-5.
    • Chiang H, Terlecky SR, Plant CP, Dice JF. A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 1989;246:382-5.
    • Science
    • Chiang, H.1
  • 63
    • 0024281421 scopus 로고    scopus 로고
    • Baldwin AS, Carthew RW, Sharp PA. Human CCAAT-binding proteins have heterologous subunits. 1988;53:11-24.
    • Chodosh LA, Baldwin AS, Carthew RW, Sharp PA. Human CCAAT-binding proteins have heterologous subunits. Cell 1988;53:11-24.
    • Cell
    • Chodosh, L.A.1
  • 64
    • 0026095265 scopus 로고    scopus 로고
    • Li B, Lin Z, Huang E, Liu AY. c AMP and cAMP-dependent protein kinase regulate the human heat shock protein 70 gene promoter activity. 1991 ;266:11858-65.
    • Choi HS, Li B, Lin Z, Huang E, Liu AY. cAMP and cAMP-dependent protein kinase regulate the human heat shock protein 70 gene promoter activity. J Biol Chem 1991 ;266:11858-65.
    • J Biol Chem
    • Choi, H.S.1
  • 65
    • 0024431368 scopus 로고    scopus 로고
    • Chen H, Ho KL, Dereski MO, Brown E, Hetzel FW, Welch KM. Transient hyperthermia protects against subsequent forebrain ischémie cell damage in the rat. 1989;39:1396-8.
    • Chopp M, Chen H, Ho KL, Dereski MO, Brown E, Hetzel FW, Welch KM. Transient hyperthermia protects against subsequent forebrain ischémie cell damage in the rat. Neurology 1989;39:1396-8.
    • Neurology
    • Chopp, M.1
  • 66
    • 0026068098 scopus 로고    scopus 로고
    • Li Y, Dereski MO, Levine SR, Yoshida Y, Garcia JH. Neuronal injury and expression of 72-kDa heat shock protein after forebrain ischemia in the rat. 1991;83:66-71.
    • Chopp M, Li Y, Dereski MO, Levine SR, Yoshida Y, Garcia JH. Neuronal injury and expression of 72-kDa heat shock protein after forebrain ischemia in the rat. Acta Neuropathol (Berl) 1991;83:66-71.
    • Acta Neuropathol (Berl)
    • Chopp, M.1
  • 67
    • 0028199673 scopus 로고    scopus 로고
    • Goldman C, Wen K-K, Tedeschi B, Castora FJ. Heat stress induces hsc70/nuclear topoisomerase 1 complex formation in vivo: evidence for hsc70-mediated, ATP-independent reactivation in vitro. 1994;91:1751-5.
    • Ciavarra RP, Goldman C, Wen K-K, Tedeschi B, Castora FJ. Heat stress induces hsc70/nuclear topoisomerase 1 complex formation in vivo: evidence for hsc70-mediated, ATP-independent reactivation in vitro. Proc Natl Acad Sei USA 1994;91:1751-5.
    • Proc Natl Acad Sei USA
    • Ciavarra, R.P.1
  • 68
    • 0028018268 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway. 1994;79:13-21.
    • Ciechanover A. The ubiquitin-proteasome proteolytic pathway. Cell 1994;79:13-21.
    • Cell
    • Ciechanover, A.1
  • 69
    • 85177151366 scopus 로고    scopus 로고
    • Shkedy D, Oren M, Bercovich B. Degradation of the tumor suppressor protein p53 by the ubiquitin-mediated proteolytic system requires a novel species of ubiquitin-carrier protein, E2. 1994;269:9582-9.
    • Ciechanover A, Shkedy D, Oren M, Bercovich B. Degradation of the tumor suppressor protein p53 by the ubiquitin-mediated proteolytic system requires a novel species of ubiquitin-carrier protein, E2. J Biol Chem 1994;269:9582-9.
    • J Biol Chem
    • Ciechanover, A.1
  • 70
    • 0027423102 scopus 로고    scopus 로고
    • Oesterreich S, Chamness GC, McGuire WL, Fuqua SA. Biological and clinical implications of heat shock protein 27,000 (Hsp27): a review. 11993;85:1558-70.
    • Ciocca DR, Oesterreich S, Chamness GC, McGuire WL, Fuqua SA. Biological and clinical implications of heat shock protein 27,000 (Hsp27): a review. JNC11993;85:1558-70.
    • JNC
    • Ciocca, D.R.1
  • 71
    • 0028333592 scopus 로고    scopus 로고
    • Hill MP, Gonzalez MF, Smalley S, Morton MT, Sharp FR. Whisker stimulation metabolically activates thalamus following cortical transplantation but not following cortical ablation. 1994;59:975-92.
    • Ciricillo SP, Hill MP, Gonzalez MF, Smalley S, Morton MT, Sharp FR. Whisker stimulation metabolically activates thalamus following cortical transplantation but not following cortical ablation. Neuroscience 1994;59:975-92.
    • Neuroscience
    • Ciricillo, S.P.1
  • 72
    • 0022300520 scopus 로고    scopus 로고
    • Meselson M. Separate regulatory elements for the heat-inducible and ovarian expression of the Drosophila hsp26 gene. 1985;43:737-46.
    • Cohen RS, Meselson M. Separate regulatory elements for the heat-inducible and ovarian expression of the Drosophila hsp26 gene. Cell 1985;43:737-46.
    • Cell
    • Cohen, R.S.1
  • 73
    • 0024298718 scopus 로고    scopus 로고
    • Meselson M. Periodic interactions of heat shock transcriptional elements. 1988;332:856-8.
    • Cohen RS, Meselson M. Periodic interactions of heat shock transcriptional elements. Nature 1988;332:856-8.
    • Nature
    • Cohen, R.S.1
  • 74
    • 0028127716 scopus 로고    scopus 로고
    • Hyman S, Swartz BE. The human brain GLUT! glucose transporter: ultrastructural localization to the blood-brain barrier endothelia. 1994; 14:106-12.
    • Cornford EM, Hyman S, Swartz BE. The human brain GLUT! glucose transporter: ultrastructural localization to the blood-brain barrier endothelia. J Cereb Blood Flow Metab 1994; 14:106-12.
    • J Cereb Blood Flow Metab
    • Cornford, E.M.1
  • 75
    • 0020700024 scopus 로고    scopus 로고
    • Brown IR. Heat shock protein in mammalian brain and other organs after a physiologically relevant increase in body temperature induced by D-lysergic acid diethylamide. 1983;80:569-73.
    • Cosgrove JW, Brown IR. Heat shock protein in mammalian brain and other organs after a physiologically relevant increase in body temperature induced by D-lysergic acid diethylamide. Proc NatlAcad Sei USA 1983;80:569-73.
    • Proc NatlAcad Sei USA
    • Cosgrove, J.W.1
  • 76
  • 77
    • 0027323456 scopus 로고    scopus 로고
    • Chaperones: helpers along the pathways to protein folding. 1993;260:1902-3.
    • Craig EA. Chaperones: helpers along the pathways to protein folding. Science 1993;260:1902-3.
    • Science
    • Craig, E.A.1
  • 79
    • 0028363670 scopus 로고    scopus 로고
    • Rubin GM. Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. 1994;77:1027-36.
    • Cutforth T, Rubin GM. Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. Cell 1994;77:1027-36.
    • Cell
    • Cutforth, T.1
  • 80
    • 0021864865 scopus 로고    scopus 로고
    • Paulin DJ. Translational activity of mRNA coding for cytoskeletal brain proteins in newborn and adult mice: a comparative study. 1985;44:1672-8.
    • Darmon MC, Paulin DJ. Translational activity of mRNA coding for cytoskeletal brain proteins in newborn and adult mice: a comparative study. J Neurochem 1985;44:1672-8.
    • J Neurochem
    • Darmon, M.C.1
  • 81
    • 0027238089 scopus 로고    scopus 로고
    • O'Neil BJ, Frisch C, Krause GS, Skjaerlund JM, White BC, Grossman LI. Studies of the protein synthesis system in the brain cortex during global ischemia and reperfusion. 1993;25:161-70.
    • DeGracia DJ, O'Neil BJ, Frisch C, Krause GS, Skjaerlund JM, White BC, Grossman LI. Studies of the protein synthesis system in the brain cortex during global ischemia and reperfusion. Resuscitation 1993;25:161-70.
    • Resuscitation
    • Degracia, D.J.1
  • 82
    • 0024557147 scopus 로고    scopus 로고
    • Yarchuk OB. Regulation of LacZ mRNA translatability in a cell-free system at heat shock by the last four sense codons. 1989;47:251-4.
    • Denisenko ON, Yarchuk OB. Regulation of LacZ mRNA translatability in a cell-free system at heat shock by the last four sense codons. FEES Lett 1989;47:251-4.
    • FEES Lett
    • Denisenko, O.N.1
  • 83
    • 0027359805 scopus 로고    scopus 로고
    • Graham DI, Teasdale GM, McCulloch J. Alz-50 and ubiquitin immunoreactivity is induced by permanent focal cerebral ischaemia in the cat. 1993;86:623-9.
    • Dewar D, Graham DI, Teasdale GM, McCulloch J. Alz-50 and ubiquitin immunoreactivity is induced by permanent focal cerebral ischaemia in the cat. Acta Neuropathol (Berl) 1993;86:623-9.
    • Acta Neuropathol (Berl)
    • Dewar, D.1
  • 84
    • 0022893623 scopus 로고    scopus 로고
    • Kiessling M, Jacewicz M, Pulsinelli WA. Synthesis of heat shock proteins in rat brain cortex after transient ischemia. 1986;6:505-10.
    • Dienel GA, Kiessling M, Jacewicz M, Pulsinelli WA. Synthesis of heat shock proteins in rat brain cortex after transient ischemia. J Cereb Blood Flow Metab 1986;6:505-10.
    • J Cereb Blood Flow Metab
    • Dienel, G.A.1
  • 85
    • 0027263325 scopus 로고    scopus 로고
    • DeNagel DC, Dahlseid JN, Green JM, Pierce SK. Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family. 1993;13:3598-610.
    • Domanico SZ, DeNagel DC, Dahlseid JN, Green JM, Pierce SK. Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family. Mol Cell Biol 1993;13:3598-610.
    • Mol Cell Biol
    • Domanico, S.Z.1
  • 86
    • 0023597393 scopus 로고    scopus 로고
    • Bole DG, Kaufrnan RJ. The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins. 1987;105:2665-74.
    • Dorner AJ, Bole DG, Kaufrnan RJ. The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins. J Cell Biol 1987;105:2665-74.
    • J Cell Biol
    • Dorner, A.J.1
  • 88
    • 0023264984 scopus 로고    scopus 로고
    • Lee AS, Resendez EJ, Steinhardt RA. Depletion of intracellular calcium stores by calcium ionophore A23187 induces the genes for glucose-regulated proteins in hamster fibroblasts. 1987;262:12801-5.
    • Drummond IA, Lee AS, Resendez EJ, Steinhardt RA. Depletion of intracellular calcium stores by calcium ionophore A23187 induces the genes for glucose-regulated proteins in hamster fibroblasts. J Biol Chem 1987;262:12801-5.
    • J Biol Chem
    • Drummond, I.A.1
  • 89
    • 0027972656 scopus 로고    scopus 로고
    • Antel JP, Freedman MS. Cytokine induction of heat shock protein expression in human oligodendrocytes: an interleukin-1-mediated mechanism. 1994;50:17-24.
    • D'Souza SD, Antel JP, Freedman MS. Cytokine induction of heat shock protein expression in human oligodendrocytes: an interleukin-1-mediated mechanism. J Neuroimmunol 1994;50:17-24.
    • J Neuroimmunol
    • D'Souza, S.D.1
  • 92
    • 0024565713 scopus 로고    scopus 로고
    • Nishimura RN, Brown IR. Synthesis of the major inducible heat shock protein in rat hippocampus after neonatal hypoxia-ischemia. 1989; 104:28-31.
    • Dwyer BE, Nishimura RN, Brown IR. Synthesis of the major inducible heat shock protein in rat hippocampus after neonatal hypoxia-ischemia. Exp Neural 1989; 104:28-31.
    • Exp Neural
    • Dwyer, B.E.1
  • 93
    • 0025730475 scopus 로고    scopus 로고
    • Nishimura RN, de Vellis J, Clegg KB. Regulation of heat shock protein synthesis in rat astrocytes. 1991;28:352-8.
    • Dwyer BE, Nishimura RN, de Vellis J, Clegg KB. Regulation of heat shock protein synthesis in rat astrocytes. J Neumsci Res 1991;28:352-8.
    • J Neumsci Res
    • Dwyer, B.E.1
  • 94
    • 0026479335 scopus 로고    scopus 로고
    • Nishimura RN, de Vellis J, Yoshida T. Heme oxygenase is a heat shock protein and PEST protein in rat astroglial cells. 1992;5:300-5.
    • Dwyer BE, Nishimura RN, de Vellis J, Yoshida T. Heme oxygenase is a heat shock protein and PEST protein in rat astroglial cells. Glia 1992;5:300-5.
    • Glia
    • Dwyer, B.E.1
  • 95
    • 0027472210 scopus 로고    scopus 로고
    • Pardridge WM. Developmental modulation of blood-brain barrier and choroid plexus GLUT1 glucose transporter messenger ribonucleic acid and immunoreactive protein in rabbits. 1993;132:558-65.
    • Dwyer KJ, Pardridge WM. Developmental modulation of blood-brain barrier and choroid plexus GLUT1 glucose transporter messenger ribonucleic acid and immunoreactive protein in rabbits. Endocrinology 1993;132:558-65.
    • Endocrinology
    • Dwyer, K.J.1
  • 96
    • 0025969686 scopus 로고    scopus 로고
    • Garcia MD, Pettingell W, Munro HN. Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron. 1991;88:688-92.
    • Eisenstein RS, Garcia MD, Pettingell W, Munro HN. Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron. Proc NatlAcad Sei USA 1991;88:688-92.
    • Proc NatlAcad Sei USA
    • Eisenstein, R.S.1
  • 97
    • 0026599856 scopus 로고    scopus 로고
    • Fehr SC, Donelson JE. Specific functional domains of mitochondrial hsp70s suggested by sequence comparison of the trypanosome and yeast proteins. 1992;51:153-5.
    • Engman DM, Fehr SC, Donelson JE. Specific functional domains of mitochondrial hsp70s suggested by sequence comparison of the trypanosome and yeast proteins. Mol Biochem Parasitai 1992;51:153-5.
    • Mol Biochem Parasitai
    • Engman, D.M.1
  • 98
    • 0025205259 scopus 로고    scopus 로고
    • Tomasovic SP. Affinity isolation of heat shock and other calmodulin-binding proteins following hyperthermia. 1990;124:50-6.
    • Evans DP, Tomasovic SP. Affinity isolation of heat shock and other calmodulin-binding proteins following hyperthermia. Radiât Res 1990;124:50-6.
    • Radiât Res
    • Evans, D.P.1
  • 99
    • 0026542512 scopus 로고    scopus 로고
    • Haber SN, Maines MD. Normal and heat-induced patterns of expression of heme oxygenase-1 (HSP32) in rat brain: hyperthermia causes rapid induction of mRNA and protein. 1992;58:1140-9.
    • Ewing JF, Haber SN, Maines MD. Normal and heat-induced patterns of expression of heme oxygenase-1 (HSP32) in rat brain: hyperthermia causes rapid induction of mRNA and protein. J Neurochem 1992;58:1140-9.
    • J Neurochem
    • Ewing, J.F.1
  • 100
    • 0026012324 scopus 로고    scopus 로고
    • Maines MD. Rapid induction of heme oxygenase 1 mRNA and protein by hyperthermia in rat brain: heme oxygenase 2 is not a heat shock protein. 1991 ;88:5364-8.
    • Ewing JF, Maines MD. Rapid induction of heme oxygenase 1 mRNA and protein by hyperthermia in rat brain: heme oxygenase 2 is not a heat shock protein. Proc NatlAcad Sei USA 1991 ;88:5364-8.
    • Proc NatlAcad Sei USA
    • Ewing, J.F.1
  • 101
    • 0027523219 scopus 로고    scopus 로고
    • Maines MD. Glutathione depletion induces heme oxygenase-1 (HSP32) mRNA and protein in rat brain. 1993;60:1512-9.
    • Ewing JF, Maines MD. Glutathione depletion induces heme oxygenase-1 (HSP32) mRNA and protein in rat brain. J Neurochem 1993;60:1512-9.
    • J Neurochem
    • Ewing, J.F.1
  • 103
    • 0026675224 scopus 로고    scopus 로고
    • Boado RJ, Pardridge WM. Enhanced GLUT1 glucose transporter and cytoskeleton gene expression in cultured bovine brain capillary endothelial cells after treatment with phorbol esters and serum. 1992;15:221-6.
    • Farrell CR, Boado RJ, Pardridge WM. Enhanced GLUT1 glucose transporter and cytoskeleton gene expression in cultured bovine brain capillary endothelial cells after treatment with phorbol esters and serum. Brain Res Mol Brain Res 1992;15:221-6.
    • Brain Res Mol Brain Res
    • Farrell, C.R.1
  • 104
    • 0025272645 scopus 로고    scopus 로고
    • Soberano HQ, Simon RP, Sharp FR. Hypoxia-ischemia induces heat shock protein-like (HSP72) immunoreactivity in neonatal rat brain. 1990;53:145-50.
    • Fernere DM, Soberano HQ, Simon RP, Sharp FR. Hypoxia-ischemia induces heat shock protein-like (HSP72) immunoreactivity in neonatal rat brain. Brain Res Dev Brain Res 1990;53:145-50.
    • Brain Res Dev Brain Res
    • Fernere, D.M.1
  • 105
    • 0021720349 scopus 로고    scopus 로고
    • Falcioni R, Delpino A, Cavalière R, Zupi G, Natali PG. Heat shock proteins produced by two human melanoma cell lines: absence of correlation with thermosensitivity. 1984:34:651-5.
    • Ferrini U, Falcioni R, Delpino A, Cavalière R, Zupi G, Natali PG. Heat shock proteins produced by two human melanoma cell lines: absence of correlation with thermosensitivity. Int J Cancer 1984:34:651-5.
