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Volumn 61, Issue , 1999, Pages 243-282

Heat-shock proteins, molecular chaperones, and the stress response: Evolutionary and ecological physiology

Author keywords

Bsp; Environmental gradients; Inducible tolerance; Protein denaturation and folding; Temperature

Indexed keywords

BIOLOGICAL MARKER; CHAPERONE; HEAT SHOCK PROTEIN;

EID: 0033057848     PISSN: 00664278     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.physiol.61.1.243     Document Type: Review
Times cited : (3461)

References (374)
  • 1
    • 0030154255 scopus 로고    scopus 로고
    • Discovery of the heat shock response
    • 1. Ritossa F. 1996. Discovery of the heat shock response. Cell Stress Chaperones 1:97-98
    • (1996) Cell Stress Chaperones , vol.1 , pp. 97-98
    • Ritossa, F.1
  • 2
    • 0022555843 scopus 로고
    • The heat-shock re-sponse
    • 2. Lindquist S. 1986. The heat-shock re-sponse. Annu. Rev. Biochem. 55:1151-91
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 3
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • 3. Gething MJ, Sambrook J. 1992. Protein folding in the cell. Nature 355:33-45
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 5
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • 5. Hartl FU. 1996. Molecular chaperones in cellular protein folding. Nature 381:571-80
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 7
    • 0028856292 scopus 로고
    • Defective protein folding as a basis of human disease
    • 7. Thomas PJ, Qu BH, Pedersen PL. 1995. Defective protein folding as a basis of human disease. Trends Biochem. Sci. 20:456-59
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 456-459
    • Thomas, P.J.1    Qu, B.H.2    Pedersen, P.L.3
  • 8
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • 8. Boston RS, Viitanen PV, Vierling E. 1996. Molecular chaperones and protein folding in plants. Plant Mol. Biol. 32:191-222
    • (1996) Plant Mol. Biol. , vol.32 , pp. 191-222
    • Boston, R.S.1    Viitanen, P.V.2    Vierling, E.3
  • 10
    • 0000040966 scopus 로고
    • The stress response and stress proteins
    • ed. JJ Lemasters, C Oliver, Boca Raton, FL: CRC
    • 10. Feder ME, Parsell DA, Lindquist SL. 1995. The stress response and stress proteins. In Cell Biology of Trauma, ed. JJ Lemasters, C Oliver, pp. 177-91. Boca Raton, FL: CRC
    • (1995) Cell Biology of Trauma , pp. 177-191
    • Feder, M.E.1    Parsell, D.A.2    Lindquist, S.L.3
  • 12
    • 0028949615 scopus 로고
    • Proteins and temperature
    • 12. Somero GN. 1995. Proteins and temperature. Annu. Rev. Physiol. 57:43-68
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 43-68
    • Somero, G.N.1
  • 14
    • 0020534613 scopus 로고
    • Adaptation of Drosophila melanogaster to temperature. Heat-shock proteins and survival in Drosophila Melanogaster
    • 14. Stephanou G, Alahiotis SN, Christodoulou C, Marmaras VJ. 1983. Adaptation of Drosophila melanogaster to temperature. Heat-shock proteins and survival in Drosophila melanogaster. Dev. Genet. 3:299-308
    • (1983) Dev. Genet. , vol.3 , pp. 299-308
    • Stephanou, G.1    Alahiotis, S.N.2    Christodoulou, C.3    Marmaras, V.J.4
  • 15
    • 0013633698 scopus 로고
    • Temperature adaptation of Drosophila populations. The heat shock proteins system
    • 15. Alahiotis SN, Stephanou G. 1982. Temperature adaptation of Drosophila populations. The heat shock proteins system. Comp. Biochem. Physiol. 73B:529-33
    • (1982) Comp. Biochem. Physiol. , vol.73 B , pp. 529-533
    • Alahiotis, S.N.1    Stephanou, G.2
  • 17
    • 0029004007 scopus 로고
    • Desert ants
    • 17. Hightower LE. 1995. Desert ants. Science 166:1417
    • (1995) Science , vol.166 , pp. 1417
    • Hightower, L.E.1
  • 18
    • 0013613537 scopus 로고    scopus 로고
    • Engineering candidate genes in studies of adaptation: The heat-shock protein Hsp70 in Drosophila melanogaster
    • In press
    • 18. Feder ME. 1998. Engineering candidate genes in studies of adaptation: the heat-shock protein Hsp70 in Drosophila melanogaster. Am. Nat. In press
    • (1998) Am. Nat.
    • Feder, M.E.1
  • 19
    • 0004581102 scopus 로고    scopus 로고
    • Natural and genetic engineering of thermotolerance in Drosophila melanogaster
    • 19. Feder ME, Krebs RA. 1998. Natural and genetic engineering of thermotolerance in Drosophila melanogaster. Am. Zool. 38:503-17
    • (1998) Am. Zool. , vol.38 , pp. 503-517
    • Feder, M.E.1    Krebs, R.A.2
  • 20
    • 0030634892 scopus 로고    scopus 로고
    • Ecological and evolutionary physiology of heat-shock proteins and the stress response in Drosophila: Complementary insights from genetic engineering and natural variation
    • ed. R Bijlsma, V Loeschcke, Basel: Birkhäuser
    • 20. Feder ME, Krebs RA. 1997. Ecological and evolutionary physiology of heat-shock proteins and the stress response in Drosophila: complementary insights from genetic engineering and natural variation. In Stress, Adaptation, and Evolution, ed. R Bijlsma, V Loeschcke, pp. 155-73. Basel: Birkhäuser
    • (1997) Stress, Adaptation, and Evolution , pp. 155-173
    • Feder, M.E.1    Krebs, R.A.2
  • 21
    • 0000197850 scopus 로고    scopus 로고
    • Ecological and evolutionary physiology of stress proteins and the stress response: The Drosophila melanogaster model
    • ed. IA Johnston, AF Bennett, Cambridge, UK: Cambridge Univ. Press
    • 21. Feder ME. 1996. Ecological and evolutionary physiology of stress proteins and the stress response: the Drosophila melanogaster model. In Animals and Temperature: Phenotypic and Evolutionary Adaptation, ed. IA Johnston, AF Bennett, pp. 79-102. Cambridge, UK: Cambridge Univ. Press
    • (1996) Animals and Temperature: Phenotypic and Evolutionary Adaptation , pp. 79-102
    • Feder, M.E.1
  • 22
    • 0001787091 scopus 로고
    • Physiological adjustments to fluctuating thermal environments: An ecological and evolutionary perspective
    • ed. RI Morimoto, A Tissieres, C Georgopoulos, Cold Spring Harbor, NY: Cold Spring Harbor Lab. Press
    • 22. Huey RB, Bennett AF. 1990. Physiological adjustments to fluctuating thermal environments: an ecological and evolutionary perspective. In Stress Proteins in Biology and Medicine, ed. RI Morimoto, A Tissieres, C Georgopoulos, pp. 37-59. Cold Spring Harbor, NY: Cold Spring Harbor Lab. Press
    • (1990) Stress Proteins in Biology and Medicine , pp. 37-59
    • Huey, R.B.1    Bennett, A.F.2
  • 23
    • 0002923619 scopus 로고
    • Physiological consequences of habitat selection
    • 23. Huey RB. 1991. Physiological consequences of habitat selection. Am. Nat. 137:S91-115
    • (1991) Am. Nat. , vol.137
    • Huey, R.B.1
  • 24
    • 0013772403 scopus 로고
    • The roles of physiology and behaviour in the maintenance of homeostasis in the desert environment
    • ed. GM Hughes Cambridge, UK: Cambridge Univ. Press
    • 24. Bartholomew GA. 1964. The roles of physiology and behaviour in the maintenance of homeostasis in the desert environment. In Homeostasis and Feedback Mechanisms, ed. GM Hughes, pp. 7-29. Cambridge, UK: Cambridge Univ. Press
    • (1964) Homeostasis and Feedback Mechanisms , pp. 7-29
    • Bartholomew, G.A.1
  • 25
    • 0030899714 scopus 로고    scopus 로고
    • Heat shock protein (HSP 70) expression in the tropical reef coral Goniopora djiboutiensis
    • 25. Sharp VA, Brown BE, Miller D. 1997. Heat shock protein (HSP 70) expression in the tropical reef coral Goniopora djiboutiensis. J. Therm. Biol. 22:11-19
    • (1997) J. Therm. Biol. , vol.22 , pp. 11-19
    • Sharp, V.A.1    Brown, B.E.2    Miller, D.3
  • 26
    • 0029257302 scopus 로고
    • Induction of 70-kD heat shock protein in scleractinian corals by elevated temperature: Significance for coral bleaching
    • 26. Hayes RL, King CM. 1995. Induction of 70-kD heat shock protein in scleractinian corals by elevated temperature: significance for coral bleaching. Mol. Mar. Biol. Biotechnol. 4:36-42
    • (1995) Mol. Mar. Biol. Biotechnol. , vol.4 , pp. 36-42
    • Hayes, R.L.1    King, C.M.2
  • 27
    • 0000107718 scopus 로고
    • Characterization of the stress protein response in two species of Collisella limpets with different temperature tolerances
    • 27. Sanders BM, Hope C, Pascoe VM, Martin LS. 1991. Characterization of the stress protein response in two species of Collisella limpets with different temperature tolerances. Physiol. Zool. 64:1471-89
    • (1991) Physiol. Zool. , vol.64 , pp. 1471-1489
    • Sanders, B.M.1    Hope, C.2    Pascoe, V.M.3    Martin, L.S.4
  • 29
    • 0030466706 scopus 로고    scopus 로고
    • Protein ubiquitination and stress protein synthesis in Mytilus trossulus occurs during recovery from tidal emersion
    • 29. Hofmann GE, Somero GN. 1996. Protein ubiquitination and stress protein synthesis in Mytilus trossulus occurs during recovery from tidal emersion. Mol. Mar. Biol. Biotechnol. 5:175-84
    • (1996) Mol. Mar. Biol. Biotechnol. , vol.5 , pp. 175-184
    • Hofmann, G.E.1    Somero, G.N.2
  • 30
    • 0028154168 scopus 로고
    • Expression of low molecular weight HSP 70 related polypeptides from the symbiotic sea anemone Anemonia viridis Forskal in response to heat shock
    • 30. Sharp VA, Miller D, Bythell JC, Brown BE. 1994. Expression of low molecular weight HSP 70 related polypeptides from the symbiotic sea anemone Anemonia viridis Forskal in response to heat shock. J. Exp. Mar. Biol. Ecol. 179:179-93
    • (1994) J. Exp. Mar. Biol. Ecol. , vol.179 , pp. 179-193
    • Sharp, V.A.1    Miller, D.2    Bythell, J.C.3    Brown, B.E.4
  • 31
    • 0001532355 scopus 로고
    • Evidence for protein damage at environmental temperatures: Seasonal changes in levels of ubiquitin conjugates and hsp70 in the intertidal mussel Mytilus trossulus
    • 31. Hofmann GE, Somero GN. 1995. Evidence for protein damage at environmental temperatures: seasonal changes in levels of ubiquitin conjugates and hsp70 in the intertidal mussel Mytilus trossulus. J. Exp. Biol. 198:1509-18
    • (1995) J. Exp. Biol. , vol.198 , pp. 1509-1518
    • Hofmann, G.E.1    Somero, G.N.2
  • 32
    • 0000038312 scopus 로고
    • The heat shock response of the cryptobiotic brine shrimp Anemia. I. A comparison of the thermotolerance of cysts and larvae
    • 32. Miller D, McLennan AG. 1988. The heat shock response of the cryptobiotic brine shrimp Anemia. I. A comparison of the thermotolerance of cysts and larvae. J. Therm. Biol. 13:119-24
    • (1988) J. Therm. Biol. , vol.13 , pp. 119-124
    • Miller, D.1    McLennan, A.G.2
  • 33
    • 0000107501 scopus 로고
    • The heat shock response of the cryptobiotic brine shrimp Artemia. II. Heat shock proteins
    • 33. Miller D, McLennan AG. 1988. The heat shock response of the cryptobiotic brine shrimp Artemia. II. Heat shock proteins. J. Therm. Biol. 13:125-34
    • (1988) J. Therm. Biol. , vol.13 , pp. 125-134
    • Miller, D.1    McLennan, A.G.2
  • 34
    • 0026553389 scopus 로고
    • The threshold induction temperature of the 90-kDa heat shock protein is subject to acclimatization in eurythermal goby fishes (genus Gillichthys)
    • 34. Dietz TJ, Somero GN. 1992. The threshold induction temperature of the 90-kDa heat shock protein is subject to acclimatization in eurythermal goby fishes (genus Gillichthys). Proc. Natl. Acad. Sci. USA 89:3389-93
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3389-3393
    • Dietz, T.J.1    Somero, G.N.2
  • 35
    • 0028003295 scopus 로고
    • Seasonal variation in heat shock proteins (hsp70) in stream fish under natural conditions
    • 35. Fader SC, Yu Z, Spotila JR. 1994. Seasonal variation in heat shock proteins (hsp70) in stream fish under natural conditions. J. Therm. Biol. 19:335-41
    • (1994) J. Therm. Biol. , vol.19 , pp. 335-341
    • Fader, S.C.1    Yu, Z.2    Spotila, J.R.3
  • 36
    • 0025630059 scopus 로고
    • Heat shock protein 70 gene expression in intact salamanders Eurycea bislineata in response to calibrated heat shocks and to high temperatures encountered in the field
    • 36. Near JC, Easton DP, Rutledge PS, Dickinson DP. Spotila JS. 1990. Heat shock protein 70 gene expression in intact salamanders Eurycea bislineata in response to calibrated heat shocks and to high temperatures encountered in the field. J. Exp. Zool. 256:303-14
    • (1990) J. Exp. Zool. , vol.256 , pp. 303-314
    • Near, J.C.1    Easton, D.P.2    Rutledge, P.S.3    Dickinson, D.P.4    Spotila, J.S.5
  • 38
    • 0001324001 scopus 로고
    • Concomitant changes in high-temperature tolerance and heat-shock proteins in desert succulents
    • 38. Kee SC, Nobel PS. 1986. Concomitant changes in high-temperature tolerance and heat-shock proteins in desert succulents. Plant Physiol. 80:596-98
    • (1986) Plant Physiol. , vol.80 , pp. 596-598
    • Kee, S.C.1    Nobel, P.S.2
  • 39
    • 0025023094 scopus 로고
    • Molecular and cellular biology of the heat-shock response
    • 39. Nagao RT, Kimpel JA, Key JL. 1990. Molecular and cellular biology of the heat-shock response. Adv. Genet. 28:235-74
    • (1990) Adv. Genet. , vol.28 , pp. 235-274
    • Nagao, R.T.1    Kimpel, J.A.2    Key, J.L.3
  • 40
    • 0013629928 scopus 로고
    • The heat-shock response and expression of heat-shock proteins in wheat under diurnal heat stress and field conditions
    • 40. Nguyen HT, Joshi CP, Klueva N, Weng J, Hendershot KL, Blum A. 1994. The heat-shock response and expression of heat-shock proteins in wheat under diurnal heat stress and field conditions. Aust. J. Plant Physiol. 21:857-67
    • (1994) Aust. J. Plant Physiol. , vol.21 , pp. 857-867
    • Nguyen, H.T.1    Joshi, C.P.2    Klueva, N.3    Weng, J.4    Hendershot, K.L.5    Blum, A.6
  • 41
    • 0013613539 scopus 로고    scopus 로고
    • Heat shock proteins are produced by field-grown naturally occurring plants in the summer in the temperate northeast U.S.
    • Abstr.
    • 41. Hamilton EW, Heckathorn SA, Downs CA, Schwarz TE, Coleman JS, Hallberg RL. 1996. Heat shock proteins are produced by field-grown naturally occurring plants in the summer in the temperate northeast U.S. Bull. Ecol. Soc. Am. 77, Suppl. Part 2:180 (Abstr.)
