메뉴 건너뛰기




Volumn 25, Issue 3, 2006, Pages 493-501

Thermoprotection of synaptic transmission in a Drosophila heat shock factor mutant is accompanied by increased expression of Hsp83 and DnaJ-1

Author keywords

Heat stress; Microarray; Neuromuscular junction; Thermotolerance

Indexed keywords

CHAPERONE; GLUTATHIONE TRANSFERASE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; MUTANT PROTEIN; PROTEIN DNAJ; PROTEIN HSP83; UNCLASSIFIED DRUG;

EID: 33646778105     PISSN: 10948341     EISSN: 15312267     Source Type: Journal    
DOI: 10.1152/physiolgenomics.00195.2005     Document Type: Article
Times cited : (31)

References (59)
  • 2
    • 0042510237 scopus 로고    scopus 로고
    • Role for calcium in heat shock-mediated synaptic thermoprotection in Drosophila larvae
    • Barclay JW and Robertson RM. Role for calcium in heat shock-mediated synaptic thermoprotection in Drosophila larvae. J Neurobiol 56: 360-371, 2003.
    • (2003) J Neurobiol , vol.56 , pp. 360-371
    • Barclay, J.W.1    Robertson, R.M.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254, 1976.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0025288608 scopus 로고
    • Purification of Drosophila hsp 83 and immunoelectron microscopic localization
    • Carbajal ME, Valet JP, Charest PM, and Tanguay RM. Purification of Drosophila hsp 83 and immunoelectron microscopic localization. Eur J Cell Biol 52: 147-156, 1990.
    • (1990) Eur J Cell Biol , vol.52 , pp. 147-156
    • Carbajal, M.E.1    Valet, J.P.2    Charest, P.M.3    Tanguay, R.M.4
  • 10
    • 0034663177 scopus 로고    scopus 로고
    • Cysteine-string protein increases the calcium sensitivity of neurotransmitter exocytosis in Drosophila
    • Dawson-Scully K, Bronk P, Atwood HL, and Zinsmaier KE. Cysteine-string protein increases the calcium sensitivity of neurotransmitter exocytosis in Drosophila. J Neurosci 20: 6039-6047, 2000.
    • (2000) J Neurosci , vol.20 , pp. 6039-6047
    • Dawson-Scully, K.1    Bronk, P.2    Atwood, H.L.3    Zinsmaier, K.E.4
  • 11
    • 0028231927 scopus 로고
    • Preferential deadenylation of Hsp70 mRNA plays a key role in regulating Hsp70 expression in Drosophila melanogaster
    • Dellavalle RP, Petersen R, and Lindquist S. Preferential deadenylation of Hsp70 mRNA plays a key role in regulating Hsp70 expression in Drosophila melanogaster. Mol Cell Biol 14: 3646-3659, 1994.
    • (1994) Mol Cell Biol , vol.14 , pp. 3646-3659
    • Dellavalle, R.P.1    Petersen, R.2    Lindquist, S.3
  • 12
    • 0027674382 scopus 로고
    • Localized RNAs and their functions
    • Ding D and Lipshitz HD. Localized RNAs and their functions. Bioessays 15: 651-658, 1993.
    • (1993) Bioessays , vol.15 , pp. 651-658
    • Ding, D.1    Lipshitz, H.D.2
  • 13
    • 0032571320 scopus 로고    scopus 로고
    • The role of DnaJ-like proteins in glucocorticoid receptor. hsp90 heterocomplex assembly by the reconstituted hsp90 p60 hsp70 foldosome complex
    • Dittmar KD, Banach M, Galigniana MD, and Pratt WB. The role of DnaJ-like proteins in glucocorticoid receptor. hsp90 heterocomplex assembly by the reconstituted hsp90 p60 hsp70 foldosome complex. J Biol Chem 273: 7358-7366, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 7358-7366
    • Dittmar, K.D.1    Banach, M.2    Galigniana, M.D.3    Pratt, W.B.4
  • 14
    • 0030217968 scopus 로고    scopus 로고
    • Effect of engineering Hsp70 copy number on Hsp70 expression and tolerance of ecologically relevant heat shock in larvae and pupae of Drosophila melanogaster
    • Feder ME, Cartano NV, Milos L, Krebs RA, and Lindquist SL. Effect of engineering Hsp70 copy number on Hsp70 expression and tolerance of ecologically relevant heat shock in larvae and pupae of Drosophila melanogaster. J Exp Biol 199: 1837-1844, 1996.