    • Int J Cancer
    • Ferrini, U.1
  • 106
    • 0027521274 scopus 로고    scopus 로고
    • Horn JW, Wightman KA, Johnson CA, Long GG, Storts RW, Farber N, Wozniak DF, Olney JW. Neuronal vacuolization and necrosis induced by the noncompetitive /V-methyl-D-aspartate (NMDA) antagonist MK(+)801 (dizocilpine maleate): a light and electron microscopic evaluation of the rat retrosplenial cortex. 1993;123:204-15.
    • Fix AS, Horn JW, Wightman KA, Johnson CA, Long GG, Storts RW, Farber N, Wozniak DF, Olney JW. Neuronal vacuolization and necrosis induced by the noncompetitive /V-methyl-D-aspartate (NMDA) antagonist MK(+)801 (dizocilpine maleate): a light and electron microscopic evaluation of the rat retrosplenial cortex. Exp Neural 1993;123:204-15.
    • Exp Neural
    • Fix, A.S.1
  • 107
    • 0024393778 scopus 로고    scopus 로고
    • Chappell TG, Rothman JE. Peptide binding and release by proteins implicated as catalysts of protein assembly. 1989;245:385-90.
    • Flynn GC, Chappell TG, Rothman JE. Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 1989;245:385-90.
    • Science
    • Flynn, G.C.1
  • 108
    • 0028015872 scopus 로고    scopus 로고
    • Rawlinson L, Guesdon F, Jones E, Cowley S, Hsuan J, Saklatvala J. Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of Hsp27. 1994;78:1039-49.
    • Freshney NW, Rawlinson L, Guesdon F, Jones E, Cowley S, Hsuan J, Saklatvala J. Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of Hsp27. Cell 1994;78:1039-49.
    • Cell
    • Freshney, N.W.1
  • 109
    • 0022552149 scopus 로고    scopus 로고
    • McCammon K, Sambrook J. Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport. 1986;46:939-50.
    • Gething MJ, McCammon K, Sambrook J. Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport. Cell 1986;46:939-50.
    • Cell
    • Gething, M.J.1
  • 110
    • 0026584271 scopus 로고    scopus 로고
    • Sambrook J. Protein folding in the cell. 1992;355:33-45.
    • Gething MJ, Sambrook J. Protein folding in the cell. Nature 1992;355:33-45.
    • Nature
    • Gething, M.J.1
  • 111
    • 0026777132 scopus 로고    scopus 로고
    • Auger EA, Koong A, Terris DJ, Minchinton AI, Hahn GM, Brown JM. Activation of the heat shock transcription factor by hypoxia in normal and tumor cell lines in vivo and in vitro. 1992:23:891-7.
    • Giaccia AJ, Auger EA, Koong A, Terris DJ, Minchinton AI, Hahn GM, Brown JM. Activation of the heat shock transcription factor by hypoxia in normal and tumor cell lines in vivo and in vitro. Int J Radiât Oncol Ao/PAys 1992:23:891-7.
    • Int J Radiât Oncol Ao/PAys
    • Giaccia, A.J.1
  • 112
    • 0026089183 scopus 로고    scopus 로고
    • Murray AW, Kirschner MW. Cyclin is degraded by the ubiquitin pathway. 1991;349: 132-8.
    • Glotzer M, Murray AW, Kirschner MW. Cyclin is degraded by the ubiquitin pathway. Nature 1991;349: 132-8.
    • Nature
    • Glotzer, M.1
  • 113
    • 0026113376 scopus 로고    scopus 로고
    • Luna M, Ferrario A, Rucker N. Increased transcription and translation of heme oxygenase in Chinese hamster fibroblasts following photodynamic stress or Photofrin II incubation. 1991:53:275-9.
    • Gomer CJ, Luna M, Ferrario A, Rucker N. Increased transcription and translation of heme oxygenase in Chinese hamster fibroblasts following photodynamic stress or Photofrin II incubation. Photochem Photobiol 1991:53:275-9.
    • Photochem Photobiol
    • Gomer, C.J.1
  • 114
    • 0025007697 scopus 로고    scopus 로고
    • Rucker N, Wong S. Porphyrin photosensitivity in cell lines expressing a heat-resistant phenotype. 1990;50:5365-8.
    • Gomer CJ, Rucker N, Wong S. Porphyrin photosensitivity in cell lines expressing a heat-resistant phenotype. Cancer Res 1990;50:5365-8.
    • Cancer Res
    • Gomer, C.J.1
  • 115
    • 0025976586 scopus 로고    scopus 로고
    • Lowenstein D, Fernyak S, Hisanaga K, Simon R, Sharp FR. Induction of heat shock protein 72-like immunoreactivity in the hippocampal formation following transient global ischemia. 1991;26:241-50.
    • Gonzalez MF, Lowenstein D, Fernyak S, Hisanaga K, Simon R, Sharp FR. Induction of heat shock protein 72-like immunoreactivity in the hippocampal formation following transient global ischemia. Brain Res Bull 1991;26:241-50.
    • Brain Res Bull
    • Gonzalez, M.F.1
  • 116
    • 0024376193 scopus 로고    scopus 로고
    • Shiraishi K, Hisanaga K, Sagar SM, Mandabach M, Sharp FR. Heat shock proteins as markers of neural injury. 1989;6:93-100.
    • Gonzalez MF, Shiraishi K, Hisanaga K, Sagar SM, Mandabach M, Sharp FR. Heat shock proteins as markers of neural injury. Brain Res Mol Brain Res 1989;6:93-100.
    • Brain Res Mol Brain Res
    • Gonzalez, M.F.1
  • 117
    • 0027531309 scopus 로고    scopus 로고
    • Chen J, Sharp FR, Simon RP. Limiting ischémie injury by inhibition of excitatory amino acid release. 1993:13:88-97.
    • Graham SH, Chen J, Sharp FR, Simon RP. Limiting ischémie injury by inhibition of excitatory amino acid release. J Cereb Blood Flow Metab 1993:13:88-97.
    • J Cereb Blood Flow Metab
    • Graham, S.H.1
  • 118
    • 0021076098 scopus 로고    scopus 로고
    • Wabl M. Immunoglobulin heavy chain binding protein. 1983;306:387-9.
    • Haas IG, Wabl M. Immunoglobulin heavy chain binding protein. Nature 1983;306:387-9.
    • Nature
    • Haas, I.G.1
  • 119
    • 0027294037 scopus 로고    scopus 로고
    • Rigby M, Smith D, Hill RG. Lack of effect of L-687,414 ((+)-cis-4-methyl-HA-966), an NMDA receptor antagonist acting at the glycine site, on cerebral glucose metabolism and cortical neuronal morphology. 1993;! 10:36-42.
    • Hargreaves RJ, Rigby M, Smith D, Hill RG. Lack of effect of L-687,414 ((+)-cis-4-methyl-HA-966), an NMDA receptor antagonist acting at the glycine site, on cerebral glucose metabolism and cortical neuronal morphology. Br JPharmacol 1993;! 10:36-42.
    • Br JPharmacol
    • Hargreaves, R.J.1
  • 120
    • 0027427150 scopus 로고    scopus 로고
    • Rigby M, Smith D, Hill RG, Iversen LL. Competitive as well as uncompetitive /V-methyl-Daspartate receptor antagonists affect cortical neuronal morphology and cerebral glucose metabolism. 1993;18:1263-9.
    • Hargreaves RJ, Rigby M, Smith D, Hill RG, Iversen LL. Competitive as well as uncompetitive /V-methyl-Daspartate receptor antagonists affect cortical neuronal morphology and cerebral glucose metabolism. NeurochemRes 1993;18:1263-9.
    • NeurochemRes
    • Hargreaves, R.J.1
  • 121
    • 0027958045 scopus 로고    scopus 로고
    • Bohm AA, Nelson HC. Crystal structure of the DNA binding domain of the heat shock transcription factor. 1994;263:224-7.
    • Harrison CJ, Bohm AA, Nelson HC. Crystal structure of the DNA binding domain of the heat shock transcription factor. Science 1994;263:224-7.
    • Science
    • Harrison, C.J.1
  • 122
    • 0023179598 scopus 로고    scopus 로고
    • Drabkin HA, Kao FT, Hartz J, Hart IM, Chu EH, Wu BJ, Morimoto RI. Chromosomal location of human genes encoding major heat shock protein HSP70. 1987;13:119-30.
    • Harrison OS, Drabkin HA, Kao FT, Hartz J, Hart IM, Chu EH, Wu BJ, Morimoto RI. Chromosomal location of human genes encoding major heat shock protein HSP70. Somatic Cell Mol Genet 1987;13:119-30.
    • Somatic Cell Mol Genet
    • Harrison, O.S.1
  • 123
    • 0026773208 scopus 로고    scopus 로고
    • Martin J, Neupert W. Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60. 1992;21:293-322.
    • Hartl FU, Martin J, Neupert W. Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60. Annu Rev Biophys Biomol Struct 1992;21:293-322.
    • Annu Rev Biophys Biomol Struct
    • Hartl, F.U.1
  • 124
    • 0027451554 scopus 로고    scopus 로고
    • Asai Y, Wakatsuki T, Kitamura T, Imahara H. Regulation of hsp70 induction in thermotolerant HeLa cells. 1993;! 179:109-16.
    • Hatayama T, Asai Y, Wakatsuki T, Kitamura T, Imahara H. Regulation of hsp70 induction in thermotolerant HeLa cells. Biochim Biophys Acta 1993;! 179:109-16.
    • Biochim Biophys Acta
    • Hatayama, T.1
  • 125
    • 0026323448 scopus 로고    scopus 로고
    • Takada K, Matsuda M. Changes in ubiquitin and ubiquitin-protein conjugates in the CA, neurons after transient sublethal ischemia. 1991:15:75-82.
    • Hayashi T, Takada K, Matsuda M. Changes in ubiquitin and ubiquitin-protein conjugates in the CA, neurons after transient sublethal ischemia. Mol Chem Neuropalhol 1991:15:75-82.
    • Mol Chem Neuropalhol
    • Hayashi, T.1
  • 126
    • 0026663450 scopus 로고    scopus 로고
    • Takada K, Matsuda M. Post-transient ischemia increase in ubiquitin conjugates in the early reperfusion. 1992;3:519-20.
    • Hayashi T, Takada K, Matsuda M. Post-transient ischemia increase in ubiquitin conjugates in the early reperfusion. Neuroreport 1992;3:519-20.
    • Neuroreport
    • Hayashi, T.1
  • 127
    • 0026665665 scopus 로고    scopus 로고
    • Takada K, Matsuda M. Subcellular distribution of ubiquitin-protein conjugates in the hippocampus following transient ischemia. 1992;31:561-4.
    • Hayashi T, Takada K, Matsuda M. Subcellular distribution of ubiquitin-protein conjugates in the hippocampus following transient ischemia. J Neurosci Res 1992;31:561-4.
    • J Neurosci Res
    • Hayashi, T.1
  • 128
    • 0027162520 scopus 로고    scopus 로고
    • Tanaka J, Kamikubo T, Takada K, Matsuda M. Increase in ubiquitin conjugates dependent on ischémie damage. 1993;620:171-3.
    • Hayashi T, Tanaka J, Kamikubo T, Takada K, Matsuda M. Increase in ubiquitin conjugates dependent on ischémie damage. Brain Res 1993;620:171-3.
    • Brain Res
    • Hayashi, T.1
  • 129
    • 0027968222 scopus 로고    scopus 로고
    • Corbin E, Goldman JE. Coordinate and independent regulation of alpha B-crystallin and hsp27 expression in response to physiological stress. 1994; 159:41-50.
    • Head MW, Corbin E, Goldman JE. Coordinate and independent regulation of alpha B-crystallin and hsp27 expression in response to physiological stress. J Cell Physiol 1994; 159:41-50.
    • J Cell Physiol
    • Head, M.W.1
  • 130
    • 0023684672 scopus 로고    scopus 로고
    • Ting J, Lee AS. Identity of the immunoglobulin heavy-chain-binding protein with the 78,000dalton glucose-regulated protein and the role of posttranslational modifications in its binding function. 1988:8:4250-6.
    • Hendershot LM, Ting J, Lee AS. Identity of the immunoglobulin heavy-chain-binding protein with the 78,000dalton glucose-regulated protein and the role of posttranslational modifications in its binding function. Mol CellBiol 1988:8:4250-6.
    • Mol CellBiol
    • Hendershot, L.M.1
  • 131
    • 0028198372 scopus 로고    scopus 로고
    • Valentine VA, Lee AS, Morris SW, Shapiro DN. Localization of the gene encoding human BJP/GRP78, the endoplasmic reticulum cognate of the HSP70 family, to chromosome 9q34. 1994;20:281-4.
    • Hendershot LM, Valentine VA, Lee AS, Morris SW, Shapiro DN. Localization of the gene encoding human BJP/GRP78, the endoplasmic reticulum cognate of the HSP70 family, to chromosome 9q34. Genomics 1994;20:281-4.
    • Genomics
    • Hendershot, L.M.1
  • 132
    • 0027184721 scopus 로고    scopus 로고
    • Hartl FU. Molecular chaperone functions of heat shock proteins. 1993;62:349-84.
    • Hendrick JP, Hartl FU. Molecular chaperone functions of heat shock proteins. Annu Rev Biochem 1993;62:349-84.
    • Annu Rev Biochem
    • Hendrick, J.P.1
  • 133
    • 0027936558 scopus 로고    scopus 로고
    • Heng MC. Heat shock protein 65 and activated gamma/delta T cells in injured arteries. 1994:44:921-3.
    • Heng MK, Heng MC. Heat shock protein 65 and activated gamma/delta T cells in injured arteries. Lancet 1994:44:921-3.
    • Lancet
    • Heng, M.K.1
  • 134
    • 0025208339 scopus 로고    scopus 로고
    • Hunt CR, Calderwood SK, Housman DE, Kingston RE. DNA binding of heat shock factor to the heat shock element is insufficient for transcriptional activation in murine erythroleukemia cells. 1990:10:1600-8.
    • Hensold JO, Hunt CR, Calderwood SK, Housman DE, Kingston RE. DNA binding of heat shock factor to the heat shock element is insufficient for transcriptional activation in murine erythroleukemia cells. Mol Cell Biol 1990:10:1600-8.
    • Mol Cell Biol
    • Hensold, J.O.1
  • 135
    • 0022508113 scopus 로고    scopus 로고
    • Brandon SE, Sadis S, Smale G, Weber LA. Molecular cloning of sequences encoding the human heat shock proteins and their expression during hyperthermia. 1986;43:147-54.
    • Hickey E, Brandon SE, Sadis S, Smale G, Weber LA. Molecular cloning of sequences encoding the human heat shock proteins and their expression during hyperthermia. Gene 1986;43:147-54.
    • Gene
    • Hickey, E.1
  • 136
    • 0028229757 scopus 로고    scopus 로고
    • Takechi H, Uemura Y, Kikuchi H, Nagata K. Differential induction of mRNA species encoding several classes of stress proteins following focal cerebral ischemia in rats. 1994:650:239-418.
    • Higashi T, Takechi H, Uemura Y, Kikuchi H, Nagata K. Differential induction of mRNA species encoding several classes of stress proteins following focal cerebral ischemia in rats. Brain Res 1994:650:239-418.
    • Brain Res
    • Higashi, T.1
  • 137
    • 0026532253 scopus 로고    scopus 로고
    • Carlson SG, Choi AM, Fargnoli J. Induction of HSP70 gene expression by the antiproliferative prostaglandin PGA2: a growth-dependent response mediated by activation of heat shock transcription factor. 1992:12:1528-34.
    • Holbrook NJ, Carlson SG, Choi AM, Fargnoli J. Induction of HSP70 gene expression by the antiproliferative prostaglandin PGA2: a growth-dependent response mediated by activation of heat shock transcription factor. Mol Cell Biol 1992:12:1528-34.
    • Mol Cell Biol
    • Holbrook, N.J.1
  • 138
    • 0027051672 scopus 로고    scopus 로고
    • Sy J, Bradshaw RA, Arfin SM. Dipeptide inhibitors of ubiquitin-mediated protein turnover prevent growth factor-induced neurite outgrowth in rat pheochromocytoma PC 12 cells. 1992; 189:280-8.
    • Hondermarck H, Sy J, Bradshaw RA, Arfin SM. Dipeptide inhibitors of ubiquitin-mediated protein turnover prevent growth factor-induced neurite outgrowth in rat pheochromocytoma PC 12 cells. Biochem Biophys Res Commun 1992; 189:280-8.
    • Biochem Biophys Res Commun
    • Hondermarck, H.1
  • 139
    • 0027298139 scopus 로고    scopus 로고
    • Disturbances of cerebral protein synthesis and ischémie cell death. 1993:96:161-77.
    • Hossmann K-A. Disturbances of cerebral protein synthesis and ischémie cell death. Prog Brain Res 1993:96:161-77.
    • Prog Brain Res
    • Hossmann, K.-A.1
  • 140
    • 0027760815 scopus 로고    scopus 로고
    • Ischemia-mediated neuronal injury. 1993:26:225-35.
    • Hossmann K-A. Ischemia-mediated neuronal injury. Resuscitation 1993:26:225-35.
    • Resuscitation
    • Hossmann, K.-A.1
  • 141
    • 0027715708 scopus 로고    scopus 로고
    • Nunnally I, Lindquist S, Taulien J, Perdrizet G, Karl I. Hyperthermia protects mice against the lethal effects of endotoxin. 1993;256:R1447-57.
    • Hotchkiss R, Nunnally I, Lindquist S, Taulien J, Perdrizet G, Karl I. Hyperthermia protects mice against the lethal effects of endotoxin. Am J Physio! 1993;256:R1447-57.
    • Am J Physio!
    • Hotchkiss, R.1
  • 142
    • 0027459409 scopus 로고    scopus 로고
    • Shen CH, Lee WC, Lai YK. Okadaic acid as an inducer of the 78-kDa glucose-regulated protein in 9L rat brain tumor cells. 1993;51:91-101.
    • Hou MC, Shen CH, Lee WC, Lai YK. Okadaic acid as an inducer of the 78-kDa glucose-regulated protein in 9L rat brain tumor cells. J Cell Biochem 1993;51:91-101.