    • (1996) Bull. Ecol. Soc. Am. , vol.77 , Issue.SUPPL. PART 2 , pp. 180
    • Hamilton, E.W.1    Heckathorn, S.A.2    Downs, C.A.3    Schwarz, T.E.4    Coleman, J.S.5    Hallberg, R.L.6
  • 42
    • 0000602720 scopus 로고
    • Presence of heat shock mRNAs in field grown soybeans
    • 42. Kimpel JA, Key JL. 1985. Presence of heat shock mRNAs in field grown soybeans. Plant Physiol. 79:672-78
    • (1985) Plant Physiol. , vol.79 , pp. 672-678
    • Kimpel, J.A.1    Key, J.L.2
  • 43
    • 0000052340 scopus 로고
    • Expression of low molecluar weight heat-shock proteins under field conditions
    • 43. Hernandez LD, Vierling E. 1993. Expression of low molecluar weight heat-shock proteins under field conditions. Plant Physiol. 101:1209-16
    • (1993) Plant Physiol. , vol.101 , pp. 1209-1216
    • Hernandez, L.D.1    Vierling, E.2
  • 44
    • 0000974039 scopus 로고
    • Induction temperature of heat-shock protein synthesis in wheat
    • 44. Hendershot KL, Weng J, Nguyen HT. 1992. Induction temperature of heat-shock protein synthesis in wheat. Crop Sci. 32:256-61
    • (1992) Crop Sci. , vol.32 , pp. 256-261
    • Hendershot, K.L.1    Weng, J.2    Nguyen, H.T.3
  • 46
    • 0029139201 scopus 로고
    • Diurnal variation in beat tolerance and heat shock protein expression in black spruce (Picea mariana)
    • 46. Colombo SJ, Timmer VR, Colclough ML, Blumwald E. 1995. Diurnal variation in beat tolerance and heat shock protein expression in black spruce (Picea mariana). Can. J. Forest Res. 25:369-75
    • (1995) Can. J. Forest Res. , vol.25 , pp. 369-375
    • Colombo, S.J.1    Timmer, V.R.2    Colclough, M.L.3    Blumwald, E.4
  • 48
    • 0026166215 scopus 로고
    • Gene expression during cold and heat shock in wheat
    • 48. Danyluk J, Rassart E, Sarhan F. 1991. Gene expression during cold and heat shock in wheat. Biochem. Cell Biol. 69:383-91
    • (1991) Biochem. Cell Biol. , vol.69 , pp. 383-391
    • Danyluk, J.1    Rassart, E.2    Sarhan, F.3
  • 49
    • 0029106880 scopus 로고
    • Cold-induced accumulation of hsp90 transcripts in Brassica napus
    • 49. Krishna P, Sacco M, Cherutti JF, Hill S. 1995. Cold-induced accumulation of hsp90 transcripts in Brassica napus. Plant Physiol. 107:915-23
    • (1995) Plant Physiol. , vol.107 , pp. 915-923
    • Krishna, P.1    Sacco, M.2    Cherutti, J.F.3    Hill, S.4
  • 50
    • 0001702297 scopus 로고
    • Association of 70-kilodalton heat-shock cognate proteins with acclimation to cold
    • 50. Neven LG, Haskell DW, Guy CL, Denslow N, Klein PA, et al. 1992. Association of 70-kilodalton heat-shock cognate proteins with acclimation to cold. Plant Physiol. 99:1362-69
    • (1992) Plant Physiol. , vol.99 , pp. 1362-1369
    • Neven, L.G.1    Haskell, D.W.2    Guy, C.L.3    Denslow, N.4    Klein, P.A.5
  • 51
    • 0028372239 scopus 로고
    • Transcripts accumulating during cold storage of potato (Solanum tuberosum L.) tubers are sequence related to stress-responsive genes
    • 51. Van Berkel J, Salamini F, Gebhardt C. 1994. Transcripts accumulating during cold storage of potato (Solanum tuberosum L.) tubers are sequence related to stress-responsive genes. Plant Physiol. 104:445-52
    • (1994) Plant Physiol. , vol.104 , pp. 445-452
    • Van Berkel, J.1    Salamini, F.2    Gebhardt, C.3
  • 52
    • 0026005387 scopus 로고
    • Microclimate variability and the eurythermic natural of goldenrod gall fly (Eurosta solidaginis) larvae (Diptera: Tephritidae)
    • 52. Layne JR. 1991. Microclimate variability and the eurythermic natural of goldenrod gall fly (Eurosta solidaginis) larvae (Diptera: Tephritidae). Can. J. Zool. 69:614-17
    • (1991) Can. J. Zool. , vol.69 , pp. 614-617
    • Layne, J.R.1
  • 53
    • 0031003093 scopus 로고    scopus 로고
    • Natural thermal stress and heat-shock protein expression in Drosophila larvae and pupae
    • 53. Feder ME, Blair N, Figueras H. 1997. Natural thermal stress and heat-shock protein expression in Drosophila larvae and pupae. Funct. Ecol. 11:90-100
    • (1997) Funct. Ecol. , vol.11 , pp. 90-100
    • Feder, M.E.1    Blair, N.2    Figueras, H.3
  • 54
    • 0030979084 scopus 로고    scopus 로고
    • Necrotic fruit: A novel model system for thermal ecologists
    • 54. Feder ME. 1997. Necrotic fruit: a novel model system for thermal ecologists. J. Therm. Biol. 22:1-9
    • (1997) J. Therm. Biol. , vol.22 , pp. 1-9
    • Feder, M.E.1
  • 55
    • 0026592771 scopus 로고
    • Desert ants on a thermal tightrope
    • 55. Wehner R, Marsh AC, Wehner S. 1992. Desert ants on a thermal tightrope. Nature 357:586-87
    • (1992) Nature , vol.357 , pp. 586-587
    • Wehner, R.1    Marsh, A.C.2    Wehner, S.3
  • 56
    • 0028923827 scopus 로고
    • Heat shock protein synthesis and thermotolerance in Cataglyphis, an ant from the Sahara desert
    • 56. Gehring WJ, Wehner R. 1995. Heat shock protein synthesis and thermotolerance in Cataglyphis, an ant from the Sahara desert. Proc. Natl. Acad. Sci. USA 92:2994-98
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2994-2998
    • Gehring, W.J.1    Wehner, R.2
  • 57
    • 0029310491 scopus 로고
    • Stress proteins: The exercise response
    • 57. Locke M, Noble EG. 1995. Stress proteins: the exercise response. Can. J. Appl. Physiol. 20:155-67
    • (1995) Can. J. Appl. Physiol. , vol.20 , pp. 155-167
    • Locke, M.1    Noble, E.G.2
  • 58
    • 0029970359 scopus 로고    scopus 로고
    • In vivo activation of neural heat shock transcription factor HSF1 by a physiologically relevant increase in body temperature
    • 58. Brown IR, Rush SJ. 1996. In vivo activation of neural heat shock transcription factor HSF1 by a physiologically relevant increase in body temperature. J. Neurosci. Res. 44:52-57
    • (1996) J. Neurosci. Res. , vol.44 , pp. 52-57
    • Brown, I.R.1    Rush, S.J.2
  • 59
    • 0030741077 scopus 로고    scopus 로고
    • Distribution of HSP70, protein kinase C, and spectrin is altered in lymphocytes during a fever-like hyperthermia exposure
    • 59. Di YP, Repasky EA, Subjeck JR. 1997. Distribution of HSP70, protein kinase C, and spectrin is altered in lymphocytes during a fever-like hyperthermia exposure. J. Cell. Physiol. 172:44-54
    • (1997) J. Cell. Physiol. , vol.172 , pp. 44-54
    • Di, Y.P.1    Repasky, E.A.2    Subjeck, J.R.3
  • 60
    • 0000922807 scopus 로고
    • Developmental and tissue specific control of the heat shock induced 70 kDa related proteins in the flesh fly, Sarcophaga crassipalpis
    • 60. Joplin KH, Denlinger DL. 1990. Developmental and tissue specific control of the heat shock induced 70 kDa related proteins in the flesh fly, Sarcophaga crassipalpis. J. Insect Physiol. 36:239-49
    • (1990) J. Insect Physiol. , vol.36 , pp. 239-249
    • Joplin, K.H.1    Denlinger, D.L.2
  • 61
    • 0000990781 scopus 로고
    • Cold shock elicits expression of heat shock proteins in the flesh fly Sarcophaga crassipalpis
    • 61. Joplin KH, Yocum GD, Denlinger DL. 1990. Cold shock elicits expression of heat shock proteins in the flesh fly Sarcophaga crassipalpis. J. Insect Physiol. 36:825-34
    • (1990) J. Insect Physiol. , vol.36 , pp. 825-834
    • Joplin, K.H.1    Yocum, G.D.2    Denlinger, D.L.3
  • 62
    • 84990419576 scopus 로고
    • Expression of heat shock proteins in response to high and low temperature extremes in diapausing pharate larvae of the gypsy moth Lymantria dispar
    • 62. Yocum GD, Joplin KH, Denlinger DL. 1991. Expression of heat shock proteins in response to high and low temperature extremes in diapausing pharate larvae of the gypsy moth Lymantria dispar. Arch. Insect Biochem. Physiol. 18:239-50
    • (1991) Arch. Insect Biochem. Physiol. , vol.18 , pp. 239-250
    • Yocum, G.D.1    Joplin, K.H.2    Denlinger, D.L.3
  • 63
    • 0000574452 scopus 로고
    • Cryobiology of the freeze-tolerant gall fly Eurosta solidaginis: Overwintering energetics and heat shock proteins
    • 63. Lee RE, Dommel RA, Joplin KH, Denlinger DL. 1995. Cryobiology of the freeze-tolerant gall fly Eurosta solidaginis: overwintering energetics and heat shock proteins. Climate Res. 5:61-67
    • (1995) Climate Res. , vol.5 , pp. 61-67
    • Lee, R.E.1    Dommel, R.A.2    Joplin, K.H.3    Denlinger, D.L.4
  • 64
    • 84990439391 scopus 로고
    • Role of chilling in the acquisition of cold tolerance and the capacitation to express stress proteins in diapausing pharate larvae of the gypsy moth Lymantria dispar
    • 64. Denlinger DL, Lee RE, Yocum GD, Kukal O. 1992. Role of chilling in the acquisition of cold tolerance and the capacitation to express stress proteins in diapausing pharate larvae of the gypsy moth Lymantria dispar. Arch. Insect Biochem. Physiol. 21:271-80
    • (1992) Arch. Insect Biochem. Physiol. , vol.21 , pp. 271-280
    • Denlinger, D.L.1    Lee, R.E.2    Yocum, G.D.3    Kukal, O.4
  • 65
    • 0342935989 scopus 로고    scopus 로고
    • Cold-induced heat shock protein expression in rat aorta and brown adipose tissue
    • 65. Matz JM, LaVoi KP, Moen RJ, Blake MJ. 1996. Cold-induced heat shock protein expression in rat aorta and brown adipose tissue. Physiol. Behav. 60:1369-74
    • (1996) Physiol. Behav. , vol.60 , pp. 1369-1374
    • Matz, J.M.1    LaVoi, K.P.2    Moen, R.J.3    Blake, M.J.4
  • 66
    • 84880916433 scopus 로고    scopus 로고
    • Stress protein expression in a mammalian hibernator
    • 66. Sills NS, Gorham DA, Carey HV. 1998. Stress protein expression in a mammalian hibernator. FASEB J. 12:A379
    • (1998) FASEB J. , vol.12
    • Sills, N.S.1    Gorham, D.A.2    Carey, H.V.3
  • 68
    • 0029616226 scopus 로고
    • Constitutive expression of small heat shock proteins in vegetative tissues of the resurrection plant Craterostigma plantagineum
    • 68. Alamillo J, Almoguera C, Bartels D, Jordano J. 1995. Constitutive expression of small heat shock proteins in vegetative tissues of the resurrection plant Craterostigma plantagineum. Plant Mol. Biol. 29:1093-99
    • (1995) Plant Mol. Biol. , vol.29 , pp. 1093-1099
    • Alamillo, J.1    Almoguera, C.2    Bartels, D.3    Jordano, J.4
  • 69
    • 0031591585 scopus 로고    scopus 로고
    • Distribution patterns of HSP 90 protein in rice
    • 69. Pareek A, Singla SL, Kush AK, Grover A. 1997. Distribution patterns of HSP 90 protein in rice. Plant Sci. 125:221-30
    • (1997) Plant Sci. , vol.125 , pp. 221-230
    • Pareek, A.1    Singla, S.L.2    Kush, A.K.3    Grover, A.4
  • 70
    • 0030923034 scopus 로고    scopus 로고
    • Anoxia regulates gene expression in the central nervous system of Drosophila melanogaster
    • 70. Ma E, Haddad GG. 1997. Anoxia regulates gene expression in the central nervous system of Drosophila melanogaster. Brain Res. Mol. Brain Res. 46:325-28
    • (1997) Brain Res. Mol. Brain Res. , vol.46 , pp. 325-328
    • Ma, E.1    Haddad, G.G.2
  • 71
    • 0029909406 scopus 로고    scopus 로고
    • Plasticity and stressor specificity of osmotic and heat shock responses of Gillichthys mirabilis gill cells
    • 71. Kultz D. 1996. Plasticity and Stressor specificity of osmotic and heat shock responses of Gillichthys mirabilis gill cells. Am. J. Physiol. 271:C1181-93
    • (1996) Am. J. Physiol. , vol.271
    • Kultz, D.1
  • 72
    • 0029883933 scopus 로고    scopus 로고
    • Heat-shock proteins as biomarkers of pollution
    • 72. de Pomerai D. 1996. Heat-shock proteins as biomarkers of pollution. Hum. Exp. Toxicol. 15:279-85
    • (1996) Hum. Exp. Toxicol. , vol.15 , pp. 279-285
    • De Pomerai, D.1
  • 74
    • 0027509808 scopus 로고
    • Stress proteins in aquatic organisms: An environmental perspective
    • 74. Sanders BM. 1993. Stress proteins in aquatic organisms: an environmental perspective. Crit. Rev. Toxicol. 23:49-75
    • (1993) Crit. Rev. Toxicol. , vol.23 , pp. 49-75
    • Sanders, B.M.1
  • 76
    • 0029037081 scopus 로고
    • Combinatory effects of temperature stress and nonionic organic pollutants on stress protein (hsp70) gene expression in the freshwater sponge Ephydatia fluviatilis
    • 76. Mueller WEG, Koziol C, Kurelec B, Dapper J, Batel R, Rinkevich B. 1995. Combinatory effects of temperature stress and nonionic organic pollutants on stress protein (hsp70) gene expression in the freshwater sponge Ephydatia fluviatilis. Environ. Toxicol. Chem. 14:1203-8
    • (1995) Environ. Toxicol. Chem. , vol.14 , pp. 1203-1208
    • Mueller, W.E.G.1    Koziol, C.2    Kurelec, B.3    Dapper, J.4    Batel, R.5    Rinkevich, B.6
  • 77
    • 0026019316 scopus 로고
    • Effects of copper and tributylin on stress protein abundance in the rotifer Brachionus plicatilis
    • 77. Cochrane BJ, Irby RB, Snell TW. 1991. Effects of copper and tributylin on stress protein abundance in the rotifer Brachionus plicatilis. Comp. Biochem. Physiol. 98C:385-90
    • (1991) Comp. Biochem. Physiol. , vol.98 C , pp. 385-390
    • Cochrane, B.J.1    Irby, R.B.2    Snell, T.W.3
  • 78
    • 0030906046 scopus 로고    scopus 로고
    • Diagnosis of sublethal stress in the marine sponge Geodia cydonium: Application of the 70 kDa heat-shock protein and a novel biomarker, the Rab GDP dissociation inhibitor, as probes
    • 78. Krasko A, Scheffer U, Koziol C, Pancer Z, Batel R, et al. 1997. Diagnosis of sublethal stress in the marine sponge Geodia cydonium: application of the 70 kDa heat-shock protein and a novel biomarker, the Rab GDP dissociation inhibitor, as probes. Aquat. Toxicol. 37:157-68
    • (1997) Aquat. Toxicol. , vol.37 , pp. 157-168
    • Krasko, A.1    Scheffer, U.2    Koziol, C.3    Pancer, Z.4    Batel, R.5
  • 79
    • 0030757558 scopus 로고    scopus 로고
    • Stress proteins HSP60 and HSP70 in 3 species of amphipods exposed to cadmium, diazinon, dieldrin and fluoranthene
    • 79. Werner I, Nagel R. 1997. Stress proteins HSP60 and HSP70 in 3 species of amphipods exposed to cadmium, diazinon, dieldrin and fluoranthene. Environ. Toxicol. Chem. 16:2393-403
    • (1997) Environ. Toxicol. Chem. , vol.16 , pp. 2393-2403
    • Werner, I.1    Nagel, R.2
  • 80
    • 0027968023 scopus 로고
    • Stress protein in the polychaete annelid Nereis diversicolor induced by heat shock or cadmium exposure
    • 80. Ruffin P, Demuynck S, Hubert JL, Dhainaut A. 1994. Stress protein in the polychaete annelid Nereis diversicolor induced by heat shock or cadmium exposure. Biochimie 76:423-27
    • (1994) Biochimie , vol.76 , pp. 423-427
    • Ruffin, P.1    Demuynck, S.2    Hubert, J.L.3    Dhainaut, A.4
  • 81
    • 0023538979 scopus 로고
    • Expression of heat shock proteins and metallothionein in mussels exposed to heat stress and metal ion challenge
    • 81. Steinert SA, Pickwell GV. 1988. Expression of heat shock proteins and metallothionein in mussels exposed to heat stress and metal ion challenge. Mar. Environ. Res. 24:211-14
    • (1988) Mar. Environ. Res. , vol.24 , pp. 211-214
    • Steinert, S.A.1    Pickwell, G.V.2
  • 82
    • 0025931740 scopus 로고
    • Synthesis of stress proteins under normal and heat shock conditions in gill tissue of sea mussels (Mytilus edulis) after chronic exposure to cadmium
    • 82. Veldhuizen Tsoerkan MB, Holwerda DA, van der Mast CA, Zandee DI. 1991. Synthesis of stress proteins under normal and heat shock conditions in gill tissue of sea mussels (Mytilus edulis) after chronic exposure to cadmium. Comp. Biochem. Physiol. 100C:699-706
    • (1991) Comp. Biochem. Physiol. , vol.100 C , pp. 699-706
    • Veldhuizen Tsoerkan, M.B.1    Holwerda, D.A.2    Van Der Mast, C.A.3    Zandee, D.I.4
  • 83
    • 0030301741 scopus 로고    scopus 로고
    • Heat shock protein response to thermal stress in the Asiatic clam, Corbicula fluminea
    • 83. Nascimento IA, Dickson KL, Zimmerman EG. 1996. Heat shock protein re-sponse to thermal stress in the Asiatic clam, Corbicula fluminea. J. Aquat. Ecosystem Health 5:231-38
    • (1996) J. Aquat. Ecosystem Health , vol.5 , pp. 231-238
    • Nascimento, I.A.1    Dickson, K.L.2    Zimmerman, E.G.3
  • 84
    • 0028325239 scopus 로고
    • Tissue-specific differences in accumulation of stress proteins in Mytilus edulis exposed to a range of copper concentrations
    • 84. Sanders BM, Martin LS, Howe SR, Nelson WG, Hegre ES, Phelps DK. 1994. Tissue-specific differences in accumulation of stress proteins in Mytilus edulis exposed to a range of copper concentrations. Toxicol. Appl. Pharmacol. 125:206-13
    • (1994) Toxicol. Appl. Pharmacol. , vol.125 , pp. 206-213
    • Sanders, B.M.1    Martin, L.S.2    Howe, S.R.3    Nelson, W.G.4    Hegre, E.S.5    Phelps, D.K.6
  • 85
    • 0028483991 scopus 로고
    • Evaluation of heavy-metal ion toxicity in fish cells using a combined stress protein and cytotoxicity assay
    • 85. Ryan JA, Hightower LE. 1994. Evaluation of heavy-metal ion toxicity in fish cells using a combined stress protein and cytotoxicity assay. Environ. Toxicol. Chem. 13:1231-40
    • (1994) Environ. Toxicol. Chem. , vol.13 , pp. 1231-1240
    • Ryan, J.A.1    Hightower, L.E.2
  • 86
    • 0027309220 scopus 로고
    • Synthesis and accumulation of stress proteins in tissues of arsenite-exposed fathead minnows Pimephales promelas
    • 86. Dyer SD, Brooks GL, Dickson KL, Sanders BM, Zimmerman EG. 1993. Synthesis and accumulation of stress proteins in tissues of arsenite-exposed fathead minnows Pimephales promelas. Environ. Toxicol. Chem. 12:913-24
    • (1993) Environ. Toxicol. Chem. , vol.12 , pp. 913-924
    • Dyer, S.D.1    Brooks, G.L.2    Dickson, K.L.3    Sanders, B.M.4    Zimmerman, E.G.5
  • 87
    • 0030968232 scopus 로고    scopus 로고
    • Handling stress does not affect the expression of hepatic heat shock protein 70 and conjugation enzymes in rainbow trout treated with beta-naphthoflavone
    • 87. Vijayan MM, Pereira C, Forsyth RB, Kennedy CJ, Iwama GK. 1997. Handling stress does not affect the expression of hepatic heat shock protein 70 and conjugation enzymes in rainbow trout treated with beta-naphthoflavone. Life Sci. 61:117-27
    • (1997) Life Sci. , vol.61 , pp. 117-127
    • Vijayan, M.M.1    Pereira, C.2    Forsyth, R.B.3    Kennedy, C.J.4    Iwama, G.K.5
  • 90
    • 0026573666 scopus 로고
    • The 70 kD heat shock protein (hsp 70) in soil invertebrates: A possible tool for monitoring environmental toxicants
    • 90. Kohler HR, Triehskorn R, Stocker W, Kloetzel PM, Alberti G. 1992. The 70 kD heat shock protein (hsp 70) in soil invertebrates: a possible tool for monitoring environmental toxicants. Arch. Environ. Contam. Toxicol. 22:334-38
    • (1992) Arch. Environ. Contam. Toxicol. , vol.22 , pp. 334-338
    • Kohler, H.R.1    Triehskorn, R.2    Stocker, W.3    Kloetzel, P.M.4    Alberti, G.5
  • 91
    • 0031418196 scopus 로고    scopus 로고
    • Heat-shock proteins (Hsp70) as biomarkers in ecotoxicological studies
    • 91. Pyza E, Mak P, Kramarz P, Laskowski R. 1997. Heat-shock proteins (Hsp70) as biomarkers in ecotoxicological studies. Ecotoxicol. Environ. Safety 38:244-51
    • (1997) Ecotoxicol. Environ. Safety , vol.38 , pp. 244-251
    • Pyza, E.1    Mak, P.2    Kramarz, P.3    Laskowski, R.4
  • 92
    • 0028166732 scopus 로고
    • Transgenic hsp16-IacZ strains of the soil nematode Caenorhabditis elegans as biological monitors of environmental stress
    • 92. Stringham EG, Candido EPM. 1994. Transgenic hsp16-IacZ strains of the soil nematode Caenorhabditis elegans as biological monitors of environmental stress. Environ. Toxicol. Chem. 13: 1211-20
    • (1994) Environ. Toxicol. Chem. , vol.13 , pp. 1211-1220
    • Stringham, E.G.1    Candido, E.P.M.2
  • 95
    • 0024110459 scopus 로고
    • Thermotolerance and synthesis of heat shock proteins: These re-sponses are present in Hydra attenuata but absent in Hydra oligactis
    • 95. Bosch TC, Krylow SM, Bode HR, Steele RE. 1988. Thermotolerance and synthesis of heat shock proteins: These re-sponses are present in Hydra attenuata but absent in Hydra oligactis. Proc. Natl. Acad. Sci. USA 85:7927-31
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7927-7931
    • Bosch, T.C.1    Krylow, S.M.2    Bode, H.R.3    Steele, R.E.4
  • 96
    • 0027051403 scopus 로고
    • Cloning and expression of a heat-inducible hsp70 gene in two species of Hydra which differ in their stress response
    • 96. Gellner K, Praetzel G, Bosch TC. 1992. Cloning and expression of a heat-inducible hsp70 gene in two species of Hydra which differ in their stress re-sponse. Eur. J. Biochem. 210:683-91
    • (1992) Eur. J. Biochem. , vol.210 , pp. 683-691
    • Gellner, K.1    Praetzel, G.2    Bosch, T.C.3
  • 97
    • 0029783164 scopus 로고    scopus 로고
    • Interspecific variation in thermal denaturation of proteins in the congeneric mussels Mytilus trossulus and M. Gallopmvincialis: Evidence from the heat-shock response and protein ubiquitination
    • 97. Hofmann GE, Somero GN. 1996. Interspecific variation in thermal denaturation of proteins in the congeneric mussels Mytilus trossulus and M. gallopmvincialis: evidence from the heat-shock response and protein ubiquitination. Mar. Biol. 126:65-75
    • (1996) Mar. Biol. , vol.126 , pp. 65-75
    • Hofmann, G.E.1    Somero, G.N.2
  • 98
    • 0013615790 scopus 로고    scopus 로고
    • The effect of temperature on protein synthesis in snails of the genus Tegula from the sub- and intertidal zone
    • 98. Tomanek L, Somero GN. 1997. The effect of temperature on protein synthesis in snails of the genus Tegula from the sub-and intertidal zone. Am. Zool. 37:188A
    • (1997) Am. Zool. , vol.37
    • Tomanek, L.1    Somero, G.N.2
  • 99
    • 0027953185 scopus 로고
    • The heat shock response of an Antarctic alga is evident at 5 degrees C
    • 99. Vayda ME, Yuan ML. 1994. The heat shock response of an Antarctic alga is evident at 5 degrees C. Plant Mol. Biol. 24:229-33
    • (1994) Plant Mol. Biol. , vol.24 , pp. 229-233
    • Vayda, M.E.1    Yuan, M.L.2
  • 100
    • 0001765941 scopus 로고
    • Stress proteins and thermotolerance in psychrotrophic yeasts from Arctic environments
    • 100. Berg GR, Inniss WE, Heikkila JJ. 1987. Stress proteins and thermotolerance in psychrotrophic yeasts from Arctic environments. Can. J. Microbiol. 33:383-89
    • (1987) Can. J. Microbiol. , vol.33 , pp. 383-389
    • Berg, G.R.1    Inniss, W.E.2    Heikkila, J.J.3
  • 101
    • 0030806276 scopus 로고    scopus 로고
    • Stress proteins and stress tolerance in an Antarctic, psychrophilic yeast, Candida psychrophila
    • 101. Deegenaars ML, Watson K. 1997. Stress proteins and stress tolerance in an Antarctic, psychrophilic yeast, Candida psychrophila. FEMS Microbiol. Lett. 151:191-96
    • (1997) FEMS Microbiol. Lett. , vol.151 , pp. 191-196
    • Deegenaars, M.L.1    Watson, K.2
  • 102
    • 4243342143 scopus 로고    scopus 로고
    • Evolutionary adaptation of hsp70 gene in Antarctic fish
    • Abstr.
