메뉴 건너뛰기




Volumn 206, Issue , 2010, Pages 1-27

Physiological adaptations of stressed fish to polluted environments: Role of heat shock proteins

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN;

EID: 77956088193     PISSN: 01795953     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-6260-7_1     Document Type: Article
Times cited : (31)

References (199)
  • 1
    • 4644242217 scopus 로고    scopus 로고
    • Formation of reactive species and induction of antioxidant defense systems in polar and temperate marine invertebrates and fish
    • Abele D, Puntarulo S (2004) Formation of reactive species and induction of antioxidant defense systems in polar and temperate marine invertebrates and fish. Comp Biochem Physiol B 138:405-415
    • (2004) Comp Biochem Physiol B , vol.138 , pp. 405-415
    • Abele, D.1    Puntarulo, S.2
  • 3
    • 0034283359 scopus 로고    scopus 로고
    • Induction of hepatic antioxidants in freshwater catfish (Channa punctatus Bloch.) is a biomarker of paper mill effluent exposure
    • Ahmad I, Hamid T, Fatima M, Chand HS, Jain SK, Athar M, Raisuddin S (2000) Induction of hepatic antioxidants in freshwater catfish (Channa punctatus Bloch.) is a biomarker of paper mill effluent exposure. Biochim Biophys Acta 1523:37-48
    • (2000) Biochim Biophys Acta , vol.1523 , pp. 37-48
    • Ahmad, I.1    Hamid, T.2    Fatima, M.3    Chand, H.S.4    Jain, S.K.5    Athar, M.6    Raisuddin, S.7
  • 4
    • 0032168649 scopus 로고    scopus 로고
    • Effects of heat shock and hypoxia on protein synthesis in rainbow trout (Oncorhynchus mykiss) cells
    • Airaksinen S, Rabergh CM, Sistonen L, Nikinmaa M (1998) Effects of heat shock and hypoxia on protein synthesis in rainbow trout (Oncorhynchus mykiss) cells. J Exp Biol 201: 2543-2551
    • (1998) J Exp Biol , vol.201 , pp. 2543-2551
    • Airaksinen, S.1    Rabergh, C.M.2    Sistonen, L.3    Nikinmaa, M.4
  • 6
    • 0033863883 scopus 로고    scopus 로고
    • The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome
    • An WG, Schulte TW, Neckers LM (2000) The heat shock protein 90 antagonist geldanamycin alters chaperone association with p210bcr-abl and v-src proteins before their degradation by the proteasome. Cell Growth Differ 11:355-360
    • (2000) Cell Growth Differ , vol.11 , pp. 355-360
    • An, W.G.1    Schulte, T.W.2    Neckers, L.M.3
  • 7
    • 0029047994 scopus 로고
    • Cloning and characterization of cDNAs for 70-kDa heat-shock proteins (Hsp70) from two fish species of the genus Oryzias
    • Arai A, Naruse K, Mitani H, Shima A (1995) Cloning and characterization of cDNAs for 70-kDa heat-shock proteins (Hsp70) from two fish species of the genus Oryzias. Jpn J Genet 70: 423-433
    • (1995) Jpn J Genet , vol.70 , pp. 423-433
    • Arai, A.1    Naruse, K.2    Mitani, H.3    Shima, A.4
  • 8
    • 0036186869 scopus 로고    scopus 로고
    • HSP27: Novel regulator of intracellular redox state
    • Arrigo AP (2001) HSP27: novel regulator of intracellular redox state. IUBMB Life 52:303-307
    • (2001) IUBMB Life , vol.52 , pp. 303-307
    • Arrigo, A.P.1
  • 9
    • 0033972463 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial DNA is inversely related to maximum life span in the heart and brain of mammals
    • Barja G, Herrero A (2000) Oxidative damage to mitochondrial DNA is inversely related to maximum life span in the heart and brain of mammals. FASEB J 14:312-318
    • (2000) FASEB J , vol.14 , pp. 312-318
    • Barja, G.1    Herrero, A.2
  • 10
    • 0036625843 scopus 로고    scopus 로고
    • Stress in fishes: A diversity of responses with particular reference to changes in circulating corticosteroids
    • Barton BA (2002) Stress in fishes: a diversity of responses with particular reference to changes in circulating corticosteroids. Integr Comp Biol 42:517-525
    • (2002) Integr Comp Biol , vol.42 , pp. 517-525
    • Barton, B.A.1
  • 11
    • 0038647034 scopus 로고    scopus 로고
    • Physiological and condition-related indicators of environmental stress in fish
    • Adams SM (ed). American Fisheries Society, Bethesda, MD
    • Barton BA, Morgan JD, Vijayan MM (2002) Physiological and condition-related indicators of environmental stress in fish. In: Adams SM (ed) Biological indicators of aquatic ecosystem stress. American Fisheries Society, Bethesda, MD, pp 111-148
    • (2002) Biological Indicators of Aquatic Ecosystem Stress , pp. 111-148
    • Barton, B.A.1    Morgan, J.D.2    Vijayan, M.M.3
  • 12
    • 0037131187 scopus 로고    scopus 로고
    • Akt forms an intracellular complex with heat shock protein 90 (HSP90) and Cdc37 and is destabilized by inhibitors of HSP90 function
    • Basso AD, Solit DB, Chiosis G, Giri B, Tsichlis P, Rosen N (2002) Akt forms an intracellular complex with heat shock protein 90 (HSP90) and Cdc37 and is destabilized by inhibitors of HSP90 function. J Biol Chem 277:39858-39866
    • (2002) J Biol Chem , vol.277 , pp. 39858-39866
    • Basso, A.D.1    Solit, D.B.2    Chiosis, G.3    Giri, B.4    Tsichlis, P.5    Rosen, N.6
  • 13
    • 0034753513 scopus 로고    scopus 로고
    • The effects of cortisol on heat shock protein 70 levels in two fish species
    • Basu N, Nakano T, Grau EG, Iwama GK (2001) The effects of cortisol on heat shock protein 70 levels in two fish species. Gen Comp Endocrinol 124:97-105
    • (2001) Gen Comp Endocrinol , vol.124 , pp. 97-105
    • Basu, N.1    Nakano, T.2    Grau, E.G.3    Iwama, G.K.4
  • 15
    • 3242879188 scopus 로고    scopus 로고
    • 'The stress of dying': The role of heat shock proteins in the regulation of apoptosis
    • Beere HM (2004) 'The stress of dying': the role of heat shock proteins in the regulation of apoptosis. J Cell Sci 117:2641-2651
    • (2004) J Cell Sci , vol.117 , pp. 2641-2651
    • Beere, H.M.1
  • 17
    • 0032572603 scopus 로고    scopus 로고
    • Stress (heat shock) proteins: Molecular chaperones in cardiovascular biology and disease
    • Benjamin IJ, McMillan DR (1998) Stress (heat shock) proteins: molecular chaperones in cardiovascular biology and disease. Circ Res 83:117-132
    • (1998) Circ Res , vol.83 , pp. 117-132
    • Benjamin, I.J.1    McMillan, D.R.2
  • 18
    • 85047695528 scopus 로고    scopus 로고
    • HSP90 associated oncoproteins: Multiple targets of geldanamycin and its analogs
    • Blagosklonny MV (2002) HSP90 associated oncoproteins: multiple targets of geldanamycin and its analogs. Leukemia 16:455-462
    • (2002) Leukemia , vol.16 , pp. 455-462
    • Blagosklonny, M.V.1
  • 19
    • 0026591027 scopus 로고
    • Thermoprotection of a functional epithelium: Heat stress effects on transepithelial transport by flounder renal tubule in primary monolayer culture