    • J Cell Biochem
    • Hou, M.C.1
  • 143
    • 0027476419 scopus 로고    scopus 로고
    • Wieloch T. Stress-induced inhibition of protein synthesis initiation: modulation of initiation factor 2 and guanine nucleotide exchange factor activities following transient cerebral ischemia in the rat. 1993:13:1830-8.
    • Hu BR, Wieloch T. Stress-induced inhibition of protein synthesis initiation: modulation of initiation factor 2 and guanine nucleotide exchange factor activities following transient cerebral ischemia in the rat. J Neurosci 1993:13:1830-8.
    • J Neurosci
    • Hu, B.R.1
  • 144
    • 0025988318 scopus 로고    scopus 로고
    • Roy G, Lambert H, Chrétien P, Landry J. Increased survival after treatments with anticancer agents of Chinese hamster cells expressing the human Mr 27,000 heat shock protein. 1991;51:5245-52.
    • Huot J, Roy G, Lambert H, Chrétien P, Landry J. Increased survival after treatments with anticancer agents of Chinese hamster cells expressing the human Mr 27,000 heat shock protein. Cancer Res 1991;51:5245-52.
    • Cancer Res
    • Huot, J.1
  • 145
    • 0024400060 scopus 로고    scopus 로고
    • Bole DG, Hoover LH, Helenius A, Copeland CS. Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). 1989; 108:2117-26.
    • Hurtley SM, Bole DG, Hoover LH, Helenius A, Copeland CS. Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J Cell Biol 1989; 108:2117-26.
    • J Cell Biol
    • Hurtley, S.M.1
  • 146
    • 0028181755 scopus 로고    scopus 로고
    • Takahashi K, Katada T. Association of the beta gamma subunits of trimeric GTP-binding proteins with 90-kDa heat shock protein. hsp90. 1994; 115:486-92.
    • Inanobe A, Takahashi K, Katada T. Association of the beta gamma subunits of trimeric GTP-binding proteins with 90-kDa heat shock protein. hsp90. J Biochem (Tokyo) 1994; 115:486-92.
    • J Biochem (Tokyo)
    • Inanobe, A.1
  • 147
    • 0027524138 scopus 로고    scopus 로고
    • Tashima Y, Eishi Y, Okeda R. Localization of HSP90 in rat brain. 1993;25:93-9.
    • Itoh H, Tashima Y, Eishi Y, Okeda R. Localization of HSP90 in rat brain. Int J Biochem 1993;25:93-9.
    • Int J Biochem
    • Itoh, H.1
  • 148
    • 0025085532 scopus 로고    scopus 로고
    • Toyoshima I, Mizunuma H, Kobayashi R, Tashima Y. Three-step purification method and characterization of the bovine brain 90-kDa heat shock protein. 1990;282:290-6.
    • Itoh H, Toyoshima I, Mizunuma H, Kobayashi R, Tashima Y. Three-step purification method and characterization of the bovine brain 90-kDa heat shock protein. Arch Biochem Biophvs 1990;282:290-6.
    • Arch Biochem Biophvs
    • Itoh, H.1
  • 149
    • 0027238595 scopus 로고    scopus 로고
    • Chi SH, Dillmann WH, Mestril R. Induction of HSP70 in cultured rat neonatal cardiomyocytes by hypoxia and metabolic stress. 1993;87:2023-32.
    • Iwaki K, Chi SH, Dillmann WH, Mestril R. Induction of HSP70 in cultured rat neonatal cardiomyocytes by hypoxia and metabolic stress. Circulation 1993;87:2023-32.
    • Circulation
    • Iwaki, K.1
  • 150
    • 85177144798 scopus 로고    scopus 로고
    • Iwaki A, Tateishi J, Goldman JE. Sense and antisense modification of glial alpha B-crystallin production results in alterations of stress fiber formation and thermoresistance. 1994:125:1385-93.
    • Iwaki T, Iwaki A, Tateishi J, Goldman JE. Sense and antisense modification of glial alpha B-crystallin production results in alterations of stress fiber formation and thermoresistance. J Cell Biol 1994:125:1385-93.
    • J Cell Biol
    • Iwaki, T.1
  • 151
    • 0027742866 scopus 로고    scopus 로고
    • Iwaki A, Tateishi J, Sakaki Y, Goldman JE. Alpha B-crystallin and 27-kd heat shock protein are regulated by stress conditions in the central nervous system and accumulate in Rosenthal fibers. 1993:143:487-95.
    • Iwaki T, Iwaki A, Tateishi J, Sakaki Y, Goldman JE. Alpha B-crystallin and 27-kd heat shock protein are regulated by stress conditions in the central nervous system and accumulate in Rosenthal fibers. Am J Pathol 1993:143:487-95.
    • Am J Pathol
    • Iwaki, T.1
  • 154
    • 0022547814 scopus 로고    scopus 로고
    • Kiessling M, Pulsinelli WA. Selective gene expression in focal cerebral ischemia. 1986:6:263-72.
    • Jacewicz M, Kiessling M, Pulsinelli WA. Selective gene expression in focal cerebral ischemia. J Cereb Blood FlowMetab 1986:6:263-72.
    • J Cereb Blood FlowMetab
    • Jacewicz, M.1
  • 155
    • 0028284571 scopus 로고    scopus 로고
    • Buchner J. Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones. 1994; 19:205-11.
    • Jakob U, Buchner J. Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones. Trends Biochem Sei 1994; 19:205-11.
    • Trends Biochem Sei
    • Jakob, U.1
  • 156
    • 0027391629 scopus 로고    scopus 로고
    • Gaestel M, Engel K, Buchner J. Small heat shock proteins are molecular chaperones. 1993;268:1517-20.
    • Jakob U, Gaestel M, Engel K, Buchner J. Small heat shock proteins are molecular chaperones. J Biol Chem 1993;268:1517-20.
    • J Biol Chem
    • Jakob, U.1
  • 158
    • 0027113344 scopus 로고    scopus 로고
    • Sistonen L, Kroes RA, Morimoto RI. Effect of sodium salicylate on the human heat shock response. 1992;255:1243-5.
    • Jurivich DA, Sistonen L, Kroes RA, Morimoto RI. Effect of sodium salicylate on the human heat shock response. Science 1992;255:1243-5.
    • Science
    • Jurivich, D.A.1
  • 163
    • 0027181247 scopus 로고    scopus 로고
    • ChenT, Liu XH, Nakata N, Kogure K. Immunohistochemical localization of ubiquitin in gerbil hippocampus with induced tolerance to ischemia. 1993;619:339-43.
    • Kalo H, ChenT, Liu XH, Nakata N, Kogure K. Immunohistochemical localization of ubiquitin in gerbil hippocampus with induced tolerance to ischemia. Bruin Rex 1993;619:339-43.
    • Bruin Rex
    • Kalo, H.1
  • 164
    • 0027231612 scopus 로고    scopus 로고
    • Liu XH, Nakata N, Kogure K. Immunohistochemical visualization of heat shock protein-70 in the gerbil hippocampus following repeated brief cerebral ischemia. 1993:615:240-44.
    • Kato H, Liu XH, Nakata N, Kogure K. Immunohistochemical visualization of heat shock protein-70 in the gerbil hippocampus following repeated brief cerebral ischemia. Brain Res 1993:615:240-44.
    • Brain Res
    • Kato, H.1
  • 165
    • 0026608622 scopus 로고    scopus 로고
    • LiuY, ArakiT, Kogure K. MK-801, but not anisomycin, inhibits the induction of tolerance to ischemia in the gerbil hippocampus. 1992; 139:118-21.
    • Kato H, LiuY, ArakiT, Kogure K. MK-801, but not anisomycin, inhibits the induction of tolerance to ischemia in the gerbil hippocampus. Neurosci Lett 1992; 139:118-21.
    • Neurosci Lett
    • Kato, H.1
  • 166
    • 0028144647 scopus 로고    scopus 로고
    • LiuY, Kogure K, Kato K. Induction of 27-kDa heat shock protein following cerebral ischemia in a rat model of ischémie tolerance. 1994:634:235-44.
    • Kato H, LiuY, Kogure K, Kato K. Induction of 27-kDa heat shock protein following cerebral ischemia in a rat model of ischémie tolerance. Brain Res 1994:634:235-44.
    • Brain Res
    • Kato, H.1
  • 168
    • 0027055868 scopus 로고    scopus 로고
    • Abe K, Kogure K. Different thresholds of HSP70 and HSC70 heat shock mRNA induction in post-ischemic gerbil brain. 1992:599:197-203.
    • Kawagoe J, Abe K, Kogure K. Different thresholds of HSP70 and HSC70 heat shock mRNA induction in post-ischemic gerbil brain. Brain Rex 1992:599:197-203.
    • Brain Rex
    • Kawagoe, J.1
  • 170
    • 0027309545 scopus 로고    scopus 로고
    • Abe K, Kogure K. Regional difference of HSP70 and HSC70 heat shock mRNA inductions in rat hippocampus after transient global ischemia. 1993; 153:165-8.
    • Kawagoe J, Abe K, Kogure K. Regional difference of HSP70 and HSC70 heat shock mRNA inductions in rat hippocampus after transient global ischemia. Neurosci Lett 1993; 153:165-8.
    • Neurosci Lett
    • Kawagoe, J.1
  • 171
    • 0026779186 scopus 로고    scopus 로고
    • Abe K, Sato S, Nagano I, Nakamura S, Kogure K. Distributions of heat shock protein (HSP) 70 and heat shock cognate protein (HSC) 70 mRNAs after transient focal ischemia in rat brain. 1992:587:195-202.
    • Kawagoe J, Abe K, Sato S, Nagano I, Nakamura S, Kogure K. Distributions of heat shock protein (HSP) 70 and heat shock cognate protein (HSC) 70 mRNAs after transient focal ischemia in rat brain. Brain Res 1992:587:195-202.
    • Brain Res
    • Kawagoe, J.1
  • 173
    • 0023922806 scopus 로고    scopus 로고
    • Hoover RL, Karnovsky MJ. Effects of hyperthermia on cell survival and patterns of protein synthesis in endothelial cells from different origins. 1988;48:2101-6.
    • Ketis NV, Hoover RL, Karnovsky MJ. Effects of hyperthermia on cell survival and patterns of protein synthesis in endothelial cells from different origins. Cancer Res 1988;48:2101-6.
    • Cancer Res
    • Ketis, N.V.1
  • 174
    • 0027741433 scopus 로고    scopus 로고
    • Lawler J, Bendena WG. Extracellular matrix components affect the pattern of protein synthesis of endothelial cells responding to hyperthermia. 1993;29A:768-72.
    • Ketis NV, Lawler J, Bendena WG. Extracellular matrix components affect the pattern of protein synthesis of endothelial cells responding to hyperthermia. In Vitro Cell Dev Biol Anim 1993;29A:768-72.
    • In Vitro Cell Dev Biol Anim
    • Ketis, N.V.1
  • 175
    • 0024514829 scopus 로고    scopus 로고
    • Sotelo J. Heat shock stress is deleterious to CNS cultured neurons microinjected with anti-HSP70 antibodies. 1989;65:I99-202.
    • Khan NA, Sotelo J. Heat shock stress is deleterious to CNS cultured neurons microinjected with anti-HSP70 antibodies. Biol Cell 1989;65:I99-202.
    • Biol Cell
    • Khan, N.A.1
  • 176
    • 0025348378 scopus 로고    scopus 로고
    • Kirn YK, Lee AS. Expression of the glucose-regulated proteins (GRP94 and GRP78) in differentiated and undifferentiated mouse embryonic cells and the use of the GRP78 promoter as an expression system in embryonic cells. 1990;42:153-9.
    • Kim SK, Kirn YK, Lee AS. Expression of the glucose-regulated proteins (GRP94 and GRP78) in differentiated and undifferentiated mouse embryonic cells and the use of the GRP78 promoter as an expression system in embryonic cells. Differentiation 1990;42:153-9.
    • Differentiation
    • Kim, S.K.1
  • 177
    • 0027223296 scopus 로고    scopus 로고
    • Inhibition of tyrosine phosphorylation prevents delayed neuronal death following cerebral ischemia. 1993; 13:372-7.
    • Kindy MS. Inhibition of tyrosine phosphorylation prevents delayed neuronal death following cerebral ischemia. J Cereb Blood Flow Metab 1993; 13:372-7.
    • J Cereb Blood Flow Metab
    • Kindy, M.S.1
  • 178
    • 0027994103 scopus 로고    scopus 로고
    • Sharp FR, Chan PH, Koistinaho J, Sagar SM, Yoshimoto T. Induction of c-fos, junB, c-jun, and hsp70 mRNA in cortex, thalamus, basal ganglia, and hippocampus following middle cerebral artery occlusion. 1994; 14:808-17.
    • Kinouchi H, Sharp FR, Chan PH, Koistinaho J, Sagar SM, Yoshimoto T. Induction of c-fos, junB, c-jun, and hsp70 mRNA in cortex, thalamus, basal ganglia, and hippocampus following middle cerebral artery occlusion. J Cereb Blood Flow Metab 1994; 14:808-17.
    • J Cereb Blood Flow Metab
    • Kinouchi, H.1
  • 179
    • 0028169828 scopus 로고    scopus 로고
    • Sharp FR, Chan PH, Mikawa S, Kamii H, Aral S, Yoshimoto T. MK801 inhibits the induction of immediate early genes in cortex, hippocampus but not in the
    • Kinouchi H, Sharp FR, Chan PH, Mikawa S, Kamii H, Aral S, Yoshimoto T. MK801 inhibits the induction of immediate early genes in cortex, hippocampus but not in the substantia nigra following middle cerebral artery occlusion. Neurosci Lett 1994; 179:111-4.
    • Neurosci Lett
    • Kinouchi, H.1
  • 180
    • 0027492357 scopus 로고    scopus 로고
    • Sharp FR, Hill MR Koistinaho J, Sagar SM, Chan PH. Induction of 70-kDa heat shock protein and hsp70 mRNA following transient focal cerebral ischemia in the rat. 1993;13:105-15.
    • Kinouchi H, Sharp FR, Hill MR Koistinaho J, Sagar SM, Chan PH. Induction of 70-kDa heat shock protein and hsp70 mRNA following transient focal cerebral ischemia in the rat. J Cereb Blood Flow Metab 1993;13:105-15.
    • J Cereb Blood Flow Metab
    • Kinouchi, H.1
  • 181
    • 0027320667 scopus 로고    scopus 로고
    • Sharp FR, Koistinaho J, Hicks K, Kamii H, Chan PH. Induction of heat shock hsp70 mRNA and HSP70 kDa protein in neurons in the "penumbra" following focal cerebral ischemia in the rat. 1993;619:334-8.
    • Kinouchi H, Sharp FR, Koistinaho J, Hicks K, Kamii H, Chan PH. Induction of heat shock hsp70 mRNA and HSP70 kDa protein in neurons in the "penumbra" following focal cerebral ischemia in the rat. Brain Res 1993;619:334-8.
    • Brain Res
    • Kinouchi, H.1
  • 182
    • 0026100685 scopus 로고    scopus 로고
    • Tsujita Y, Tamura A. Induced tolerance to ischemia in gerbil hippocampal neurons. 1991;11:299-307.
    • KirinoT, Tsujita Y, Tamura A. Induced tolerance to ischemia in gerbil hippocampal neurons. J Cereb Blood Flow Metab 1991;11:299-307.
    • J Cereb Blood Flow Metab
    • KirinoT1
  • 184
    • 0025172696 scopus 로고    scopus 로고
    • Matsumoto M, Tagaya M, Hata R, Ueda H, Niinobe M, Handa N, Fukunaga R, Kimura K, Mikoshiba K, Kamada T. " Ischémie tolerance" phenomenon found in the brain. 1990;528:21-4t.
    • Kitagawa K, Matsumoto M, Tagaya M, Hata R, Ueda H, Niinobe M, Handa N, Fukunaga R, Kimura K, Mikoshiba K, Kamada T. "Ischémie tolerance" phenomenon found in the brain. Brain Res 1990;528:21-4t.
    • Brain Res
    • Kitagawa, K.1
  • 186
    • 0025797337 scopus 로고    scopus 로고
    • Frohli E, Steiger RH, Schafer R, Aoyama A. Alpha B-crystallin is a small heat shock protein. 1991 ;88:3652 -6.
    • Klemenz R, Frohli E, Steiger RH, Schafer R, Aoyama A. Alpha B-crystallin is a small heat shock protein. Pwc NatlAcad Sei USA 1991 ;88:3652 -6.
    • Pwc NatlAcad Sei USA
    • Klemenz, R.1
  • 187
    • 0027426797 scopus 로고    scopus 로고
    • Kalo H. Altered gene expression in cerebral ischemia. 1993;24:2121-7.
    • Kogure K, Kalo H. Altered gene expression in cerebral ischemia. Stroke 1993;24:2121-7.
    • Stroke
    • Kogure, K.1
  • 189
    • 0028314546 scopus 로고    scopus 로고
    • Chen EY, Lee AS, Brown JM, Giaccia AJ. Increased cytotoxicity of chronic hypoxic cells by molecular inhibition of GRP78 induction. 1994:28:661-6.
    • Koong AC, Chen EY, Lee AS, Brown JM, Giaccia AJ. Increased cytotoxicity of chronic hypoxic cells by molecular inhibition of GRP78 induction. Int J Radial Omol Biol Phys 1994:28:661-6.
    • Int J Radial Omol Biol Phys
    • Koong, A.C.1
  • 190
    • 0028032360 scopus 로고    scopus 로고
    • Chen EY. Denko NC, Stambrook P, Giaccia AJ. Hypoxie activation of nuclear factor-kappa B is mediated by a Ras and Raf signaling pathway and does not involve MAP kinase (ERKI or ERK2). Cancer Run 1994:54:5273-9.
    • Koong AC. Chen EY. Mivechi NF, Denko NC, Stambrook P, Giaccia AJ. Hypoxie activation of nuclear factor-kappa B is mediated by a Ras and Raf signaling pathway and does not involve MAP kinase (ERKI or ERK2). Cancer Run 1994:54:5273-9.
    • Mivechi NF
    • Koong, A.C.1
  • 191
    • 0023852783 scopus 로고    scopus 로고
    • Segal M, Normington K, Gething MJ, Sambrook J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. 1988:332:462-4.
    • Kozutsumi Y, Segal M, Normington K, Gething MJ, Sambrook J. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 1988:332:462-4.