    • (1996) J Exp Biol , vol.199 , pp. 1837-1844
    • Feder, M.E.1    Cartano, N.V.2    Milos, L.3    Krebs, R.A.4    Lindquist, S.L.5
  • 15
    • 0035162698 scopus 로고    scopus 로고
    • Genomic expression responses to DNA-damaging agents and the regulatory role of the yeast ATR homolog Mec1p
    • Gasch AP, Huang M, Metzner S, Botstein D, Elledge SJ, and Brown PO. Genomic expression responses to DNA-damaging agents and the regulatory role of the yeast ATR homolog Mec1p. Mol Biol Cell 12: 2987-3003, 2001.
    • (2001) Mol Biol Cell , vol.12 , pp. 2987-3003
    • Gasch, A.P.1    Huang, M.2    Metzner, S.3    Botstein, D.4    Elledge, S.J.5    Brown, P.O.6
  • 16
    • 2442682934 scopus 로고    scopus 로고
    • Independent functions of hsp90 in neurotransmitter release and in the continuous synaptic cycling of AMPA receptors
    • Gerges NZ, Tran IC, Backos DS, Harrell JM, Chinkers M, Pratt WB, and Esteban JA. Independent functions of hsp90 in neurotransmitter release and in the continuous synaptic cycling of AMPA receptors. J Neurosci 24: 4758-4766, 2004.
    • (2004) J Neurosci , vol.24 , pp. 4758-4766
    • Gerges, N.Z.1    Tran, I.C.2    Backos, D.S.3    Harrell, J.M.4    Chinkers, M.5    Pratt, W.B.6    Esteban, J.A.7
  • 17
    • 2942598422 scopus 로고    scopus 로고
    • Genome-wide analysis of the biology of stress responses through heat shock transcription factor
    • Hahn JS, Hu Z, Thiele DJ, and Iyer VR. Genome-wide analysis of the biology of stress responses through heat shock transcription factor. Mol Cell Biol 24: 5249-5256, 2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 5249-5256
    • Hahn, J.S.1    Hu, Z.2    Thiele, D.J.3    Iyer, V.R.4
  • 18
    • 1942518714 scopus 로고    scopus 로고
    • Phosphorylation of the yeast heat shock transcription factor is implicated in gene-specific activation dependent on the architecture of the heat shock element
    • Hashikawa N and Sakurai H. Phosphorylation of the yeast heat shock transcription factor is implicated in gene-specific activation dependent on the architecture of the heat shock element. Mol Cell Biol 24: 3648-3659, 2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 3648-3659
    • Hashikawa, N.1    Sakurai, H.2
  • 20
    • 0030985251 scopus 로고    scopus 로고
    • Multiple functions of Drosophila heat shock transcription factor in vivo
    • Jedlicka P, Mortin MA, and Wu C. Multiple functions of Drosophila heat shock transcription factor in vivo. EMBO J 16: 2452-2462, 1997.
    • (1997) EMBO J , vol.16 , pp. 2452-2462
    • Jedlicka, P.1    Mortin, M.A.2    Wu, C.3
  • 21
    • 0036177499 scopus 로고    scopus 로고
    • Enhancement of presynaptic performance in transgenic Drosophila overexpressing heat shock protein Hsp70
    • Karunanithi S, Barclay JW, Brown IR, Robertson RM, and Atwood HL. Enhancement of presynaptic performance in transgenic Drosophila overexpressing heat shock protein Hsp70. Synapse 44: 8-14, 2002.
    • (2002) Synapse , vol.44 , pp. 8-14
    • Karunanithi, S.1    Barclay, J.W.2    Brown, I.R.3    Robertson, R.M.4    Atwood, H.L.5
  • 23
    • 18744431083 scopus 로고    scopus 로고
    • Thermal preconditioning and heat-shock protein 72 preserve synaptic transmission during thermal stress
    • Kelty JD, Noseworthy PA, Feder ME, Robertson RM, and Ramirez JM. Thermal preconditioning and heat-shock protein 72 preserve synaptic transmission during thermal stress. J Neurosci 22: RC193, 2002.