    • 102. Carratu L, Maresca B. 1997. Evolutionary adaptation of hsp70 gene in Antarctic fish. Exp. Biol. Online 2:C5.1 (Abstr.)
    • (1997) Exp. Biol. Online , vol.2
    • Carratu, L.1    Maresca, B.2
  • 103
    • 0031005531 scopus 로고    scopus 로고
    • Heat-shock protein expression in Mytilus californianus: Acclimatization (seasonal and tidal-height comparisons) and acclimation effects
    • 103. Roberts DA, Hofmann GE, Somero GN. 1997. Heat-shock protein expression in Mytilus californianus: acclimatization (seasonal and tidal-height comparisons) and acclimation effects. Biol. Bull. 192:309-20
    • (1997) Biol. Bull. , vol.192 , pp. 309-320
    • Roberts, D.A.1    Hofmann, G.E.2    Somero, G.N.3
  • 104
    • 0028864657 scopus 로고
    • Variation in heat shock proteins within tropical and desert species of poeciliid fishes
    • 104. Norris CE, diIorio PJ, Schultz RJ, Hightower LE. 1995. Variation in heat shock proteins within tropical and desert species of poeciliid fishes. Mol. Biol. Evol. 12:1048-62
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 1048-1062
    • Norris, C.E.1    Diiorio, P.J.2    Schultz, R.J.3    Hightower, L.E.4
  • 105
    • 0028097732 scopus 로고
    • Variation in heat-shock proteins among species of desert fishes (Poeciliidae, Poeciliopsis)
    • 105. White CM, Hightower LE, Schultz RJ. 1994. Variation in heat-shock proteins among species of desert fishes (Poeciliidae, Poeciliopsis). Mol. Biol. Evol. 11:106-19
    • (1994) Mol. Biol. Evol. , vol.11 , pp. 106-119
    • White, C.M.1    Hightower, L.E.2    Schultz, R.J.3
  • 106
    • 0000486169 scopus 로고
    • Heat shock and cold adaptation in Antarctic fishes: A molecular approach
    • 105a. Maresca B, Patriarcha E, Goldenberg C, Sacco M. 1988. Heat shock and cold adaptation in Antarctic fishes: a molecular approach. Comp. Biochem. Physiol. 90B: 623-29
    • (1988) Comp. Biochem. Physiol. , vol.90 B , pp. 623-629
    • Maresca, B.1    Patriarcha, E.2    Goldenberg, C.3    Sacco, M.4
  • 107
    • 0029862011 scopus 로고    scopus 로고
    • Dehydration, damage to cellular membranes, and heat-shock proteins in maize hybrids from different climates
    • 106. Ristic Z, Williams G, Yang G, Martin B, Fullerton S. 1996. Dehydration, damage to cellular membranes, and heat-shock proteins in maize hybrids from different climates. J. Plant Physiol. 149:424-32
    • (1996) J. Plant Physiol. , vol.149 , pp. 424-432
    • Ristic, Z.1    Williams, G.2    Yang, G.3    Martin, B.4    Fullerton, S.5
  • 109
    • 0031062337 scopus 로고    scopus 로고
    • Variations in the heat-induced protein pattern of several Drosophila montium subgroup species (Diptera: Drosophilidae)
    • 108. Konstantopoulou I, Drosopoulou E, Scouras ZG. 1997. Variations in the heat-induced protein pattern of several Drosophila montium subgroup species (Diptera: Drosophilidae). Genome 40: 132-37
    • (1997) Genome , vol.40 , pp. 132-137
    • Konstantopoulou, I.1    Drosopoulou, E.2    Scouras, Z.G.3
  • 110
    • 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
    • 109. Feder ME, Cartaño NV, Milos L, Krebs RA, Lindquist SL. 1996. 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. 199:1837-44
    • (1996) J. Exp. Biol. , vol.199 , pp. 1837-1844
    • Feder, M.E.1    Cartaño, N.V.2    Milos, L.3    Krebs, R.A.4    Lindquist, S.L.5
  • 111
    • 0000180158 scopus 로고
    • Heat-shock response in a tropical Chironomus: Seasonal variation in response and the effect of developmental stage and tissue type on heat shock protein synthesis
    • 110. Nath BB, Lakhotia SC. 1989. Heat-shock response in a tropical Chironomus: seasonal variation in response and the effect of developmental stage and tissue type on heat shock protein synthesis. Genome 32:676-86
    • (1989) Genome , vol.32 , pp. 676-686
    • Nath, B.B.1    Lakhotia, S.C.2
  • 112
    • 4243351662 scopus 로고    scopus 로고
    • Molecular chaperone activity of the stress protein Hsc70 purified from an eurythermal goby, Gillichthys mirabilis
    • 111. Hofmann GE. 1996. Molecular chaperone activity of the stress protein Hsc70 purified from an eurythermal goby, Gillichthys mirabilis. Am. Zool. 36:36A
    • (1996) Am. Zool. , vol.36
    • Hofmann, G.E.1
  • 113
    • 0025369515 scopus 로고
    • A comparative study of the thermal stability of the vertebrate eye lens: Antarctic fish to the desert iguana
    • 112. McFall-Ngai M, Horwitz J. 1990. A comparative study of the thermal stability of the vertebrate eye lens: Antarctic fish to the desert iguana. Exp. Eye Res. 50:703-9
    • (1990) Exp. Eye Res. , vol.50 , pp. 703-709
    • McFall-Ngai, M.1    Horwitz, J.2
  • 114
    • 0027220057 scopus 로고
    • Induction temperature of human heat shock factor is reprogrammed in a Drosophila cell environment
    • 113. Clos J, Rabindran S, Wisniewski J, Wu C. 1993. Induction temperature of human heat shock factor is reprogrammed in a Drosophila cell environment. Nature 364:252-55
    • (1993) Nature , vol.364 , pp. 252-255
    • Clos, J.1    Rabindran, S.2    Wisniewski, J.3    Wu, C.4
  • 115
    • 0029913811 scopus 로고    scopus 로고
    • Membrane lipid perturbation modifies the set point of the temperature of heat shock response in yeast
    • 114. Carratu L, Franceschelli S, Pardini CL, Kobayashi GS, Horvath I, et al. 1996. Membrane lipid perturbation modifies the set point of the temperature of heat shock response in yeast. Proc. Natl. Acad. Sci. USA 93:3870-75
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3870-3875
    • Carratu, L.1    Franceschelli, S.2    Pardini, C.L.3    Kobayashi, G.S.4    Horvath, I.5
  • 116
    • 0028173175 scopus 로고
    • Hsp70 in parasites: As an inducible protective protein and as an antigen
    • 115. Maresca B, Kobayashi GS. 1994. Hsp70 in parasites: as an inducible protective protein and as an antigen. Experientia 50:1067-74
    • (1994) Experientia , vol.50 , pp. 1067-1074
    • Maresca, B.1    Kobayashi, G.S.2
  • 117
    • 0026726575 scopus 로고
    • The cellular immune response to heat shock proteins
    • 116. Kaufmann SH. 1992. The cellular immune response to heat shock proteins. Experientia 48:640-43
    • (1992) Experientia , vol.48 , pp. 640-643
    • Kaufmann, S.H.1
  • 118
    • 0025894722 scopus 로고
    • Heat shock proteins in host-parasite interactions
    • 117. Polla BS. 1991. Heat shock proteins in host-parasite interactions. Immunol. Today 12:A38-41
    • (1991) Immunol. Today , vol.12
    • Polla, B.S.1
  • 119
    • 0025985684 scopus 로고
    • Heat shock proteins as vaccine candidates
    • 118. Newport GR. 1991. Heat shock proteins as vaccine candidates. Semin. Immunol. 3:17-24
    • (1991) Semin. Immunol. , vol.3 , pp. 17-24
    • Newport, G.R.1
  • 120
    • 0031060613 scopus 로고    scopus 로고
    • Expression of a 70-kDa heat-shock-related protein during transformation from free-living infective larvae to the parasitic stage in Strongyloides venezuelensis
    • 119. Tsuji N, Ohta M, Fujisaki K. 1997. Expression of a 70-kDa heat-shock-related protein during transformation from free-living infective larvae to the parasitic stage in Strongyloides venezuelensis. Parasitol. Res. 83:99-102
    • (1997) Parasitol. Res. , vol.83 , pp. 99-102
    • Tsuji, N.1    Ohta, M.2    Fujisaki, K.3
  • 121
    • 0021866913 scopus 로고
    • Heat shock genes: Regulatory role for differentiation in parasitic protozoa
    • 120. Van der Ploeg LH, Giannini SH, Cantor CR. 1985. Heat shock genes: regulatory role for differentiation in parasitic protozoa. Science 228:1443-46
    • (1985) Science , vol.228 , pp. 1443-1446
    • Van Der Ploeg, L.H.1    Giannini, S.H.2    Cantor, C.R.3
  • 122
    • 0027526305 scopus 로고
    • Regulation of HSP70 gene expression during the life cycle of the parasitic helminth Schistosoma mansoni
    • 121. Neumann S, Ziv E, Lantner F, Schechter I. 1993. Regulation of HSP70 gene expression during the life cycle of the parasitic helminth Schistosoma mansoni. Eur. J. Biochem. 212:589-96
    • (1993) Eur. J. Biochem. , vol.212 , pp. 589-596
    • Neumann, S.1    Ziv, E.2    Lantner, F.3    Schechter, I.4
  • 123
    • 0028822959 scopus 로고
    • Heat-shock and stress response of the parasitic nematode Haemonchus contortus
    • 122. van Leeuwen MA. 1995. Heat-shock and stress response of the parasitic nematode Haemonchus contortus. Parasitol. Res. 81:706-9
    • (1995) Parasitol. Res. , vol.81 , pp. 706-709
    • Van Leeuwen, M.A.1
  • 124
    • 0027241290 scopus 로고
    • Release of stress proteins from Mesocestoides corti is a brefeldin A-inhibitable process: Evidence for active export of stress proteins
    • 123. Ernani FP, Teale JM. 1993. Release of stress proteins from Mesocestoides corti is a brefeldin A-inhibitable process: evidence for active export of stress proteins. Infect. Immun. 61:2596-601
    • (1993) Infect. Immun. , vol.61 , pp. 2596-2601
    • Ernani, F.P.1    Teale, J.M.2
  • 125
    • 0030200510 scopus 로고    scopus 로고
    • Cloning of a Plasmodium falciparum gene related to the human 60-kDa heat shock protein
    • 124. Syin C, Goldman ND. 1996. Cloning of a Plasmodium falciparum gene related to the human 60-kDa heat shock protein. Mol. Biochem. Parasitol. 79:13-19
    • (1996) Mol. Biochem. Parasitol. , vol.79 , pp. 13-19
    • Syin, C.1    Goldman, N.D.2
  • 126
    • 0025231680 scopus 로고
    • Thermoregulation of protein synthesis in Borrelia burgdorferi
    • 125. Cluss RG, Boothby JT. 1990. Thermoregulation of protein synthesis in Borrelia burgdorferi. Infect. Immun. 58:1038-42
    • (1990) Infect. Immun. , vol.58 , pp. 1038-1042
    • Cluss, R.G.1    Boothby, J.T.2
  • 127
    • 1842337450 scopus 로고    scopus 로고
    • The Leishmania major Hsp100 is required chiefly in the mammalian stage of the parasite
    • 126. Hubel A, Krobitsch S, Horauf A, Clos J. 1997. The Leishmania major Hsp100 is required chiefly in the mammalian stage of the parasite. Mol. Cell. Biol. 17:5987-95
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5987-5995
    • Hubel, A.1    Krobitsch, S.2    Horauf, A.3    Clos, J.4
  • 128
    • 0030218808 scopus 로고    scopus 로고
    • Characterization and cellular distribution of heat-shock proteins HSP70 and HSP60 in Trypanosoma cruzi
    • 127. Giambiagi-de Marval M, Souto-Padron T, Rondinelli E. 1996. Characterization and cellular distribution of heat-shock proteins HSP70 and HSP60 in Trypanosoma cruzi. Exp. Parasitol. 83:335-45
    • (1996) Exp. Parasitol. , vol.83 , pp. 335-345
    • Giambiagi-De Marval, M.1    Souto-Padron, T.2    Rondinelli, E.3
  • 129
    • 0030965626 scopus 로고    scopus 로고
    • Molecular characterisation of a cognate 70 kDa heat shock protein of the protozoan Theileria parva
    • 128. Daubenberger C, Heussler V, Gobright E, Wijngaard P, Clevers HC, et al. 1997. Molecular characterisation of a cognate 70 kDa heat shock protein of the protozoan Theileria parva. Mol. Biochem. Parasitol. 85:265-69
    • (1997) Mol. Biochem. Parasitol. , vol.85 , pp. 265-269
    • Daubenberger, C.1    Heussler, V.2    Gobright, E.3    Wijngaard, P.4    Clevers, H.C.5
  • 130
    • 0023545320 scopus 로고
    • Heat-shock proteins induced during the mycelial-to-yeast transitions of strains of Histoplasma capsulatum
    • 129. Shearer GJ, Birge CH, Yuckenberg PD, Kobayashi GS, Medoff G. 1987. Heat-shock proteins induced during the mycelial-to-yeast transitions of strains of Histoplasma capsulatum. J. Gen. Microbiol. 133:3375-82
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 3375-3382
    • Shearer, G.J.1    Birge, C.H.2    Yuckenberg, P.D.3    Kobayashi, G.S.4    Medoff, G.5
  • 131
    • 0029189478 scopus 로고
    • Unraveling the secrets of Histoplasma capsulatum. A model to study morphogenic adaptation during parasite host/host interaction
    • 130. Maresca B. 1995. Unraveling the secrets of Histoplasma capsulatum. A model to study morphogenic adaptation during parasite host/host interaction. Verh. K. Acad. Geneeskd. Belg. 57:133-56
    • (1995) Verh. K. Acad. Geneeskd. Belg. , vol.57 , pp. 133-156
    • Maresca, B.1
  • 132
    • 0029941313 scopus 로고    scopus 로고
    • Developmental expression of heat shock protein 90 in Eimeria bovis
    • 131. Clark TG, Abrahamsen MS, White MW. 1996. Developmental expression of heat shock protein 90 in Eimeria bovis. Mol. Biochem. Parasitol. 78:259-63
    • (1996) Mol. Biochem. Parasitol. , vol.78 , pp. 259-263
    • Clark, T.G.1    Abrahamsen, M.S.2    White, M.W.3
  • 134
    • 0024211889 scopus 로고
    • Molecular mechanisms of adaptation to hyperthermia in higher organisms. III. Induction of heat-shock proteins in two Leishmania species
    • 133. Ulmasov KA, Ovezmukhammedov A, Karaev KK, Evgenev MB. 1988. Molecular mechanisms of adaptation to hyperthermia in higher organisms. III. induction of heat-shock proteins in two Leishmania species. Mol. Biol. 22: 1583-89
    • (1988) Mol. Biol. , vol.22 , pp. 1583-1589
    • Ulmasov, K.A.1    Ovezmukhammedov, A.2    Karaev, K.K.3    Evgenev, M.B.4
  • 135
  • 136
    • 0030844640 scopus 로고    scopus 로고
    • Evidence for loss of mitochondria in microsporidia from a mitochondrial-type HSP70 in Nosema locustae
    • 135. Germot A, Philippe H, Le Guyader H. 1997. Evidence for loss of mitochondria in microsporidia from a mitochondrial-type HSP70 in Nosema locustae. Mol. Biochem. Parasitol. 87:159-68
    • (1997) Mol. Biochem. Parasitol. , vol.87 , pp. 159-168
    • Germot, A.1    Philippe, H.2    Le Guyader, H.3
  • 137
    • 0029817685 scopus 로고    scopus 로고
    • A common evolutionary origin for mitochondria and hydrogenosomes
    • 136. Bui ET, Bradley PJ, Johnson PJ. 1996. A common evolutionary origin for mitochondria and hydrogenosomes. Proc. Natl. Acad. Sci. USA 93:9651-56
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9651-9656
    • Bui, E.T.1    Bradley, P.J.2    Johnson, P.J.3
  • 138
    • 0031148712 scopus 로고    scopus 로고
    • Organelle origins: Energy-producing symbionts in early eukaryotes?