    • Nature
    • Kozutsumi, Y.1
  • 193
    • 0027284925 scopus 로고    scopus 로고
    • Tiffany BR. Suppression of protein synthesis in the reperfused brain. 1993:24:747 -56.
    • Krause GS,Tiffany BR. Suppression of protein synthesis in the reperfused brain. Stroke 1993:24:747 -56.
    • Stroke
    • Krause, G.S.1
  • 195
    • 0023655527 scopus 로고    scopus 로고
    • Fullilove S, Read R, Kramer G, I lardesty B. Identification of spectrin-related peptides associated with the reticulocyte heme-controlled alpha suhunit of eukaryotic translational initiation factor 2 kinase and of Mr 95.000 peptide that appears to be the catalytic subunit. 1987:262:9695-701.
    • Kudlicki W, Fullilove S, Read R, Kramer G, I lardesty B. Identification of spectrin-related peptides associated with the reticulocyte heme-controlled alpha suhunit of eukaryotic translational initiation factor 2 kinase and of Mr 95.000 peptide that appears to be the catalytic subunit. J Biol Client 1987:262:9695-701.
    • J Biol Client
    • Kudlicki, W.1
  • 198
    • 0028924759 scopus 로고    scopus 로고
    • Lambert H, Hickey E, Weber LA, Landry J. Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. 1995:15:505-16.
    • Lavoie JN, Lambert H, Hickey E, Weber LA, Landry J. Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. Mol Cell Biol 1995:15:505-16.
    • Mol Cell Biol
    • Lavoie, J.N.1
  • 199
    • 0027376149 scopus 로고    scopus 로고
    • Schwartzman ML, Abraham NG. Novel regulatory sites of the human home oxygenase-1 promoter region. 1993; 196:336-41.
    • Lavrovsky Y, Schwartzman ML, Abraham NG. Novel regulatory sites of the human home oxygenase-1 promoter region. Biochem Biophy.s Res Commun 1993; 196:336-41.
    • Biochem Biophy.s Res Commun
    • Lavrovsky, Y.1
  • 202
    • 0026675676 scopus 로고    scopus 로고
    • Lin KY, Chen KD, Lai YK. Induction of HSP70 is associated with vincristine resistance in heat shocked 9L rat brain tumour cells. 1992:66:653 9.
    • Lee WC, Lin KY, Chen KD, Lai YK. Induction of HSP70 is associated with vincristine resistance in heat shocked 9L rat brain tumour cells. BrJCimar 1992:66:653 9.
    • BrJCimar
    • Lee, W.C.1
  • 205
    • 0025674402 scopus 로고    scopus 로고
    • Ledford BE. Reversible ADP-ribosylation of the 78 kDa glucose-regulated protein. 1990:276:29-33.
    • Leno GH, Ledford BE. Reversible ADP-ribosylation of the 78 kDa glucose-regulated protein. FF.BS Lett 1990:276:29-33.
    • FF.BS Lett
    • Leno, G.H.1
  • 208
    • 0026507980 scopus 로고    scopus 로고
    • Li L, Liu RY, Rehman M, Lee WM. Heat shock protein hspVO protects cells from thermal stress even after deletion of its ATP-binding domain. 1992:89:2036 40.
    • Li GC, Li L, Liu RY, Rehman M, Lee WM. Heat shock protein hspVO protects cells from thermal stress even after deletion of its ATP-binding domain. Proi Natl Acad Sei L:SA 1992:89:2036 40.
    • Proi Natl Acad Sei L:SA
    • Li, G.C.1
  • 210
    • 0027314535 scopus 로고    scopus 로고
    • Alexandre S, Cao X, Lee AS. Transactivation of the grp78 promoter by Ca; depletion. 23187 and the endoplasmic reticulum Ca(2 )-ATPase inhibitor thapsigargin. J Biol Chcm 1993:268:12003-9.
    • Li WW, Alexandre S, Cao X, Lee AS. Transactivation of the grp78 promoter by Ca; depletion. A comparative analysis with A23187 and the endoplasmic reticulum Ca(2 )-ATPase inhibitor thapsigargin. J Biol Chcm 1993:268:12003-9.
    • A Comparative Analysis with a
    • Li, W.W.1
  • 215
    • 0027136174 scopus 로고    scopus 로고
    • Masso WP, Di YP, Cai JW, Shen JW, Subjeck JR. The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds iramunoglobulin. 1993;4:1109-19.
    • Lin HY, Masso WP, Di YP, Cai JW, Shen JW, Subjeck JR. The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds iramunoglobulin. Mol Biol CM 1993;4:1109-19.
    • Mol Biol CM
    • Lin, H.Y.1
  • 216
    • 0027220589 scopus 로고    scopus 로고
    • Wu C. Protein traffic on the heat shock promoter: parking, stalling, and trucking along. 1993;74:1-4.
    • Lis J, Wu C. Protein traffic on the heat shock promoter: parking, stalling, and trucking along. Cell 1993;74:1-4.
    • Cell
    • Lis, J.1
  • 217
    • 0026702946 scopus 로고    scopus 로고
    • Kalo H, Nakata N, Kogure K. Protection of rat hippocampus against ischémie neuronal damage by pretreatment with sublethal ischemia. 1992;586:121-4t.
    • Liu Y, Kalo H, Nakata N, Kogure K. Protection of rat hippocampus against ischémie neuronal damage by pretreatment with sublethal ischemia. Brain Res 1992;586:121-4t.
    • Brain Res
    • Liu, Y.1
  • 218
    • 0027500938 scopus 로고    scopus 로고
    • Kato H, Nakata N, Kogure K. Temporal profile of heat shock protein 70 synthesis in ischémie tolerance induced by preconditioning ischemia in rat hippocampus. 1993;56:921-7.
    • Liu Y, Kato H, Nakata N, Kogure K. Temporal profile of heat shock protein 70 synthesis in ischémie tolerance induced by preconditioning ischemia in rat hippocampus. Neuroscience 1993;56:921-7.
    • Neuroscience
    • Liu, Y.1
  • 219
    • 0024494427 scopus 로고    scopus 로고
    • Weinstein PR, Carlson S, Cummins R. Reversible middle cerebral artery occlusion without craniectomy in rats. 1989;20:84-91.
    • Longa EZ, Weinstein PR, Carlson S, Cummins R. Reversible middle cerebral artery occlusion without craniectomy in rats. Stroke 1989;20:84-91.
    • Stroke
    • Longa, E.Z.1
  • 220
    • 0027495570 scopus 로고    scopus 로고
    • Wang S, Narasimhan P, Zhang JS, Chen J, Massa SM, Sharp FR. c DNA cloning and expression of stress-inducible rat hsp70 in normal and injured rat brain. 1993;36:325-35.
    • Longo FM, Wang S, Narasimhan P, Zhang JS, Chen J, Massa SM, Sharp FR. cDNA cloning and expression of stress-inducible rat hsp70 in normal and injured rat brain. JNeurosci Res 1993;36:325-35.
    • JNeurosci Res
    • Longo, F.M.1
  • 221
    • 0025981251 scopus 로고    scopus 로고
    • Magal E, Brixi A, Steinberg R, Yavin E, Vincendon G. Reduction of protein kinase C activity in the adult rat brain following transient forebrain ischemia. 1991 ;541:171 -4.
    • Louis JC, Magal E, Brixi A, Steinberg R, Yavin E, Vincendon G. Reduction of protein kinase C activity in the adult rat brain following transient forebrain ischemia. Brain Res 1991 ;541:171 -4.
    • Brain Res
    • Louis, J.C.1
  • 222
    • 0026328490 scopus 로고    scopus 로고
    • Chan PH, Miles MF. The stress protein response in cultured neurons: characterization and evidence for a protective role in excitotoxicity. 1991;7:1053-60.
    • Lowenstein DH, Chan PH, Miles MF. The stress protein response in cultured neurons: characterization and evidence for a protective role in excitotoxicity. Neuron 1991;7:1053-60.
    • Neuron
    • Lowenstein, D.H.1
  • 223
    • 0028044860 scopus 로고    scopus 로고
    • Gwinn RP, Seren MS, Simon RP, Mclntosh TK. Increased expression of mRNA encoding calbindin-D28K, the glucose-regulated proteins, or the 72 kDa heat shock protein in three models of acute CNS injury. 1994;22:299-308.
    • Lowenstein DH, Gwinn RP, Seren MS, Simon RP, Mclntosh TK. Increased expression of mRNA encoding calbindin-D28K, the glucose-regulated proteins, or the 72 kDa heat shock protein in three models of acute CNS injury. Brain Res Mol Brain Res 1994;22:299-308.
    • Brain Res Mol Brain Res
    • Lowenstein, D.H.1
  • 224
    • 0025077712 scopus 로고    scopus 로고
    • Simon RP, Sharp FR. The pattern of 72-kDa heat shock protein-like immunoreactivity in the rat brain following flurothyl-induced status epilepticus. 1990;531:173-82.
    • Lowenstein DH, Simon RP, Sharp FR. The pattern of 72-kDa heat shock protein-like immunoreactivity in the rat brain following flurothyl-induced status epilepticus. Brain Res 1990;531:173-82.
    • Brain Res
    • Lowenstein, D.H.1
  • 225
    • 0026636665 scopus 로고    scopus 로고
    • Hsu S, Vaewhongs M, Wu B. The hsp70 gene CCAAT-binding factor mediates transcriptional activation by the adenovirus Ela protein. 1992;12:2599-605.
    • Lum LS, Hsu S, Vaewhongs M, Wu B. The hsp70 gene CCAAT-binding factor mediates transcriptional activation by the adenovirus Ela protein. Mol Cell Biol 1992;12:2599-605.
    • Mol Cell Biol
    • Lum, L.S.1
  • 226
    • 0025883162 scopus 로고    scopus 로고
    • Sarnow P. Internal initiation of translation mediated by the 5' leader of a cellular mRNA. 1991;353:90-4.
    • Macejak DG, Sarnow P. Internal initiation of translation mediated by the 5' leader of a cellular mRNA. Nature 1991;353:90-4.
    • Nature
    • Macejak, D.G.1
  • 227
    • 0024558756 scopus 로고    scopus 로고
    • Wieloch T. Impairment of protein ubiquitination may cause delayed neuronal death.
    • Magnusson K, Wieloch T. Impairment of protein ubiquitination may cause delayed neuronal death. Neurosci Z,ettl989;96:264-70.
    • Neurosci Z,ettl989;96:264-70.
    • Magnusson, K.1
  • 228
    • 0000664619 scopus 로고    scopus 로고
    • Davies-Hill TM, Lysko PG, Henneberry RC, Simpson IA. Expression of two glucose transporters, GLUT1 and GLUT3, in cultured cerebellar neurons: evidence for neuron-specific expression of GLUT3. 1991 ;2:351 -60.
    • Mäher F, Davies-Hill TM, Lysko PG, Henneberry RC, Simpson IA. Expression of two glucose transporters, GLUT1 and GLUT3, in cultured cerebellar neurons: evidence for neuron-specific expression of GLUT3. Mol Cell Neurosci 1991 ;2:351 -60.
    • Mol Cell Neurosci
    • Mäher, F.1
  • 229
    • 0027993604 scopus 로고    scopus 로고
    • Simpson IA. Modulation of expression of glucose transporters GLUT3 and GLUT1 by potassium and A'-methyl-D-aspartate in cultured cerebellar granule neurons. 1994;5:369-75.
    • Mäher F, Simpson IA. Modulation of expression of glucose transporters GLUT3 and GLUT1 by potassium and A'-methyl-D-aspartate in cultured cerebellar granule neurons. Mol Cell Neurosci 1994;5:369-75.
    • Mol Cell Neurosci
    • Mäher, F.1
  • 230
    • 0027970863 scopus 로고    scopus 로고
    • Vannucci SJ, Simpson IA. Glucose transporter proteins in brain. 1994;8:1003-11.
    • Mäher F, Vannucci SJ, Simpson IA. Glucose transporter proteins in brain. FASEB J 1994;8:1003-11.
    • FASEB J
    • Mäher, F.1
  • 231
    • 0026543986 scopus 로고    scopus 로고
    • Vannucci S, Takeda J, Simpson IA. Expression of mouse-GLUT3 and human-GLUT3 glucose transporter proteins in brain. 1992; 182:703-11.
    • Mäher F, Vannucci S, Takeda J, Simpson IA. Expression of mouse-GLUT3 and human-GLUT3 glucose transporter proteins in brain. Biochem Biophys Res Commun 1992; 182:703-11.
    • Biochem Biophys Res Commun
    • Mäher, F.1
  • 232
    • 0027260315 scopus 로고    scopus 로고
    • Howard MK, Latchman DS. Heat shock protects neuronal cells from programmed cell death by apoptosis. 1993;55:621-7.
    • Mailhos C, Howard MK, Latchman DS. Heat shock protects neuronal cells from programmed cell death by apoptosis. Neuroscience 1993;55:621-7.
    • Neuroscience
    • Mailhos, C.1
  • 233
    • 0027973005 scopus 로고    scopus 로고
    • Howard MK, Latchman DS. Heat shock proteins hsp90 and hsp70 protect neuronal cells from thermal stress but not from programmed cell death. 1994;63:1787-95.
    • Mailhos C, Howard MK, Latchman DS. Heat shock proteins hsp90 and hsp70 protect neuronal cells from thermal stress but not from programmed cell death. J Neurochem 1994;63:1787-95.
    • J Neurochem
    • Mailhos, C.1
  • 234
    • 0023731036 scopus 로고    scopus 로고
    • multiplicity, regulatory mechanisms, and clinical applications. /v45£B 71988;2:2557-68.
    • Maines MD. Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications. /v45£B71988;2:2557-68.
    • Heme Oxygenase: Function
    • Maines, M.D.1
  • 236
    • 0027370113 scopus 로고    scopus 로고
    • Sansoni P, Badiali, De Giorgi L, Gallinella G, Ferrari C, Brianti V, Fagnoni FF, Ruegg CL, De Panfilis G, Pasquinelli G. New insights suggesting a possible role of a heat shock protein 70-kD family-related protein in antigen processing/presentation phenomenon in humans. 1993;82:2865-71.
    • Manara GC, Sansoni P, Badiali, De Giorgi L, Gallinella G, Ferrari C, Brianti V, Fagnoni FF, Ruegg CL, De Panfilis G, Pasquinelli G. New insights suggesting a possible role of a heat shock protein 70-kD family-related protein in antigen processing/presentation phenomenon in humans. Blood 1993;82:2865-71.
    • Blood
    • Manara, G.C.1
  • 237
    • 0027490256 scopus 로고    scopus 로고
    • Rush SJ, Brown IR. Temporal and spatial distribution of heat shock mRNA and protein (hsp70) in the rabbit cerebellum in response to hyperthermia. 1993;36:480-90.
    • Manzerra P, Rush SJ, Brown IR. Temporal and spatial distribution of heat shock mRNA and protein (hsp70) in the rabbit cerebellum in response to hyperthermia. J Neurosci Res 1993;36:480-90.
    • J Neurosci Res
    • Manzerra, P.1
  • 238
    • 33845203760 scopus 로고    scopus 로고
    • Rush, SJ, Brown IR. Constitutive expression of heat shock protein 70 (HSP70) in the rabbit nervous system. 1994;20:619.1.
    • Manzerra P, Rush, SJ, Brown IR. Constitutive expression of heat shock protein 70 (HSP70) in the rabbit nervous system. Soc Neurosci Abstr 1994;20:619.1.
    • Soc Neurosci Abstr
    • Manzerra, P.1
  • 239
    • 0025253442 scopus 로고    scopus 로고
    • Kozuka M, Lipsky RH, Nowak TJ. 70-kilodalton heat shock protein induction in cerebellar astrocytes and cerebellar granule cells in vitro: comparison with immunocytochemical localization after hyperthermia in vivo. 1990;54:1509-16.
    • Marini AM, Kozuka M, Lipsky RH, Nowak TJ. 70-kilodalton heat shock protein induction in cerebellar astrocytes and cerebellar granule cells in vitro: comparison with immunocytochemical localization after hyperthermia in vivo. J Neurochem 1990;54:1509-16.
    • J Neurochem
    • Marini, A.M.1
  • 240
    • 0027170620 scopus 로고    scopus 로고
    • Swash M, Mather K, Leigh PN. Expression of the human groEL stress-protein homologue in the brain and spinal cord. 1993;118:202-6.
    • Martin JE, Swash M, Mather K, Leigh PN. Expression of the human groEL stress-protein homologue in the brain and spinal cord. J Neural Sei 1993;118:202-6.
    • J Neural Sei
    • Martin, J.E.1
  • 241
    • 0028902781 scopus 로고    scopus 로고
    • Longo FM, Zuo J, Wang S, Chen J, Sharp FR. Cloning of rat grp75, an hsp70 family member, and its expression in normal and ischémie brain. 1995;40:807-19.
    • 241a.Massa SM, Longo FM, Zuo J, Wang S, Chen J, Sharp FR. Cloning of rat grp75, an hsp70 family member, and its expression in normal and ischémie brain. J Neurosci Res 1995;40:807-19.
    • J Neurosci Res
    • Massa, S.M.1
  • 242
    • 0027445116 scopus 로고    scopus 로고
    • Cheng B. Growth factors protect neurons against excitotoxic/ischemic damage by stabilizing calcium homeostasis. 1993;24:I136-40,I144-5.
    • Mattson MP, Cheng B. Growth factors protect neurons against excitotoxic/ischemic damage by stabilizing calcium homeostasis. Stroke 1993;24:I136-40,I144-5.
    • Stroke
    • Mattson, M.P.1
  • 243
    • 0028223563 scopus 로고    scopus 로고
    • Marcus N, Haugejorden SM, Balcarek JM, Baldassare JJ, Roy B, Li LJ, Lee AS, Green M. Erpôl is GRP58, a stress-inducible luminal endoplasmic reticulum protein, but is devoid of phosphatidylinositide-specific phospholipase C activity. 1994;308:454-60.
    • Mazzarella RA, Marcus N, Haugejorden SM, Balcarek JM, Baldassare JJ, Roy B, Li LJ, Lee AS, Green M. Erpôl is GRP58, a stress-inducible luminal endoplasmic reticulum protein, but is devoid of phosphatidylinositide-specific phospholipase C activity. Arch Biochem Biophys 1994;308:454-60.