    • (2002) J Neurosci , vol.22
    • Kelty, J.D.1    Noseworthy, P.A.2    Feder, M.E.3    Robertson, R.M.4    Ramirez, J.M.5
  • 24
    • 0036084783 scopus 로고    scopus 로고
    • Heat shock proteins: Modifying factors in physiological stress responses and acquired thermotolerance
    • Kregel KC. Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance. J Appl Physiol 92: 2177-2186, 2002.
    • (2002) J Appl Physiol , vol.92 , pp. 2177-2186
    • Kregel, K.C.1
  • 26
    • 0029069981 scopus 로고
    • Transient acquired thermotolerance in Drosophila, correlated with rapid degradation of Hsp70 during recovery
    • Li D and Duncan RF. Transient acquired thermotolerance in Drosophila, correlated with rapid degradation of Hsp70 during recovery. Eur J Biochem 231: 454-465, 1995.
    • (1995) Eur J Biochem , vol.231 , pp. 454-465
    • Li, D.1    Duncan, R.F.2
  • 27
    • 0035254534 scopus 로고    scopus 로고
    • Modulation of Drosophila heat shock transcription factor activity by the molecular chaperone DROJ1
    • Marchler G and Wu C. Modulation of Drosophila heat shock transcription factor activity by the molecular chaperone DROJ1. EMBO J 20: 499-509, 2001.
    • (2001) EMBO J , vol.20 , pp. 499-509
    • Marchler, G.1    Wu, C.2
  • 28
    • 0030048735 scopus 로고    scopus 로고
    • Regulatory differences in the stress response of hippocampal neurons and glial cells after heat shock
    • Marcuccilli CJ, Mathur SK, Morimoto RI, and Miller RJ. Regulatory differences in the stress response of hippocampal neurons and glial cells after heat shock. J Neurosci 16: 478-485, 1996.
    • (1996) J Neurosci , vol.16 , pp. 478-485
    • Marcuccilli, C.J.1    Mathur, S.K.2    Morimoto, R.I.3    Miller, R.J.4
  • 29
    • 0000628109 scopus 로고
    • Use of blue food to select synchronous, late third-instar larvae
    • Maroni G and Stamey SC. Use of blue food to select synchronous, late third-instar larvae. Drosophila Information Service 59: 142-143, 1983.
    • (1983) Drosophila Information Service , vol.59 , pp. 142-143
    • Maroni, G.1    Stamey, S.C.2
  • 30
    • 0022133046 scopus 로고
    • The preferential translation of Drosophila hsp70 mRNA requires sequences in the untranslated leader
    • McGarry TJ and Lindquist S. The preferential translation of Drosophila hsp70 mRNA requires sequences in the untranslated leader. Cell 42: 903-911, 1985.
    • (1985) Cell , vol.42 , pp. 903-911
    • McGarry, T.J.1    Lindquist, S.2
  • 31
    • 0030776395 scopus 로고    scopus 로고
    • Cell-specific expression and heat-shock induction of Hsps during spermatogenesis in Drosophila melanogaster
    • Michaud S, Marin R, Westwood JT, and Tanguay RM. Cell-specific expression and heat-shock induction of Hsps during spermatogenesis in Drosophila melanogaster. J Cell Sci 110: 1989-1997, 1997.
    • (1997) J Cell Sci , vol.110 , pp. 1989-1997
    • Michaud, S.1    Marin, R.2    Westwood, J.T.3    Tanguay, R.M.4
  • 32
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto RI. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev 12: 3788-3796, 1998.
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 33
    • 0030724378 scopus 로고    scopus 로고
    • Heat shock proteins and heat adaptation of the whole organism
    • Moseley PL. Heat shock proteins and heat adaptation of the whole organism. J Appl Physiol 83: 1413-1417, 1997.