    • Brown MA, Upender RP, Hightower LE, Renfro JL (1992) Thermoprotection of a functional epithelium: heat stress effects on transepithelial transport by flounder renal tubule in primary monolayer culture. Proc Natl Acad Sci USA 89:3246-3250
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3246-3250
    • Brown, M.A.1    Upender, R.P.2    Hightower, L.E.3    Renfro, J.L.4
  • 21
    • 0032924953 scopus 로고    scopus 로고
    • HSP90 and co - A holding for folding
    • Buchner J (1999) HSP90 and co - a holding for folding. Trends Biochem Sci 24:136-141
    • (1999) Trends Biochem Sci , vol.24 , pp. 136-141
    • Buchner, J.1
  • 22
    • 8444247983 scopus 로고    scopus 로고
    • Regulation of heat shock genes in isolated hepatocytes from an Antarctic fish, Trematomus bernacchii
    • Buckley BA, Place SP, Hofmann GE (2004) Regulation of heat shock genes in isolated hepatocytes from an Antarctic fish, Trematomus bernacchii. J Exp Biol 207:3649-3656
    • (2004) J Exp Biol , vol.207 , pp. 3649-3656
    • Buckley, B.A.1    Place, S.P.2    Hofmann, G.E.3
  • 23
    • 34047094983 scopus 로고    scopus 로고
    • Changes in oxidative stress parameters in fish as response to direct uranium exposure
    • Buet A, Barilloet S, Camilleri V (2002) Changes in oxidative stress parameters in fish as response to direct uranium exposure. Radioprot Suppl 40:S151-S155
    • (2002) Radioprot Suppl , vol.40
    • Buet, A.1    Barilloet, S.2    Camilleri, V.3
  • 24
    • 0033809220 scopus 로고    scopus 로고
    • Free radicals, oxidants and antioxidants
    • Buettner GR, Schafer FQ (2000) Free radicals, oxidants and antioxidants. Teratol 62:234
    • (2000) Teratol , vol.62 , pp. 234
    • Buettner, G.R.1    Schafer, F.Q.2
  • 25
    • 0032489016 scopus 로고    scopus 로고
    • The HSP70 and HSP60 chaperone machines
    • Bukau B, Horwich AL (1998) The HSP70 and HSP60 chaperone machines. Cell 92:351-366
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 26
    • 0036212575 scopus 로고    scopus 로고
    • Regional distribution of heme oxygenase, HSP70, and glutathione in brain: Relevance for endogenous oxidant/antioxidant balance and stress tolerance
    • Calabrese V, Scapagnini G, Ravagna A, Fariello RG, Giuffrida Stella AM, Abraham NG (2002) Regional distribution of heme oxygenase, HSP70, and glutathione in brain: relevance for endogenous oxidant/antioxidant balance and stress tolerance. J Neurosci Res 68: 65-75
    • (2002) J Neurosci Res , vol.68 , pp. 65-75
    • Calabrese, V.1    Scapagnini, G.2    Ravagna, A.3    Fariello, R.G.4    Giuffrida Stella, A.M.5    Abraham, N.G.6
  • 27
    • 77956074077 scopus 로고    scopus 로고
    • A review and synthesis of Australian Fisheries Habitat Research: Major threats, issues and gaps in knowledge of coastal and marine fisheries habitats
    • Cappo M, Alongi DM,Williams D, Duke N (1998) A review and synthesis of Australian Fisheries Habitat Research: major threats, issues and gaps in knowledge of coastal and marine fisheries habitats. Fish Res Dev Corp. pp. 53
    • (1998) Fish Res Dev Corp , pp. 53
    • Cappo, M.1    Alongi, D.M.2    Williams, D.3    Duke, N.4
  • 28
    • 27844464029 scopus 로고    scopus 로고
    • Food-deprivation induces HSP70 and HSP90 protein expression in larval gilthead sea bream and rainbow trout
    • Cara JB, Aluru N, Moyano FJ, Vijayan MM (2005) Food-deprivation induces HSP70 and HSP90 protein expression in larval gilthead sea bream and rainbow trout. Comp Biochem Physiol B 142:426-431
    • (2005) Comp Biochem Physiol B , vol.142 , pp. 426-431
    • Cara, J.B.1    Aluru, N.2    Moyano, F.J.3    Vijayan, M.M.4
  • 29
    • 0034065975 scopus 로고    scopus 로고
    • Expression of 70 kDa heat shock proteins in Antarctic and New Zealand notothenioid fish
    • Carpenter CM, Hofmann GE (2000) Expression of 70 kDa heat shock proteins in Antarctic and New Zealand notothenioid fish. Comp Biochem Physiol A Physiol 125:229-238
    • (2000) Comp Biochem Physiol A Physiol , vol.125 , pp. 229-238
    • Carpenter, C.M.1    Hofmann, G.E.2
  • 31
    • 0032585144 scopus 로고    scopus 로고
    • Seasonal changes in stress-70 protein levels reflect thermal tolerance in the marine bivalve Mytilus edulis L
    • Chapple JP, Smerdon GR, Berry RJ, Hawkins AJS (1998) Seasonal changes in stress-70 protein levels reflect thermal tolerance in the marine bivalve Mytilus edulis L. J Exp Mar Biol Ecol 229:53-68
    • (1998) J Exp Mar Biol Ecol , vol.229 , pp. 53-68
    • Chapple, J.P.1    Smerdon, G.R.2    Berry, R.J.3    Hawkins, A.J.S.4
  • 34
    • 33748708261 scopus 로고    scopus 로고
    • Heat shock protein 70 gene expression in four hatchery Pacific Abalone Haliotis discus hannai Ino populations using for marker-assisted selection
    • Cheng P, Liu X, Zhang G, Deng Y (2006) Heat shock protein 70 gene expression in four hatchery Pacific Abalone Haliotis discus hannai Ino populations using for marker-assisted selection. Aquaculture Res 37:1290-1296
    • (2006) Aquaculture Res , vol.37 , pp. 1290-1296
    • Cheng, P.1    Liu, X.2    Zhang, G.3    Deng, Y.4
  • 35
    • 0034629290 scopus 로고    scopus 로고
    • Disruption of Raf-1/heat shock protein 90 complex and Raf signaling by dexamethasone in mast cells
    • Cissel DS, Beaven MA (2000) Disruption of Raf-1/heat shock protein 90 complex and Raf signaling by dexamethasone in mast cells. J Biol Chem 275:7066-7070
    • (2000) J Biol Chem , vol.275 , pp. 7066-7070
    • Cissel, D.S.1    Beaven, M.A.2
  • 36
    • 14644399198 scopus 로고    scopus 로고
    • Exhaustive exercise and the cellular stress response in rainbow trout, Oncorhynchus mykiss
    • Clarkson K, Kieffer JD, Currie S (2005) Exhaustive exercise and the cellular stress response in rainbow trout, Oncorhynchus mykiss. Comp Biochem Physiol A 140:225-232
    • (2005) Comp Biochem Physiol A , vol.140 , pp. 225-232
    • Clarkson, K.1    Kieffer, J.D.2    Currie, S.3
  • 37
    • 0031280403 scopus 로고    scopus 로고
    • Glutathione reductase, selenium-dependent glutathione peroxidase, glutathione levels and lipid peroxidation in freshwater bivalves, Unio tumidus, as biomarkers of aquatic contamination in field studies
    • Cossu C, Doyotte A, Jacquin MC, Babut M, Exinger A, Vasseur P (1997) Glutathione reductase, selenium-dependent glutathione peroxidase, glutathione levels and lipid peroxidation in freshwater bivalves, Unio tumidus, as biomarkers of aquatic contamination in field studies. Ecotoxicol Environ Saf 38:122-131
    • (1997) Ecotoxicol Environ Saf , vol.38 , pp. 122-131
    • Cossu, C.1    Doyotte, A.2    Jacquin, M.C.3    Babut, M.4    Exinger, A.5    Vasseur, P.6