    • Arch Biochem Biophys
    • Mazzarella, R.A.1
  • 244
    • 0027330091 scopus 로고    scopus 로고
    • Simon RP. Hyperthermia induces 72kDa heat shock protein expression in rat brain in non-neuronal cells. 1993;159:163-5.
    • McCabe T, Simon RP. Hyperthermia induces 72kDa heat shock protein expression in rat brain in non-neuronal cells. Neurosci Leu 1993;159:163-5.
    • Neurosci Leu
    • McCabe, T.1
  • 245
    • 0026801469 scopus 로고    scopus 로고
    • Yang YS, Wilson J, Sontheimer RD, Capra JD. The 5'-flanking region of the human calreticulin gene shares homology with the human GRP78, GRP94, and protein disulfide isomerase promoters. 1992;267:2557-62.
    • McCauliffe DP, Yang YS, Wilson J, Sontheimer RD, Capra JD. The 5'-flanking region of the human calreticulin gene shares homology with the human GRP78, GRP94, and protein disulfide isomerase promoters. J BiolChem 1992;267:2557-62.
    • J BiolChem
    • McCauliffe, D.P.1
  • 246
    • 0028331627 scopus 로고    scopus 로고
    • Maines MD. The structure, organization and differential expression of the gene encoding rat heme oxygenase-2. 1994; 139:155-61.
    • McCoubrey WJ, Maines MD. The structure, organization and differential expression of the gene encoding rat heme oxygenase-2. Gene 1994; 139:155-61.
    • Gene
    • McCoubrey, W.J.1
  • 247
    • 0022133046 scopus 로고    scopus 로고
    • Lindquist S. The preferential translation ofDrosophila hsp70 mRNA requires sequences in the untranslated leader. 1985;42:903-11.
    • McGarry TJ, Lindquist S. The preferential translation ofDrosophila hsp70 mRNA requires sequences in the untranslated leader. Cell 1985;42:903-11.
    • Cell
    • McGarry, T.J.1
  • 248
    • 0028817419 scopus 로고    scopus 로고
    • Preville X, Chareyron P, Briolay J, Klemenz R, Arrigo AP. Constitutive expression of human hsp27, Drosophila hsp27, or human alpha B-crystallin confers resistance to TNF- and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts. 1995; 154:363-74.
    • Mehlen P, Preville X, Chareyron P, Briolay J, Klemenz R, Arrigo AP. Constitutive expression of human hsp27, Drosophila hsp27, or human alpha B-crystallin confers resistance to TNF- and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts. J Immunol 1995; 154:363-74.
    • J Immunol
    • Mehlen, P.1
  • 249
    • 85177154163 scopus 로고    scopus 로고
    • de Haro C. Casein kinase II is implicated in the regulation of heme-controlled translational inhibitor of reticulocyte lysates. 1994;269:6170-6.
    • Mendez R, de Haro C. Casein kinase II is implicated in the regulation of heme-controlled translational inhibitor of reticulocyte lysates. J Biol Chem 1994;269:6170-6.
    • J Biol Chem
    • Mendez, R.1
  • 250
    • 0027524175 scopus 로고    scopus 로고
    • Groenen PJ, Voorter CE, de Haard-Hoekman WA, Horwitz J, Bloemendal H, de Jong WW. Structural and functional similarities of bovine alpha-crystallin and mouse small heat shock protein. 1993;268:1046-52.
    • Merck KB, Groenen PJ, Voorter CE, de Haard-Hoekman WA, Horwitz J, Bloemendal H, de Jong WW. Structural and functional similarities of bovine alpha-crystallin and mouse small heat shock protein. A family of chaperones. J Biol Chem 1993;268:1046-52.
    • A Family of Chaperones. J Biol Chem
    • Merck, K.B.1
  • 251
    • 0028293462 scopus 로고    scopus 로고
    • Chi SH, Sayen MR, O'Reilly K, Dillmann WH. Expression of inducible stress protein 70 in rat heart myogenic cells confers protection against simulated ischemia-induced injury. 1994;93:759-67.
    • Mestril R, Chi SH, Sayen MR, O'Reilly K, Dillmann WH. Expression of inducible stress protein 70 in rat heart myogenic cells confers protection against simulated ischemia-induced injury. J Clin Invest 1994;93:759-67.
    • J Clin Invest
    • Mestril, R.1
  • 252
    • 0022839236 scopus 로고    scopus 로고
    • West CM, Chau V Antibodies directed against ubiquitin inhibit high affinity [37H]choline uptake in rat cerebral cortical synaptosomes. 1986:261:14365-8.
    • Meyer EM, West CM, Chau V Antibodies directed against ubiquitin inhibit high affinity [37H]choline uptake in rat cerebral cortical synaptosomes. J Biol Chem 1986:261:14365-8.
    • J Biol Chem
    • Meyer, E.M.1
  • 253
    • 0027508163 scopus 로고    scopus 로고
    • BabaT, AraiY, SakakuraT, Kusakabe M. Structure and organization of the gene encoding a mouse mitochondrial stress-70 protein. 1993;336:27-33.
    • MichikawaY, BabaT, AraiY, SakakuraT, Kusakabe M. Structure and organization of the gene encoding a mouse mitochondrial stress-70 protein. FEBS Lett 1993;336:27-33.
    • FEBS Lett
    • MichikawaY1
  • 254
    • 0027508163 scopus 로고    scopus 로고
    • BabaT, AraiY, SakakuraT, Kusakabe M. Structure and organization of the gene encoding a mouse mitochondrial stress-70 protein. 1993;336:27-33.
    • MichikawaY, BabaT, AraiY, SakakuraT, Kusakabe M. Structure and organization of the gene encoding a mouse mitochondrial stress-70 protein. FEBS Lett 1993;336:27-33.
    • FEBS Lett
    • MichikawaY1
  • 255
    • 0027495272 scopus 로고    scopus 로고
    • Baba T, Arai Y, Sakakura T, Tanaka M, Kusakabe M. Antigenic protein specific for C3H strain mouse is a mitochondrial stress-70 protein. 1993; 196:223-32.
    • Michikawa Y, Baba T, Arai Y, Sakakura T, Tanaka M, Kusakabe M. Antigenic protein specific for C3H strain mouse is a mitochondrial stress-70 protein. Biochem Biophys Res Commun 1993; 196:223-32.
    • Biochem Biophys Res Commun
    • Michikawa, Y.1
  • 256
    • 0025950408 scopus 로고    scopus 로고
    • Ishimaru S, XieY, Seo K, Hossmann K-A. Ischémie thresholds of cerebral protein synthesis and energy state following middle cerebral artery occlusion in rat. 1991;! 1:753-61.
    • Mies G, Ishimaru S, XieY, Seo K, Hossmann K-A. Ischémie thresholds of cerebral protein synthesis and energy state following middle cerebral artery occlusion in rat. JCereb Blood Flow Metab 1991;! 1:753-61.
    • JCereb Blood Flow Metab
    • Mies, G.1
  • 257
    • 0006849332 scopus 로고    scopus 로고
    • Morimoto RI. Expression of human HSP70 during the synthetic phase of the cell cycle. 1986;83:9517-21.
    • Milarski KL, Morimoto RI. Expression of human HSP70 during the synthetic phase of the cell cycle. Proc Nat/AcadSei USA 1986;83:9517-21.
    • Proc Nat/AcadSei USA
    • Milarski, K.L.1
  • 258
    • 0025999941 scopus 로고    scopus 로고
    • Raese JD, Morrison BM. Expression of heat shock protein 70 and heat shock cognate 70 messenger RNAs in rat cortex and cerebellum after heat shock or amphetamine treatment. 1991;56:2060-71.
    • Miller EK, Raese JD, Morrison BM. Expression of heat shock protein 70 and heat shock cognate 70 messenger RNAs in rat cortex and cerebellum after heat shock or amphetamine treatment. J Neurochem 1991;56:2060-71.
    • J Neurochem
    • Miller, E.K.1
  • 259
    • 0025813543 scopus 로고    scopus 로고
    • Vancompernolle K, Vandekerckhove J, Wilchek M, Geiger B. A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein. 1991:114:255-61.
    • Miron T, Vancompernolle K, Vandekerckhove J, Wilchek M, Geiger B. A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein. J Cell Biol 1991:114:255-61.
    • J Cell Biol
    • Miron, T.1
  • 260
    • 0025873375 scopus 로고    scopus 로고
    • Fujita H, Sassa S, Kappas A. A heat-inducible nuclear factor that binds to the heat shock element of the human haem oxygenase gene. 1991;277:895-7.
    • Mitani K, Fujita H, Sassa S, Kappas A. A heat-inducible nuclear factor that binds to the heat shock element of the human haem oxygenase gene. Biochem J 1991;277:895-7.
    • Biochem J
    • Mitani, K.1
  • 261
    • 0028258965 scopus 로고    scopus 로고
    • Abe H, Nakajima T, Ishikawa A, Nishiura SM, Naritomi H, Tanaka R, Sawada T. Glutamate release in the gerbil hippocampus after middle cerebral artery occlusion. 1994;5:945-8.
    • Miyashita K, Abe H, Nakajima T, Ishikawa A, Nishiura SM, Naritomi H, Tanaka R, Sawada T. Glutamate release in the gerbil hippocampus after middle cerebral artery occlusion. Neuroreport 1994;5:945-8.
    • Neuroreport
    • Miyashita, K.1
  • 262
    • 0026669310 scopus 로고    scopus 로고
    • Yahara I. The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from selfaggregation and enhances its kinase activity. 1992;267:7042-7.
    • Miyata Y, Yahara I. The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from selfaggregation and enhances its kinase activity. J Biol Chem 1992;267:7042-7.
    • J Biol Chem
    • Miyata, Y.1
  • 263
    • 0024380865 scopus 로고    scopus 로고
    • Chang C, Carrels JI, Welch WJ. Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein. 1989;264:20664-75.
    • Mizzen LA, Chang C, Carrels JI, Welch WJ. Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein. J Biol Chem 1989;264:20664-75.
    • J Biol Chem
    • Mizzen, L.A.1
  • 264
    • 0026114522 scopus 로고    scopus 로고
    • Kabiling AN, Welch WJ. The two mammalian mitochondrial stress proteins, grp 75 and hsp 58, transiently interact with newly synthesized mitochondrial proteins. 1991;2:165-79.
    • Mizzen LA, Kabiling AN, Welch WJ. The two mammalian mitochondrial stress proteins, grp 75 and hsp 58, transiently interact with newly synthesized mitochondrial proteins. Cell Regul 1991;2:165-79.
    • Cell Regul
    • Mizzen, L.A.1
  • 266
    • 0027202273 scopus 로고    scopus 로고
    • Duchaine J, Massie B. The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by hsp70. 1993; 13:5427-38.
    • Mosser DD, Duchaine J, Massie B. The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by hsp70. Mol Cell Biol 1993; 13:5427-38.
    • Mol Cell Biol
    • Mosser, D.D.1
  • 267
    • 0025300038 scopus 로고    scopus 로고
    • Kotzbauer PT, Sarge KD, Morimoto RI. In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation. 1990:87:3748-52.
    • Mosser DD, Kotzbauer PT, Sarge KD, Morimoto RI. In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation. Proc Nat! Acad Sei USA 1990:87:3748-52.
    • Proc Nat! Acad Sei USA
    • Mosser, D.D.1
  • 268
    • 0023654799 scopus 로고    scopus 로고
    • Taguchi H, Shibahara S. Nucleotide sequence and organization of the rat heme oxygenase gene. 1987;262:6795-802.
    • Muller RM, Taguchi H, Shibahara S. Nucleotide sequence and organization of the rat heme oxygenase gene. J BiolChem 1987;262:6795-802.
    • J BiolChem
    • Muller, R.M.1
  • 269
    • 0023052239 scopus 로고    scopus 로고
    • Pelham HR. An HspVO-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. 1986;46:291-300.
    • Munro S, Pelham HR. An HspVO-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 1986;46:291-300.
    • Cell
    • Munro, S.1
  • 270
    • 0023652396 scopus 로고    scopus 로고
    • Pelham HR. A C-terminal signal prevents secretion of luminal ER proteins. 1987;48:899-907.
    • Munro S, Pelham HR. A C-terminal signal prevents secretion of luminal ER proteins. Cell 1987;48:899-907.
    • Cell
    • Munro, S.1
  • 271
    • 0025868208 scopus 로고    scopus 로고
    • Laderoute KR, Short SM, Sutherland RM. The identification of heme oxygenase as a major hypoxic stress protein in Chinese hamster ovary cells. 1991;64:69-73.
    • Murphy BJ, Laderoute KR, Short SM, Sutherland RM. The identification of heme oxygenase as a major hypoxic stress protein in Chinese hamster ovary cells. Br JCancer 1991;64:69-73.
    • Br JCancer
    • Murphy, B.J.1
  • 272
    • 0027424799 scopus 로고    scopus 로고
    • Liang JJ, Schipper HM. Role of the cellular stress response in the biogenesis of cysteamineinduced astrocytic inclusions in primary culture. 1993;61:1755-65.
    • Mydlarski MB, Liang JJ, Schipper HM. Role of the cellular stress response in the biogenesis of cysteamineinduced astrocytic inclusions in primary culture. JNeumchem 1993;61:1755-65.
    • JNeumchem
    • Mydlarski, M.B.1
  • 273
    • 0027521446 scopus 로고    scopus 로고
    • Schipper HM. Stress protein co-localization to autofluorescent astrocytic inclusions in situ and in cysteamine-treated glial cultures. 1993;627:113-21.
    • Mydlarski MB, Schipper HM. Stress protein co-localization to autofluorescent astrocytic inclusions in situ and in cysteamine-treated glial cultures. Brain Res 1993;627:113-21.
    • Brain Res
    • Mydlarski, M.B.1
  • 274
    • 0027406535 scopus 로고    scopus 로고
    • Morimoto RI. Characterization of a novel chicken heat shock transcription factor, heat shock factor 3, suggests a new regulatory pathway. 1993;13:1983-97.
    • Nakai A, Morimoto RI. Characterization of a novel chicken heat shock transcription factor, heat shock factor 3, suggests a new regulatory pathway. Mol Cell Biol 1993;13:1983-97.
    • Mol Cell Biol
    • Nakai, A.1
  • 275
    • 0027213211 scopus 로고    scopus 로고
    • Kalo H, Kogure K. Inhibition of ischaemic tolerance in the gerbil hippocampus by quercetin and anti-heat shock protein-70 antibody. 1993;4:695-8.
    • Nakata N, Kalo H, Kogure K. Inhibition of ischaemic tolerance in the gerbil hippocampus by quercetin and anti-heat shock protein-70 antibody. Neuroreport 1993;4:695-8.
    • Neuroreport
    • Nakata, N.1
  • 276
    • 0027276467 scopus 로고    scopus 로고
    • Taki W, Uemura Y, Higashi T, Kikuchi H, Kudoh H, Satoh M, Nagata K. Ischémie tolerance due to the induction of HSP70 in a rat ischémie recirculation model. 1993;615:281-8.
    • Nishi S, Taki W, Uemura Y, Higashi T, Kikuchi H, Kudoh H, Satoh M, Nagata K. Ischémie tolerance due to the induction of HSP70 in a rat ischémie recirculation model. Brain Res 1993;615:281-8.
    • Brain Res
    • Nishi, S.1
  • 277
    • 0025917624 scopus 로고    scopus 로고
    • Dwyer BE, Clegg K, Cole R, de Vellis J. Comparison of the heat shock response in cultured cortical neurons and astrocytes. 1991 ;9:39-45.
    • Nishimura RN, Dwyer BE, Clegg K, Cole R, de Vellis J. Comparison of the heat shock response in cultured cortical neurons and astrocytes. Brain Res Mol Brain Res 1991 ;9:39-45.
    • Brain Res Mol Brain Res
    • Nishimura, R.N.1
  • 279
    • 0024537963 scopus 로고    scopus 로고
    • Dwyer BE, Cole R, de Vellis J, Picard K. Induction of the major inducible 68-kDa heat shock protein after rapid changes of extracellular pH in cultured rat astrocytes. 1989; 180:276-80.
    • Nishimura RN, Dwyer BE, Cole R, de Vellis J, Picard K. Induction of the major inducible 68-kDa heat shock protein after rapid changes of extracellular pH in cultured rat astrocytes. Exp Cell Res 1989; 180:276-80.
    • Exp Cell Res
    • Nishimura, R.N.1
  • 280
    • 0026515216 scopus 로고    scopus 로고
    • Dwyer BE, de Vellis J, Clegg KB. Characterization of the major 68 kDa heat shock protein in a rat transformed astroglial cell line. 1992; 12:203-8.
    • Nishimura RN, Dwyer BE, de Vellis J, Clegg KB. Characterization of the major 68 kDa heat shock protein in a rat transformed astroglial cell line. Brain Res Mol Brain Res 1992; 12:203-8.
    • Brain Res Mol Brain Res
    • Nishimura, R.N.1
  • 281
    • 0025782940 scopus 로고    scopus 로고
    • Dwyer BE, Vinters H V, de Vellis J, Cole R. Heat shock in cultured neurons and astrocytes : correlation of ultrastructure and heat shock protein synthesis. 1991; 17:139-47.
    • Nishimura RN, Dwyer BE, Vinters H V, de Vellis J, Cole R. Heat shock in cultured neurons and astrocytes : correlation of ultrastructure and heat shock protein synthesis. Neuropathol Appl Neurobiol 1991; 17:139-47.
    • Neuropathol Appl Neurobiol
    • Nishimura, R.N.1
  • 282
    • 0023801914 scopus 로고    scopus 로고
    • Dwyer BE, Welch W, Cole R, de Vellis J, Liotta K. The induction of the major heat-stress protein in purified rat glial cells. 1988;20:12-8.
    • Nishimura RN, Dwyer BE, Welch W, Cole R, de Vellis J, Liotta K. The induction of the major heat-stress protein in purified rat glial cells. J Neurosci Res 1988;20:12-8.