    • (1997) J Appl Physiol , vol.83 , pp. 1413-1417
    • Moseley, P.L.1
  • 34
    • 0345358575 scopus 로고    scopus 로고
    • Construction of a cDNA-based microarray for Drosophila melanogaster: A comparison of gene transcription profiles from SL2 and Kc167 cells
    • Neal SJ, Gibson ML, So AK, and Westwood JT. Construction of a cDNA-based microarray for Drosophila melanogaster: a comparison of gene transcription profiles from SL2 and Kc167 cells. Genome 46: 879-892, 2003.
    • (2003) Genome , vol.46 , pp. 879-892
    • Neal, S.J.1    Gibson, M.L.2    So, A.K.3    Westwood, J.T.4
  • 37
    • 0037435395 scopus 로고    scopus 로고
    • Assumption-free analysis of quantitative real-time polymerase chain reaction (PCR) data
    • Ramakers C, Ruijter JM, Deprez RH, and Moorman AF. Assumption-free analysis of quantitative real-time polymerase chain reaction (PCR) data. Neurosci Lett 339: 62-66, 2003.
    • (2003) Neurosci Lett , vol.339 , pp. 62-66
    • Ramakers, C.1    Ruijter, J.M.2    Deprez, R.H.3    Moorman, A.F.4
  • 38
    • 18144426050 scopus 로고    scopus 로고
    • Drosophila soluble guanylyl cyclase mutants exhibit increased foraging locomotion: Behavioral and genomic investigations
    • Riedl CA, Neal SJ, Robichon A, Westwood JT, and Sokolowski MB. Drosophila soluble guanylyl cyclase mutants exhibit increased foraging locomotion: behavioral and genomic investigations. Behav Genet 35: 231-244, 2005.
    • (2005) Behav Genet , vol.35 , pp. 231-244
    • Riedl, C.A.1    Neal, S.J.2    Robichon, A.3    Westwood, J.T.4    Sokolowski, M.B.5
  • 39
    • 0033990048 scopus 로고    scopus 로고
    • Primer3 on the WWW for general users and for biologist programmers
    • Rozen S and Skaletsky H. Primer3 on the WWW for general users and for biologist programmers. Methods Mol Biol 132: 365-386, 2000.
    • (2000) Methods Mol Biol , vol.132 , pp. 365-386
    • Rozen, S.1    Skaletsky, H.2
  • 40
    • 0037110754 scopus 로고    scopus 로고
    • Rab-alphaGDI activity is regulated by a Hsp90 chaperone complex
    • Sakisaka T, Meerlo T, Matteson J, Plutner H, and Balch WE. Rab-alphaGDI activity is regulated by a Hsp90 chaperone complex. EMBO J 21: 6125-6135, 2002.
    • (2002) EMBO J , vol.21 , pp. 6125-6135
    • Sakisaka, T.1    Meerlo, T.2    Matteson, J.3    Plutner, H.4    Balch, W.E.5
  • 42
    • 0037337927 scopus 로고    scopus 로고
    • Cloning, expression and biochemical characterization of one epsilon-class (GST-3) and ten delta-class (GST-1) glutathione S-transferases from Drosophila melanogaster, and identification of additional nine members of the epsilon class
    • Sawicki R, Singh SP, Mondal AK, Benes H, and Zimniak P. Cloning, expression and biochemical characterization of one epsilon-class (GST-3) and ten delta-class (GST-1) glutathione S-transferases from Drosophila melanogaster, and identification of additional nine members of the epsilon class. Biochem J 370: 661-669, 2003.
    • (2003) Biochem J , vol.370 , pp. 661-669
    • Sawicki, R.1    Singh, S.P.2    Mondal, A.K.3    Benes, H.4    Zimniak, P.5
  • 43
    • 0034637117 scopus 로고    scopus 로고
    • Interaction of the human DnaJ homologue, HSJ1b with the 90 kDa heat shock protein, Hsp90
    • Schnaider T, Soti C, Cheetham ME, Miyata Y, Yahara I, and Csermely P. Interaction of the human DnaJ homologue, HSJ1b with the 90 kDa heat shock protein, Hsp90. Life Sci 67: 1455-1465, 2000.