  • 38
    • 0033950088 scopus 로고    scopus 로고
    • Antioxidant biomarkers in freshwater bivalves, Unio tumidus, in response to different contamination profiles of aquatic sediments
    • Cossu C, Doyotte A, Babut M, Exinger A, Vasseur P (2000) Antioxidant biomarkers in freshwater bivalves, Unio tumidus, in response to different contamination profiles of aquatic sediments. Ecotoxicol Environ Saf 45:106-121
    • (2000) Ecotoxicol Environ Saf , vol.45 , pp. 106-121
    • Cossu, C.1    Doyotte, A.2    Babut, M.3    Exinger, A.4    Vasseur, P.5
  • 39
    • 3242743000 scopus 로고    scopus 로고
    • Strong links are important, but weak links stabilize them
    • Csermely P (2004) Strong links are important, but weak links stabilize them. Trends Biochem Sci 29:331-334
    • (2004) Trends Biochem Sci , vol.29 , pp. 331-334
    • Csermely, P.1
  • 40
    • 0031873752 scopus 로고    scopus 로고
    • The 90-kDa molecular chaperone family: Structure, function and clinical applications. A comprehensive review
    • Csermely P, Schnaider T, Soti C, Prohaszka Z, Nadai G (1998) The 90-kDa molecular chaperone family: structure, function and clinical applications. A comprehensive review. Pharmacol Ther 79:129-168
    • (1998) Pharmacol Ther , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohaszka, Z.4    Nadai, G.5
  • 41
    • 0030840317 scopus 로고    scopus 로고
    • Synthesis of stress protein 70 (HSP70) in rainbow trout (Oncorhynchus mykiss) of red blood cells
    • Currie S, Tufts BL (1997) Synthesis of stress protein 70 (HSP70) in rainbow trout (Oncorhynchus mykiss) of red blood cells. J Exp Biol 200:607-614
    • (1997) J Exp Biol , vol.200 , pp. 607-614
    • Currie, S.1    Tufts, B.L.2
  • 42
    • 0032951465 scopus 로고    scopus 로고
    • Influence of bioenergetic stress on heat shock protein gene expression in nucleated red blood cells of fish
    • Currie S, Tufts BL, Moyes CD (1999) Influence of bioenergetic stress on heat shock protein gene expression in nucleated red blood cells of fish. Am J Physiol Regul Integr Comp Physiol 276:R990-R996
    • (1999) Am J Physiol Regul Integr Comp Physiol , vol.276
    • Currie, S.1    Tufts, B.L.2    Moyes, C.D.3
  • 43
    • 0033845244 scopus 로고    scopus 로고
    • The effects of heat shock and acclimation temperature on hsp70 and hsp30 mRNA expression in rainbow trout: In vivo and in vitro comparisons
    • Currie S, Moyes CD, Tufts BL (2000) The effects of heat shock and acclimation temperature on hsp70 and hsp30 mRNA expression in rainbow trout: in vivo and in vitro comparisons. J Fish Biol 56:398-408
    • (2000) J Fish Biol , vol.56 , pp. 398-408
    • Currie, S.1    Moyes, C.D.2    Tufts, B.L.3
  • 44
    • 57149085658 scopus 로고    scopus 로고
    • Gill and head kidney antioxidant processes and innate immune system responses of yellow perch (Perca flavescens) exposed to different contaminants in the St. Lawrence River, Canada
    • Dautremepuits C, Marcogliese DJ, Gendron AD, Fournier M (2009) Gill and head kidney antioxidant processes and innate immune system responses of yellow perch (Perca flavescens) exposed to different contaminants in the St. Lawrence River, Canada. Sci Total Environ 407: 1055-1064
    • (2009) Sci Total Environ , vol.407 , pp. 1055-1064
    • Dautremepuits, C.1    Marcogliese, D.J.2    Gendron, A.D.3    Fournier, M.4
  • 45
    • 2442509842 scopus 로고    scopus 로고
    • Hypoxic conditions induce Hsp70 production in blood, brain and head kidney of juvenile Nile tilapia Oreochromis niloticus (L.)
    • Delaney MA, Klesius PH (2004) Hypoxic conditions induce Hsp70 production in blood, brain and head kidney of juvenile Nile tilapia Oreochromis niloticus (L.). Aquaculture 236:633-644
    • (2004) Aquaculture , vol.236 , pp. 633-644
    • Delaney, M.A.1    Klesius, P.H.2
  • 46
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
    • Demand J, Alberte S, Patterson C, Höhfeld J (2001) Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr Biol 11:1569-1577
    • (2001) Curr Biol , vol.11 , pp. 1569-1577
    • Demand, J.1    Alberte, S.2    Patterson, C.3    Höhfeld, J.4
  • 48
    • 0036530301 scopus 로고    scopus 로고
    • VEGF (165) promotes survival of leukemic cells by HSP90-mediated induction of Bcl-2 expression and apoptosis inhibition
    • Dias S, Shmelkov SV, Lam G, Rafii S (2002) VEGF (165) promotes survival of leukemic cells by HSP90-mediated induction of Bcl-2 expression and apoptosis inhibition. Blood 99:2532-2540
    • (2002) Blood , vol.99 , pp. 2532-2540
    • Dias, S.1    Shmelkov, S.V.2    Lam, G.3    Rafii, S.4
  • 49
    • 0026553389 scopus 로고
    • The threshold induction temperature of the 90 kDa heat shock protein is subject to acclimatization in eurythermal goby fishes (Genus Gillichthys)
    • 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 89:3389-3393
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3389-3393
    • Dietz, T.J.1    Somero, G.N.2
  • 50
    • 0027143812 scopus 로고
    • Species- and tissue-specific synthesis patterns for heat shock proteins HSP70 and HSP90 in several marine teleost fishes
    • 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 66:863-880
    • (1993) Physiol Zool , vol.66 , pp. 863-880
    • Dietz, T.J.1    Somero, G.N.2
  • 51
    • 0030824222 scopus 로고    scopus 로고
    • Antioxidant enzymes, glutathione and lipid peroxidation of experimental or field exposure in the gills and the digestive gland of the freshwater bivalve Unio tumidus
    • Doyotte AC, Jacquin MC, Babut M, Vasseur P (1997) Antioxidant enzymes, glutathione and lipid peroxidation of experimental or field exposure in the gills and the digestive gland of the freshwater bivalve Unio tumidus. Aquat Toxicol 39:93-110
    • (1997) Aquat Toxicol , vol.39 , pp. 93-110
    • Doyotte, A.C.1    Jacquin, M.C.2    Babut, M.3    Vasseur, P.4
  • 52
    • 33745762927 scopus 로고    scopus 로고
    • Molecular chaperones of the HSP110 family act as nucleotide exchange factors of HSP70s
    • Dragovic Z, Broadley SA, Shomura Y (2006) Molecular chaperones of the HSP110 family act as nucleotide exchange factors of HSP70s. EMBO J 25:2519-2528
    • (2006) EMBO J , vol.25 , pp. 2519-2528
    • Dragovic, Z.1    Broadley, S.A.2    Shomura, Y.3
  • 53
    • 0032191841 scopus 로고    scopus 로고
    • Thermal shock of salmon in vivo induces the heat shock protein (HSP70) and confers protection against osmotic shock
    • Dubeau SF, Pan F, Tremblay GC, Bradley TM (1998) Thermal shock of salmon in vivo induces the heat shock protein (HSP70) and confers protection against osmotic shock. Aquaculture 168:311-323
    • (1998) Aquaculture , vol.168 , pp. 311-323