    • J Neurosci Res
    • Nishimura, R.N.1
  • 283
    • 0027264692 scopus 로고    scopus 로고
    • Furuno N, Okazaki K, Tanaka H, OgawaY, Sagata N. Degradation of Mos by the N-terminal proline (Pro2)-dependent ubiquitin pathway on fertilization ofXenopus eggs: possible significance of natural selection forPro2 in Mos. 1993;12:4021-7.
    • Nishizawa M, Furuno N, Okazaki K, Tanaka H, OgawaY, Sagata N. Degradation of Mos by the N-terminal proline (Pro2)-dependent ubiquitin pathway on fertilization ofXenopus eggs: possible significance of natural selection forPro2 in Mos. EMBOJ 1993;12:4021-7.
    • EMBOJ
    • Nishizawa, M.1
  • 284
    • 0027383493 scopus 로고    scopus 로고
    • States B, Hardy M, Pleasure J, Nissim I. Effect of glutamine on heat shock-induced mRNA and stress proteins. 1993; 157:313-8.
    • Nissim I, States B, Hardy M, Pleasure J, Nissim I. Effect of glutamine on heat shock-induced mRNA and stress proteins. J Cell Physiol 1993; 157:313-8.
    • J Cell Physiol
    • Nissim, I.1
  • 286
    • 0022243905 scopus 로고    scopus 로고
    • Synthesis of a stress protein following transient ischemia in the gerbil. 1985;45:1635-41.
    • Nowak TJ. Synthesis of a stress protein following transient ischemia in the gerbil. J Neumchem 1985;45:1635-41.
    • J Neumchem
    • Nowak, T.J.1
  • 287
    • 0025617461 scopus 로고    scopus 로고
    • Protein synthesis and the heart shock/stress response after ischemia. 1990;2:345-66.
    • Nowak TJ. Protein synthesis and the heart shock/stress response after ischemia. Cerebrovasc Brain Metab Rev 1990;2:345-66.
    • Cerebrovasc Brain Metab Rev
    • Nowak, T.J.1
  • 288
    • 0025793665 scopus 로고    scopus 로고
    • Localization of 70 kDa stress protein mRNA induction in gerbil brain after ischemia. 1991 ; 11:432-9.
    • Nowak TJ. Localization of 70 kDa stress protein mRNA induction in gerbil brain after ischemia. J Cereb Blood Flow Metab 1991 ; 11:432-9.
    • J Cereb Blood Flow Metab
    • Nowak, T.J.1
  • 289
    • 0025190058 scopus 로고    scopus 로고
    • Bond U, Schlesinger MJ. Heat shock RNA levels in brain and other tissues after hyperthermia and transient ischemia. 1990;54:451-8.
    • Nowak TJ, Bond U, Schlesinger MJ. Heat shock RNA levels in brain and other tissues after hyperthermia and transient ischemia. J Neumchem 1990;54:451-8.
    • J Neumchem
    • Nowak, T.J.1
  • 291
    • 0025727517 scopus 로고    scopus 로고
    • Ishikawa M, Mizushima Y. Identification of a ubiquitin- and ATP-dependent protein degradation pathway in rat cerebral cortex. 1991;1073:514-20.
    • Okada M, Ishikawa M, Mizushima Y. Identification of a ubiquitin- and ATP-dependent protein degradation pathway in rat cerebral cortex. Biochim BiophysActa 1991;1073:514-20.
    • Biochim BiophysActa
    • Okada, M.1
  • 293
    • 0026525371 scopus 로고    scopus 로고
    • PfaffDW, Mobbs CV. Estrogenic regulation of heat shock protein 90 kDa in the rat ventromedial hypothalamus and uterus. 1992;84:175-83.
    • Olazabal UE, PfaffDW, Mobbs CV. Estrogenic regulation of heat shock protein 90 kDa in the rat ventromedial hypothalamus and uterus. Mol Cell Endocrinol 1992;84:175-83.
    • Mol Cell Endocrinol
    • Olazabal, U.E.1
  • 294
    • 0024338054 scopus 로고    scopus 로고
    • Labruyere J, Price MT. Pathological changes induced in cerebrocortical neurons by phencyclidine and related drugs. 1989;244:1360-2.
    • Olney JW, Labruyere J, Price MT. Pathological changes induced in cerebrocortical neurons by phencyclidine and related drugs. Science 1989;244:1360-2.
    • Science
    • Olney, J.W.1
  • 295
    • 0026339216 scopus 로고    scopus 로고
    • Labruyere J, Wang G, Wozniak DF, Price MT, Sesma MA. NMDA antagonist neurotoxicity: mechanism and prevention. 1991;254:1515-8.
    • Olney JW, Labruyere J, Wang G, Wozniak DF, Price MT, Sesma MA. NMDA antagonist neurotoxicity: mechanism and prevention. Science 1991;254:1515-8.
    • Science
    • Olney, J.W.1
  • 296
    • 0028071199 scopus 로고    scopus 로고
    • Nadeau KC, Sullivan MA, Winquist AG, Donelson JE, Walsh CT, Engman DM. Molecular and biochemical comparison of the 70-kDa heat shock proteins of Trypanosoma cruzi. 1994;269:3868-74.
    • Oison CL, Nadeau KC, Sullivan MA, Winquist AG, Donelson JE, Walsh CT, Engman DM. Molecular and biochemical comparison of the 70-kDa heat shock proteins of Trypanosoma cruzi. J Biol Chem 1994;269:3868-74.
    • J Biol Chem
    • Oison, C.L.1
  • 297
    • 0021219338 scopus 로고    scopus 로고
    • Lanks KW. Heat shock protein synthesis and cell survival in clones of normal and simian virus 40-transformed mouse embryo cells. 1984;44:3976-82.
    • Omar RA, Lanks KW. Heat shock protein synthesis and cell survival in clones of normal and simian virus 40-transformed mouse embryo cells. Cancer Res 1984;44:3976-82.
    • Cancer Res
    • Omar, R.A.1
  • 298
    • 0027311128 scopus 로고    scopus 로고
    • Pappolla M Oxygen free radicals as inducers of heat shock protein synthesis in cultured human neuroblastoma cells: relevance to neurodegenerative disease. 1993;242:262-7.
    • Omar R, Pappolla M Oxygen free radicals as inducers of heat shock protein synthesis in cultured human neuroblastoma cells: relevance to neurodegenerative disease. Ear Arch Psychiatry Clin Neumsci 1993;242:262-7.
    • Ear Arch Psychiatry Clin Neumsci
    • Omar, R.1
  • 299
    • 0026607460 scopus 로고    scopus 로고
    • Murakami Y, Eki T, Soeda E, Yokoyama K. Mapping of the gene family for human heat shock protein 90 alpha to chromosomes 1,4, 11, and 14. 1992;12:214-20.
    • Ozawa K, Murakami Y, Eki T, Soeda E, Yokoyama K. Mapping of the gene family for human heat shock protein 90 alpha to chromosomes 1,4, 11, and 14. Genomics 1992;12:214-20.
    • Genomics
    • Ozawa, K.1
  • 300
    • 0027980321 scopus 로고    scopus 로고
    • Rando OJ, Goldberg AL, Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-kappa Bl precursor protein and the activation of NF-kappa B. 1994;78:773-85.
    • Palombella VJ, Rando OJ, Goldberg AL, Maniatis T. The ubiquitin-proteasome pathway is required for processing the NF-kappa Bl precursor protein and the activation of NF-kappa B. Cell 1994;78:773-85.
    • Cell
    • Palombella, V.J.1
  • 301
    • 0027076820 scopus 로고    scopus 로고
    • Treier M, Chavrier C, Bohmann D. Targeted degradation of c-Fos, but not v-Fos, by a phosphorylation-dependent signal on c-Jun. 1992;258:1941-4.
    • Papavassiliou AG, Treier M, Chavrier C, Bohmann D. Targeted degradation of c-Fos, but not v-Fos, by a phosphorylation-dependent signal on c-Jun. Science 1992;258:1941-4.
    • Science
    • Papavassiliou, A.G.1
  • 303
    • 0018234882 scopus 로고    scopus 로고
    • Lamb RA, Choppin PW. Infection with paramyxoviruses stimulates synthesis of cellular polypeptides that are also stimulated in cells transformed by Rous sarcoma virus or deprived of glucose. 1978;75:6120-4t.
    • Peluso RW, Lamb RA, Choppin PW. Infection with paramyxoviruses stimulates synthesis of cellular polypeptides that are also stimulated in cells transformed by Rous sarcoma virus or deprived of glucose. Proc Natl AcadSciUSA 1978;75:6120-4t.
    • Proc Natl AcadSciUSA
    • Peluso, R.W.1
  • 304
    • 0026621935 scopus 로고    scopus 로고
    • Nelson HC. Trimerization of the heat shock transcription factor by a triple-stranded alphahelical coiled-coil. 1992;31:12272-6.
    • Peteranderl R, Nelson HC. Trimerization of the heat shock transcription factor by a triple-stranded alphahelical coiled-coil. Biochemistry 1992;31:12272-6.
    • Biochemistry
    • Peteranderl, R.1
  • 305
    • 0024217528 scopus 로고    scopus 로고
    • Lindquist S. The Drosophila hsp70 message is rapidly degraded at normal temperatures and stabilized by heat shock. 1988;72:161-8.
    • Petersen R, Lindquist S. The Drosophila hsp70 message is rapidly degraded at normal temperatures and stabilized by heat shock. Gene 1988;72:161-8.
    • Gene
    • Petersen, R.1
  • 306
    • 0024755682 scopus 로고    scopus 로고
    • Lindquist S. Regulation of HSP70 synthesis by messenger RNA degradation. 1989;l:135-49.
    • Petersen RB, Lindquist S. Regulation of HSP70 synthesis by messenger RNA degradation. Cell Regul 1989;l:135-49.
    • Cell Regul
    • Petersen, R.B.1
  • 307
    • 0027451956 scopus 로고    scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. 1993;268:21455-8.
    • Pratt WB. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J Biol Chem 1993;268:21455-8.
    • J Biol Chem
    • Pratt, W.B.1
  • 308
    • 0025922155 scopus 로고    scopus 로고
    • Calderwood SK. Ca2t is essential for multistep activation of the heat shock factor in permeabilized cells. 1991;! 1:3365-8.
    • Price BD, Calderwood SK. Ca2t is essential for multistep activation of the heat shock factor in permeabilized cells. MolCellBiol 1991;! 1:3365-8.
    • MolCellBiol
    • Price, B.D.1
  • 309
    • 0026632457 scopus 로고    scopus 로고
    • Calderwood SK. Gadd45 and Gaddl53 messenger RNA levels are increased during hypoxia and after exposure of cells to agents which elevate the levels of the glucose-regulated proteins. 1992;52:3814-7.
    • Price BD, Calderwood SK. Gadd45 and Gaddl53 messenger RNA levels are increased during hypoxia and after exposure of cells to agents which elevate the levels of the glucose-regulated proteins. Cancer Res 1992;52:3814-7.
    • Cancer Res
    • Price, B.D.1
  • 310
    • 0026611735 scopus 로고    scopus 로고
    • Mannheim RL, Calderwood SK. Brefeldin A, thapsigargin, and AIF4- stimulate the accumulation of GRP78 mRNA in a cycloheximide dependent manner, whilst induction by hypoxia is independent of protein synthesis. 1992; 152:545-52.
    • Price BD, Mannheim RL, Calderwood SK. Brefeldin A, thapsigargin, and AIF4- stimulate the accumulation of GRP78 mRNA in a cycloheximide dependent manner, whilst induction by hypoxia is independent of protein synthesis. J Cell Physio/ 1992; 152:545-52.
    • J Cell Physio
    • Price, B.D.1
  • 312
    • 0026774289 scopus 로고    scopus 로고
    • Dawson G. Hypoxia induces synthesis of a novel 22-kDa protein in neonatal rat oligodendrocytes. 1992;59:1709-16.
    • Qi Y, Dawson G. Hypoxia induces synthesis of a novel 22-kDa protein in neonatal rat oligodendrocytes. J Neurochem 1992;59:1709-16.
    • J Neurochem
    • Qi, Y.1
  • 313
    • 0025864313 scopus 로고    scopus 로고
    • Giorgi G, Clos J, Wu C. Molecular cloning and expression of a human heat shock factor, HSF1. 1991;88:6906-10.
    • Rabindran SK, Giorgi G, Clos J, Wu C. Molecular cloning and expression of a human heat shock factor, HSF1. Proc NatlAcadSci USA 1991;88:6906-10.
    • Proc NatlAcadSci USA
    • Rabindran, S.K.1
  • 314
    • 0027452754 scopus 로고    scopus 로고
    • Haroun RI, Clos J, Wisniewski J, Wu C. Regulation of heat shock factor trimer formation: role of a conserved leucine zipper. 1993;259:230-44.
    • Rabindran SK, Haroun RI, Clos J, Wisniewski J, Wu C. Regulation of heat shock factor trimer formation: role of a conserved leucine zipper. Science 1993;259:230-44.
    • Science
    • Rabindran, S.K.1
  • 315
    • 0028246870 scopus 로고    scopus 로고
    • Murphy TH, Baraban JM. Macromolecular synthesis inhibitors prevent oxidative stress-induced apoptosis in embryonic cortical neurons by shunting cysteine from protein synthesis to glutathione. 1994; 14:43 85-92.
    • Ratan RR, Murphy TH, Baraban JM. Macromolecular synthesis inhibitors prevent oxidative stress-induced apoptosis in embryonic cortical neurons by shunting cysteine from protein synthesis to glutathione. J Neurosci 1994; 14:43 85-92.
    • J Neurosci
    • Ratan, R.R.1
  • 316
    • 0023003446 scopus 로고    scopus 로고
    • Ting J, Kim KS, Wooden SK, Lee AS. Calcium ionophore A23187 as a regulator of gene expression in mammalian cells. 1986; 103:2145-52.
    • Resendez EJ, Ting J, Kim KS, Wooden SK, Lee AS. Calcium ionophore A23187 as a regulator of gene expression in mammalian cells. J Cell Biol 1986; 103:2145-52.
    • J Cell Biol
    • Resendez, E.J.1
  • 317
    • 0024293984 scopus 로고    scopus 로고
    • Mizzen LA, Welch WJ. Heat shock is lethal to fibroblasts microinjected with antibodies against hsp70. 1988;242:433-6.
    • Riabowol KT, Mizzen LA, Welch WJ. Heat shock is lethal to fibroblasts microinjected with antibodies against hsp70. Science 1988;242:433-6.
    • Science
    • Riabowol, K.T.1
  • 318
    • 34250561475 scopus 로고    scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in Drosophila. 1962;18:571-3.
    • Ritossa F. A new puffing pattern induced by temperature shock and DNP in Drosophila. Experientia 1962;18:571-3.
    • Experientia
    • Ritossa, F.1
  • 319
    • 0027372622 scopus 로고    scopus 로고
    • Ritz MF, Malviya AN. Impaired gene transcription and nuclear protein kinase C activation in the brain and liver of aged rats. 1993;334:351-4t.
    • Rogue PJ, Ritz MF, Malviya AN. Impaired gene transcription and nuclear protein kinase C activation in the brain and liver of aged rats. FEBSLett 1993;334:351-4t.
    • FEBSLett
    • Rogue, P.J.1
  • 320
    • 0025774184 scopus 로고    scopus 로고
    • Murphy BJ, Laderoute KR, Sutherland RM, Smith HC. Oxygen regulated 80 kDa protein and glucose regulated 78kDa protein are identical. 1991; 103:141-8.
    • Roll DE, Murphy BJ, Laderoute KR, Sutherland RM, Smith HC. Oxygen regulated 80 kDa protein and glucose regulated 78kDa protein are identical. Mol Cell Biochem 1991; 103:141-8.
    • Mol Cell Biochem
    • Roll, D.E.1
  • 321
    • 0026336621 scopus 로고    scopus 로고
    • Koroshetz WJ, Bonventre JV. Heat shock protects cultured neurons from glutamate toxicity. 1991;7:1043-51.
    • Rordorf G, Koroshetz WJ, Bonventre JV. Heat shock protects cultured neurons from glutamate toxicity. Neuron 1991;7:1043-51.
    • Neuron
    • Rordorf, G.1
  • 322
    • 0024543749 scopus 로고    scopus 로고
    • Welch WJ, Krämer G, Hardesty B. Possible involvement of the 90-kDa heat shock protein in the regulation of protein synthesis. 1989;264:6239-44.
    • Rose DW, Welch WJ, Krämer G, Hardesty B. Possible involvement of the 90-kDa heat shock protein in the regulation of protein synthesis. J Biol Chem 1989;264:6239-44.
    • J Biol Chem
    • Rose, D.W.1
  • 324
    • 0025970342 scopus 로고    scopus 로고
    • Kon C. Glutamine is a powerful effector of heat shock protein expression in Drosophila Kc cells. 1991 ; 146:180-90.
    • Sanders MM, Kon C. Glutamine is a powerful effector of heat shock protein expression in Drosophila Kc cells. J Cell Physio! 1991 ; 146:180-90.
    • J Cell Physio!
    • Sanders, M.M.1
  • 325
    • 0027761274 scopus 로고    scopus 로고
    • Potential behavioral modification of glucocorticoid damage to the hippocampus. 1993:57:175-82.
    • Sapolsky RM. Potential behavioral modification of glucocorticoid damage to the hippocampus. Behav Brain Res 1993:57:175-82.
    • Behav Brain Res
    • Sapolsky, R.M.1
  • 326
    • 0027461364 scopus 로고    scopus 로고
    • Murphy SP, Morimoto RI. 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. 1993;! 3:1392-407.
    • Sarge KD, Murphy SP, Morimoto RI. 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 Bio/ 1993;! 3:1392-407.
    • Mol Cell Bio
    • Sarge, K.D.1
  • 327
    • 0027092426 scopus 로고    scopus 로고
    • Abe K, Kawagoe J, Aoki M, Kogure K. Isolation of complementary DNAs for heat shock protein (HSP) 70 and heat shock cognate protein (HSC) 70 genes and the expressions in post-ischemic gerbil brain. 1992; 14:375-80.
    • Sato S, Abe K, Kawagoe J, Aoki M, Kogure K. Isolation of complementary DNAs for heat shock protein (HSP) 70 and heat shock cognate protein (HSC) 70 genes and the expressions in post-ischemic gerbil brain. Neural Res 1992; 14:375-80.