    • (2000) Life Sci , vol.67 , pp. 1455-1465
    • Schnaider, T.1    Soti, C.2    Cheetham, M.E.3    Miyata, Y.4    Yahara, I.5    Csermely, P.6
  • 44
    • 13944274507 scopus 로고    scopus 로고
    • Smaug recruits the CCR4/POP2/NOT deadenylase complex to trigger maternal transcript localization in the early Drosophila embryo
    • Semotok JL, Cooperstock RL, Pinder BD, Vari HK, Lipshitz HD, and Smibert CA. Smaug recruits the CCR4/POP2/NOT deadenylase complex to trigger maternal transcript localization in the early Drosophila embryo. Curr Biol 15: 284-294, 2005.
    • (2005) Curr Biol , vol.15 , pp. 284-294
    • Semotok, J.L.1    Cooperstock, R.L.2    Pinder, B.D.3    Vari, H.K.4    Lipshitz, H.D.5    Smibert, C.A.6
  • 45
    • 0037118054 scopus 로고    scopus 로고
    • Stress response genes protect against lethal effects of sleep deprivation in Drosophila
    • Shaw PJ, Tononi G, Greenspan RJ, and Robinson DF. Stress response genes protect against lethal effects of sleep deprivation in Drosophila. Nature 417: 287-291, 2002.
    • (2002) Nature , vol.417 , pp. 287-291
    • Shaw, P.J.1    Tononi, G.2    Greenspan, R.J.3    Robinson, D.F.4
  • 46
    • 0027290760 scopus 로고
    • Tissue-specific alternative splicing of the Drosophila dopa decarboxylase gene is affected by heat shock
    • Shen J, Beall CJ, and Hirsh J. Tissue-specific alternative splicing of the Drosophila dopa decarboxylase gene is affected by heat shock. Mol Cell Biol 13: 4549-4555, 1993.
    • (1993) Mol Cell Biol , vol.13 , pp. 4549-4555
    • Shen, J.1    Beall, C.J.2    Hirsh, J.3
  • 47
    • 0029792137 scopus 로고    scopus 로고
    • HSF recruitment and loss at most Drosophila heat shock loci is coordinated and depends on proximal promoter sequences
    • Shopland LS and Lis JT. HSF recruitment and loss at most Drosophila heat shock loci is coordinated and depends on proximal promoter sequences. Chromosoma 105: 158-171, 1996.
    • (1996) Chromosoma , vol.105 , pp. 158-171
    • Shopland, L.S.1    Lis, J.T.2
  • 48
    • 0032080510 scopus 로고    scopus 로고
    • Cloning, characterization and expression of carbonic anhydrase from the cyanobacterium Synechocystis PCC6803
    • So AK and Espie GS. Cloning, characterization and expression of carbonic anhydrase from the cyanobacterium Synechocystis PCC6803. Plant Mol Biol 37: 205-215, 1998.
    • (1998) Plant Mol Biol , vol.37 , pp. 205-215
    • So, A.K.1    Espie, G.S.2
  • 49
    • 0242574386 scopus 로고    scopus 로고
    • The evolutionary and ecological role of heat shock proteins
    • Sorensen JG, Kristensen TN, Loeschcke V. The evolutionary and ecological role of heat shock proteins. Ecol Lett 6: 1025-1037, 2003.
    • (2003) Ecol Lett , vol.6 , pp. 1025-1037
    • Sorensen, J.G.1    Kristensen, T.N.2    Loeschcke, V.3
  • 50
    • 0028483237 scopus 로고
    • Improved stability of Drosophila larval neuromuscular preparations in haemolymph-like physiological solutions
    • Stewart BA, Atwood HL, Renger JJ, Wang J, and Wu CF. Improved stability of Drosophila larval neuromuscular preparations in haemolymph-like physiological solutions. J Comp Physiol [A] 175: 179 -191, 1994.
    • (1994) J Comp Physiol [A] , vol.175 , pp. 179-191
    • Stewart, B.A.1    Atwood, H.L.2    Renger, J.J.3    Wang, J.4    Wu, C.F.5
  • 51
    • 0033573767 scopus 로고    scopus 로고
    • Presence of molecular chaperones, heat shock cognate (Hsc) 70 and heat shock proteins (Hsp) 40, in the postsynaptic structures of rat brain
    • Suzuki T, Usuda N, Murata S, Nakazawa A, Ohtsuka K, and Takagi H. Presence of molecular chaperones, heat shock cognate (Hsc) 70 and heat shock proteins (Hsp) 40, in the postsynaptic structures of rat brain. Brain Res 816: 99-110, 1999.