    • Dubeau, S.F.1    Pan, F.2    Tremblay, G.C.3    Bradley, T.M.4
  • 54
    • 0032852690 scopus 로고    scopus 로고
    • Comparative baseline levels of mercury, HSP70 and HSP60 in subsistence fish from the Yukon-Kuskokwim delta region of Alaska
    • Duffy LK, Scofield E, Rodgers T, Patton M, Bowyer RT (1999) Comparative baseline levels of mercury, HSP70 and HSP60 in subsistence fish from the Yukon-Kuskokwim delta region of Alaska. Comp Biochem Physiol Toxicol Pharmacol 124:181-186
    • (1999) Comp Biochem Physiol Toxicol Pharmacol , vol.124 , pp. 181-186
    • Duffy, L.K.1    Scofield, E.2    Rodgers, T.3    Patton, M.4    Bowyer, R.T.5
  • 55
    • 0030982965 scopus 로고    scopus 로고
    • Biochemical responses to sediment-associated contaminants in brown bullhead (Ameiurus nebulosus) from the Niagara River ecosystem
    • Eufemia NA, Collier TK, Stein JE, Watson DE, Di Giulio RT (1997) Biochemical responses to sediment-associated contaminants in brown bullhead (Ameiurus nebulosus) from the Niagara River ecosystem. Ecotoxicology 6:13-34
    • (1997) Ecotoxicology , vol.6 , pp. 13-34
    • Eufemia, N.A.1    Collier, T.K.2    Stein, J.E.3    Watson, D.E.4    Di Giulio, R.T.5
  • 56
    • 11344280957 scopus 로고    scopus 로고
    • Extracellular roles for the molecular chaperone, HSP90
    • Eustace BK, Jay DG (2004) Extracellular roles for the molecular chaperone, HSP90. Cell Cycle 3:1098-1100
    • (2004) Cell Cycle , vol.3 , pp. 1098-1100
    • Eustace, B.K.1    Jay, D.G.2
  • 57
    • 0028003295 scopus 로고
    • Seasonal variation in heat shock proteins (HSP70) in stream fish under natural conditions
    • Fader SC, Yu Z, Spotila JR (1994) Seasonal variation in heat shock proteins (HSP70) in stream fish under natural conditions. J Therm Biol 19:335-341
    • (1994) J Therm Biol , vol.19 , pp. 335-341
    • Fader, S.C.1    Yu, Z.2    Spotila, J.R.3
  • 58
    • 54049152301 scopus 로고    scopus 로고
    • Hepatic transcriptomic profiles of European flounder (Platichthys flesus) from field sites and computational approaches to predict site from stress gene responses following exposure to model toxicants
    • Falciani F, Diab AM, Sabine V, Williams TD, Ortega F, George SG, Chipman JK (2008) Hepatic transcriptomic profiles of European flounder (Platichthys flesus) from field sites and computational approaches to predict site from stress gene responses following exposure to model toxicants. Aquat Toxicol 90:92-101
    • (2008) Aquat Toxicol , vol.90 , pp. 92-101
    • Falciani, F.1    Diab, A.M.2    Sabine, V.3    Williams, T.D.4    Ortega, F.5    George, S.G.6    Chipman, J.K.7
  • 59
    • 0031931412 scopus 로고    scopus 로고
    • Intramolecular repression of mouse heat shock factor1
    • Farkas T, Kutskova YA, Zimarino V (1998) Intramolecular repression of mouse heat shock factor1. Mol Cell Biol 18:906-918
    • (1998) Mol Cell Biol , vol.18 , pp. 906-918
    • Farkas, T.1    Kutskova, Y.A.2    Zimarino, V.3
  • 60
    • 0033057848 scopus 로고    scopus 로고
    • Heat-shock proteins, molecular chaperones, and the stress response: Evolutionary and ecological physiology
    • Feder ME, Hofmann GE (1999) Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu Rev Physiol 61:243-282
    • (1999) Annu Rev Physiol , vol.61 , pp. 243-282
    • Feder, M.E.1    Hofmann, G.E.2
  • 61
    • 0004581102 scopus 로고    scopus 로고
    • Natural and genetic engineering of thermotolerance in Drosophila melanogaster
    • Feder ME, Krebs RA (1998) Natural and genetic engineering of thermotolerance in Drosophila melanogaster. Am Zool 38:503-517
    • (1998) Am Zool , vol.38 , pp. 503-517
    • Feder, M.E.1    Krebs, R.A.2
  • 62
    • 33748132549 scopus 로고    scopus 로고
    • Redox regulatory mechanisms in cellular stress responses
    • Fedoroff N (2006) Redox regulatory mechanisms in cellular stress responses. Ann Bot 98:289-300
    • (2006) Ann Bot , vol.98 , pp. 289-300
    • Fedoroff, N.1
  • 63
    • 0029660889 scopus 로고    scopus 로고
    • Hepatic enzymatic activities of the European eel Anguilla anguilla as a tool for biomonitoring fresh-water streams: Laboratory and field caging studies
    • Fenet H, Casellas C, Bontoux J (1996) Hepatic enzymatic activities of the European eel Anguilla anguilla as a tool for biomonitoring fresh-water streams: laboratory and field caging studies. Water Sci Technol 33:321-329
    • (1996) Water Sci Technol , vol.33 , pp. 321-329
    • Fenet, H.1    Casellas, C.2    Bontoux, J.3
  • 64
    • 0002616870 scopus 로고
    • Structure and regulation of heat shock gene promoters
    • Morimoto RI, Tissieres A, Georgopoulos C (eds). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Fernandes M, O'Brien T, Lis JT (1994) Structure and regulation of heat shock gene promoters. In: Morimoto RI, Tissieres A, Georgopoulos C (eds) The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp 375-393
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 375-393
    • Fernandes, M.1    O'Brien, T.2    Lis, J.T.3
  • 66
    • 0025647514 scopus 로고
    • Does heat shock enhance oxidative stress? Studies with ferrous and ferric iron
    • Freeman ML, Spitz DR, Meredith MJ (1990) Does heat shock enhance oxidative stress? Studies with ferrous and ferric iron. Radiat Res 124:288-293
    • (1990) Radiat Res , vol.124 , pp. 288-293
    • Freeman, M.L.1    Spitz, D.R.2    Meredith, M.J.3
  • 67
    • 0036090023 scopus 로고    scopus 로고
    • Interplay between molecular chaperones and signaling pathways in survival of heat shock
    • Gabai VL, Sherman MY (2002) Interplay between molecular chaperones and signaling pathways in survival of heat shock. J Appl Physiol 92:1743-1748
    • (2002) J Appl Physiol , vol.92 , pp. 1743-1748
    • Gabai, V.L.1    Sherman, M.Y.2
  • 68
    • 34249769205 scopus 로고
    • Experimental control of stress hormone levels in fishes: Techniques and applications
    • Gamperl AK, Vijayan MM, Boutilier RG (1994) Experimental control of stress hormone levels in fishes: techniques and applications. Rev Fish Biol Fish 4:215-255
    • (1994) Rev Fish Biol Fish , vol.4 , pp. 215-255
    • Gamperl, A.K.1    Vijayan, M.M.2    Boutilier, R.G.3
  • 69
    • 0035042529 scopus 로고    scopus 로고
    • Hsp70-DnaJ chaperone pairs prevent nitric oxide-mediated apoptosis in RAW 264.7 macrophages
    • Gotoh T, Terada K, Mori M (2001) hsp70-DnaJ chaperone pairs prevent nitric oxide-mediated apoptosis in RAW 264.7 macrophages. Cell Death Differ 8:357-366
    • (2001) Cell Death Differ , vol.8 , pp. 357-366
    • Gotoh, T.1    Terada, K.2    Mori, M.3
  • 70
    • 25844489031 scopus 로고    scopus 로고