    • Neural Res
    • Sato, S.1
  • 328
    • 0026467749 scopus 로고    scopus 로고
    • Nomaguchi H, Tabira T. Constitutive expression of 65-kDa heat shock protein (HSP65)-like immunoreactivity in cultured mouse oligodendrocytes. 1992;595:281-90.
    • Satoh J, Nomaguchi H, Tabira T. Constitutive expression of 65-kDa heat shock protein (HSP65)-like immunoreactivity in cultured mouse oligodendrocytes. Brain Res 1992;595:281-90.
    • Brain Res
    • Satoh, J.1
  • 329
    • 0026536520 scopus 로고    scopus 로고
    • Yamamura T, Kunishita T, Tabira T. Heterogeneous induction of 72-kDa heat shock protein (HSP72) in cultured mouse oligodendrocytes and astrocytes. 1992:573:37-43.
    • Satoh J, Yamamura T, Kunishita T, Tabira T. Heterogeneous induction of 72-kDa heat shock protein (HSP72) in cultured mouse oligodendrocytes and astrocytes. Brain Res 1992:573:37-43.
    • Brain Res
    • Satoh, J.1
  • 330
    • 0017897608 scopus 로고    scopus 로고
    • Artavanis TS, Steward R, Gehring WJ, Mirault ME, Goldschmidt CM, Moran L, Tissieres A. Two hybrid plasmids with D. melanogaster DNA sequences complementary to mRNA coding for the major heat shock protein. 1978:14:921-9.
    • Schedl P, Artavanis TS, Steward R, Gehring WJ, Mirault ME, Goldschmidt CM, Moran L, Tissieres A. Two hybrid plasmids with D. melanogaster DNA sequences complementary to mRNA coding for the major heat shock protein. Cell 1978:14:921-9.
    • Cell
    • Schedl, P.1
  • 331
    • 0023688079 scopus 로고    scopus 로고
    • Amin J, Ananthan J, Brown ME, Scott WA, Voellmy R. Cis-acting elements involved in the regulated expression of a human HSP70 gene. 1988;203:97-105.
    • Schiller P, Amin J, Ananthan J, Brown ME, Scott WA, Voellmy R. Cis-acting elements involved in the regulated expression of a human HSP70 gene. J Mol Biol 1988;203:97-105.
    • J Mol Biol
    • Schiller, P.1
  • 332
    • 0027318211 scopus 로고    scopus 로고
    • Mydlarski MB, Wang X. Cysteamine gliopathy in situ: a cellular stress model for the biogenesis of astrocytic inclusions. 1993:52:399-410.
    • Schipper HM, Mydlarski MB, Wang X. Cysteamine gliopathy in situ: a cellular stress model for the biogenesis of astrocytic inclusions. JNeuropathol Exp Neural 1993:52:399-410.
    • JNeuropathol Exp Neural
    • Schipper, H.M.1
  • 333
    • 0028268243 scopus 로고    scopus 로고
    • Baici A, Gehring H, Christen P. Kinetics of molecular chaperone action. 1994;263:971-3.
    • Schmid D, Baici A, Gehring H, Christen P. Kinetics of molecular chaperone action. Science 1994;263:971-3.
    • Science
    • Schmid, D.1
  • 334
    • 0011488224 scopus 로고    scopus 로고
    • Subjeck JR, Hughes CS. Induction of glucose-regulated proteins during anaerobic exposure and of heat shock proteins after reoxygenation. 1984;81:4843-7.
    • Sciandra JJ, Subjeck JR, Hughes CS. Induction of glucose-regulated proteins during anaerobic exposure and of heat shock proteins after reoxygenation. Proc NatlAcad Sei USA 1984;81:4843-7.
    • Proc NatlAcad Sei USA
    • Sciandra, J.J.1
  • 335
    • 0026609563 scopus 로고    scopus 로고
    • Brosnan CF, Raine CS. Expression of heat shock protein-65 by oligodendrocytes in vivo and in vitro: implications for multiple sclerosis. 1992;42:795-800.
    • Selmaj K, Brosnan CF, Raine CS. Expression of heat shock protein-65 by oligodendrocytes in vivo and in vitro: implications for multiple sclerosis. Neurology 1992;42:795-800.
    • Neurology
    • Selmaj, K.1
  • 336
    • 0026475990 scopus 로고    scopus 로고
    • Butman M, Wang S, Koistinaho J, Graham SH, Sagar SM, Noble L, Berger P, Longo FM. Haloperidol prevents induction of the hsp70 heat shock gene in neurons injured by phencyclidine (PCP), MK801, and ketamine. 1992;33:605-16.
    • Sharp FR, Butman M, Wang S, Koistinaho J, Graham SH, Sagar SM, Noble L, Berger P, Longo FM. Haloperidol prevents induction of the hsp70 heat shock gene in neurons injured by phencyclidine (PCP), MK801, and ketamine. JNeurosci Res 1992;33:605-16.
    • JNeurosci Res
    • Sharp, F.R.1
  • 337
    • 0025785711 scopus 로고    scopus 로고
    • Lowenstein D, Simon R, Hisanaga K. Heat shock protein hsp72 induction in cortical and striatal astrocytes and neurons following infarction. 1991 ; 11:621-7.
    • Sharp FR, Lowenstein D, Simon R, Hisanaga K. Heat shock protein hsp72 induction in cortical and striatal astrocytes and neurons following infarction. J Cereb Blood Flow Metab 1991 ; 11:621-7.
    • J Cereb Blood Flow Metab
    • Sharp, F.R.1
  • 338
    • 0028225971 scopus 로고    scopus 로고
    • Sagar SM. Alterations in gene expression as an index of neuronal injury: heat shock and the immediate early gene response. 1994; 15:51-9.
    • Sharp FR, Sagar SM. Alterations in gene expression as an index of neuronal injury: heat shock and the immediate early gene response. Neurotoxicology 1994; 15:51-9.
    • Neurotoxicology
    • Sharp, F.R.1
  • 339
    • 0027177579 scopus 로고    scopus 로고
    • Kingston RE. Hydrophobie coiled-coil domains regulate the subcellular localization of human heat shock factor 2. 1993;7:1549-58.
    • Sheldon LA, Kingston RE. Hydrophobie coiled-coil domains regulate the subcellular localization of human heat shock factor 2. Genes Dev 1993;7:1549-58.
    • Genes Dev
    • Sheldon, L.A.1
  • 340
    • 0026503521 scopus 로고    scopus 로고
    • So YT, Simon RP. Distribution of HSP72 induction and neuronal death following limbic seizures. 1992;138:202-6.
    • Shimosaka S, So YT, Simon RP. Distribution of HSP72 induction and neuronal death following limbic seizures. Neurosci Lett 1992;138:202-6.
    • Neurosci Lett
    • Shimosaka, S.1
  • 341
    • 0024314035 scopus 로고    scopus 로고
    • Sharp FR, Simon RP. Sequential metabolic changes in rat brain following middle cerebral artery occlusion: a 2-deoxyglucose study. 1989;9:765-73.
    • Shiraishi K, Sharp FR, Simon RP. Sequential metabolic changes in rat brain following middle cerebral artery occlusion: a 2-deoxyglucose study. J Cereb Blood Flow Metab 1989;9:765-73.
    • J Cereb Blood Flow Metab
    • Shiraishi, K.1
  • 342
    • 0023987021 scopus 로고    scopus 로고
    • Pollock M, Bowman PD, Atkinson BG. The effect of heat shock on primary cultures of brain capillary endothelium: inhibition of assembly of zonulae occludentes and the synthesis of heat shook proteins. 198846:181-95.
    • Shivers RR, Pollock M, Bowman PD, Atkinson BG. The effect of heat shock on primary cultures of brain capillary endothelium: inhibition of assembly of zonulae occludentes and the synthesis of heat shook proteins. Eur J Cell Biol 198846:181-95.
    • Eur J Cell Biol
    • Shivers, R.R.1
  • 343
    • 0028342731 scopus 로고    scopus 로고
    • Gonen H, Bercovich B, Ciechanover A. Complete reconstitution of conjugation and subsequent degradation of the tumor suppressor protein p53 by purified components of the ubiquitin proteolytic system. 1994;348:126-30.
    • Shkedy D, Gonen H, Bercovich B, Ciechanover A. Complete reconstitution of conjugation and subsequent degradation of the tumor suppressor protein p53 by purified components of the ubiquitin proteolytic system. FEBSLett 1994;348:126-30.
    • FEBSLett
    • Shkedy, D.1
  • 344
    • 0027746759 scopus 로고    scopus 로고
    • Smith T, Norris K, Pileggi R, Sauk JJ. Hsp 47 is localized to regions of type I collagen production in developing murine femurs and molars. 1993:29:273-86.
    • Shroff B, Smith T, Norris K, Pileggi R, Sauk JJ. Hsp 47 is localized to regions of type I collagen production in developing murine femurs and molars. Connect Tissue Res 1993:29:273-86.
    • Connect Tissue Res
    • Shroff, B.1
  • 345
    • 0024284087 scopus 로고    scopus 로고
    • Fisch TM, Benecke BJ, Nevins JR, Heintz N. Definition of multiple, functionally distinct TATA elements, one of which is a target in the hsp70 promoter for E1A regulation. 1988;52:723-9.
    • Simon MC, Fisch TM, Benecke BJ, Nevins JR, Heintz N. Definition of multiple, functionally distinct TATA elements, one of which is a target in the hsp70 promoter for E1A regulation. Cell 1988;52:723-9.
    • Cell
    • Simon, M.C.1
  • 346
    • 0023394002 scopus 로고    scopus 로고
    • Kitchener K, Kao HT, Hickey E, Weber L, Voellmy R, Heintz N, Nevins JR. Selective induction of human heat shock gene transcription by the adenovirus El A gene products, including the 12S El A product. 1987:7:2884-90.
    • Simon MC, Kitchener K, Kao HT, Hickey E, Weber L, Voellmy R, Heintz N, Nevins JR. Selective induction of human heat shock gene transcription by the adenovirus El A gene products, including the 12S El A product. Mol Cell Biol 1987:7:2884-90.
    • Mol Cell Biol
    • Simon, M.C.1
  • 347
    • 0026042945 scopus 로고    scopus 로고
    • Cho H, Gwinn R, Lowenstein DH. The temporal profile of 72-kDa heat shock protein expression following global ischemia. 1991;! 1:881-9.
    • Simon RP, Cho H, Gwinn R, Lowenstein DH. The temporal profile of 72-kDa heat shock protein expression following global ischemia. J Neurosci 1991;! 1:881-9.
    • J Neurosci
    • Simon, R.P.1
  • 348
    • 0027144042 scopus 로고    scopus 로고
    • Niiro M, Gwinn R. Prior ischémie stress protects against experimental stroke. 1993:163:135-7.
    • Simon RP, Niiro M, Gwinn R. Prior ischémie stress protects against experimental stroke. Neurosci Lett 1993:163:135-7.
    • Neurosci Lett
    • Simon, R.P.1
  • 349
    • 0026746491 scopus 로고    scopus 로고
    • Sarge KD, Phillips B, Abravaya K, Morimoto RI. Activation of heat shock factor 2 during hemininduced differentiation of human erythroleukemia cells. 1992; 12:4104-11.
    • Sistonen L, Sarge KD, Phillips B, Abravaya K, Morimoto RI. Activation of heat shock factor 2 during hemininduced differentiation of human erythroleukemia cells. Mol Cell Biol 1992; 12:4104-11.
    • Mol Cell Biol
    • Sistonen, L.1
  • 350
    • 33845198133 scopus 로고    scopus 로고
    • Caday CG, Berlove DJ, Kemmou A, Brown RH, Finkelstein SP. Identification by differential screening of heat shock protein-86 induced in gerbil hippocampus following transient global ischemia. 1993;19:676.12.
    • Sklar RM, Caday CG, Berlove DJ, Kemmou A, Brown RH, Finkelstein SP. Identification by differential screening of heat shock protein-86 induced in gerbil hippocampus following transient global ischemia. Soc Neurosci Abstr 1993;19:676.12.
    • Soc Neurosci Abstr
    • Sklar, R.M.1
  • 351
    • 0026721889 scopus 로고    scopus 로고
    • Lowenstein DH. Heat shock protein expression in vulnerable cells of the rat hippocampus as an indicator of excitation-induced neuronal stress. 1992;12:3004-9.
    • Sloviter RS, Lowenstein DH. Heat shock protein expression in vulnerable cells of the rat hippocampus as an indicator of excitation-induced neuronal stress. J Neurosci 1992;12:3004-9.
    • J Neurosci
    • Sloviter, R.S.1
  • 352
    • 0026322998 scopus 로고    scopus 로고
    • Yaffe MR Uncoupling thermotolerance from the induction of heat shock proteins. 1991;88:11091-4.
    • Smith BJ, Yaffe MR Uncoupling thermotolerance from the induction of heat shock proteins. Proc NatlAcad Sei USA 1991;88:11091-4.
    • Proc NatlAcad Sei USA
    • Smith, B.J.1
  • 353
    • 0025233648 scopus 로고    scopus 로고
    • Faber LE, Toft DO. Purification of unactivated progesterone receptor and identification of novel receptor-associated proteins. 1990;265:3996-4003.
    • Smith DF, Faber LE, Toft DO. Purification of unactivated progesterone receptor and identification of novel receptor-associated proteins. JBiol Chem 1990;265:3996-4003.
    • JBiol Chem
    • Smith, D.F.1
  • 354
    • 0025787706 scopus 로고    scopus 로고
    • Rossi JM, Colic K, McGarry T, Lindquist S. Changes in hsp70 alter thermotolerance and heat shock regulation inDrosophila. 1991 ;3:1106-20.
    • Solomon JM, Rossi JM, Colic K, McGarry T, Lindquist S. Changes in hsp70 alter thermotolerance and heat shock regulation inDrosophila. New Bio! 1991 ;3:1106-20.
    • New Bio!
    • Solomon, J.M.1
  • 355
    • 33845222558 scopus 로고    scopus 로고
    • Chow YH, Hutchison KA, Perdew GH, Jove R, Pratt WB. Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system. 1993;268:21711-6.
    • Stancato LF, Chow YH, Hutchison KA, Perdew GH, Jove R, Pratt WB. Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in
    • J Biol Chem
    • Stancato, L.F.1
  • 356
    • 0027296209 scopus 로고    scopus 로고
    • Wang Y. Reversal of long-term potentiation by inhibitors of haem oxygenase. 1993;364:147-9.
    • Stevens CF, Wang Y. Reversal of long-term potentiation by inhibitors of haem oxygenase. Nature 1993;364:147-9.
    • Nature
    • Stevens, C.F.1
  • 357
    • 0025058171 scopus 로고    scopus 로고
    • Calderwood SK. Members of the 70-kilodalton heat shock protein family contain a highly conserved calmodulin-binding domain. 1990; 10:1234-8.
    • Stevenson MA, Calderwood SK. Members of the 70-kilodalton heat shock protein family contain a highly conserved calmodulin-binding domain. Mol Cell Biol 1990; 10:1234-8.
    • Mol Cell Biol
    • Stevenson, M.A.1
  • 358
    • 0025303671 scopus 로고    scopus 로고
    • Rotenberg MO, Maines MD. Developmental expression of heme oxygenase isozymes in rat brain. 1990;265:8212-7.
    • Sun Y, Rotenberg MO, Maines MD. Developmental expression of heme oxygenase isozymes in rat brain. Two HO-2 mRNAs are detected. J Biol Chem 1990;265:8212-7.
    • Two HO-2 MRNAs Are Detected. J Biol Chem
    • Sun, Y.1
  • 359
    • 0027023997 scopus 로고    scopus 로고
    • Sharp FR. Zinc toxicity and induction of the 72 kD heat shock protein in primary astrocyte culture. 1992;6:198-205.
    • Swanson RA, Sharp FR. Zinc toxicity and induction of the 72 kD heat shock protein in primary astrocyte culture. Clia 1992;6:198-205.
    • Clia
    • Swanson, R.A.1
  • 360
    • 0024515528 scopus 로고    scopus 로고
    • Kramer G, Hardesty B. The phosphorylation state of the reticulocyte 90-kDa heat shock protein affects its ability to increase phosphorylation of peptide initiation factor 2 alpha subunit by the heme-sensitive kinase. 1989;28:1435-8.
    • Szyszka R, Kramer G, Hardesty B. The phosphorylation state of the reticulocyte 90-kDa heat shock protein affects its ability to increase phosphorylation of peptide initiation factor 2 alpha subunit by the heme-sensitive kinase. Biochemistry 1989;28:1435-8.
    • Biochemistry
    • Szyszka, R.1
  • 361
    • 0028017675 scopus 로고    scopus 로고
    • Kanda T, Ohkawa K, Matsuda M. Ubiquitin and ubiquitin-protein conjugates in PC12h cells: changes during neuronal differentiation. 1994;19:391-8.
    • Takada K, Kanda T, Ohkawa K, Matsuda M. Ubiquitin and ubiquitin-protein conjugates in PC12h cells: changes during neuronal differentiation. Ncurochem Res 1994;19:391-8.
    • Ncurochem Res
    • Takada, K.1
  • 362
    • 0028107267 scopus 로고    scopus 로고
    • Hosokawa N, Hirayoshi K, Nagata K. Alternative 5' splice site selection induced by heat shock. 1994;14:567-75.
    • Takechi H, Hosokawa N, Hirayoshi K, Nagata K. Alternative 5' splice site selection induced by heat shock. Mol Cell Biol 1994;14:567-75.
    • Mol Cell Biol
    • Takechi, H.1
  • 366
    • 0028055116 scopus 로고    scopus 로고
    • Decker PB, Wu C. ATP-dependent nucleosome disruption at a heat shock promoter mediated by binding of GAGA transcription factor. 1994;367:525-32.
    • Tsukiyama T, Decker PB, Wu C. ATP-dependent nucleosome disruption at a heat shock promoter mediated by binding of GAGA transcription factor. Nature 1994;367:525-32.
    • Nature
    • Tsukiyama, T.1
  • 367
    • 0027389083 scopus 로고    scopus 로고
    • Anderton BH, Thomas SM. Changes in heat shock protein 70 and ubiquitin mRNA levels in C1300 N2A mouse neuroblastoma cells following treatment with iron. 1993;60:659-65.