    • 137. Sogin ML. 1997. Organelle origins: energy-producing symbionts in early eukaryotes? Curr. Biol. 7:R315-17
    • (1997) Curr. Biol. , vol.7
    • Sogin, M.L.1
  • 139
    • 0028340378 scopus 로고
    • The smallest known eukaryotic genomes encode a protein gene: Towards an understanding of nucleomorph functions
    • 138. Hofmann CJ, Rensing SA, Hauber MM, Martin WF, Muller SB, et al. 1994. The smallest known eukaryotic genomes encode a protein gene: towards an understanding of nucleomorph functions. Mol. Gen. Genet. 243:600-4
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 600-604
    • Hofmann, C.J.1    Rensing, S.A.2    Hauber, M.M.3    Martin, W.F.4    Muller, S.B.5
  • 140
    • 0029963676 scopus 로고    scopus 로고
    • Presence of a mitochondrialtype 70-kDa heat shock protein in Trichomonas vaginalis suggests a very early mitochondrial endosymbiosis in eukaryotes
    • 139. Germot A, Philippe H, Le Guyader H. 1996. Presence of a mitochondrialtype 70-kDa heat shock protein in Trichomonas vaginalis suggests a very early mitochondrial endosymbiosis in eukaryotes. Proc. Natl. Acad. Sci. USA 93:14614-17
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14614-14617
    • Germot, A.1    Philippe, H.2    Le Guyader, H.3
  • 141
    • 0031013397 scopus 로고    scopus 로고
    • The evolution and genetics of aphid endosymbionts
    • 140. Baumann P, Moran NA, Baumann L. 1997. The evolution and genetics of aphid endosymbionts. BioScience 47:12-20
    • (1997) BioScience , vol.47 , pp. 12-20
    • Baumann, P.1    Moran, N.A.2    Baumann, L.3
  • 142
    • 0029240197 scopus 로고
    • Molecular analysis of the endosymbionts of tsetse flies: 16S rDNA locus and over-expression of a chaperonin
    • 141. Aksoy S. 1995. Molecular analysis of the endosymbionts of tsetse flies: 16S rDNA locus and over-expression of a chaperonin. Insect Mol. Biol. 4:23-29
    • (1995) Insect Mol. Biol. , vol.4 , pp. 23-29
    • Aksoy, S.1
  • 143
    • 0029565877 scopus 로고
    • Faster evolutionary rates in endosymbiotic bacteria than in cospeciating insect hosts
    • 142. Moran NA, Von Dohlen CD, Baumann P. 1995. Faster evolutionary rates in endosymbiotic bacteria than in cospeciating insect hosts. J. Mol. Evol. 41:727-31
    • (1995) J. Mol. Evol. , vol.41 , pp. 727-731
    • Moran, N.A.1    Von Dohlen, C.D.2    Baumann, P.3
  • 144
    • 0029866448 scopus 로고    scopus 로고
    • Accelerated evolution and Muller's rachet in endosymbiotic bacteria
    • 143. Moran NA. 1996. Accelerated evolution and Muller's rachet in endosymbiotic bacteria. Proc. Natl. Acad. Sci. USA 93:2873-78
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2873-2878
    • Moran, N.A.1
  • 145
    • 0026507312 scopus 로고
    • Mutualism based on stress: Selective synthesis and phosphorylation of a stress protein by an intracellular symbiont
    • 144. Morioka M, Ishikawa H. 1992. Mutualism based on stress: selective synthesis and phosphorylation of a stress protein by an intracellular symbiont. J. Biochem. 111:431-35
    • (1992) J. Biochem. , vol.111 , pp. 431-435
    • Morioka, M.1    Ishikawa, H.2
  • 146
    • 0013632631 scopus 로고
    • Molecular biological studies on the heat-shock responses in Amoeba proteus: I. Detection of heat-shock proteins
    • 145. Hong HK, Choi JY, Ahn TI. 1994. Molecular biological studies on the heat-shock responses in Amoeba proteus: I. Detection of heat-shock proteins. Korean J. Zool. 37:554-64
    • (1994) Korean J. Zool. , vol.37 , pp. 554-564
    • Hong, H.K.1    Choi, J.Y.2    Ahn, T.I.3
  • 147
    • 0025816057 scopus 로고
    • Elevated levels of stress proteins associated with bacterial symbiosis m Amoeba proleus and soybean root nodule cells
    • 146. Choi EY, Ahn GS, Jeon KW. 1991. Elevated levels of stress proteins associated with bacterial symbiosis m Amoeba proleus and soybean root nodule cells. Biosystems 25:205-12
    • (1991) Biosystems , vol.25 , pp. 205-212
    • Choi, E.Y.1    Ahn, G.S.2    Jeon, K.W.3
  • 148
    • 4243388646 scopus 로고    scopus 로고
    • Evolutionarily significant consequences of the heat shock response for Drosophila and its endosymbiont Wolbachia
    • 147. Feder ME, Karr TL. 1997. Evolutionarily significant consequences of the heat shock response for Drosophila and its endosymbiont Wolbachia. Am. Zool. 37:8A
    • (1997) Am. Zool. , vol.37
    • Feder, M.E.1    Karr, T.L.2
  • 149
    • 0030815911 scopus 로고    scopus 로고
    • Hsp70 expression and function during gametogenesis
    • 148. Dix DJ. 1997. Hsp70 expression and function during gametogenesis. Cell Stress Chaperones 2:73-77
    • (1997) Cell Stress Chaperones , vol.2 , pp. 73-77
    • Dix, D.J.1
  • 150
    • 0027301001 scopus 로고
    • Heat shock gene expression and development. I. An overview of fungal, plant, and poikilothermic animal developmental systems
    • 149. Lin JC, Song CW. 1993. Heat shock gene expression and development. I. An overview of fungal, plant, and poikilothermic animal developmental systems. Dev. Genet. 14:1-5
    • (1993) Dev. Genet. , vol.14 , pp. 1-5
    • Lin, J.C.1    Song, C.W.2
  • 151
    • 0026271466 scopus 로고
    • The expression of heat shock protein and cognate genes during plant development
    • 150. Winter J, Sinibaldi R. 1991. The expression of heat shock protein and cognate genes during plant development. Results Prob. Cell Differ. 17:85-105
    • (1991) Results Prob. Cell Differ. , vol.17 , pp. 85-105
    • Winter, J.1    Sinibaldi, R.2
  • 152
    • 0027159965 scopus 로고
    • Heat shock gene expression and development. II. An overview of mammalian and avian developmental systems
    • 151. Mosser DD, Duchaine J, Bourget L, Martin LH. 1993. Heat shock gene expression and development. II. An overview of mammalian and avian developmental systems. Dev. Genet. 14: 87-91
    • (1993) Dev. Genet. , vol.14 , pp. 87-91
    • Mosser, D.D.1    Duchaine, J.2    Bourget, L.3    Martin, L.H.4
  • 153
    • 0030766710 scopus 로고    scopus 로고
    • Heat shock protein gene expression during Xenopus development
    • 152. Heikkila JJ, Ohan N, Tam Y, Ali A. 1997. Heat shock protein gene expression during Xenopus development. Cell. Mol. Life Sci. 53:114-21
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 114-121
    • Heikkila, J.J.1    Ohan, N.2    Tam, Y.3    Ali, A.4
  • 154
    • 0022295913 scopus 로고
    • Heat does not induce synthesis of heat shock proteins or thermotolerance in the earliest stage of mouse embryo development
    • 153. Muller WU, Li GC, Goldstein LS. 1985. Heat does not induce synthesis of heat shock proteins or thermotolerance in the earliest stage of mouse embryo development. Int. J. Hypertherm. 1:97-102
    • (1985) Int. J. Hypertherm. , vol.1 , pp. 97-102
    • Muller, W.U.1    Li, G.C.2    Goldstein, L.S.3
  • 155
    • 0030740171 scopus 로고    scopus 로고
    • Ontogeny of temperature-regulated heat shock protein 70 synthesis in preimplantation bovine embryos
    • 154. Edwards JL, Ealy AD, Monterroso VH, Hansen PJ. 1997. Ontogeny of temperature-regulated heat shock protein 70 synthesis in preimplantation bovine embryos. Mol. Reprod. Dev. 48: 25-33
    • (1997) Mol. Reprod. Dev. , vol.48 , pp. 25-33
    • Edwards, J.L.1    Ealy, A.D.2    Monterroso, V.H.3    Hansen, P.J.4
  • 156
    • 0019742892 scopus 로고
    • Stage dependent synthesis of heat shock induced proteins in early embryos of Drosophila melanogaster
    • 155. Dura JM. 1981. Stage dependent synthesis of heat shock induced proteins in early embryos of Drosophila melanogaster. Mol. Gen. Genet. 184: 381-85
    • (1981) Mol. Gen. Genet. , vol.184 , pp. 381-385
    • Dura, J.M.1
  • 157
    • 0027144416 scopus 로고
    • A new method for manipulating transgenes: Engineering heat tolerance in a complex, multicellular organism
    • 156. Weite MA, Tetrault JM, Dellavalle RP, Lindquist SL. 1993. A new method for manipulating transgenes: engineering heat tolerance in a complex, multicellular organism. Curr. Biol. 3:842-53
    • (1993) Curr. Biol. , vol.3 , pp. 842-853
    • Weite, M.A.1    Tetrault, J.M.2    Dellavalle, R.P.3    Lindquist, S.L.4
  • 158
    • 0029411225 scopus 로고
    • Expression of heat shock factor and heat shock protein 70 genes during maize pollen development
    • 157. Gagliardi D, Breton C, Chaboud A, Vergne P, Dumas C. 1995. Expression of heat shock factor and heat shock protein 70 genes during maize pollen development. Plant Mol. Biol. 29:841-56
    • (1995) Plant Mol. Biol. , vol.29 , pp. 841-856
    • Gagliardi, D.1    Breton, C.2    Chaboud, A.3    Vergne, P.4    Dumas, C.5
  • 159
    • 0026016447 scopus 로고
    • Thermolability of mouse oocytes is due to the lack of expression and/or inducibility of Hsp70
    • 158. Hendrey J, Kola I. 1991. Thermolability of mouse oocytes is due to the lack of expression and/or inducibility of Hsp70. Mol. Reprod. Dev. 28:1-8
    • (1991) Mol. Reprod. Dev. , vol.28 , pp. 1-8
    • Hendrey, J.1    Kola, I.2
  • 160
    • 0023414744 scopus 로고
    • Lack of heat-shock response in pre-ovulatory mouse oocytes
    • 159. Curci A, Bevilacqua A, Mangia F. 1987. Lack of heat-shock response in pre-ovulatory mouse oocytes. Dev. Biol. 123:154-60
    • (1987) Dev. Biol. , vol.123 , pp. 154-160
    • Curci, A.1    Bevilacqua, A.2    Mangia, F.3
  • 161
    • 0025806278 scopus 로고
    • Developmental regulation of heat-shock response in mouse oogenesis: Identification of differentially responsive oocyte classes during Graafian follicle development
    • 160. Curci A, Bevilacqua A, Fiorenza MT, Mangia F. 1991. Developmental regulation of heat-shock response in mouse oogenesis: identification of differentially responsive oocyte classes during Graafian follicle development. Dev. Biol. 144:362-68
    • (1991) Dev. Biol. , vol.144 , pp. 362-368
    • Curci, A.1    Bevilacqua, A.2    Fiorenza, M.T.3    Mangia, F.4
  • 162
    • 0025151869 scopus 로고
    • Characterization and inducibility of hsp 70 proteins in the male mouse germ line
    • 161. Zakeri ZF, Welch WJ, Wolgemuth DJ. 1990. Characterization and inducibility of hsp 70 proteins in the male mouse germ line. J. Cell Biol. 111:1785-92
    • (1990) J. Cell Biol. , vol.111 , pp. 1785-1792
    • Zakeri, Z.F.1    Welch, W.J.2    Wolgemuth, D.J.3
  • 163
    • 0022779172 scopus 로고
    • Translational activation of maternal mRNA encoding the heat-shock protein hsp90 during sea urchin embryogenesis
    • 162. Bedard PA, Brandhorst BP. 1986. Translational activation of maternal mRNA encoding the heat-shock protein hsp90 during sea urchin embryogenesis. Dev. Biol. 117:286-93
    • (1986) Dev. Biol. , vol.117 , pp. 286-293
    • Bedard, P.A.1    Brandhorst, B.P.2
  • 164
    • 0031042615 scopus 로고    scopus 로고
    • Distinct stress-inducible and developmentally regulated heat shock transcription factors in Xenopus oocytes
    • 163. Gordon S, Bharadwaj S, Hnatov A, Ali A, Ovsenek N. 1997. Distinct stress-inducible and developmentally regulated heat shock transcription factors in Xenopus oocytes. Dev. Biol. 181:47-63
    • (1997) Dev. Biol. , vol.181 , pp. 47-63
    • Gordon, S.1    Bharadwaj, S.2    Hnatov, A.3    Ali, A.4    Ovsenek, N.5
  • 165
    • 0026645957 scopus 로고
    • The consequences of expressing Hsp70 in Drosophila cells at normal temperatures
    • 164. Feder JH, Rossi JM, Solomon J, Solomon N, Lindquist S. 1992. The consequences of expressing Hsp70 in Drosophila cells at normal temperatures. Genes Dev. 6:1402-13
    • (1992) Genes Dev. , vol.6 , pp. 1402-1413
    • Feder, J.H.1    Rossi, J.M.2    Solomon, J.3    Solomon, N.4    Lindquist, S.5
  • 167
    • 0029142471 scopus 로고
    • The basis for a heat-induced developmental defect: Defining crucial lesions
    • 166. Welte MA, Duncan I, Lindquist S. 1995. The basis for a heat-induced developmental defect: defining crucial lesions. Genes Dev. 9:2240-50
    • (1995) Genes Dev. , vol.9 , pp. 2240-2250
    • Welte, M.A.1    Duncan, I.2    Lindquist, S.3
  • 168
    • 0030265854 scopus 로고    scopus 로고
    • Synthesis of small heat-shock proteins is part of the developmental program of late seed maturation
    • 167. Wehmeyer N, Hernandez LD, Finkelstein RR, Vierling E. 1996. Synthesis of small heat-shock proteins is part of the developmental program of late seed maturation. Plant Physiol. 112:747-57
    • (1996) Plant Physiol. , vol.112 , pp. 747-757
    • Wehmeyer, N.1    Hernandez, L.D.2    Finkelstein, R.R.3    Vierling, E.4
  • 169
    • 0001532945 scopus 로고
    • Heat shock protein Hsp70 cognate gene expression in vegetative and reproductive organs of Lycopersicon esculentum
    • 168. Duck N, McCormick S, Winter J. 1989. Heat shock protein Hsp70 cognate gene expression in vegetative and reproductive organs of Lycopersicon esculentum. Proc. Natl. Acad. Sci. USA 86:3674-78
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3674-3678
    • Duck, N.1    McCormick, S.2    Winter, J.3
  • 170
    • 0028448479 scopus 로고
    • Expression of sunflower low-molecular-weight heat-shock proteins during embryogenesis and persistence after germination: Localization and possible functional implications
    • 169. Coca MA, Almoguera C, Jordano J. 1994. Expression of sunflower low-molecular-weight heat-shock proteins during embryogenesis and persistence after germination: localization and possible functional implications. Plant Mol. Biol. 25:479-92
    • (1994) Plant Mol. Biol. , vol.25 , pp. 479-492
    • Coca, M.A.1    Almoguera, C.2    Jordano, J.3
  • 171
    • 0000347251 scopus 로고
    • Heat-shock response of germinating embryos of wheat: Effects of imbibition time and seed vigor
    • 170. Helm KW, Petersen NS, Abernethy RH. 1989. Heat-shock response of germinating embryos of wheat: effects of imbibition time and seed vigor. Plant Physiol. 90:598-605
    • (1989) Plant Physiol. , vol.90 , pp. 598-605
    • Helm, K.W.1    Petersen, N.S.2    Abernethy, R.H.3
  • 172
    • 0026523626 scopus 로고
    • Hsp104 is required for tolerance to many forms of stress
    • 171. Sanchez Y, Taulien J, Borkovich KA, Lindquist S. 1992. Hsp104 is required for tolerance to many forms of stress. EMBO J. 11:2357-64
    • (1992) EMBO J. , vol.11 , pp. 2357-2364
    • Sanchez, Y.1    Taulien, J.2    Borkovich, K.A.3    Lindquist, S.4
  • 174
    • 0030755398 scopus 로고    scopus 로고
    • Molecular characterization of a small heat shock/alpha-crystallin protein in encysted Artemia embryos
    • 173. Liang P, Amons R, Clegg JS, MacRae TH. 1997. Molecular characterization of a small heat shock/alpha-crystallin protein in encysted Artemia embryos. J. Biol. Chem. 272:19051-58
    • (1997) J. Biol. Chem. , vol.272 , pp. 19051-19058
    • Liang, P.1    Amons, R.2    Clegg, J.S.3    MacRae, T.H.4
  • 175
    • 0031020927 scopus 로고    scopus 로고
    • Purification, structure and in vitro molecular-chaperone activity of Artemia p26, a small heat-shock/alpha-crystallin protein
    • 174. Liang P, Amons R, Macrae TH, Clegg JS. 1997. Purification, structure and in vitro molecular-chaperone activity of Artemia p26, a small heat-shock/alpha-crystallin protein. Eur. J. Biochem. 243: 225-32
    • (1997) Eur. J. Biochem. , vol.243 , pp. 225-232
    • Liang, P.1    Amons, R.2    Macrae, T.H.3    Clegg, J.S.4
  • 176
    • 0013630359 scopus 로고    scopus 로고
    • Ontogeny of low molecular weight stress protein p26 during early development of the brine shrimp, Artemia franciscana
    • 175. Jackson SA, Clegg JS. 1996. Ontogeny of low molecular weight stress protein p26 during early development of the brine shrimp, Artemia franciscana. J. Exp. Biol. 200:467-75
    • (1996) J. Exp. Biol. , vol.200 , pp. 467-475
    • Jackson, S.A.1    Clegg, J.S.2
  • 177
    • 0029115241 scopus 로고
    • Nuclear-cytoplasmic translocations of protein p26 during aerobicanoxic transitions in embryos of Artemia franciscana
    • 176. Clegg JS, Jackson SA, Liang P, MacRae TH. 1995. Nuclear-cytoplasmic translocations of protein p26 during aerobicanoxic transitions in embryos of Artemia franciscana. Exp. Cell Res. 219:1-7
    • (1995) Exp. Cell Res. , vol.219 , pp. 1-7
    • Clegg, J.S.1    Jackson, S.A.2    Liang, P.3    MacRae, T.H.4
  • 178
    • 0028365340 scopus 로고
    • Extensive intracellular translocations of a major protein accompany anoxia in embryos of Artemia franciscana
    • 177. Clegg JS, Jackson SA, Warner AH. 1994. Extensive intracellular translocations of a major protein accompany anoxia in embryos of Artemia franciscana. Exp. Cell Res. 212:77-83
    • (1994) Exp. Cell Res. , vol.212 , pp. 77-83
    • Clegg, J.S.1    Jackson, S.A.2    Warner, A.H.3
  • 179
    • 0026605621 scopus 로고
    • Aerobic heat shock activates trehalose synthesis in embryos of Artemia franciscana
    • 178. Clegg JS, Jackson SA. 1992. Aerobic heat shock activates trehalose synthesis in embryos of Artemia franciscana. FEES Lett. 303:45-47
    • (1992) FEES Lett. , vol.303 , pp. 45-47
    • Clegg, J.S.1    Jackson, S.A.2
  • 180
    • 0028008192 scopus 로고
    • Acute blockage of the ubiquitin-mediated proteolytic pathway during invertebrate quiescence
    • 179. Anchordoguy TJ, Hand SC. 1994. Acute blockage of the ubiquitin-mediated proteolytic pathway during invertebrate quiescence. Am. J. Physiol. 267:R895-900
    • (1994) Am. J. Physiol. , vol.267
    • Anchordoguy, T.J.1    Hand, S.C.2
  • 181
    • 0031925948 scopus 로고    scopus 로고
    • Heritability of expression of the 70-kD heat-shock protein in Drosophila melanogaster and its relevance to the evolution of thermotolerance
    • 180. Krebs RA, Feder ME, Lee J. 1998. Heritability of expression of the 70-kD heat-shock protein in Drosophila melanogaster and its relevance to the evolution of thermotolerance. Evolution 52:841-47
    • (1998) Evolution , vol.52 , pp. 841-847
    • Krebs, R.A.1    Feder, M.E.2    Lee, J.3
  • 182
    • 0028344824 scopus 로고
    • Immunolocalization of ubiquitin in degenerating insect flight muscle
    • 181. Davis WL, Jacoby BH, Goodman DB. 1994. Immunolocalization of ubiquitin in degenerating insect flight muscle. Histochem. J. 26:298-305
    • (1994) Histochem. J. , vol.26 , pp. 298-305
    • Davis, W.L.1    Jacoby, B.H.2    Goodman, D.B.3
  • 183
    • 0028907352 scopus 로고
    • Altered stress response in testis
    • 182. Sarge KD, Bray AE, Goodson ML. 1995. Altered stress response in testis. Nature 374:126
    • (1995) Nature , vol.374 , pp. 126
    • Sarge, K.D.1    Bray, A.E.2    Goodson, M.L.3
  • 184
    • 0029154777 scopus 로고
    • Male germ cell-specific alteration in temperature set point of the cellular stress response
    • 183. Sarge KD. 1995. Male germ cell-specific alteration in temperature set point of the cellular stress response. J. Biol. Chem. 270:18745-48
    • (1995) J. Biol. Chem. , vol.270 , pp. 18745-18748
    • Sarge, K.D.1
  • 186
    • 0029784653 scopus 로고    scopus 로고
    • Heat shock response, heat shock transcription factor and cell aging
    • 185. Lee YK, Manalo D, Liu AY. 1996. Heat shock response, heat shock transcription factor and cell aging. Biol. Signals 5:180-91
    • (1996) Biol. Signals , vol.5 , pp. 180-191
    • Lee, Y.K.1    Manalo, D.2    Liu, A.Y.3
  • 187
    • 0031037063 scopus 로고    scopus 로고
    • Alterations in the chaperone activity of HSP70 in aging organisms
    • 186. Shpund S, Gershon D. 1997. Alterations in the chaperone activity of HSP70 in aging organisms. Arch. Gerontol. Geriatr. 24:125-31
    • (1997) Arch. Gerontol. Geriatr. , vol.24 , pp. 125-131
    • Shpund, S.1    Gershon, D.2
  • 188
    • 0028826029 scopus 로고
    • Muscle-specific expression of Drosophila hsp70 in response to aging and oxidative stress
    • 187. Wheeler JC, Bieschke ET, Tower J. 1995. Muscle-specific expression of Drosophila hsp70 in response to aging and oxidative stress. Proc. Natl. Acad. Sci. USA 92:10408-12
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10408-10412
    • Wheeler, J.C.1    Bieschke, E.T.2    Tower, J.3
  • 189
    • 0027312448 scopus 로고
    • Heat shock induces changes in the expression and binding of ubiquitin in senescent Drosophila melanogaster
    • 188. Marin R, Valet JP, Tanguay RM. 1993. Heat shock induces changes in the expression and binding of ubiquitin in senescent Drosophila melanogaster. Dev. Genet. 14:78-86
    • (1993) Dev. Genet. , vol.14 , pp. 78-86
    • Marin, R.1    Valet, J.P.2    Tanguay, R.M.3
  • 190
    • 0027945612 scopus 로고
    • Thermotolerance of a long-lived mutant of Caenorhabditis elegans
    • 189. Lithgow GJ, White TM, Hinerfeld DA, Johnson TE. 1994. Thermotolerance of a long-lived mutant of Caenorhabditis elegans. J. Gerontol. 49B:270-76
    • (1994) J. Gerontol. , vol.49 B , pp. 270-276
    • Lithgow, G.J.1    White, T.M.2    Hinerfeld, D.A.3    Johnson, T.E.4
  • 191
    • 0029123058 scopus 로고
    • Thermotolerance and extended life-span conferred by single-gene mutations and induced by thermal stress
    • 190. Lithgow GJ, White TM, Melov S, Johnson TE. 1995. Thermotolerance and extended life-span conferred by single-gene mutations and induced by thermal stress. Proc. Natl. Acad. Sci. USA 92:7540-44
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7540-7544
    • Lithgow, G.J.1    White, T.M.2    Melov, S.3    Johnson, T.E.4
  • 192
    • 0030272505 scopus 로고    scopus 로고
    • Invertebrate gerontology: The age mutations of Caenorhabditis elegans
    • 191. Lithgow GJ. 1996. Invertebrate gerontology: the age mutations of Caenorhabditis elegans. BioEssays 18:809-15
    • (1996) BioEssays , vol.18 , pp. 809-815
    • Lithgow, G.J.1
  • 193
    • 0027515439 scopus 로고
    • Age-dependent expression of proteins in the cladoceran Daphnia magna under normal and heat-stress conditions
    • 192. Bond JA, Gonzalez CRM, Bradley BP. 1993. Age-dependent expression of proteins in the cladoceran Daphnia magna under normal and heat-stress conditions. Comp. Biochem. Physiol. 106B:913-17
    • (1993) Comp. Biochem. Physiol. , vol.106 B , pp. 913-917
    • Bond, J.A.1    Gonzalez, C.R.M.2    Bradley, B.P.3
  • 194
    • 0031021432 scopus 로고    scopus 로고
    • Heat-induced longevity extension in Drosophila. I. Heat treatment, mortality, and thermotolerance
    • 193. Khazaeli AA, Tatar M, Pletcher SD, Curtsinger JW. 1997. Heat-induced longevity extension in Drosophila. I. Heat treatment, mortality, and thermotolerance. J. Gerontol. 52A:B48-52
    • (1997) J. Gerontol. , vol.52 A
    • Khazaeli, A.A.1    Tatar, M.2    Pletcher, S.D.3    Curtsinger, J.W.4
  • 196
    • 0030882921 scopus 로고    scopus 로고
    • Dietary energy tissue-specifically regulates endoplasmic reticulum chaperone gene expression in the liver of mice
    • 195. Dhahbi JM, Mote PL, Tillman JB, Walford RL, Spindler SR. 1997. Dietary energy tissue-specifically regulates endoplasmic reticulum chaperone gene expression in the liver of mice. J. Nutr. 127:1758-64
    • (1997) J. Nutr. , vol.127 , pp. 1758-1764
    • Dhahbi, J.M.1    Mote, P.L.2    Tillman, J.B.3    Walford, R.L.4    Spindler, S.R.5
  • 197
    • 0028842285 scopus 로고
    • Expression of heat shock genes in hepatocytes is affected by age and food restriction in rats
    • 196. Heydari AR, Conrad CC, Richardson A. 1995. Expression of heat shock genes in hepatocytes is affected by age and food restriction in rats. J. Nutr. 125:410-18
    • (1995) J. Nutr. , vol.125 , pp. 410-418
    • Heydari, A.R.1    Conrad, C.C.2    Richardson, A.3
  • 198
    • 0029788073 scopus 로고    scopus 로고
    • Expression of heat shock protein 70 in rat spleen lymphocytes is affected by age but not by food restriction
    • 197. Pahlavani MA, Harris MD, Moore SA, Richardson A. 1996. Expression of heat shock protein 70 in rat spleen lymphocytes is affected by age but not by food restriction. J. Nutr. 126:2069-75
    • (1996) J. Nutr. , vol.126 , pp. 2069-2075
    • Pahlavani, M.A.1    Harris, M.D.2    Moore, S.A.3    Richardson, A.4
  • 199
    • 0027154719 scopus 로고
    • Expression of heat shock protein 70 is altered by age and diet at the level of transcription
    • 198. Lu Q, Wallrath LL, Granok H, Elgin SC. 1993. Expression of heat shock protein 70 is altered by age and diet at the level of transcription. Mol. Cell Biol. 13:2909-18
    • (1993) Mol. Cell Biol. , vol.13 , pp. 2909-2918
    • Lu, Q.1    Wallrath, L.L.2    Granok, H.3    Elgin, S.C.4
  • 200
    • 0030451815 scopus 로고    scopus 로고
    • Possible mechanisms underlying the antiaging actions of caloric restriction
    • 199. Masoro EJ. 1996. Possible mechanisms underlying the antiaging actions of caloric restriction. Toxicol. Pathol. 24:738-41
    • (1996) Toxicol. Pathol. , vol.24 , pp. 738-741
    • Masoro, E.J.1
  • 201
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • 200. Parsell DA, Lindquist S. 1993. The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu. Rev. Genet. 27:437-96
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 204
    • 0030154699 scopus 로고    scopus 로고
    • Quantitative evidence that both Hsc70 and Hsp70 contribute to thermal adaptation in hybrids of the livebearing fishes Poeciliopsis
    • 203. diIorio PJ, Holsinger K, Schultz RJ, Hightower LE. 1996. Quantitative evidence that both Hsc70 and Hsp70 contribute to thermal adaptation in hybrids of the livebearing fishes Poeciliopsis. Cell Stress Chaperones 1:139-47
    • (1996) Cell Stress Chaperones , vol.1 , pp. 139-147
    • Diiorio, P.J.1    Holsinger, K.2    Schultz, R.J.3    Hightower, L.E.4
  • 205
    • 4243829950 scopus 로고
    • Evolutionary loss of a heat shock protein
    • Abstr.