    • Biomarker protein expression in primary cultures of salmon (Salmo salar L) hepatocytes exposed to environmental pollutants
    • Grosvik BE, Goksoyr A (1996) Biomarker protein expression in primary cultures of salmon (Salmo salar L) hepatocytes exposed to environmental pollutants. Biomarkers 1:45-53
    • (1996) Biomarkers , vol.1 , pp. 45-53
    • Grosvik, B.E.1    Goksoyr, A.2
  • 71
    • 0037432156 scopus 로고    scopus 로고
    • Regulation of telomerase activity and anti-apoptotic function by protein-protein interaction and phosphorylation
    • Haendeler J, Hoffmann J, Rahman S, Zeiher AM, Dimmeler S (2003) Regulation of telomerase activity and anti-apoptotic function by protein-protein interaction and phosphorylation. FEBS Lett 536:180-186
    • (2003) FEBS Lett , vol.536 , pp. 180-186
    • Haendeler, J.1    Hoffmann, J.2    Rahman, S.3    Zeiher, A.M.4    Dimmeler, S.5
  • 72
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381:571-579
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 73
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl FU, Hayer-HartlM(2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852-1858
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 75
    • 18344405907 scopus 로고    scopus 로고
    • Response of carp central nervous system to hyperammonemic conditions: An immunocytochemical study of glutamine synthetase (GS), glial fibrillary acidic protein (GFAP) and 70 kDa heat-shock protein (HSP70)
    • Hernandez C,MartinM, Bodega G, Suarez I, Perez J, Fernandez B (1999) Response of carp central nervous system to hyperammonemic conditions: an immunocytochemical study of glutamine synthetase (GS), glial fibrillary acidic protein (GFAP) and 70 kDa heat-shock protein (HSP70). Aquat Toxicol 45:195-207
    • (1999) Aquat Toxicol , vol.45 , pp. 195-207
    • Hernandez, C.1    Martin, M.2    Bodega, G.3    Suarez, I.4    Perez, J.5    Fernandez, B.6
  • 76
    • 0033836161 scopus 로고    scopus 로고
    • Heat shock protein expression is absent in the Antarctic fish Trematomus bernachhii (family Nototheniidae)
    • Hofmann G, Buckley BA, Airaksinen S, Keen JE, Somero GN (2000) Heat shock protein expression is absent in the Antarctic fish Trematomus bernachhii (family Nototheniidae). J Exp Biol 203:2331-2339
    • (2000) J Exp Biol , vol.203 , pp. 2331-2339
    • Hofmann, G.1    Buckley, B.A.2    Airaksinen, S.3    Keen, J.E.4    Somero, G.N.5
  • 77
    • 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
    • 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 198:1509-1518
    • (1995) J Exp Biol , vol.198 , pp. 1509-1518
    • Hofmann, G.E.1    Somero, G.N.2
  • 81
    • 0034739793 scopus 로고    scopus 로고
    • Transcriptome analysis of channel catfish (Ictalurus punctatus): Genes and expression profile from the brain
    • Ju Z, Karsi A, Kocabas A, Patterson A, Li P, Cao D, Dunham R, Liu Z (2000) Transcriptome analysis of channel catfish (Ictalurus punctatus): genes and expression profile from the brain. Gene 261:373-382
    • (2000) Gene , vol.261 , pp. 373-382
    • Ju, Z.1    Karsi, A.2    Kocabas, A.3    Patterson, A.4    Li, P.5    Cao, D.6    Dunham, R.7    Liu, Z.8
  • 82
    • 2942555103 scopus 로고    scopus 로고
    • Superoxide dismutase mimetics elevate superoxide dismutase activity in vivo but do not retard aging in the nematode Caenorhabditis elegans
    • Keaney M, Matthijssens F, Sharpe M, Vanfletern J, Gems D (2004) Superoxide dismutase mimetics elevate superoxide dismutase activity in vivo but do not retard aging in the nematode Caenorhabditis elegans. Free Radic Biol Med 37:239-250
    • (2004) Free Radic Biol Med , vol.37 , pp. 239-250
    • Keaney, M.1    Matthijssens, F.2    Sharpe, M.3    Vanfletern, J.4    Gems, D.5
  • 83
  • 84
    • 0000002246 scopus 로고    scopus 로고
    • Expression of the heat shock proteins in HeLa and CHSE-214 cells exposed to heat shock
    • Kong HJ, Kang HS, Kim HD (1996) Expression of the heat shock proteins in HeLa and CHSE-214 cells exposed to heat shock. Korean J Zool 39:123-131
    • (1996) Korean J Zool , vol.39 , pp. 123-131
    • Kong, H.J.1    Kang, H.S.2    Kim, H.D.3
  • 85
    • 0021678194 scopus 로고
    • The heat-shock phenomenon in cultured cells of rainbow trout: Hsp70 mRNA synthesis and turnover
    • Kothary RK, Burgess EA, Candido EPM (1984) The heat-shock phenomenon in cultured cells of rainbow trout: hsp70 mRNA synthesis and turnover. Biochim Biophys Acta 783:137-143
    • (1984) Biochim Biophys Acta , vol.783 , pp. 137-143
    • Kothary, R.K.1    Burgess, E.A.2    Candido, E.P.M.3
  • 86
    • 0031311669 scopus 로고    scopus 로고
    • Heat shock genes and the heat shock response in zebrafish embryos
    • Krone PH, Lele Z, Sass JB (1997) Heat shock genes and the heat shock response in zebrafish embryos. Biochem Cell Biol 75:487-497
    • (1997) Biochem Cell Biol , vol.75 , pp. 487-497
    • Krone, P.H.1    Lele, Z.2    Sass, J.B.3
  • 87
    • 0028171452 scopus 로고
    • Hsp90α and hsp90β genes are present in the zebrafish and are differentially regulated in developing embryos
    • Krone PH, Sass JB (1994) Hsp90α and hsp90β genes are present in the zebrafish and are differentially regulated in developing embryos. Biochem Biophys Res Commun 204:746-752
    • (1994) Biochem Biophys Res Commun , vol.204 , pp. 746-752
    • Krone, P.H.1    Sass, J.B.2
  • 88
    • 33751116125 scopus 로고    scopus 로고
    • Baseline expression of HSPs of a 'thermotolerant' Mediterranean marine species largely influenced by natural temperature fluctuations
    • Lejeusne C, Perez T, Sarrazin V, Chevaldonne P (2006) Baseline expression of HSPs of a 'thermotolerant' Mediterranean marine species largely influenced by natural temperature fluctuations. Can J Fish Aquat Sci 63:2028-2037
    • (2006) Can J Fish Aquat Sci , vol.63 , pp. 2028-2037
    • Lejeusne, C.1    Perez, T.2    Sarrazin, V.3    Chevaldonne, P.4
  • 89
    • 0030764256 scopus 로고    scopus 로고
    • Hsp47 and hsp70 gene expression is differentially regulated in a stress- and tissue-specific manner in zebrafish embryos
    • Lele Z, Engel S, Krone PH (1997) Hsp47 and hsp70 gene expression is differentially regulated in a stress- and tissue-specific manner in zebrafish embryos. Dev Genet 21:123-133
    • (1997) Dev Genet , vol.21 , pp. 123-133
    • Lele, Z.1    Engel, S.2    Krone, P.H.3
  • 90
    • 0001490732 scopus 로고
    • Pro-oxidant/antioxidant processes and organic xenobiotic interactions in marine organisms, in particular the flounder Platichthys flesus and the mussel Mytilus edulis