    • Uney JB, Anderton BH, Thomas SM. Changes in heat shock protein 70 and ubiquitin mRNA levels in C1300 N2A mouse neuroblastoma cells following treatment with iron. JNeurochem 1993;60:659-65.
    • JNeurochem
    • Uney, J.B.1
  • 368
    • 0027508171 scopus 로고    scopus 로고
    • Kew JN, Staley K, Tyers P, Sofroniew MV Transfection-mediated expression of human Hsp70i protects rat dorsal root ganglian neurones and glia from severe heat stress. 1993;334:313-6.
    • Uney JB, Kew JN, Staley K, Tyers P, Sofroniew MV Transfection-mediated expression of human Hsp70i protects rat dorsal root ganglian neurones and glia from severe heat stress. FEES Lett 1993;334:313-6.
    • FEES Lett
    • Uney, J.B.1
  • 369
    • 0027304485 scopus 로고    scopus 로고
    • Fukuhara K, Patchev V, Chrousos GP. Effect of single and repeated immobilization stress on the heat shock protein 70/90 system of the rat: glucocorticoid-independent, reversible reduction of Hsp90 in the liver and spleen. 1993;57:1057-65.
    • Vamvakopoulos NC, Fukuhara K, Patchev V, Chrousos GP. Effect of single and repeated immobilization stress on the heat shock protein 70/90 system of the rat: glucocorticoid-independent, reversible reduction of Hsp90 in the liver and spleen. Neuroendocrinology 1993;57:1057-65.
    • Neuroendocrinology
    • Vamvakopoulos, N.C.1
  • 370
    • 0025981503 scopus 로고    scopus 로고
    • DeNagel DC, Guagliardi LE, Brodsky FM, Pierce SK. Cellular and subcellular distribution of PBP72/74, a peptide-binding protein that plays a role in antigen processing. 1991;146:500-6.
    • VanBuskirk AM, DeNagel DC, Guagliardi LE, Brodsky FM, Pierce SK. Cellular and subcellular distribution of PBP72/74, a peptide-binding protein that plays a role in antigen processing. J Immunol 1991;146:500-6.
    • J Immunol
    • Vanbuskirk, A.M.1
  • 371
    • 0028044497 scopus 로고    scopus 로고
    • Developmental expression of GLUT 1 and GLUT3 glucose transporters in rat brain. 1994;62:240-6.
    • Vannucci SJ. Developmental expression of GLUT 1 and GLUT3 glucose transporters in rat brain. J/V
    • J/V
    • Vannucci, S.J.1
  • 372
    • 0024590250 scopus 로고    scopus 로고
    • Berger ML, NowakTJ, Welch WJ, Lassmann H. Induction of stress protein HSP70 in nerve cells after status epilepticus in the rat. 1989; 100:259-64.
    • Vass K, Berger ML, NowakTJ, Welch WJ, Lassmann H. Induction of stress protein HSP70 in nerve cells after status epilepticus in the rat. Neurosci Lett 1989; 100:259-64.
    • Neurosci Lett
    • Vass, K.1
  • 373
    • 0024204164 scopus 로고    scopus 로고
    • Welch WJ, Nowak TJ. Localization of 70-kDa stress protein induction in gerbil brain after ischemia. 1988;77:128-35.
    • Vass K, Welch WJ, Nowak TJ. Localization of 70-kDa stress protein induction in gerbil brain after ischemia. Ada Neuropathol (Berl) 1988;77:128-35.
    • Ada Neuropathol (Berl)
    • Vass, K.1
  • 374
    • 0027458551 scopus 로고    scopus 로고
    • Hirsch DJ, Glatt CE, Ronnett GV, Snyder SH. Carbon monoxide: a putative neural messenger. 1993;259:381-4.
    • Verma A, Hirsch DJ, Glatt CE, Ronnett GV, Snyder SH. Carbon monoxide: a putative neural messenger. Science 1993;259:381-4.
    • Science
    • Verma, A.1
  • 375
    • 0027352972 scopus 로고    scopus 로고
    • Ranty B, Dillenschneider M, Charpenteau M, Ranjeva R. Molecular characterization of a 70 kDa heat shock protein of bean mitochondria. 1993;3:143-50.
    • Vidai V, Ranty B, Dillenschneider M, Charpenteau M, Ranjeva R. Molecular characterization of a 70 kDa heat shock protein of bean mitochondria. Plant J 1993;3:143-50.
    • Plant J
    • Vidai, V.1
  • 376
    • 0028140088 scopus 로고    scopus 로고
    • de Haard-Hoekman WA, Merck KB, Bloemendal H, de Jong WW. Elastase inhibition by the Cterminal domains of alpha-crystallin and small heat shock protein. 1994;l204:43-7.
    • Voorter CE, de Haard-Hoekman WA, Merck KB, Bloemendal H, de Jong WW. Elastase inhibition by the Cterminal domains of alpha-crystallin and small heat shock protein. Biochim Biophys Acta 1994;l204:43-7.
    • Biochim Biophys Acta
    • Voorter, C.E.1
  • 377
    • 0027414085 scopus 로고    scopus 로고
    • Kaul SC, Ikawa Y, SugimotoY. Identification of a novel member of mouse hsp70 family. 1993;268:6615-21.
    • Wadhwa R, Kaul SC, Ikawa Y, SugimotoY. Identification of a novel member of mouse hsp70 family. Its association with cellular mortal phenotype. J Biol Chem 1993;268:6615-21.
    • Its Association with Cellular Mortal Phenotype. J Biol Chem
    • Wadhwa, R.1
  • 378
    • 0027227379 scopus 로고    scopus 로고
    • Kaul SC, Mitsui Y, Sugimoto Y. Differential subcellular distribution of mortalin in mortal and immortal mouse and human fibroblasts. 1993:207:442-8.
    • Wadhwa R, Kaul SC, Mitsui Y, Sugimoto Y. Differential subcellular distribution of mortalin in mortal and immortal mouse and human fibroblasts. Exp Cell Res 1993:207:442-8.
    • Exp Cell Res
    • Wadhwa, R.1
  • 379
    • 0027425062 scopus 로고    scopus 로고
    • Kaul SC, Sugimoto Y, Mitsui Y. Induction of cellular senescence by transfection of cytosolic mortalin cDNA in NIH 3T3 cells. 1993;268:22239-42.
    • Wadhwa R, Kaul SC, Sugimoto Y, Mitsui Y. Induction of cellular senescence by transfection of cytosolic mortalin cDNA in NIH 3T3 cells. JBio! Chem 1993;268:22239-42.
    • JBio! Chem
    • Wadhwa, R.1
  • 380
    • 0027371985 scopus 로고    scopus 로고
    • Kaul SC, Sugimoto Y, Mitsui Y Spontaneous immortalization of mouse fibroblasts involves structural changes in senescence inducing protein, mortalin. 1993;197:202-6.
    • Wadhwa R, Kaul SC, Sugimoto Y, Mitsui Y Spontaneous immortalization of mouse fibroblasts involves structural changes in senescence inducing protein, mortalin. Biochem Biophys Res Commun 1993;197:202-6.
    • Biochem Biophys Res Commun
    • Wadhwa, R.1
  • 381
    • 0024477879 scopus 로고    scopus 로고
    • Foulds WS. Response of cultured Muller cells to heat shock-an immunocytochemical study of heat shock and intermediate filament proteins in response to temperature elevation. 1989;48:337-50.
    • Wakakura M, Foulds WS. Response of cultured Muller cells to heat shock-an immunocytochemical study of heat shock and intermediate filament proteins in response to temperature elevation. Exp Eye Res 1989;48:337-50.
    • Exp Eye Res
    • Wakakura, M.1
  • 382
    • 0027517597 scopus 로고    scopus 로고
    • Longo FM, Chen J, Butman M, Graham SH, Haglid KG, Sharp FR. Induction of glucose regulated protein (grp78) and inducible heat shock protein (hsp70) mRNAs in rat brain after kainic acid seizures and focal ischemia. 1993:23:575-82.
    • Wang S, Longo FM, Chen J, Butman M, Graham SH, Haglid KG, Sharp FR. Induction of glucose regulated protein (grp78) and inducible heat shock protein (hsp70) mRNAs in rat brain after kainic acid seizures and focal ischemia. Neurochem Int 1993:23:575-82.
    • Neurochem Int
    • Wang, S.1
  • 383
    • 0020565766 scopus 로고    scopus 로고
    • Garrels JI, Thomas GP, Lin JJ, Feramisco JR. Biochemical characterization of the mammalian stress proteins and identification of two stress proteins as glucose- and Ca2+-ionophore-regulated proteins. 7102-ll.
    • Welch WJ, Garrels JI, Thomas GP, Lin JJ, Feramisco JR. Biochemical characterization of the mammalian stress proteins and identification of two stress proteins as glucose- and Ca2+-ionophore-regulated proteins. J Sio/CAewl983;258:7102-ll.
    • J Sio/CAewl983;258
    • Welch, W.J.1
  • 384
    • 0022976650 scopus 로고    scopus 로고
    • Suhan JP. Cellular and biochemical events in mammalian cells during and after recovery from physiological stress. 1986;103:2035-52.
    • Welch WJ, Suhan JP. Cellular and biochemical events in mammalian cells during and after recovery from physiological stress. J Cell Biol 1986;103:2035-52.
    • J Cell Biol
    • Welch, W.J.1
  • 385
    • 0026604773 scopus 로고    scopus 로고
    • Moyer DJ, Harris VA. Regional expression of heat shock protein-70 mRNA and c-fos mRNA following focal ischemia in rat brain. 1992; 12:204-12.
    • Welsh FA, Moyer DJ, Harris VA. Regional expression of heat shock protein-70 mRNA and c-fos mRNA following focal ischemia in rat brain. J Cereb Blood Flow Metab 1992; 12:204-12.
    • J Cereb Blood Flow Metab
    • Welsh, F.A.1
  • 386
    • 0026019757 scopus 로고    scopus 로고
    • Sasson S, Cerasi E, Ben NY. The ubiquitous glucose transporter GLUT-1 belongs to the glucose-regulated protein family of stress-inducible proteins. 1991:88:2525-9.
    • Wertheimer E, Sasson S, Cerasi E, Ben NY. The ubiquitous glucose transporter GLUT-1 belongs to the glucose-regulated protein family of stress-inducible proteins. Proc Natl Acad Sei USA 1991:88:2525-9.
    • Proc Natl Acad Sei USA
    • Wertheimer, E.1
  • 387
    • 0025955517 scopus 로고    scopus 로고
    • Clos J, Wu C. Stress-induced oligomerization and chromosomal relocalization of heat shock factor. 1991;353:822-7.
    • Westwood JT, Clos J, Wu C. Stress-induced oligomerization and chromosomal relocalization of heat shock factor. Nature 1991;353:822-7.
    • Nature
    • Westwood, J.T.1
  • 388
    • 0022352547 scopus 로고    scopus 로고
    • Hightower LE. Differential induction of glucose-regulated and heat shock proteins: effects of pH and sulfhydryl-reducing agents on chicken embryo cells. 1985;125:251-8.
    • Whelan SA, Hightower LE. Differential induction of glucose-regulated and heat shock proteins: effects of pH and sulfhydryl-reducing agents on chicken embryo cells. J Cell Physiol 1985;125:251-8.
    • J Cell Physiol
    • Whelan, S.A.1
  • 389
    • 0025924585 scopus 로고    scopus 로고
    • Kuroiwa T, Bonnekoh P, Hossmann K-A. 14 CLeucine incorporation into brain proteins in gerbils after transient ischemia: relationship to selective vulnerability of hippocampus. 1991;56:789-96.
    • Widmann R, Kuroiwa T, Bonnekoh P, Hossmann K-A. [14C]Leucine incorporation into brain proteins in gerbils after transient ischemia: relationship to selective vulnerability of hippocampus. J Neurochem 1991;56:789-96.
    • J Neurochem
    • Widmann, R.1
  • 390
    • 0027267382 scopus 로고    scopus 로고
    • MiyazawaT, Hossmann K-A. Protective effect of hypothermia on hippocampal injury after 30 minutes of forebrain ischemia in rats is mediated by postischemic recovery of protein synthesis. 1993;61:200-9.
    • Widmann R, MiyazawaT, Hossmann K-A. Protective effect of hypothermia on hippocampal injury after 30 minutes of forebrain ischemia in rats is mediated by postischemic recovery of protein synthesis. J Neurochem 1993;61:200-9.
    • J Neurochem
    • Widmann, R.1
  • 391
    • 0026525959 scopus 로고    scopus 로고
    • Weber C, Bonnekoh P, Schlenker M, Hossmann K-A. Neuronal damage after repeated 5 minutes of ischemia in the gerbil is preceded by prolonged impairment of protein metabolism. 1992;12:425-53.
    • Widmann R, Weber C, Bonnekoh P, Schlenker M, Hossmann K-A. Neuronal damage after repeated 5 minutes of ischemia in the gerbil is preceded by prolonged impairment of protein metabolism. J Cereb Blood Flow Metab 1992;12:425-53.
    • J Cereb Blood Flow Metab
    • Widmann, R.1
  • 392
    • 0026778032 scopus 로고    scopus 로고
    • Buchner J, Zimmermann R, Jakob U. Hsp90 chaperones protein folding in vitro. 1992;358:169-70.
    • Wiech H, Buchner J, Zimmermann R, Jakob U. Hsp90 chaperones protein folding in vitro. Nature 1992;358:169-70.
    • Nature
    • Wiech, H.1
  • 393
    • 0026600989 scopus 로고    scopus 로고
    • Weiss SR, Gold PW, Doi SQ, Banerjee S, Licinio J, Lad R, Post RM, Smith MA. Induction of constitutive heat shock protein 73 mRNA in the dentate gyrus by seizures. 1992;13:19-25.
    • Wong ML, Weiss SR, Gold PW, Doi SQ, Banerjee S, Licinio J, Lad R, Post RM, Smith MA. Induction of constitutive heat shock protein 73 mRNA in the dentate gyrus by seizures. Brain Res Mol Brain Res 1992;13:19-25.
    • Brain Res Mol Brain Res
    • Wong, M.L.1
  • 394
    • 0026076021 scopus 로고    scopus 로고
    • Li LJ, Navarro D, Qadri I, Pereira L, Lee AS. Transactivation of the grp78 promoter by malfolded proteins, glycosylation block, and calcium ionophore is mediated through a proximal region containing a CCAAT motif which interacts with CTF/NF-I. 1991 ; 11:5612-23.
    • Wooden SK, Li LJ, Navarro D, Qadri I, Pereira L, Lee AS. Transactivation of the grp78 promoter by malfolded proteins, glycosylation block, and calcium ionophore is mediated through a proximal region containing a CCAAT motif which interacts with CTF/NF-I. Mol Cell Biol 1991 ; 11:5612-23.
    • Mol Cell Biol
    • Wooden, S.K.1
  • 395
    • 0028168920 scopus 로고    scopus 로고
    • Smith MW, Maki A, Berezesky IK, Trump BF. Role of cytosolic Ca2 and protein kinases in the induction of the hsp70 gene. 1991;45:1093-104.
    • Yamamoto N, Smith MW, Maki A, Berezesky IK, Trump BF. Role of cytosolic Ca2 and protein kinases in the induction of the hsp70 gene. Kidney Int 1991;45:1093-104.
    • Kidney Int
    • Yamamoto, N.1
  • 396
    • 0025788105 scopus 로고    scopus 로고
    • Eguchi Y, Kajiwara K, Ito H. Mild hypothermia ameliorates ubiquitin synthesis and prevents delayed neuronal death in the gerbil hippocampus. 1991;22:1574-81.
    • Yamashita K, Eguchi Y, Kajiwara K, Ito H. Mild hypothermia ameliorates ubiquitin synthesis and prevents delayed neuronal death in the gerbil hippocampus. Stroke 1991;22:1574-81.
    • Stroke
    • Yamashita, K.1
  • 397
    • 0024268031 scopus 로고    scopus 로고
    • Lindquist S. Translation of unspliced transcripts after heat shock. 1988:242:1544-8.
    • Yost HJ, Lindquist S. Translation of unspliced transcripts after heat shock. Science 1988:242:1544-8.
    • Science
    • Yost, H.J.1
  • 398
    • 0025277461 scopus 로고    scopus 로고
    • Petersen RB, Lindquist S. RNA metabolism: strategies for regulation in the heat shock response. 1990;6:223-7.
    • Yost HJ, Petersen RB, Lindquist S. RNA metabolism: strategies for regulation in the heat shock response. Trends Genet 1990;6:223-7.
    • Trends Genet
    • Yost, H.J.1
  • 399
    • 0025277461 scopus 로고    scopus 로고
    • Petersen RB, Lindquist S. RNA metabolism: strategies for regulation in the heat shock response. 1990;6:223-27.
    • Yost HJ, Petersen RB, Lindquist S. RNA metabolism: strategies for regulation in the heat shock response. Trends Genet 1990;6:223-27.
    • Trends Genet
    • Yost, H.J.1
  • 400
    • 0025371740 scopus 로고    scopus 로고
    • Wang C. Glucose transporter immunoreactivity in the hypothalamus and area postrema. 1990;24:525-8.
    • Young JK, Wang C. Glucose transporter immunoreactivity in the hypothalamus and area postrema. Brain Res Bull 1990;24:525-8.
    • Brain Res Bull
    • Young, J.K.1
  • 401
    • 33845230652 scopus 로고    scopus 로고
    • Swanson R, Sharp F, Sagar S. Dexamethasone potentiates heat shock protein 72 induction in primary astrocyte cultures. 1992;18:533.10
    • Zhang S, Swanson R, Sharp F, Sagar S. Dexamethasone potentiates heat shock protein 72 induction in primary astrocyte cultures. Soc Neurosci Abs 1992;18:533.10
    • Soc Neurosci Abs
    • Zhang, S.1
  • 402
    • 0025905225 scopus 로고    scopus 로고
    • Levine RA, Farber HW. Hypoxia induces a specific set of stress proteins in cultured endothelial cells. 1991;87:908-14.
    • Zimmerman LH, Levine RA, Farber HW. Hypoxia induces a specific set of stress proteins in cultured endothelial cells. J Clin Invest 1991;87:908-14.
    • J Clin Invest
    • Zimmerman, L.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.