    • 204. Feder ME, Lindquist SL. 1992. Evolutionary loss of a heat shock protein. Am. Zool. 32:51A(Abstr.)
    • (1992) Am. Zool. , vol.32
    • Feder, M.E.1    Lindquist, S.L.2
  • 206
    • 0029973294 scopus 로고    scopus 로고
    • Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells
    • 205. Whitesell L, Cook P. 1996. Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. Mol. Endocrinol. 10:705-12
    • (1996) Mol. Endocrinol. , vol.10 , pp. 705-712
    • Whitesell, L.1    Cook, P.2
  • 207
    • 0028279371 scopus 로고
    • Regulation of heat shock protein synthesis by quercetin in human erythroleukaemia cells
    • 206. Elia G, Santoro MG. 1994. Regulation of heat shock protein synthesis by quercetin in human erythroleukaemia cells. Biochem. J. 300:201-9
    • (1994) Biochem. J. , vol.300 , pp. 201-209
    • Elia, G.1    Santoro, M.G.2
  • 208
    • 0001699985 scopus 로고
    • Establishment of thermotolerance in maize by exposure to stresses other than a heat shock does not require heat shock protein synthesis
    • 207. Bonham-Smith PC, Kapoor M, Bewley JD. 1987. Establishment of thermotolerance in maize by exposure to stresses other than a heat shock does not require heat shock protein synthesis. Plant Physiol. 85:575-80
    • (1987) Plant Physiol. , vol.85 , pp. 575-580
    • Bonham-Smith, P.C.1    Kapoor, M.2    Bewley, J.D.3
  • 209
    • 0000464477 scopus 로고
    • High temperature-induced thermotolerance in pollen tubes of Tradescantia and heat-shock proteins
    • 208. Xiao CM, Mascarenhas JP. 1985. High temperature-induced thermotolerance in pollen tubes of Tradescantia and heat-shock proteins. Plant Physiol. 78:887-90
    • (1985) Plant Physiol. , vol.78 , pp. 887-890
    • Xiao, C.M.1    Mascarenhas, J.P.2
  • 210
    • 0023391343 scopus 로고
    • Induction of the heat shock regulon does not produce thermotolerance in Escherichia coli
    • 209. VanBogelen RA, Acton MA, Neidhardt FC. 1987. Induction of the heat shock regulon does not produce thermotolerance in Escherichia coli. Genes Dev. 1:525-31
    • (1987) Genes Dev. , vol.1 , pp. 525-531
    • VanBogelen, R.A.1    Acton, M.A.2    Neidhardt, F.C.3
  • 211
    • 38249009646 scopus 로고
    • Prolonged thermotolerance in the flesh fly Sarcophaga crassipalpis does not require continuous expression or persistence of the 72 kDa heat-shock protein
    • 210. Yocum GD, Denlinger DL. 1992. Prolonged thermotolerance in the flesh fly Sarcophaga crassipalpis does not require continuous expression or persistence of the 72 kDa heat-shock protein. J. Insect Physiol. 38:603-9
    • (1992) J. Insect Physiol. , vol.38 , pp. 603-609
    • Yocum, G.D.1    Denlinger, D.L.2
  • 213
    • 0026322998 scopus 로고
    • Uncoupling thermotolerance from the induction of heat shock proteins
    • 212. Smith BJ, Yaffe MP. 1991. Uncoupling thermotolerance from the induction of heat shock proteins. Proc. Natl. Acad. Sci. USA 88:11091-94
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11091-11094
    • Smith, B.J.1    Yaffe, M.P.2
  • 214
    • 0023146149 scopus 로고
    • Heat shock protein induction and induced thermal tolerance are independent in adult salamanders
    • 213. Easton DP, Rutledge PS, Spotila JR. 1987. Heat shock protein induction and induced thermal tolerance are independent in adult salamanders. J. Exp. Zool. 241:263-67
    • (1987) J. Exp. Zool. , vol.241 , pp. 263-267
    • Easton, D.P.1    Rutledge, P.S.2    Spotila, J.R.3
  • 215
    • 0014314793 scopus 로고
    • Temperature acclimatization in the absence of protein synthesis of Drosophila subobscura
    • 214. Dingley F, Maynard Smith J. 1968. Temperature acclimatization in the absence of protein synthesis of Drosophila subobscura. J. Insect Physiol. 14:1185-94
    • (1968) J. Insect Physiol. , vol.14 , pp. 1185-1194
    • Dingley, F.1    Maynard Smith, J.2
  • 216
    • 0027300674 scopus 로고
    • Lack of concordance between heat shock proteins and the development of tolerance to teratogen-induced neural tube defects
    • 215. Finnell RH, Van Waes M, Bennett GD, Eberwine JH. 1993. Lack of concordance between heat shock proteins and the development of tolerance to teratogen-induced neural tube defects. Dev. Genet. 14:137-47
    • (1993) Dev. Genet. , vol.14 , pp. 137-147
    • Finnell, R.H.1    Van Waes, M.2    Bennett, G.D.3    Eberwine, J.H.4
  • 217
    • 0026694998 scopus 로고
    • Thermotolerance in the absence of induced heat shock proteins in a murine lymphoma
    • 216. Fisher B, Kraft P, Hahn GM, Anderson RL. 1992. Thermotolerance in the absence of induced heat shock proteins in a murine lymphoma. Cancer Res. 52:2854-61
    • (1992) Cancer Res. , vol.52 , pp. 2854-2861
    • Fisher, B.1    Kraft, P.2    Hahn, G.M.3    Anderson, R.L.4
  • 218
    • 0021758881 scopus 로고
    • Mitochondrial and cytoplasmic protein syntheses are not required for heat shock acquisition of ethanol and thermotolerance in yeast
    • 217. Watson K, Dunlop G, Cavicchioli R. 1984. Mitochondrial and cytoplasmic protein syntheses are not required for heat shock acquisition of ethanol and thermotolerance in yeast. FEES Lett. 172:299-302
    • (1984) FEES Lett. , vol.172 , pp. 299-302
    • Watson, K.1    Dunlop, G.2    Cavicchioli, R.3
  • 219
    • 0022636161 scopus 로고
    • Effects of cycloheximide on thermotolerance expression, heat shock protein synthesis, and heat shock protein mRNA accumulation in rat fibroblasts
    • 218. Widelitz RB, Magun BE, Gerner EW. 1986. Effects of cycloheximide on thermotolerance expression, heat shock protein synthesis, and heat shock protein mRNA accumulation in rat fibroblasts. Mol. Cell Biol. 6:1088-94
    • (1986) Mol. Cell Biol. , vol.6 , pp. 1088-1094
    • Widelitz, R.B.1    Magun, B.E.2    Gerner, E.W.3
  • 220
    • 0027065101 scopus 로고
    • Role of membrane components in thermal injury of cells and development of thermotolerance
    • 219. Jozwiak Z, Leyko W. 1992. Role of membrane components in thermal injury of cells and development of thermotolerance. Int. J. Radiat. Biol. 62:743-56
    • (1992) Int. J. Radiat. Biol. , vol.62 , pp. 743-756
    • Jozwiak, Z.1    Leyko, W.2
  • 221
    • 0001760629 scopus 로고
    • Autoregulation of the heat-shock response
    • ed. J Ilan, New York: Plenum
    • 220. Lindquist S. 1993. Autoregulation of the heat-shock response. In Translational Regulation of Gene Expression 2, ed. J Ilan, pp. 279-320. New York: Plenum
    • (1993) Translational Regulation of Gene Expression , vol.2 , pp. 279-320
    • Lindquist, S.1
  • 222
    • 0032212173 scopus 로고    scopus 로고
    • Hsp70 and larval thermotolerance in Drosophila melanogaster. How much is enough and when is more too much?
    • 221. Krebs RA, Feder ME. 1998. Hsp70 and larval thermotolerance in Drosophila melanogaster. How much is enough and when is more too much? J. Insect Physiol. 44:1091-1101
    • (1998) J. Insect Physiol. , vol.44 , pp. 1091-1101
    • Krebs, R.A.1    Feder, M.E.2
  • 223
    • 0030942057 scopus 로고    scopus 로고
    • Deleterious consequences of Hsp70 overexpression in Drosophila melanogaster larvae
    • 222. Krebs RA, Feder ME. 1997. Deleterious consequences of Hsp70 overexpression in Drosophila melanogaster larvae. Cell Stress Chaperones 2:60-71
    • (1997) Cell Stress Chaperones , vol.2 , pp. 60-71
    • Krebs, R.A.1    Feder, M.E.2
  • 224
    • 0030899725 scopus 로고    scopus 로고
    • Natural variation in the expression of the heat-shock protein Hsp70 in a population of Drosophila melanogaster, and its correlation with tolerance of ecologically relevant thermal stress
    • 223. Krebs RA, Feder ME. 1997. Natural variation in the expression of the heat-shock protein Hsp70 in a population of Drosophila melanogaster, and its correlation with tolerance of ecologically relevant thermal stress. Evolution 51: 173-79
    • (1997) Evolution , vol.51 , pp. 173-179
    • Krebs, R.A.1    Feder, M.E.2
  • 226
    • 0031862070 scopus 로고    scopus 로고
    • Experimental manipulation of the cost of thermal acclimation in Drosophila melanogaster
    • 225. Krebs RA, Feder ME. 1998. Experimental manipulation of the cost of thermal acclimation in Drosophila melanogaster. Biol. J. Linn. Soc. 63: 593-601
    • (1998) Biol. J. Linn. Soc. , vol.63 , pp. 593-601
    • Krebs, R.A.1    Feder, M.E.2
  • 227
    • 0029103632 scopus 로고
    • Acclimation: Increasing survival at a cost
    • 226. Hoffmann AA. 1995. Acclimation: increasing survival at a cost. Trends Ecol. Evol. 10:1-2
    • (1995) Trends Ecol. Evol. , vol.10 , pp. 1-2
    • Hoffmann, A.A.1
  • 228
    • 0025762410 scopus 로고
    • Physiological costs of combating chemical toxicants: Ecological implications
    • 227. Calow P. 1991. Physiological costs of combating chemical toxicants: ecological implications. Comp. Biochem. Physiol. 100C:3-6
    • (1991) Comp. Biochem. Physiol. , vol.100 C , pp. 3-6
    • Calow, P.1
  • 229
    • 0024939726 scopus 로고
    • Towards a physiological and genetical understanding of the energetics of the stress response
    • 228. Koehn RK, Bayne BL. 1989. Towards a physiological and genetical understanding of the energetics of the stress re-sponse. Biol. J. Linn. Soc. 37:157-71
    • (1989) Biol. J. Linn. Soc. , vol.37 , pp. 157-171
    • Koehn, R.K.1    Bayne, B.L.2
  • 230
    • 0023708177 scopus 로고
    • Reduction of endogenous GRP78 levels improves secretion of a heterologous protein in CHO cells
    • 229. Dorner AJ, Krane MG, Kaufman RJ. 1988. Reduction of endogenous GRP78 levels improves secretion of a heterologous protein in CHO cells. Mol. Cell Biol. 8:4063-70
    • (1988) Mol. Cell Biol. , vol.8 , pp. 4063-4070
    • Dorner, A.J.1    Krane, M.G.2    Kaufman, R.J.3
  • 231
    • 0026511824 scopus 로고
    • Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells
    • 230. Dorner AJ, Wasley LC, Kaufman RJ. 1992. Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells. EMBO J. 11:1563-71
    • (1992) EMBO J. , vol.11 , pp. 1563-1571
    • Dorner, A.J.1    Wasley, L.C.2    Kaufman, R.J.3
  • 232
    • 0028291264 scopus 로고
    • The levels of endoplasmic reticulum proteins and ATP affect folding and secretion of selective proteins
    • 231. Dorner AJ, Kaufman RJ. 1994. The levels of endoplasmic reticulum proteins and ATP affect folding and secretion of selective proteins. Biologicals 22:103-12
    • (1994) Biologicals , vol.22 , pp. 103-112
    • Dorner, A.J.1    Kaufman, R.J.2
  • 233
    • 0027076315 scopus 로고
    • Inhibitory effects of Hsp70 chaperones on nascent polypeptides
    • 232. Ryan C, Stevens TH, Schlesinger MJ. 1992. Inhibitory effects of HSP70 chaperones on nascent polypeptides. Protein Sci. 1:980-85
    • (1992) Protein Sci. , vol.1 , pp. 980-985
    • Ryan, C.1    Stevens, T.H.2    Schlesinger, M.J.3
  • 234
    • 0030044899 scopus 로고    scopus 로고
    • Nitrogen availability alters patterns of accumulation of heat stress-induced proteins in plants
    • 233. Heckathorn SA, Poeller GJ, Coleman JS, Hallberg RL. 1996. Nitrogen availability alters patterns of accumulation of heat stress-induced proteins in plants. Oecologia 105:413-18
    • (1996) Oecologia , vol.105 , pp. 413-418
    • Heckathorn, S.A.1    Poeller, G.J.2    Coleman, J.S.3    Hallberg, R.L.4
  • 235
    • 0030466221 scopus 로고    scopus 로고
    • Nitrogen availability and vegetative development influence the response of ribulose 1,5-bisphosphate carboxylase/oxygenase, phosphoenolpyruvate carboxylase, and heat-shock protein content to heat stress in Zea mays L
    • 234. Heckathorn SA, Poeller GJ, Coleman JS, Hallberg RL. 1996. Nitrogen availability and vegetative development influence the response of ribulose 1,5-bisphosphate carboxylase/oxygenase, phosphoenolpyruvate carboxylase, and heat-shock protein content to heat stress in Zea mays L. Int. J. Plant Sci. 157:588-95
    • (1996) Int. J. Plant Sci. , vol.157 , pp. 588-595
    • Heckathorn, S.A.1    Poeller, G.J.2    Coleman, J.S.3    Hallberg, R.L.4
  • 236
    • 0027143812 scopus 로고
    • Species-and tissue-specific synthesis patterns for heat-shock proteins hsp70 and hsp90 in several marine teleost fishes
    • 235. Dietz TJ, Somero GN. 1993. Species-and tissue-specific synthesis patterns for heat-shock proteins hsp70 and hsp90 in several marine teleost fishes. Physiol. Zool. 66:863-80
    • (1993) Physiol. Zool. , vol.66 , pp. 863-880
    • Dietz, T.J.1    Somero, G.N.2
  • 237
    • 0025935407 scopus 로고
    • Attenuation of the heat shock response in HeLa cells is mediated by the release of bound heat shock transcription factor and is modulated by changes in growth and in heat shock temperatures
    • 236. Abravaya K, Phillips B, Morimoto RI. 1991. Attenuation of the heat shock re-sponse 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. 5:2117-27
    • (1991) Genes Dev. , vol.5 , pp. 2117-2127
    • Abravaya, K.1    Phillips, B.2    Morimoto, R.I.3
  • 238
    • 0030794618 scopus 로고    scopus 로고
    • Regulation of hsp expression during rodent spermatogenesis
    • 237. Sarge KD, Cullen KE. 1997. Regulation of hsp expression during rodent spermatogenesis. Cell. Mol. Life Sci. 53:191-97
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 191-197
    • Sarge, K.D.1    Cullen, K.E.2
  • 239
    • 0000109355 scopus 로고
    • Induction of heat-shock protein synthesis in teleost hepatocytes: Effects of acclimation temperature
    • 238. Koban M, Graham G, Prosser CL. 1987. Induction of heat-shock protein synthesis in teleost hepatocytes: effects of acclimation temperature. Physiol. Zool. 60:290-96
    • (1987) Physiol. Zool. , vol.60 , pp. 290-296
    • Koban, M.1    Graham, G.2    Prosser, C.L.3
  • 240
    • 0013633519 scopus 로고    scopus 로고
    • Deleted in proof
    • 239. Deleted in proof
  • 241
    • 0030755096 scopus 로고    scopus 로고
    • Variation in hsp gene expression and Hsp polymorphism: Do they contribute to differential disease susceptibility and stress tolerance?