    • Lenaire P, Livingstone DR (1993) Pro-oxidant/antioxidant processes and organic xenobiotic interactions in marine organisms, in particular the flounder Platichthys flesus and the mussel Mytilus edulis. Trends Comp Biochem Physiol 1:1119-1150
    • (1993) Trends Comp Biochem Physiol , vol.1 , pp. 1119-1150
    • Lenaire, P.1    Livingstone, D.R.2
  • 91
    • 0029682889 scopus 로고    scopus 로고
    • Thermotolerance and heat shock proteins: Possible involvement of Ku autoantigen in regulating HSP70 expression
    • Feige U, Morimoto RI, Yahara I, Polla B (eds). Birkhäuser Verlag, Basel
    • Li GC, Nussenzweig A (1996) Thermotolerance and heat shock proteins: possible involvement of Ku autoantigen in regulating HSP70 expression. In: Feige U, Morimoto RI, Yahara I, Polla B (eds) Stress-inducible cellular responses. Birkhäuser Verlag, Basel, pp 425-449
    • (1996) Stress-inducible Cellular Responses , pp. 425-449
    • Li, G.C.1    Nussenzweig, A.2
  • 92
    • 0034682748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation
    • Li C-Y, Lee J-S, Ko Y-G, Kim J-I, Seo J-S (2000) Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation. J Biol Chem 275:25665-25671
    • (2000) J Biol Chem , vol.275 , pp. 25665-25671
    • Li, C.-Y.1    Lee, J.-S.2    Ko, Y.-G.3    Kim, J.-I.4    Seo, J.-S.5
  • 93
    • 0032897223 scopus 로고    scopus 로고
    • Short-range linkage relationships, genomic organization and sequence comparisons of a cluster of five hsp70 genes in Fugu rubripes
    • Lim EH, Brenner S (1999) Short-range linkage relationships, genomic organization and sequence comparisons of a cluster of five hsp70 genes in Fugu rubripes. Cell Mol Life Sci 55:668-678
    • (1999) Cell Mol Life Sci , vol.55 , pp. 668-678
    • Lim, E.H.1    Brenner, S.2
  • 94
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist S (1986) The heat-shock response. Annu Rev Biochem 55:1151-1191
    • (1986) Annu Rev Biochem , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 95
    • 0036433466 scopus 로고    scopus 로고
    • The effects of environmental heat stress on heat-shock mRNA and protein expression in Miramichi Atlantic salmon (Salmo salar) parr
    • Lund SG, Caissie D, Cunjak RA, Vijayan MM, Tufts BL (2002) The effects of environmental heat stress on heat-shock mRNA and protein expression in Miramichi Atlantic salmon (Salmo salar) parr. Can J Fish Aquat Sci 59:1553-1562
    • (2002) Can J Fish Aquat Sci , vol.59 , pp. 1553-1562
    • Lund, S.G.1    Caissie, D.2    Cunjak, R.A.3    Vijayan, M.M.4    Tufts, B.L.5
  • 96
    • 18344403074 scopus 로고    scopus 로고
    • Heat-shock proteins expression in fish central nervous system and its possible relation with water acidosis resistance
    • Martin M, Hernandez C, Bodega G, Suarez I, Boyano MC, Fernandez B (1998) Heat-shock proteins expression in fish central nervous system and its possible relation with water acidosis resistance. Neurosci Res 31:97-106
    • (1998) Neurosci Res , vol.31 , pp. 97-106
    • Martin, M.1    Hernandez, C.2    Bodega, G.3    Suarez, I.4    Boyano, M.C.5    Fernandez, B.6
  • 98
    • 0036798777 scopus 로고    scopus 로고
    • Stress-mediated signaling in PC12 cells - The role of the small heat shock protein, HSP27, and Akt in protecting cells from heat stress and nerve growth factor withdrawal
    • Mearow KM, Dodge ME, Rahimtula M, Yegappan C (2002) Stress-mediated signaling in PC12 cells - the role of the small heat shock protein, HSP27, and Akt in protecting cells from heat stress and nerve growth factor withdrawal. J Neurochem 83:452-462
    • (2002) J Neurochem , vol.83 , pp. 452-462
    • Mearow, K.M.1    Dodge, M.E.2    Rahimtula, M.3    Yegappan, C.4
  • 100
    • 0030863285 scopus 로고    scopus 로고
    • Developmental control of heat shock and chaperone gene expression
    • Morange M (1997) Developmental control of heat shock and chaperone gene expression. Cell Mol Life Sci 53:78-79
    • (1997) Cell Mol Life Sci , vol.53 , pp. 78-79
    • Morange, M.1
  • 101
    • 3542995049 scopus 로고    scopus 로고
    • Stress-inducible responses and heat shock proteins: New pharmacologic targets for cytoprotection
    • Morimoto RI, Santoro MG (1998) Stress-inducible responses and heat shock proteins: new pharmacologic targets for cytoprotection. Nature Biotechnol 16:833-838
    • (1998) Nature Biotechnol , vol.16 , pp. 833-838
    • Morimoto, R.I.1    Santoro, M.G.2
  • 102
    • 0026592050 scopus 로고
    • Transcriptional regulation of heat shock genes. A paradigm for inducible genomic responses
    • Morimoto RI, Sarge KD, Abravaya K (1992) Transcriptional regulation of heat shock genes. A paradigm for inducible genomic responses. J Biol Chem 267:21987-21990
    • (1992) J Biol Chem , vol.267 , pp. 21987-21990
    • Morimoto, R.I.1    Sarge, K.D.2    Abravaya, K.3
  • 103
    • 0024195787 scopus 로고
    • Relationship between heat-shock protein synthesis and thermotolerance in rainbow trout fibroblasts
    • Mosser DD, Bols NC (1988) Relationship between heat-shock protein synthesis and thermotolerance in rainbow trout fibroblasts. J Comp Physiol B 158:457-467
    • (1988) J Comp Physiol B , vol.158 , pp. 457-467
    • Mosser, D.D.1    Bols, N.C.2
  • 104
    • 0034890377 scopus 로고    scopus 로고
    • Modulation of HSP90 function by ansamycins sensitizes breast cancer cells to chemotherapy-induced apoptosis in an RB- and schedule-dependent manner
    • Munster PN, Basso A, Solit D, Norton L, Rosen N (2001) Modulation of HSP90 function by ansamycins sensitizes breast cancer cells to chemotherapy-induced apoptosis in an RB- and schedule-dependent manner. Clin Cancer Res 7:2228-2236
    • (2001) Clin Cancer Res , vol.7 , pp. 2228-2236
    • Munster, P.N.1    Basso, A.2    Solit, D.3    Norton, L.4    Rosen, N.5
  • 105
    • 0036606332 scopus 로고    scopus 로고
    • Degradation of HER2 by ansamycins induces growth arrest and apoptosis in cells with HER2 overexpression via a HER3, phosphatidylinositol 3′-kinase-AKT-dependent pathway
    • Munster PN, Marchion DC, Basso AD, Rosen N (2002) Degradation of HER2 by ansamycins induces growth arrest and apoptosis in cells with HER2 overexpression via a HER3, phosphatidylinositol 3′-kinase-AKT-dependent pathway. Cancer Res 62:3132-3137
    • (2002) Cancer Res , vol.62 , pp. 3132-3137
    • Munster, P.N.1    Marchion, D.C.2    Basso, A.D.3    Rosen, N.4
  • 106
    • 0036024293 scopus 로고    scopus 로고
    • The 70-kDa heat shock protein response in two intertidal sculpins, Oligocottus maculosus and O. snyderi: Relationship of hsp70 and thermal tolerance
    • Nakano K, Iwama GK (2002) The 70-kDa heat shock protein response in two intertidal sculpins, Oligocottus maculosus and O. snyderi: relationship of hsp70 and thermal tolerance. Comp Biochem Physiol A 133:79-94