    • (1999) Brain Res , vol.816 , pp. 99-110
    • Suzuki, T.1    Usuda, N.2    Murata, S.3    Nakazawa, A.4    Ohtsuka, K.5    Takagi, H.6
  • 52
    • 0037151119 scopus 로고    scopus 로고
    • A novel non-conventional heat shock element regulates expression of MDJ1 encoding a DnaJ homolog in Saccharomyces cerevisiae
    • Tachibana T, Astumi S, Shioda R, Ueno M, Uritani M, and Ushimaru T. A novel non-conventional heat shock element regulates expression of MDJ1 encoding a DnaJ homolog in Saccharomyces cerevisiae. J Biol Chem 277: 22140-22146, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 22140-22146
    • Tachibana, T.1    Astumi, S.2    Shioda, R.3    Ueno, M.4    Uritani, M.5    Ushimaru, T.6
  • 53
    • 0032536772 scopus 로고    scopus 로고
    • Disruption of the HSF3 gene results in the severe reduction of heat shock gene expression and loss of thermotolerance
    • Tanabe M, Kawazoe Y, Takeda S, Morimoto RI, Nagata K, and Nakai A. Disruption of the HSF3 gene results in the severe reduction of heat shock gene expression and loss of thermotolerance. EMBO J 17: 1750-1758, 1998.
    • (1998) EMBO J , vol.17 , pp. 1750-1758
    • Tanabe, M.1    Kawazoe, Y.2    Takeda, S.3    Morimoto, R.I.4    Nagata, K.5    Nakai, A.6
  • 54
    • 1542373742 scopus 로고    scopus 로고
    • The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response
    • Trinklein ND, Murray JI, Hartman SJ, Botstein D, and Myers RM. The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response. Mol Biol Cell 15: 1254-1261, 2004.
    • (2004) Mol Biol Cell , vol.15 , pp. 1254-1261
    • Trinklein, N.D.1    Murray, J.I.2    Hartman, S.J.3    Botstein, D.4    Myers, R.M.5
  • 55
    • 0035942271 scopus 로고    scopus 로고
    • Significance analysis of microarrays applied to the ionizing radiation response
    • Tusher VG, Tibshirani R, and Chu G. Significance analysis of microarrays applied to the ionizing radiation response. Proc Natl Acad Sci USA 98: 5116-5121, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5116-5121
    • Tusher, V.G.1    Tibshirani, R.2    Chu, G.3
  • 56
    • 0018847993 scopus 로고
    • Intracellular localization of heat shock proteins in Drosophila
    • Velazquez JM, DiDomenico BJ, and Lindquist S. Intracellular localization of heat shock proteins in Drosophila. Cell 20: 679-689, 1980.
    • (1980) Cell , vol.20 , pp. 679-689
    • Velazquez, J.M.1    DiDomenico, B.J.2    Lindquist, S.3
  • 57
    • 0029142471 scopus 로고
    • The basis for a heat-induced developmental defect: Defining crucial lesions
    • Welte MA, Duncan I, and Lindquist S. The basis for a heat-induced developmental defect: defining crucial lesions. Genes Dev 9: 2240-2250, 1995.
    • (1995) Genes Dev , vol.9 , pp. 2240-2250
    • Welte, M.A.1    Duncan, I.2    Lindquist, S.3
  • 59
    • 0036353722 scopus 로고    scopus 로고
    • Exogenous expression of heat shock protein 90kDa retards the cell cycle and impairs the heat shock response
    • Zhao C, Hashiguchi A, Kondoh K, Du W, Hata J, and Yamada T. Exogenous expression of heat shock protein 90kDa retards the cell cycle and impairs the heat shock response. Exp Cell Res 275: 200-214, 2002.
    • (2002) Exp Cell Res , vol.275 , pp. 200-214
    • Zhao, C.1    Hashiguchi, A.2    Kondoh, K.3    Du, W.4    Hata, J.5    Yamada, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.