    • 240. Favatier F, Bornman L, Hightower LE, Gnther E, Polla BS. 1997. Variation in hsp gene expression and Hsp polymorphism: Do they contribute to differential disease susceptibility and stress tolerance? Cell Stress Chaperones 2: 141-55
    • (1997) Cell Stress Chaperones , vol.2 , pp. 141-155
    • Favatier, F.1    Bornman, L.2    Hightower, L.E.3    Gnther, E.4    Polla, B.S.5
  • 243
    • 0023088917 scopus 로고
    • Trypanosoma cruzi exhibits inter- and intra-strain heterogeneity in molecular karyotype and chromosomal gene location
    • 242. Engman DM, Reddy LV, Donelson JE, Kirchhoff LV. 1987. Trypanosoma cruzi exhibits inter-and intra-strain heterogeneity in molecular karyotype and chromosomal gene location. Mol. Biochem. Parasitol. 22:115-23
    • (1987) Mol. Biochem. Parasitol. , vol.22 , pp. 115-123
    • Engman, D.M.1    Reddy, L.V.2    Donelson, J.E.3    Kirchhoff, L.V.4
  • 244
    • 0021158416 scopus 로고
    • A high degree of DNA strain polymorphism associated with the major heat shock gene in Caenorhabditis elegans
    • 243. Snutch TP, Baillie DL. 1984. A high degree of DNA strain polymorphism associated with the major heat shock gene in Caenorhabditis elegans. Mol. Gen. Genet. 195:329-35
    • (1984) Mol. Gen. Genet. , vol.195 , pp. 329-335
    • Snutch, T.P.1    Baillie, D.L.2
  • 245
    • 0029845620 scopus 로고    scopus 로고
    • HSP27 locus cosegregates with left ventricular mass independently of blood pressure
    • 244. Hamet P, Kaiser MA, Sun Y, Page V, Vincent M, et al. 1996. HSP27 locus cosegregates with left ventricular mass independently of blood pressure. Hypertension 28:112-17
    • (1996) Hypertension , vol.28 , pp. 112-117
    • Hamet, P.1    Kaiser, M.A.2    Sun, Y.3    Page, V.4    Vincent, M.5
  • 246
    • 0026478607 scopus 로고
    • Evaluation of genetic divergence among Borrelia burgdorferi isolates by use of OspA, fla, HSP60, and HSP70 gene probes
    • 245. Wallich R, Helmes C, Schaible UE, Lobet Y, Moter SE, et al. 1992. Evaluation of genetic divergence among Borrelia burgdorferi isolates by use of OspA, fla, HSP60, and HSP70 gene probes. Infect. Immun. 60:4856-66
    • (1992) Infect. Immun. , vol.60 , pp. 4856-4866
    • Wallich, R.1    Helmes, C.2    Schaible, U.E.3    Lobet, Y.4    Moter, S.E.5
  • 247
    • 0026504306 scopus 로고
    • Restriction fragment length polymorphism of hsp70 gene, localized in the RT1 complex, is associated with hypertension in spontaneously hypertensive rats
    • 246. Hamet P, Kong D, Pravenec M, Kunes J, Kren V, et al. 1992. Restriction fragment length polymorphism of hsp70 gene, localized in the RT1 complex, is associated with hypertension in spontaneously hypertensive rats. Hypertension 19:611-14
    • (1992) Hypertension , vol.19 , pp. 611-614
    • Hamet, P.1    Kong, D.2    Pravenec, M.3    Kunes, J.4    Kren, V.5
  • 248
    • 17044460104 scopus 로고
    • An Alul polymorphism at the bovine 70 kD heat-shock protein-1 (HSP70-1) locus
    • 247. Grosz MD, Skow LC, Stone RT. 1994. An Alul polymorphism at the bovine 70 kD heat-shock protein-1 (HSP70-1) locus. Anim. Genet. 25:196
    • (1994) Anim. Genet. , vol.25 , pp. 196
    • Grosz, M.D.1    Skow, L.C.2    Stone, R.T.3
  • 249
    • 0003001261 scopus 로고
    • Genetic analysis of heat shock proteins in maize
    • 248. Jorgensen JA, Nguyen HT. 1995. Genetic analysis of heat shock proteins in maize. Theor. Appl. Genet. 91:38-46
    • (1995) Theor. Appl. Genet. , vol.91 , pp. 38-46
    • Jorgensen, J.A.1    Nguyen, H.T.2
  • 250
    • 0000620070 scopus 로고
    • Molecular markers, RFLPs and Hsps for the genetic dissection of thermotolerance in maize
    • 249. Ottaviano E, Sari Gorla M, Pe E, Frova C. 1991. Molecular markers, RFLPs and Hsps for the genetic dissection of thermotolerance in maize. Theor. Appl. Genet. 81:713-19
    • (1991) Theor. Appl. Genet. , vol.81 , pp. 713-719
    • Ottaviano, E.1    Sari Gorla, M.2    Pe, E.3    Frova, C.4
  • 251
    • 0028083591 scopus 로고
    • Analysis of heat shock response in perennial ryegrass using maize heat shock protein clones
    • 250. Dimascio JA, Sweeney PM, Danneberger TK, Kamalay JC. 1994. Analysis of heat shock response in perennial ryegrass using maize heat shock protein clones. Crop Sci. 34:798-804
    • (1994) Crop Sci. , vol.34 , pp. 798-804
    • Dimascio, J.A.1    Sweeney, P.M.2    Danneberger, T.K.3    Kamalay, J.C.4
  • 252
    • 0018896031 scopus 로고
    • Two genes for the major heat-shock protein of Drosophila melanogaster arranged as an inverted repeat
    • 251. Goldschmidt-Clermont M. 1980. Two genes for the major heat-shock protein of Drosophila melanogaster arranged as an inverted repeat. Nucleic Acids Res. 8:235-52
    • (1980) Nucleic Acids Res. , vol.8 , pp. 235-252
    • Goldschmidt-Clermont, M.1
  • 253
    • 0019209806 scopus 로고
    • Genomic organization of the 87A7 and 87C1 heat-induced loci of Drosophila melanogaster
    • 252. Ish-Horowicz D, Pinchin SM. 1980. Genomic organization of the 87A7 and 87C1 heat-induced loci of Drosophila melanogaster. J. Mol. Biol. 142:231-45
    • (1980) J. Mol. Biol. , vol.142 , pp. 231-245
    • Ish-Horowicz, D.1    Pinchin, S.M.2
  • 254
    • 0019405928 scopus 로고
    • Evolution of the 87A and 87C heat-shock loci in Drosophila
    • 253. Leigh-Brown AJ, Ish-Horowicz D. 1981. Evolution of the 87A and 87C heat-shock loci in Drosophila. Nature 290:677-82
    • (1981) Nature , vol.290 , pp. 677-682
    • Leigh-Brown, A.J.1    Ish-Horowicz, D.2
  • 255
    • 0032478209 scopus 로고    scopus 로고
    • Both allelic variation and expression of nuclear and cytoplasmic transcripts of hsr-omega are closely associated with thermal phenotype in Drosophila
    • 254. McKechnie SW, Haiford MM, McColl G, Hoffmann AA. 1998. Both allelic variation and expression of nuclear and cytoplasmic transcripts of hsr-omega are closely associated with thermal phenotype in Drosophila. Proc. Natl. Acad. Sci. USA 95:2423-28
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2423-2428
    • McKechnie, S.W.1    Haiford, M.M.2    McColl, G.3    Hoffmann, A.A.4
  • 256
    • 0018575254 scopus 로고
    • Genetic and molecular analysis of the 87A7 and 87C1 heat-inducible loci of D. melanogaster
    • 255. Ish-Horowicz D, Pinchin SM, Schedl P, Artavanis-Tsakonas S, Mirault ME. 1979. Genetic and molecular analysis of the 87A7 and 87C1 heat-inducible loci of D. melanogaster. Cell 18:1351-58
    • (1979) Cell , vol.18 , pp. 1351-1358
    • Ish-Horowicz, D.1    Pinchin, S.M.2    Schedl, P.3    Artavanis-Tsakonas, S.4    Mirault, M.E.5
  • 257
    • 0019841399 scopus 로고
    • Genomic organization and transcription of the alpha beta heat shock DNA in Drosophila melanogaster
    • 256. Lis JT, Ish-Horowicz D, Pinchin SM. 1981. Genomic organization and transcription of the alpha beta heat shock DNA in Drosophila melanogaster. Nucleic Acids Res. 9:5297-310
    • (1981) Nucleic Acids Res. , vol.9 , pp. 5297-5310
    • Lis, J.T.1    Ish-Horowicz, D.2    Pinchin, S.M.3
  • 258
    • 0017881144 scopus 로고
    • A novel arrangement of tandemly repeated genes at a major heat shock site in D. melanogaster
    • 257. Lis JT, Prestidge L, Hogness DS. 1978. A novel arrangement of tandemly repeated genes at a major heat shock site in D. melanogaster. Cell 14:901-19
    • (1978) Cell , vol.14 , pp. 901-919
    • Lis, J.T.1    Prestidge, L.2    Hogness, D.S.3
  • 260
    • 0018415097 scopus 로고
    • Sequence organization of two recombinant plasmids containing genes for the major heat shock-induced protein of D. melanogaster
    • 259. Craig EA, McCarthy BJ, Wadsworth SC. 1979. Sequence organization of two re-combinant plasmids containing genes for the major heat shock-induced protein of D. melanogaster. Cell 16:575-88
    • (1979) Cell , vol.16 , pp. 575-588
    • Craig, E.A.1    McCarthy, B.J.2    Wadsworth, S.C.3
  • 261
    • 0018366866 scopus 로고
    • Genes for the 70,000 dalton heat shock protein in two cloned D. melanogaster DNA. segments
    • 260. Artavanis-Tsakonas S, Schedl P, Mirault ME, Moran L, Lis J. 1979. Genes for the 70,000 dalton heat shock protein in two cloned D. melanogaster DNA. segments. Cell 17:9-18
    • (1979) Cell , vol.17 , pp. 9-18
    • Artavanis-Tsakonas, S.1    Schedl, P.2    Mirault, M.E.3    Moran, L.4    Lis, J.5
  • 262
    • 0018636327 scopus 로고
    • Studies of cloned sequences from four Drosophila heat shock loci
    • 261. Holmgren R, Livak K, Morimoto R, Freund R, Meselson M. 1979. Studies of cloned sequences from four Drosophila heat shock loci. Cell 18:1359-70
    • (1979) Cell , vol.18 , pp. 1359-1370
    • Holmgren, R.1    Livak, K.2    Morimoto, R.3    Freund, R.4    Meselson, M.5
  • 263
    • 0031193641 scopus 로고    scopus 로고
    • A model for the evolution of polyubiquitin genes from the study of Arabidopsis thaliana ecotypes
    • 262. Sun CW, Griffen S, Callis J. 1997. A model for the evolution of polyubiquitin genes from the study of Arabidopsis thaliana ecotypes. Plant Mol. Biol. 34:745-58
    • (1997) Plant Mol. Biol. , vol.34 , pp. 745-758
    • Sun, C.W.1    Griffen, S.2    Callis, J.3
  • 264
    • 0000884882 scopus 로고
    • Heat shock proteins in two lines of Zea mays L. that differ in drought and heat resistance
    • 263. Ristic Z, Gifford DJ, Cass DD. 1991. Heat shock proteins in two lines of Zea mays L. that differ in drought and heat resistance. Plant Physiol. 97:1430-34
    • (1991) Plant Physiol. , vol.97 , pp. 1430-1434
    • Ristic, Z.1    Gifford, D.J.2    Cass, D.D.3
  • 265
    • 0001513337 scopus 로고
    • Clonal variation in heat tolerance and heat shock protein expression in black spruce
    • 264. Colombo SJ, Colclough ML, Timmer VR, Blumwald E. 1992. Clonal variation in heat tolerance and heat shock protein expression in black spruce. Silvae Genet. 41:234-39
    • (1992) Silvae Genet. , vol.41 , pp. 234-239
    • Colombo, S.J.1    Colclough, M.L.2    Timmer, V.R.3    Blumwald, E.4
  • 266
    • 0002560971 scopus 로고
    • Heat shock protein expression in thermotolerant and thermosensitive lines of cotton
    • 265. Fender SE, O'Connell MA. 1989. Heat shock protein expression in thermotolerant and thermosensitive lines of cotton. Plant Cell Rep. 8:37-40
    • (1989) Plant Cell Rep. , vol.8 , pp. 37-40
    • Fender, S.E.1    O'Connell, M.A.2
  • 267
    • 0025033142 scopus 로고
    • Differences between Brahman and Holstein cows in heat-shock induced alterations of protein synthesis and secretion by oviducts and uterine endometrium
    • 266. Malayer JR, Hansen PJ. 1990. Differences between Brahman and Holstein cows in heat-shock induced alterations of protein synthesis and secretion by oviducts and uterine endometrium. J. Anim. Sci. 68:266-80
    • (1990) J. Anim. Sci. , vol.68 , pp. 266-280
    • Malayer, J.R.1    Hansen, P.J.2
  • 268
    • 0030916072 scopus 로고    scopus 로고
    • Genetic variation in the expression of the six hsp genes in the presence of heat shock in Drosophila melanogaster
    • 267. Otsuka Y, Takano TS, Yamazaki T. 1997. Genetic variation in the expression of the six hsp genes in the presence of heat shock in Drosophila melanogaster. Genes Genetic Syst. 72:19-24
    • (1997) Genes Genetic Syst. , vol.72 , pp. 19-24
    • Otsuka, Y.1    Takano, T.S.2    Yamazaki, T.3
  • 269
  • 270
    • 0001738055 scopus 로고
    • Quantitative expression of maize Hsps: Genetic dissection and association with thermotolerance
    • 269. Frova C, Gorla MS. 1993. Quantitative expression of maize Hsps: genetic dissection and association with thermotolerance. Theor. Appl. Genet. 86:213-20
    • (1993) Theor. Appl. Genet. , vol.86 , pp. 213-220
    • Frova, C.1    Gorla, M.S.2
  • 271
    • 0001466343 scopus 로고
    • Differences in the heat-shock response between thermotolerant and thermosusceptible cultivars of hexaploid wheat
    • 270. Weng J, Nguyen HT. 1992. Differences in the heat-shock response between thermotolerant and thermosusceptible cultivars of hexaploid wheat. Theor. Appl. Genet. 84:941-46
    • (1992) Theor. Appl. Genet. , vol.84 , pp. 941-946
    • Weng, J.1    Nguyen, H.T.2
  • 272
    • 0028910176 scopus 로고
    • Genetic and environmental regulation of HSP70 expression
    • 271. Brown DC, Bradley BP, Tedengren M. 1995. Genetic and environmental regulation of HSP70 expression. Mar. Env. Res. 39:181-84
    • (1995) Mar. Env. Res. , vol.39 , pp. 181-184
    • Brown, D.C.1    Bradley, B.P.2    Tedengren, M.3
  • 273
    • 0023403484 scopus 로고
    • Heat shock 70 gene is differentially expressed in Histoplasma capsulatum strains with different levels of thermotolerance and pathogenicity
    • 272. Caruso M, Sacco M, Medoff G, Maresca B. 1987. Heat shock 70 gene is differentially expressed in Histoplasma capsulatum strains with different levels of thermotolerance and pathogenicity. Mol. Microbiol. 1:151-58
    • (1987) Mol. Microbiol. , vol.1 , pp. 151-158
    • Caruso, M.1    Sacco, M.2    Medoff, G.3    Maresca, B.4
  • 275
    • 4244099738 scopus 로고    scopus 로고
    • Laboratory evolution of Hsp70 expression in Drosophila melanogaster. Functional consequences and molecular bases
    • Abstr.
    • 274. Bettencourt BR, Feder ME, Cavicchi S. 1997. Laboratory evolution of Hsp70 expression in Drosophila melanogaster. functional consequences and molecular bases. Am. Zool. 37:189A (Abstr.)