    • (2002) Comp Biochem Physiol A , vol.133 , pp. 79-94
    • Nakano, K.1    Iwama, G.K.2
  • 108
    • 55549126441 scopus 로고    scopus 로고
    • Heat shock protein (Hsp70) induced by a mild heat shock slightly moderates plasma osmolarity increases upon salinity transfer in rainbow trout (Oncorhynchus mykiss)
    • Niu CJ, Rummer JL, Brauner CJ, Schulte PM (2008) Heat shock protein (Hsp70) induced by a mild heat shock slightly moderates plasma osmolarity increases upon salinity transfer in rainbow trout (Oncorhynchus mykiss). Comp Biochem Physiol C 148:437-444
    • (2008) Comp Biochem Physiol C , vol.148 , pp. 437-444
    • Niu, C.J.1    Rummer, J.L.2    Brauner, C.J.3    Schulte, P.M.4
  • 109
    • 0037099046 scopus 로고    scopus 로고
    • Chaperoning signaling pathways: Molecular chaperones as stress-sensing 'heat shock' proteins
    • Nollen EAA, Morimoto RI (2002) Chaperoning signaling pathways: molecular chaperones as stress-sensing 'heat shock' proteins. J Cell Sci 115:2809-2816
    • (2002) J Cell Sci , vol.115 , pp. 2809-2816
    • Nollen, E.A.A.1    Morimoto, R.I.2
  • 110
    • 0030929973 scopus 로고    scopus 로고
    • Low-molecular weight heat shock proteins in a desert fish (Poeciliopsis lucida): Homologs of human hsp27 and Xenopus hsp30
    • Norris CE, Brown MA, Hickey E, Weber LA, Hightower LE (1997) Low-molecular weight heat shock proteins in a desert fish (Poeciliopsis lucida): Homologs of human hsp27 and Xenopus hsp30. Mol Cell Evol 14:1050-1061
    • (1997) Mol Cell Evol , vol.14 , pp. 1050-1061
    • Norris, C.E.1    Brown, M.A.2    Hickey, E.3    Weber, L.A.4    Hightower, L.E.5
  • 111
    • 0028220114 scopus 로고
    • Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster
    • Orr WC, Sohal RS (1994) Extension of life-span by overexpression of superoxide dismutase and catalase in Drosophila melanogaster. Science 263:1128-1130
    • (1994) Science , vol.263 , pp. 1128-1130
    • Orr, W.C.1    Sohal, R.S.2
  • 112
    • 34249940983 scopus 로고    scopus 로고
    • Seasonal pollution assessment through comparative hydrobiological studies in Ennore and Kovalam estuaries
    • Padmini E, Kavitha M (2003) Seasonal pollution assessment through comparative hydrobiological studies in Ennore and Kovalam estuaries. Indian Hydrobiol 6:139-144
    • (2003) Indian Hydrobiol , vol.6 , pp. 139-144
    • Padmini, E.1    Kavitha, M.2
  • 113
    • 77956072370 scopus 로고    scopus 로고
    • Contaminant induced stress impact on the histology and biochemical alterations in the brain of estuarine grey mullets
    • Padmini E, Kavitha M (2005a) Contaminant induced stress impact on the histology and biochemical alterations in the brain of estuarine grey mullets. Pollut Res 24:177-181
    • (2005) Pollut Res , vol.24 , pp. 177-181
    • Padmini, E.1    Kavitha, M.2
  • 114
    • 29644435251 scopus 로고    scopus 로고
    • Evaluation of genotoxic effects due to contaminant mediated oxidative damage in the brain of Mugil cephalus (Linnaeus)
    • Padmini E, Kavitha M (2005b) Evaluation of genotoxic effects due to contaminant mediated oxidative damage in the brain of Mugil cephalus (Linnaeus). Pollut Res 24:33-36
    • (2005) Pollut Res , vol.24 , pp. 33-36
    • Padmini, E.1    Kavitha, M.2
  • 115
    • 77956084979 scopus 로고    scopus 로고
    • Comparative assessment of contaminant induced oxidative stress in brain of Mugil cephalus
    • Padmini E, Kavitha M (2007) Comparative assessment of contaminant induced oxidative stress in brain of Mugil cephalus. Environ Pollut Control J 10:75-79
    • (2007) Environ Pollut Control J , vol.10 , pp. 75-79
    • Padmini, E.1    Kavitha, M.2
  • 116
    • 34249935324 scopus 로고    scopus 로고
    • Environmental impact on gill mitochondrial function in Mugil cephalus
    • Padmini E, Sudha D (2004) Environmental impact on gill mitochondrial function in Mugil cephalus. Aquaculture 5:89-92
    • (2004) Aquaculture , vol.5 , pp. 89-92
    • Padmini, E.1    Sudha, D.2
  • 117
    • 52149105387 scopus 로고    scopus 로고
    • Impact of seasonal variation on HSP70 expression quantitated in stressed fish hepatocytes
    • Padmini E, Usha Rani M (2008) Impact of seasonal variation on HSP70 expression quantitated in stressed fish hepatocytes. Comp Biochem Physiol B 151:278-285
    • (2008) Comp Biochem Physiol B , vol.151 , pp. 278-285
    • Padmini, E.1    Usha Rani, M.2
  • 118
    • 62949182315 scopus 로고    scopus 로고
    • Seasonal influence on heat shock protein 90α and heat shock factor 1 expression during oxidative stress in fish hepatocytes from polluted estuary
    • Padmini E, Usha Rani M (2009a) Seasonal influence on heat shock protein 90α and heat shock factor 1 expression during oxidative stress in fish hepatocytes from polluted estuary. J Exp Mar Biol Ecol 372:1-8
    • (2009) J Exp Mar Biol Ecol , vol.372 , pp. 1-8
    • Padmini, E.1    Usha Rani, M.2
  • 119
    • 67349189498 scopus 로고    scopus 로고
    • Evaluation of oxidative stress biomarkers in hepatocytes of grey mullet inhabiting natural and polluted estuaries
    • Padmini E, Usha Rani M (2009b) Evaluation of oxidative stress biomarkers in hepatocytes of grey mullet inhabiting natural and polluted estuaries. Sci Total Environ 407:4533-4541
    • (2009) Sci Total Environ , vol.407 , pp. 4533-4541
    • Padmini, E.1    Usha Rani, M.2
  • 120
    • 72049120407 scopus 로고    scopus 로고
    • Thioredoxin and HSP90α modulate ASK1-JNK1/2 signaling in stressed hepatocytes of Mugil cephalus
    • Padmini E, Usha Rani M (2010) Thioredoxin and HSP90α modulate ASK1-JNK1/2 signaling in stressed hepatocytes of Mugil cephalus. Comp Biochem Physiol C 151:187-193
    • (2010) Comp Biochem Physiol C , vol.151 , pp. 187-193
    • Padmini, E.1    Usha Rani, M.2
  • 121
    • 34249940860 scopus 로고    scopus 로고
    • Seasonal influences on water quality parameters and pollution status of the Ennore estuary, Tamilnadu, India
    • Padmini E, Vijaya Geetha B (2007a) Seasonal influences on water quality parameters and pollution status of the Ennore estuary, Tamilnadu, India. J Environ Hydrol 15:1-15
    • (2007) J Environ Hydrol , vol.15 , pp. 1-15
    • Padmini, E.1    Vijaya Geetha, B.2
  • 122
    • 37249068438 scopus 로고    scopus 로고
    • A comparative seasonal pollution assessment study on Ennore estuary with respect to metal accumulation in the grey mullet, Mugil cephalus
    • Padmini E, Vijaya Geetha B (2007b) A comparative seasonal pollution assessment study on Ennore estuary with respect to metal accumulation in the grey mullet, Mugil cephalus. Oceanol Hydrobiol Stud 35:91-103