    • (1997) Am. Zool. , vol.37
    • Bettencourt, B.R.1    Feder, M.E.2    Cavicchi, S.3
  • 276
    • 0029848501 scopus 로고    scopus 로고
    • Response of two heat shock genes to selection for knockdown heat resistance in Drosophila melanogaster
    • 275. McColl G, Hoffmann AA, McKechnie SW. 1996. Response of two heat shock genes to selection for knockdown heat resistance in Drosophila melanogaster. Genetics 143:1615-27
    • (1996) Genetics , vol.143 , pp. 1615-1627
    • McColl, G.1    Hoffmann, A.A.2    McKechnie, S.W.3
  • 277
    • 0001419720 scopus 로고
    • Expression of the heat shock response in a tomato interspecific hybrid is not intermediate between the two parental responses
    • 276. Fender SE, O'Connell MA. 1990. Expression of the heat shock response in a tomato interspecific hybrid is not intermediate between the two parental re-sponses. Plant Physiol. 93:1140-46
    • (1990) Plant Physiol. , vol.93 , pp. 1140-1146
    • Fender, S.E.1    O'Connell, M.A.2
  • 278
    • 0031171733 scopus 로고    scopus 로고
    • Field release and environmental fate of a transgenic entomopathogenic nematode
    • 277. Gaugler R, Wilson M, Shearer P. 1997. Field release and environmental fate of a transgenic entomopathogenic nematode. Biol. Control 9:75-80
    • (1997) Biol. Control , vol.9 , pp. 75-80
    • Gaugler, R.1    Wilson, M.2    Shearer, P.3
  • 279
    • 0032526378 scopus 로고    scopus 로고
    • Thermal response of Heterorhabditis bacteriophora transformed with the Caenorhabditis elegans hsp70 encoding gene
    • 278. Hashmi S, Hashmi G, Glazer I, Gaugler R. 1998. Thermal response of Heterorhabditis bacteriophora transformed with the Caenorhabditis elegans hsp70 encoding gene. J. Exp. Zool. 281:164-70
    • (1998) J. Exp. Zool. , vol.281 , pp. 164-170
    • Hashmi, S.1    Hashmi, G.2    Glazer, I.3    Gaugler, R.4
  • 280
    • 0029920131 scopus 로고    scopus 로고
    • A review of acquired thermotolerance, heat-shock proteins, and molecular chaperones in Archaea
    • 279. Trent JD. 1996. A review of acquired thermotolerance, heat-shock proteins, and molecular chaperones in Archaea. FEMS Micro. Rev. 18:249-58
    • (1996) FEMS Micro. Rev. , vol.18 , pp. 249-258
    • Trent, J.D.1
  • 281
    • 0027223237 scopus 로고
    • Enhanced thermotolerance and temperature-induced changes in protein composition in the hyperthermophilic archaeon ES4
    • 280. Holden JF, Baross JA. 1993. Enhanced thermotolerance and temperature-induced changes in protein composition in the hyperthermophilic archaeon ES4. J. Bacteriol. 175:2839-43
    • (1993) J. Bacteriol. , vol.175 , pp. 2839-2843
    • Holden, J.F.1    Baross, J.A.2
  • 282
    • 0021871395 scopus 로고
    • Structure of genes and an insertion element in the methane producing archaebacterium Methanobrevibacter smithii
    • 281. Hamilton PT, Reeve JN. 1985. Structure of genes and an insertion element in the methane producing archaebacterium Methanobrevibacter smithii. Mol. Gen. Genet. 200:47-59
    • (1985) Mol. Gen. Genet. , vol.200 , pp. 47-59
    • Hamilton, P.T.1    Reeve, J.N.2
  • 283
    • 0028814839 scopus 로고
    • The thermosome of Thermoplasma acidophilum and its relationship to the eukaryotic chaperonin TRiC
    • 282. Waldmann T, Nimmesgern E, Nitsch M, Peters J, Pfeifer G, et al. 1995. The thermosome of Thermoplasma acidophilum and its relationship to the eukaryotic chaperonin TRiC. Eur. J. Biochem. 227: 848-56
    • (1995) Eur. J. Biochem. , vol.227 , pp. 848-856
    • Waldmann, T.1    Nimmesgern, E.2    Nitsch, M.3    Peters, J.4    Pfeifer, G.5
  • 284
    • 0027480771 scopus 로고
    • Structure of a molecular chaperone from a thermophilic archaebacterium
    • 283. Phipps BM, Typke D, Heger R, Volker S, Hoffmann A, et al. 1993. Structure of a molecular chaperone from a thermophilic archaebacterium. Nature 361:475-77
    • (1993) Nature , vol.361 , pp. 475-477
    • Phipps, B.M.1    Typke, D.2    Heger, R.3    Volker, S.4    Hoffmann, A.5
  • 285
    • 0031582064 scopus 로고    scopus 로고
    • The thermosome: Alternating alpha and beta-subunits within the chaperonin of the archaeon Thermoplasma acidophilum
    • 284. Nitsch M, Klumpp M, Lupas A, Baumeister W. 1997. The thermosome: alternating alpha and beta-subunits within the chaperonin of the archaeon Thermoplasma acidophilum. J. Mol. Biol. 267:142-49
    • (1997) J. Mol. Biol. , vol.267 , pp. 142-149
    • Nitsch, M.1    Klumpp, M.2    Lupas, A.3    Baumeister, W.4
  • 286
    • 0026683609 scopus 로고
    • T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol
    • 285. Lewis VA, Hynes GM, Zheng D, Saibil H, Willison K. 1992. T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol. Nature 358:249-52
    • (1992) Nature , vol.358 , pp. 249-252
    • Lewis, V.A.1    Hynes, G.M.2    Zheng, D.3    Saibil, H.4    Willison, K.5
  • 287
    • 0025748752 scopus 로고
    • A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
    • 286. Trent JD, Nimmesgern E, Wall JS, Hartl FU, Horwich AL. 1991. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature 354:490-93
    • (1991) Nature , vol.354 , pp. 490-493
    • Trent, J.D.1    Nimmesgern, E.2    Wall, J.S.3    Hartl, F.U.4    Horwich, A.L.5
  • 288
    • 0029566336 scopus 로고
    • The role of molecular chaperones in protein folding
    • 287. Hendrick JP, Hartl FU. 1995. The role of molecular chaperones in protein folding. FASEB J. 9:1559-69
    • (1995) FASEB J. , vol.9 , pp. 1559-1569
    • Hendrick, J.P.1    Hartl, F.U.2
  • 289
    • 0030928059 scopus 로고    scopus 로고
    • Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
    • 288. Eggers DK, Welch WJ, Hansen WJ. 1997. Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells. Mol. Biol. Cell 8:1559-73
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1559-1573
    • Eggers, D.K.1    Welch, W.J.2    Hansen, W.J.3
  • 290
    • 0029420098 scopus 로고
    • Molecular chaperones: Physical and mechanistic properties
    • 289. Burston SG, Clarke AR. 1995. Molecular chaperones: physical and mechanistic properties. Essays Biochem. 29:125-36
    • (1995) Essays Biochem. , vol.29 , pp. 125-136
    • Burston, S.G.1    Clarke, A.R.2
  • 292
    • 0025327188 scopus 로고
    • Heat shock response in mycoplasmas, genome-limited organisms
    • 291. Dascher CC, Poddar SK, Maniloff J. 1990. Heat shock response in mycoplasmas, genome-limited organisms. J. Bacteriol. 172:1823-27
    • (1990) J. Bacteriol. , vol.172 , pp. 1823-1827
    • Dascher, C.C.1    Poddar, S.K.2    Maniloff, J.3
  • 293
    • 0028674882 scopus 로고
    • Phylogenetic analysis of 70 kD heat shock protein sequences suggests a chimeric origin for the eukaryotic cell nucleus
    • 292. Gupta RS, Singh B. 1994. Phylogenetic analysis of 70 kD heat shock protein sequences suggests a chimeric origin for the eukaryotic cell nucleus. Curr. Biol. 4:1104-14
    • (1994) Curr. Biol. , vol.4 , pp. 1104-1114
    • Gupta, R.S.1    Singh, B.2
  • 294
    • 0030802669 scopus 로고    scopus 로고
    • The sequences of heat shock protein 40 (DnaJ) homologs provide evidence for a close evolutionary relationship between the Deinococcus thermus group and Cyanobacteria
    • 293. Bustard K, Gupta RS. 1997. The sequences of heat shock protein 40 (DnaJ) homologs provide evidence for a close evolutionary relationship between the Deinococcus thermus group and Cyanobacteria. J. Mol. Evol. 45:193-205
    • (1997) J. Mol. Evol. , vol.45 , pp. 193-205
    • Bustard, K.1    Gupta, R.S.2
  • 295
    • 0031022823 scopus 로고    scopus 로고
    • Sequencing of heat shock protein 70 (DnaK) homologs from Deinococcus proteolyticus and Thermomicrobium roseum and their integration in a protein-based phylogeny of prokaryotes
    • 294. Gupta RS, Bustard K, Falah M, Singh D. 1997. Sequencing of heat shock protein 70 (DnaK) homologs from Deinococcus proteolyticus and Thermomicrobium roseum and their integration in a protein-based phylogeny of prokaryotes. J. Bacteriol. 179:345-57
    • (1997) J. Bacteriol. , vol.179 , pp. 345-357
    • Gupta, R.S.1    Bustard, K.2    Falah, M.3    Singh, D.4
  • 296
    • 0028785298 scopus 로고
    • Phylogenetic analysis of the 90 kD heat shock family of protein sequences and an examination of the relationship among animals, plants, and fungi species
    • 295. Gupta RS. 1995. Phylogenetic analysis of the 90 kD heat shock family of protein sequences and an examination of the relationship among animals, plants, and fungi species. Mol. Biol. Evol. 12:1063-73
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 1063-1073
    • Gupta, R.S.1
  • 297
    • 0028344493 scopus 로고
    • Cloning of Giardia lamblia heat shock protein HSP70 homologs: Implications regarding origin of eukaryotic cells and of endoplasmic reticulum
    • 296. Gupta RS, Aitken K, Falah M, Singh B. 1994. Cloning of Giardia lamblia heat shock protein HSP70 homologs: implications regarding origin of eukaryotic cells and of endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 91:2895-99
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2895-2899
    • Gupta, R.S.1    Aitken, K.2    Falah, M.3    Singh, B.4
  • 298
    • 0026692645 scopus 로고
    • Cloning of the HSP70 gene from Halobacterium marismortui: Relatedness of archaebacterial HSP70 to its eubacterial homologs and a model for the evolution of the HSP70 gene
    • 297. Gupta RS, Singh B. 1992. Cloning of the HSP70 gene from Halobacterium marismortui: relatedness of archaebacterial HSP70 to its eubacterial homologs and a model for the evolution of the HSP70 gene. J. Bacteriol. 174:4594-605
    • (1992) J. Bacteriol. , vol.174 , pp. 4594-4605
    • Gupta, R.S.1    Singh, B.2
  • 300
    • 0027176067 scopus 로고
    • Genomic structure and sequence analysis of Drosophila melanogaster HSC70 genes
    • 299. Rubin DM, Mehta AD, Zhu J, Shoham S, Chen X, et al. 1993. Genomic structure and sequence analysis of Drosophila melanogaster HSC70 genes. Gene 128:155-63
    • (1993) Gene , vol.128 , pp. 155-163
    • Rubin, D.M.1    Mehta, A.D.2    Zhu, J.3    Shoham, S.4    Chen, X.5
  • 302
    • 0027472047 scopus 로고
    • Evolution of the alpha-crystallin/small heat-shock protein family
    • 301. de Jong WW, Leunissen JA, Voorter CE. 1993. Evolution of the alpha-crystallin/small heat-shock protein family. Mol. Biol. Evol. 10:103-26
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 103-126
    • De Jong, W.W.1    Leunissen, J.A.2    Voorter, C.E.3
  • 303
    • 0028034301 scopus 로고
    • Further examples of evolution by gene duplication revealed through DNA sequence comparisons
    • 302. Ohta T. 1994. Further examples of evolution by gene duplication revealed through DNA sequence comparisons. Genetics 138:1331-37
    • (1994) Genetics , vol.138 , pp. 1331-1337
    • Ohta, T.1
  • 304
    • 0027898418 scopus 로고
    • The Hsp70 heat-shock gene family of the mosquito Anopheles albimanus
    • 303. Benedict MQ, Cockburn AF, Seawright JA. 1993. The Hsp70 heat-shock gene family of the mosquito Anopheles albimanus. Insect Mol. Biol. 2:93-102
    • (1993) Insect Mol. Biol. , vol.2 , pp. 93-102
    • Benedict, M.Q.1    Cockburn, A.F.2    Seawright, J.A.3
  • 305
    • 0029740929 scopus 로고    scopus 로고
    • The heat shock genes in the Drosophila montium subgroup: Chromosomal localization and evolutionary implications
    • 304. Drosopoulou E, Konstantopoulou I, Scouras ZG. 1996. The heat shock genes in the Drosophila montium subgroup: chromosomal localization and evolutionary implications. Chromosoma 105:104-10
    • (1996) Chromosoma , vol.105 , pp. 104-110
    • Drosopoulou, E.1    Konstantopoulou, I.2    Scouras, Z.G.3
  • 306
    • 0030160337 scopus 로고    scopus 로고
    • The Afro-tropical Drosophila montium subgroup: Balbiani ring 1, polytene chromosomes, and heat shock response of Drosophila vulcana
    • 305. Pardali E, Feggou E, Drosopoulou E, Konstantopoulou I, Scouras ZG, Mavragani-Tsipidou P. 1996. The Afro-tropical Drosophila montium subgroup: Balbiani ring 1, polytene chromosomes, and heat shock response of Drosophila vulcana. Genome 39:588-97
    • (1996) Genome , vol.39 , pp. 588-597
    • Pardali, E.1    Feggou, E.2    Drosopoulou, E.3    Konstantopoulou, I.4    Scouras, Z.G.5    Mavragani-Tsipidou, P.6
  • 307
    • 0025193343 scopus 로고
    • HSP104 required for induced thermotolerance
    • 306. Sanchez Y, Lindquist SL. 1990. HSP104 required for induced thermotolerance. Science 248:1112-15
    • (1990) Science , vol.248 , pp. 1112-1115
    • Sanchez, Y.1    Lindquist, S.L.2
  • 308
    • 0000934632 scopus 로고
    • On the future of physiological ecology
    • 307. Feder ME, Block BA. 1991. On the future of physiological ecology. Funct. Ecol. 5:136-44
    • (1991) Funct. Ecol. , vol.5 , pp. 136-144
    • Feder, M.E.1    Block, B.A.2
  • 309
    • 0343144858 scopus 로고    scopus 로고
    • Simultaneous overexpression of two stress proteins in rat cardiomyocytes and myogenic cells confers protection against ischemia-induced injury
    • 308. Lau S, Patnaik N, Sayen MR, Mestril R. 1997. Simultaneous overexpression of two stress proteins in rat cardiomyocytes and myogenic cells confers protection against ischemia-induced injury. Circulation 96:2287-94
    • (1997) Circulation , vol.96 , pp. 2287-2294
    • Lau, S.1    Patnaik, N.2    Sayen, M.R.3    Mestril, R.4
  • 310
    • 0025988318 scopus 로고
    • Increased survival after treatments with anticancer agents of Chinese hamster cells expressing the human Mr 27,000 heat shock protein
    • 309. Huot J, Roy G, Lambert H, Chretien P, Landry J. 1991. Increased survival after treatments with anticancer agents of Chinese hamster cells expressing the human Mr 27,000 heat shock protein. Cancer Res. 51:5245-52
    • (1991) Cancer Res. , vol.51 , pp. 5245-5252
    • Huot, J.1    Roy, G.2    Lambert, H.3    Chretien, P.4    Landry, J.5
  • 311
    • 0028817419 scopus 로고
    • 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
    • 310. Mehlen P, Preville X, Chareyron P, Briolay J, Klemenz R, Arrigo AP. 1995. 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. 154:363-74
    • (1995) J. Immunol. , vol.154 , pp. 363-374
    • Mehlen, P.1    Preville, X.2    Chareyron, P.3    Briolay, J.4    Klemenz, R.5    Arrigo, A.P.6
  • 312
    • 0027469435 scopus 로고
    • Heat-shock proteins protect cells from monocyte cytotoxicity: Possible mechanism of self-protection
    • 311. Jaattela M, Wissing D. 1993. Heat-shock proteins protect cells from monocyte cytotoxicity: possible mechanism of self-protection. J. Exp. Med. 177:231-36
    • (1993) J. Exp. Med. , vol.177 , pp. 231-236
    • Jaattela, M.1    Wissing, D.2
  • 313
    • 0031148195 scopus 로고    scopus 로고
    • Overexpression of the small heat shock protein, hsp27, confers resistance to hyperthermia, but not to oxidative stress and UV-induced cell death, in a stably transfected squamous cell carcinoma cell line
    • 312. Trautinger F, Kokesch C, Herbacek I, Knobler RM, Kindas-Mugge I. 1997. Overexpression of the small heat shock protein, hsp27, confers resistance to hyperthermia, but not to oxidative stress and UV-induced cell death, in a stably transfected squamous cell carcinoma cell line. J. Photochem. Photobiol. 39B:90-95
    • (1997) J. Photochem. Photobiol. , vol.39 B , pp. 90-95
    • Trautinger, F.1    Kokesch, C.2    Herbacek, I.3    Knobler, R.M.4    Kindas-Mugge, I.5
  • 314
    • 0026691949 scopus 로고
    • Expression of Drosophila's 27 kDa heat shock protein into rodent cells confers thermal resistance
    • 313. Rollet E, Lavoie JN, Landry J, Tanguay RM. 1992. Expression of Drosophila's 27 kDa heat shock protein into rodent cells confers thermal resistance. Biochem. Biophys. Res. Commun. 185:116-20
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 116-120
    • Rollet, E.1    Lavoie, J.N.2    Landry, J.3    Tanguay, R.M.4
  • 315
    • 0027417852 scopus 로고
    • Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization
    • 314. Lavoie JN, Gingras-Breton G, Tanguay RM, Landry J. 1993. Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization. J. Biol. Chem. 268:3420-29
    • (1993) J. Biol. Chem. , vol.268 , pp. 3420-3429
    • Lavoie, J.N.1    Gingras-Breton, G.2    Tanguay, R.M.3    Landry, J.4
  • 316
    • 0024345716 scopus 로고
    • Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells
    • 315. Landry J, Chretien P, Lambert H, Hickey E, Weber LA. 1989. Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells. J. Cell Biol. 109:7-15
    • (1989) J. Cell Biol. , vol.109 , pp. 7-15
    • Landry, J.1    Chretien, P.2    Lambert, H.3    Hickey, E.4    Weber, L.A.5
  • 317
    • 0029986479 scopus 로고    scopus 로고
    • HSP27 and HSP70 increase the survival of WEHI-S cells exposed to hyperthermia
    • 316. Wissing D, Jaattela M. 1996. HSP27 and HSP70 increase the survival of WEHI-S cells exposed to hyperthermia. Int. J. Hypertherm. 12:125-38
    • (1996) Int. J. Hypertherm. , vol.12 , pp. 125-138
    • Wissing, D.1    Jaattela, M.2
  • 319
    • 0031469110 scopus 로고    scopus 로고
    • Small heat shock proteins and protection against ischemic injury in cardiac myocytes
    • 318. Martin JL, Mestril R, Hilal-Dandan R, Brunton LL, Dillmann WH. 1997. Small heat shock proteins and protection against ischemic injury in cardiac myocytes. Circulation 96:4343-48
    • (1997) Circulation , vol.96 , pp. 4343-4348
    • Martin, J.L.1    Mestril, R.2    Hilal-Dandan, R.3    Brunton, L.L.4    Dillmann, W.H.5
  • 320
    • 0028928550 scopus 로고
    • Heat-induced intranuclear protein aggregation and thermal radiosensitization
    • 319. Stege GJ, Kampinga HH, Konings AW. 1995. Heat-induced intranuclear protein aggregation and thermal radiosensitization. Int. J. Radiat. Biol. 67:203-9
    • (1995) Int. J. Radiat. Biol. , vol.67 , pp. 203-209
    • Stege, G.J.1    Kampinga, H.H.2    Konings, A.W.3
  • 321
    • 0030068206 scopus 로고    scopus 로고
    • Thermal response in murine L929 cells lacking alpha B-crystallin expression and alpha B-crystallin expressing L929 transfectants
    • 320. Blackburn R, Galoforo S, Berns CM, Ireland M, Cho JM, et al. 1996. Thermal response in murine L929 cells lacking alpha B-crystallin expression and alpha B-crystallin expressing L929 transfectants. Mol. Cell. Biochem. 155:51-60
    • (1996) Mol. Cell. Biochem. , vol.155 , pp. 51-60
    • Blackburn, R.1    Galoforo, S.2    Berns, C.M.3    Ireland, M.4    Cho, J.M.5
  • 323
    • 0029128478 scopus 로고
    • Differential cytoprotection against heat stress or hypoxia following expression of specific stress protein genes in myogenic cells
    • 322. Heads RJ, Yellon DM, Latchman DS. 1995. Differential cytoprotection against heat stress or hypoxia following expression of specific stress protein genes in myogenic cells. J. Mol. Cell. Cardiol. 27:1669-78
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , pp. 1669-1678
    • Heads, R.J.1    Yellon, D.M.2    Latchman, D.S.3
  • 324
    • 0030453530 scopus 로고    scopus 로고
    • Differential protection of primary rat cardiocytes by transfection of specific heat stress proteins
    • 323. Cumming DV, Heads RJ, Watson A, Latchman DS, Yellon DM. 1996. Differential protection of primary rat cardiocytes by transfection of specific heat stress proteins. J. Mol. Cell. Cardiol. 28:2343-49
    • (1996) J. Mol. Cell. Cardiol. , vol.28 , pp. 2343-2349
    • Cumming, D.V.1    Heads, R.J.2    Watson, A.3    Latchman, D.S.4    Yellon, D.M.5
  • 325
  • 326
    • 0027279121 scopus 로고
    • Tumor cells transfected with a bacterial heat-shock gene lose tumorigenicity and induce protection against tumors
    • 325. Lukacs KV, Lowrie DB, Stokes RW, Colston MJ. 1993. Tumor cells transfected with a bacterial heat-shock gene lose tumorigenicity and induce protection against tumors. J. Exp. Med. 178: 343-48
    • (1993) J. Exp. Med. , vol.178 , pp. 343-348
    • Lukacs, K.V.1    Lowrie, D.B.2    Stokes, R.W.3    Colston, M.J.4
  • 328
    • 0025821926 scopus 로고
    • Constitutive expression of heat-shock protein 70 in mammalian cells confers thermoresistance
    • 327. Angelidis CE, Lazaridis I, Pagoulatos GN. 1991. Constitutive expression of heat-shock protein 70 in mammalian cells confers thermoresistance. Eur. J. Biochem. 199:35-39
    • (1991) Eur. J. Biochem. , vol.199 , pp. 35-39
    • Angelidis, C.E.1    Lazaridis, I.2    Pagoulatos, G.N.3
  • 329
    • 0027973005 scopus 로고
    • Heat shock proteins hsp90 and hsp70 protect neuronal cells from thermal stress but not from programmed cell death
    • 328. Mailhos C, Howard MK, Latchman DS. 1994. Heat shock proteins hsp90 and hsp70 protect neuronal cells from thermal stress but not from programmed cell death. J. Neurochem. 63:1787-95
    • (1994) J. Neurochem. , vol.63 , pp. 1787-1795
    • Mailhos, C.1    Howard, M.K.2    Latchman, D.S.3
  • 330
    • 0030005617 scopus 로고    scopus 로고
    • Trigeminal ganglion neurons are protected by the heat shock proteins hsp70 and hsp90 from thermal stress but not from programmed cell death following nerve growth factor withdrawal
    • 329. Wyatt S, Mailhos C, Latchman DS. 1996. Trigeminal ganglion neurons are protected by the heat shock proteins hsp70 and hsp90 from thermal stress but not from programmed cell death following nerve growth factor withdrawal. Brain Res. Mol. Brain Res. 39:52-56
    • (1996) Brain Res. Mol. Brain Res. , vol.39 , pp. 52-56
    • Wyatt, S.1    Mailhos, C.2    Latchman, D.S.3
  • 331
    • 0028679510 scopus 로고
    • Transfection with hsp70i protects rat dorsal root ganglia neurones and glia from heat stress
    • 330. Uney JB, Staley K, Tyers P, Sofroniew MV, Kew JN. 1994. Transfection with hsp70i protects rat dorsal root ganglia neurones and glia from heat stress. Gene Ther. 1:S65
    • (1994) Gene Ther. , vol.1
    • Uney, J.B.1    Staley, K.2    Tyers, P.3    Sofroniew, M.V.4    Kew, J.N.5
  • 332
    • 0025787706 scopus 로고
    • Changes in Hsp70 alter thermotolerance and heat-shock regulation in Drosophila
    • 331. Solomon JM, Rossi JM, Golic K, McGarry T, Lindquist S. 1991. Changes in Hsp70 alter thermotolerance and heat-shock regulation in Drosophila. New Biol. 3:1106-20
    • (1991) New Biol. , vol.3 , pp. 1106-1120
    • Solomon, J.M.1    Rossi, J.M.2    Golic, K.3    McGarry, T.4    Lindquist, S.5
  • 333
    • 0030592803 scopus 로고    scopus 로고
    • HSP70 is essential to the neuroprotective effect of heat-shock
    • 332. Sato K, Saito H, Matsuki N. 1996. HSP70 is essential to the neuroprotective effect of heat-shock. Brain Res. 740:117-23
    • (1996) Brain Res. , vol.740 , pp. 117-123
    • Sato, K.1    Saito, H.2    Matsuki, N.3
  • 334
    • 0024293984 scopus 로고
    • Heat shock is lethal to fibroblasts microinjected with antibodies against hsp70
    • 333. Riabowol KT, Mizzen LA, Welch WJ. 1988. Heat shock is lethal to fibroblasts microinjected with antibodies against hsp70. Science 242:433-36
    • (1988) Science , vol.242 , pp. 433-436
    • Riabowol, K.T.1    Mizzen, L.A.2    Welch, W.J.3
  • 335
    • 0030465520 scopus 로고    scopus 로고
    • Adenovirus-mediated gene transfer of a heat shock protein 70 (hsp 70i) protects against simulated ischemia
    • 334. Mestril R, Giordano FJ, Conde AG, Dillmann WH. 1996. Adenovirus-mediated gene transfer of a heat shock protein 70 (hsp 70i) protects against simulated ischemia. J. Mol. Cell. Cardiol. 28:2351-58
    • (1996) J. Mol. Cell. Cardiol. , vol.28 , pp. 2351-2358
    • Mestril, R.1    Giordano, F.J.2    Conde, A.G.3    Dillmann, W.H.4
  • 336
    • 0026734257 scopus 로고
    • Expression of human hsp70 in rat fibroblasts enhances cell survival and facilitates recovery from translational and transcriptional inhibition following heat shock
    • 335. Liu RY, Li X, Li L, Li GC. 1992. Expression of human hsp70 in rat fibroblasts enhances cell survival and facilitates recovery from translational and transcriptional inhibition following heat shock. Cancer Res. 52:3667-73
    • (1992) Cancer Res. , vol.52 , pp. 3667-3673
    • Liu, R.Y.1    Li, X.2    Li, L.3    Li, G.C.4
  • 337
    • 0027213211 scopus 로고
    • Inhibition of ischaemic tolerance in the gerbil hippocampus by quercetin and anti-heat shock protein-70 antibody
    • 336. Nakata N, Kato H, Kogure K. 1993. Inhibition of ischaemic tolerance in the gerbil hippocampus by quercetin and anti-heat shock protein-70 antibody. NeuroReport 4:695-98
    • (1993) NeuroReport , vol.4 , pp. 695-698
    • Nakata, N.1    Kato, H.2    Kogure, K.3
  • 338
    • 0000463798 scopus 로고
    • Alteration of heat sensitivity by introduction of hsp70 or anti-hsp70 in CHO cells
    • 337. Lee YJ, Kim D, Hou ZZ, Curetty L, Borrelli MJ, Corry PM. 1993. Alteration of heat sensitivity by introduction of hsp70 or anti-hsp70 in CHO cells. J. Therm. Biol. 18:229-36
    • (1993) J. Therm. Biol. , vol.18 , pp. 229-236
    • Lee, Y.J.1    Kim, D.2    Hou, Z.Z.3    Curetty, L.4    Borrelli, M.J.5    Corry, P.M.6
  • 339
    • 0024290215 scopus 로고
    • Competitive inhibition of hsp70 gene expression causes thermosensitivity
    • 338. Johnston RN, Kucey BL. 1988. Competitive inhibition of hsp70 gene expression causes thermosensitivity. Science 242:1551-54
    • (1988) Science , vol.242 , pp. 1551-1554
    • Johnston, R.N.1    Kucey, B.L.2
  • 340
    • 0028238013 scopus 로고
    • Stable high level expression of a transfected human HSP70 gene protects a heart-derived muscle cell line against thermal stress
    • 339. Heads RJ, Latchman DS, Yellon DM. 1994. Stable high level expression of a transfected human HSP70 gene protects a heart-derived muscle cell line against thermal stress. J. Mol. Cell. Cardiol. 26:695-99
    • (1994) J. Mol. Cell. Cardiol. , vol.26 , pp. 695-699
    • Heads, R.J.1    Latchman, D.S.2    Yellon, D.M.3
  • 341
    • 0029962777 scopus 로고    scopus 로고
    • Over-expression of heat shock protein 70 protects neuronal cells against both thermal and ischaemic stress but with different efficiencies
    • 340. Amin V, Cumming DV, Latchman DS. 1996. Over-expression of heat shock protein 70 protects neuronal cells against both thermal and ischaemic stress but with different efficiencies. Neurosci. Lett. 206:45-48
    • (1996) Neurosci. Lett. , vol.206 , pp. 45-48
    • Amin, V.1    Cumming, D.V.2    Latchman, D.S.3
  • 342
    • 0024514829 scopus 로고
    • Heat shock stress is deleterious to CNS cultured neurons microinjected with anti-HSP70 antibodies
    • 341. Khan NA, Sotelo J. 1989. Heat shock stress is deleterious to CNS cultured neurons microinjected with anti-HSP70 antibodies. Biol. Cell 65:199-202
    • (1989) Biol. Cell , vol.65 , pp. 199-202
    • Khan, N.A.1    Sotelo, J.2
  • 343
    • 0026073457 scopus 로고
    • Thermal response of rat fibroblasts stably transfected with the human 70-kDa heat shock protein-encoding gene
    • 342. Li GC, Li LG, Liu YK, Mak JY, Chen LL, Lee WM. 1991. Thermal response of rat fibroblasts stably transfected with the human 70-kDa heat shock protein-encoding gene. Proc. Natl. Acad. Sci. USA 88:1681-85
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1681-1685
    • Li, G.C.1    Li, L.G.2    Liu, Y.K.3    Mak, J.Y.4    Chen, L.L.5    Lee, W.M.6
  • 344
    • 0027203476 scopus 로고
    • Human heat shock protein 70 (hsp70) protects murine cells from injury during metabolic stress
    • 343. Williams RS, Thomas JA, Fina M, German Z, Benjamin IJ. 1993. Human heat shock protein 70 (hsp70) protects murine cells from injury during metabolic stress. J. Clin. Invest. 92:503-8
    • (1993) J. Clin. Invest. , vol.92 , pp. 503-508
    • Williams, R.S.1    Thomas, J.A.2    Fina, M.3    German, Z.4    Benjamin, I.J.5
  • 345
    • 0028293462 scopus 로고
    • Expression of inducible stress protein 70 in rat heart myogenic cells confers protection against simulated ischemia-induced injury
    • 344. Mestril R, Chi SH, Sayen MR, O'Reilly K, Dillmann WH. 1994. Expression of inducible stress protein 70 in rat heart myogenic cells confers protection against simulated ischemia-induced injury. J. Clin. Invest. 93:759-67
    • (1994) J. Clin. Invest. , vol.93 , pp. 759-767
    • Mestril, R.1    Chi, S.H.2    Sayen, M.R.3    O'Reilly, K.4    Dillmann, W.H.5
  • 346
    • 0029620869 scopus 로고
    • Heat shock proteins in myocardial stress
    • 345. Dillmann WH, Mestril R. 1995. Heat shock proteins in myocardial stress. Z. Kardiol. 4:87-90
    • (1995) Z. Kardiol. , vol.4 , pp. 87-90
    • Dillmann, W.H.1    Mestril, R.2
  • 347
    • 0027202273 scopus 로고
    • The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by Hsp70
    • 346. Jacobs M, Andersen JB, Kontinen V, Sarvas M. 1993. The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by Hsp70. Mol. Cell Biol. 13:5427-38
    • (1993) Mol. Cell Biol. , vol.13 , pp. 5427-5438
    • Jacobs, M.1    Andersen, J.B.2    Kontinen, V.3    Sarvas, M.4
  • 348
    • 0031049718 scopus 로고    scopus 로고
    • Heat shock gene-expression in HSP-70 and HSF1 gene-transfected human epidermoid A-431 cells
    • 347. Ding XZ, Tsokos GC, Smallridge RC, Kiang JG. 1997. Heat shock gene-expression in HSP-70 and HSF1 gene-transfected human epidermoid A-431 cells. Mol. Cell. Biochem. 167:145-52
    • (1997) Mol. Cell. Biochem. , vol.167 , pp. 145-152
    • Ding, X.Z.1    Tsokos, G.C.2    Smallridge, R.C.3    Kiang, J.G.4
  • 349
    • 0029962998 scopus 로고    scopus 로고
    • Stable expression of a human HSP70 gene in a rat myogenic cell line confers protection against endotoxin
    • 348. Chi SH, Mestril R. 1996. Stable expression of a human HSP70 gene in a rat myogenic cell line confers protection against endotoxin. Am. J. Physiol. 270:C1017-21
    • (1996) Am. J. Physiol. , vol.270
    • Chi, S.H.1    Mestril, R.2
  • 350
    • 0030431691 scopus 로고    scopus 로고
    • Reduced protein denaturation in thermotolerant cells by elevated levels of HSP70
    • 349. Han MY, Park YM. 1997. Reduced protein denaturation in thermotolerant cells by elevated levels of HSP70. Korean J. Pharmacol. 32:433-44
    • (1997) Korean J. Pharmacol. , vol.32 , pp. 433-444
    • Han, M.Y.1    Park, Y.M.2
  • 351
    • 0028961801 scopus 로고
    • Over-expression of hsp70 confers tumorigenicity to mouse fibrosarcoma cells
    • 350. Jaattela M. 1995. Over-expression of hsp70 confers tumorigenicity to mouse fibrosarcoma cells. Int. J. Cancer 60: 689-93
    • (1995) Int. J. Cancer , vol.60 , pp. 689-693
    • Jaattela, M.1
  • 352
    • 0028919063 scopus 로고
    • Inhibition of proliferation and induction of apoptosis by abrogation of heat-shock protein (HSP) 70 expression in tumor cells
    • 351. Wei YQ, Zhao X, Kariya Y, Teshigawara K, Uchida A. 1995. Inhibition of proliferation and induction of apoptosis by abrogation of heat-shock protein (HSP) 70 expression in tumor cells. Cancer Immunol. Immunother. 40:73-78
    • (1995) Cancer Immunol. Immunother. , vol.40 , pp. 73-78
    • Wei, Y.Q.1    Zhao, X.2    Kariya, Y.3    Teshigawara, K.4    Uchida, A.5
  • 353
    • 0029919922 scopus 로고    scopus 로고
    • Hsp70 overexpression mediates the escape of a doxorubicin-induced G2 cell cycle arrest
    • 352. Karlseder J, Wissing D, Holzer G, Orel L, Sliutz G, et al. 1996. Hsp70 overexpression mediates the escape of a doxorubicin-induced G2 cell cycle arrest. Biochem. Biophys. Res. Commun. 220:153-59
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 153-159
    • Karlseder, J.1    Wissing, D.2    Holzer, G.3    Orel, L.4    Sliutz, G.5
  • 354
    • 0031555889 scopus 로고    scopus 로고
    • Protein glycosylation in a heat-resistant rat fibroblast cell model expressing human HSP70
    • 353. Henle KJ, Jethmalani SM, Li L, Li GC. 1997. Protein glycosylation in a heat-resistant rat fibroblast cell model expressing human HSP70. Biochem. Biophys. Res. Commun. 232:26-32
    • (1997) Biochem. Biophys. Res. Commun. , vol.232 , pp. 26-32
    • Henle, K.J.1    Jethmalani, S.M.2    Li, L.3    Li, G.C.4
  • 355
    • 0028919555 scopus 로고
    • Heat shock protein 70 overexpression affects the response to ultraviolet light in murine fibroblasts. Evidence for increased cell viability and suppression of cytokine release
    • 354. Simon MM, Reikerstorfer A, Schwarz A, Krone C, Luger TA, et al. 1995. Heat shock protein 70 overexpression affects the response to ultraviolet light in murine fibroblasts. Evidence for increased cell viability and suppression of cytokine release. J. Clin. Invest. 95:926-33
    • (1995) J. Clin. Invest. , vol.95 , pp. 926-933
    • Simon, M.M.1    Reikerstorfer, A.2    Schwarz, A.3    Krone, C.4    Luger, T.A.5
  • 356
    • 0031570448 scopus 로고    scopus 로고
    • Overexpression of the heat shock protein 70 enhances the TCR/CD3-and Fas/Apo-1/CD95-mediated apoptotic cell death in Jurkat T cells
    • 355. Liossis SN, Ding XZ, Kiang JG, Tsokos GC. 1997. Overexpression of the heat shock protein 70 enhances the TCR/CD3-and Fas/Apo-1/CD95-mediated apoptotic cell death in Jurkat T cells. J. Immunol. 158:5668-75
    • (1997) J. Immunol. , vol.158 , pp. 5668-5675
    • Liossis, S.N.1    Ding, X.Z.2    Kiang, J.G.3    Tsokos, G.C.4
  • 357
    • 0030739208 scopus 로고    scopus 로고
    • Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis
    • 356. Mosser DD, Caron AW, Bourget L, Denis-Larose C, Massie B. 1997. Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis. Mol. Cell. Biol. 17:5317-27
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5317-5327
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3    Denis-Larose, C.4    Massie, B.5
  • 358
    • 0030898927 scopus 로고    scopus 로고
    • In vivo gene transfection with heat shock protein 70 enhances myocardial tolerance to ischemia-reperfusion injury in rat
    • 357. Suzuki K, Sawa Y, Kaneda Y, Ichikawa H, Shirakura R, Matsuda H. 1997. In vivo gene transfection with heat shock protein 70 enhances myocardial tolerance to ischemia-reperfusion injury in rat. J. Clin. Invest. 99:1645-50
    • (1997) J. Clin. Invest. , vol.99 , pp. 1645-1650
    • Suzuki, K.1    Sawa, Y.2    Kaneda, Y.3    Ichikawa, H.4    Shirakura, R.5    Matsuda, H.6
  • 359
    • 0028905823 scopus 로고
    • Transgenic mice expressing the human heat shock protein 70 have improved post-ischemic myocardial recovery
    • 358. Plumier JC, Ross BM, Currie RW, Angelidis CE, Kazlaris H, et al. 1995. Transgenic mice expressing the human heat shock protein 70 have improved post-ischemic myocardial recovery. J. Clin. Invest. 95:1854-60
    • (1995) J. Clin. Invest. , vol.95 , pp. 1854-1860
    • Plumier, J.C.1    Ross, B.M.2    Currie, R.W.3    Angelidis, C.E.4    Kazlaris, H.5
  • 360
    • 0028932259 scopus 로고
    • Overexpression of the rat inducible 70-kD heat stress protein in a transgenic mouse increases the resistance of the heart to ischemic injury
    • 359. Marber MS, Mestril R, Chi SH, Sayen MR, Yellon DM, Dillmann WH. 1995. Overexpression of the rat inducible 70-kD heat stress protein in a transgenic mouse increases the resistance of the heart to ischemic injury. J. Clin. Invest. 95:1446-56
    • (1995) J. Clin. Invest. , vol.95 , pp. 1446-1456
    • Marber, M.S.1    Mestril, R.2    Chi, S.H.3    Sayen, M.R.4    Yellon, D.M.5    Dillmann, W.H.6
  • 362
    • 0029964973 scopus 로고    scopus 로고
    • An Hsp70 antisense gene affects the expression of HSP70/HSC70, the regulation of HSF, and the acquisition of thermotolerance in transgenic Arabidopsis thaliana
    • 361. Lee JH, Schoffl F. 1996. An Hsp70 antisense gene affects the expression of HSP70/HSC70, the regulation of HSF, and the acquisition of thermotolerance in transgenic Arabidopsis thaliana. Mol. Gen. Genet. 252:11-19
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 11-19
    • Lee, J.H.1    Schoffl, F.2
  • 363
    • 0030293446 scopus 로고    scopus 로고
    • Increased heat shock protein 90 (hsp90) expression leads to increased apoptosis in the monoblastoid cell line U937 following induction with TNF-alpha and cycloheximide: A possible role in immunopathology
    • 362. Galea-Lauri J, Richardson AJ, Latchman DS, Katz DR. 1996. Increased heat shock protein 90 (hsp90) expression leads to increased apoptosis in the monoblastoid cell line U937 following induction with TNF-alpha and cycloheximide: a possible role in immunopathology. J. Immunol. 157:4109-18
    • (1996) J. Immunol. , vol.157 , pp. 4109-4118
    • Galea-Lauri, J.1    Richardson, A.J.2    Latchman, D.S.3    Katz, D.R.4
  • 364
    • 0030893652 scopus 로고    scopus 로고
    • Blocking the endogenous increase in HSP 72 increases susceptibility to hypoxia and reoxygenation in isolated adult feline cardiocytes
    • 363. Nakano M, Mann DL, Knowlton AA. 1997. Blocking the endogenous increase in HSP 72 increases susceptibility to hypoxia and reoxygenation in isolated adult feline cardiocytes. Circulation 95:1523-31
    • (1997) Circulation , vol.95 , pp. 1523-1531
    • Nakano, M.1    Mann, D.L.2    Knowlton, A.A.3
  • 365
    • 0029794271 scopus 로고    scopus 로고
    • Overexpression of heat shock protein 72 in transgenic mice decreases infarct size in vivo
    • 364. Hutter JJ, Mestril R, Tam EK, Sievers RE, Dillmann WH, Wolfe CL. 1996. Overexpression of heat shock protein 72 in transgenic mice decreases infarct size in vivo. Circulation 94:1408-11
    • (1996) Circulation , vol.94 , pp. 1408-1411
    • Hutter, J.J.1    Mestril, R.2    Tam, E.K.3    Sievers, R.E.4    Dillmann, W.H.5    Wolfe, C.L.6
  • 366
    • 0030218025 scopus 로고    scopus 로고
    • The role of the 90-kDa heat shock protein in cell cycle control and differentiation of the monoblastoid cell line U937
    • 365. Galea-Lauri J, Latchman DS, Katz DR. 1996. The role of the 90-kDa heat shock protein in cell cycle control and differentiation of the monoblastoid cell line U937. Exp. Cell Res. 226:243-54
    • (1996) Exp. Cell Res. , vol.226 , pp. 243-254
    • Galea-Lauri, J.1    Latchman, D.S.2    Katz, D.R.3
  • 367
    • 0028675582 scopus 로고
    • An Arabidopsis heat shock protein complements a thermotolerance defect in yeast
    • 366. Schirmer EC, Lindquist S, Vierling E. 1994. An Arabidopsis heat shock protein complements a thermotolerance defect in yeast. Plant Cell 6:1899-909
    • (1994) Plant Cell , vol.6 , pp. 1899-1909
    • Schirmer, E.C.1    Lindquist, S.2    Vierling, E.3
  • 368
    • 17144468807 scopus 로고    scopus 로고
    • Consequences of exposure to extreme conditions in somatic cells of Drosophila melanogaster under conditions of disturbed synthesis of heat shock proteins
    • 367. Kutskova IUA, Mamon LA. 1996. Consequences of exposure to extreme conditions in somatic cells of Drosophila melanogaster under conditions of disturbed synthesis of heat shock proteins. Genetika 32:1406-16
    • (1996) Genetika , vol.32 , pp. 1406-1416
    • Kutskova, I.U.A.1    Mamon, L.A.2
  • 369
    • 0027255263 scopus 로고
    • The role of the heat-shock proteins in recovery of high temperature induced damages of mitotic chromosomes in Drosophila melanogaster
    • 368. Mamon LA, Kutskova YA. 1993. The role of the heat-shock proteins in recovery of high temperature induced damages of mitotic chromosomes in Drosophila melanogaster. Genetika 29:604-12
    • (1993) Genetika , vol.29 , pp. 604-612
    • Mamon, L.A.1    Kutskova, Y.A.2
  • 370
    • 0027337510 scopus 로고
    • The role of the heat-shock proteins in recovery of cell proliferation following high temperature treatment of Drosophila melanogaster
    • 369. Mamon LA, Kutskova YA. 1993. The role of the heat-shock proteins in recovery of cell proliferation following high temperature treatment of Drosophila melanogaster. Genetika 29:791-98
    • (1993) Genetika , vol.29 , pp. 791-798
    • Mamon, L.A.1    Kutskova, Y.A.2
  • 371
    • 0027054004 scopus 로고
    • Quercetin, an inhibitor of heat shock protein synthesis, inhibits the acquisition of thermotolerance in a human colon carcinoma cell line
    • 370. Koishi M, Hosokawa N, Sato M, Nakai A, Hirayoshi K, et al. 1992. Quercetin, an inhibitor of heat shock protein synthesis, inhibits the acquisition of thermotolerance in a human colon carcinoma cell line. Jpn. J. Cancer Res. 83:1216-22
    • (1992) Jpn. J. Cancer Res. , vol.83 , pp. 1216-1222
    • Koishi, M.1    Hosokawa, N.2    Sato, M.3    Nakai, A.4    Hirayoshi, K.5
  • 372
    • 0027129805 scopus 로고
    • Effect of pH on quercetin-induced suppression of heat shock gene expression and thermotolerance development in HT-29 cells
    • 371. Lee YJ, Curetty L, Hou ZZ, Kim SH, Kim JH, Corry PM. 1992. Effect of pH on quercetin-induced suppression of heat shock gene expression and thermotolerance development in HT-29 cells. Biochem. Biophys. Res. Commun. 186:1121-28
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 1121-1128
    • Lee, Y.J.1    Curetty, L.2    Hou, Z.Z.3    Kim, S.H.4    Kim, J.H.5    Corry, P.M.6
  • 373
    • 0030985251 scopus 로고    scopus 로고
    • Multiple functions of Drosophila heat shock transcription factor in vivo
    • 372. Jedlicka P, Mortin MA, Wu C. 1997. Multiple functions of Drosophila heat shock transcription factor in vivo. EMBO J. 16:2452-62
    • (1997) EMBO J. , vol.16 , pp. 2452-2462
    • Jedlicka, P.1    Mortin, M.A.2    Wu, C.3
  • 374
    • 0029379547 scopus 로고
    • Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis
    • 373. Lee JH, Hubel A, Schoffl F. 1995. Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis. Plant J. 8:603-12
    • (1995) Plant J. , vol.8 , pp. 603-612
    • Lee, J.H.1    Hubel, A.2    Schoffl, F.3


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