    • (2007) Oceanol Hydrobiol Stud , vol.35 , pp. 91-103
    • Padmini, E.1    Vijaya Geetha, B.2
  • 123
    • 57049111628 scopus 로고    scopus 로고
    • Oxidative stress biomarkers in the liver mitochondria of grey mullets shows seasonal variation in the Ennore estuary
    • Padmini E, Vijaya Geetha B (2007c) Oxidative stress biomarkers in the liver mitochondria of grey mullets shows seasonal variation in the Ennore estuary. J Ecophysiol Occup Health 7: 107-116
    • (2007) J Ecophysiol Occup Health , vol.7 , pp. 107-116
    • Padmini, E.1    Vijaya Geetha, B.2
  • 124
    • 48349109560 scopus 로고    scopus 로고
    • Biodegradative efficiency of recombinant Escherichia coli on heavy metal contamination and organic pollutants from Ennore estuary
    • Padmini E, Vijaya Geetha B (2008) Biodegradative efficiency of recombinant Escherichia coli on heavy metal contamination and organic pollutants from Ennore estuary. Asian J Microbiol Biotechnol Environ Sci 14:185-190
    • (2008) Asian J Microbiol Biotechnol Environ Sci , vol.14 , pp. 185-190
    • Padmini, E.1    Vijaya Geetha, B.2
  • 125
    • 61349151669 scopus 로고    scopus 로고
    • Impact of season on liver mitochondrial oxidative stress and the expression of HSP70 in greymullets from contaminated estuary
    • Padmini E, Vijaya Geetha B (2009a) Impact of season on liver mitochondrial oxidative stress and the expression of HSP70 in greymullets from contaminated estuary. Ecotoxicology 18:304-311
    • (2009) Ecotoxicology , vol.18 , pp. 304-311
    • Padmini, E.1    Vijaya Geetha, B.2
  • 126
    • 77950863959 scopus 로고    scopus 로고
    • Modulation of ASK1 expression during overexpression of Trx and HSP70 in stressed fish liver mitochondria
    • Padmini E, Vijaya Geetha B (2009b) Modulation of ASK1 expression during overexpression of Trx and HSP70 in stressed fish liver mitochondria. Cell Stress Chaperones 14:459-467
    • (2009) Cell Stress Chaperones , vol.14 , pp. 459-467
    • Padmini, E.1    Vijaya Geetha, B.2
  • 127
    • 37249076648 scopus 로고    scopus 로고
    • Environmental stress in Ennore estuary and enhanced erythrocyte micronuclei formation in mullets
    • Padmini E, Sridevi S, Vijaya Geetha B (2006) Environmental stress in Ennore estuary and enhanced erythrocyte micronuclei formation in mullets. Environ Pollut Control J 9:51-56
    • (2006) Environ Pollut Control J , vol.9 , pp. 51-56
    • Padmini, E.1    Sridevi, S.2    Vijaya Geetha, B.3
  • 128
    • 34249936314 scopus 로고    scopus 로고
    • Lipid alteration as stress markers in grey mullets (Mugil cephalus Linnaeus) caused by industrial effluents in Ennore estuary
    • Padmini E, Thendral Hepsibha B, Shanthalin Shellomith AS (2004) Lipid alteration as stress markers in grey mullets (Mugil cephalus Linnaeus) caused by industrial effluents in Ennore estuary. Aquaculture 5:115-118
    • (2004) Aquaculture , vol.5 , pp. 115-118
    • Padmini, E.1    Thendral Hepsibha, B.2    Shanthalin Shellomith, A.S.3
  • 129
    • 59849121093 scopus 로고    scopus 로고
    • Liver oxidative stress of the grey mullet Mugil cephalus presents seasonal variations in Ennore estuary
    • Padmini E, Vijaya Geetha B, Usha Rani M (2008a) Liver oxidative stress of the grey mullet Mugil cephalus presents seasonal variations in Ennore estuary. Braz J Med Biol Res 41:951-955
    • (2008) Braz J Med Biol Res , vol.41 , pp. 951-955
    • Padmini, E.1    Vijaya Geetha, B.2    Usha Rani, M.3
  • 130
    • 53349142653 scopus 로고    scopus 로고
    • Differential HSP90α expression in fish hepatocytes from polluted estuary during summer
    • Padmini E, Usha Rani M, Vijaya Geetha B (2008b) Differential HSP90α expression in fish hepatocytes from polluted estuary during summer. Fish Sci 74:1118-1126
    • (2008) Fish Sci , vol.74 , pp. 1118-1126
    • Padmini, E.1    Usha Rani, M.2    Vijaya Geetha, B.3
  • 131
    • 68149178487 scopus 로고    scopus 로고
    • Studies on antioxidant status in Mugil cephalus in response to heavy metal pollution at Ennore estuary
    • Padmini E, Usha RaniM, Vijaya Geetha B (2009a) Studies on antioxidant status in Mugil cephalus in response to heavy metal pollution at Ennore estuary. Environ Monit Assess 155:215-225
    • (2009) Environ Monit Assess , vol.155 , pp. 215-225
    • Padmini, E.1    Usha Rani, M.2    Vijaya Geetha, B.3
  • 132
    • 57049083961 scopus 로고    scopus 로고
    • Pollution induced nitrative stress and heat shock protein 70 overexpression in fish liver mitochondria
    • Padmini E, Vijaya Geetha B, Usha Rani M (2009b) Pollution induced nitrative stress and heat shock protein 70 overexpression in fish liver mitochondria. Sci Total Environ 407:1307-1317
    • (2009) Sci Total Environ , vol.407 , pp. 1307-1317
    • Padmini, E.1    Vijaya Geetha, B.2    Usha Rani, M.3
  • 133
    • 0033849644 scopus 로고    scopus 로고
    • Tissue specific induction of hsp90 mRNA and plasma cortisol response in Chinook salmon following heat shock, seawater challenge, and handling challenge
    • Palmisano AN, Winton JR, Dickhoff, WW (2000) Tissue specific induction of hsp90 mRNA and plasma cortisol response in Chinook salmon following heat shock, seawater challenge, and handling challenge. Mar Biotechnol 2:329-338
    • (2000) Mar Biotechnol , vol.2 , pp. 329-338
    • Palmisano, A.N.1    Winton, J.R.2    Dickhoff, W.W.3
  • 134
    • 0034255940 scopus 로고    scopus 로고
    • Cloning and characterization of salmon hsp90 cDNA: Upregulation by thermal and hyperosmotic stress
    • Pan F, Zarate JM, Tremblay GC, Bradley TM (2000) Cloning and characterization of salmon hsp90 cDNA: upregulation by thermal and hyperosmotic stress. J Exp Zool 287:199-212
    • (2000) J Exp Zool , vol.287 , pp. 199-212
    • Pan, F.1    Zarate, J.M.2    Tremblay, G.C.3    Bradley, T.M.4
  • 136
    • 0034843403 scopus 로고    scopus 로고
    • Effect of endosulfan on antioxidants of freshwater fish Channa punctatus Bloch: 1. Protection against lipid peroxidation in liver by copper preexposure
    • Pandey S, Ahmad I, Parvez S, Bin-Hafeez B, Haque R, Raisuddin S (2001) Effect of endosulfan on antioxidants of freshwater fish Channa punctatus Bloch: 1. Protection against lipid peroxidation in liver by copper preexposure. Arch Environ Contam Toxicol 41:345-352
    • (2001) Arch Environ Contam Toxicol , vol.41 , pp. 345-352
    • Pandey, S.1    Ahmad, I.2    Parvez, S.3    Bin-Hafeez, B.4    Haque, R.5    Raisuddin, S.6
  • 137
    • 0037870404 scopus 로고    scopus 로고
    • Biomarkers of oxidative stress: A comparative study of river Yamuna fish Wallago attu (Bl. & Schn.)
    • Pandey S, Parvez S, Sayeed I, Haque R, Bin-Hafeez B, Raisuddin S (2003) Biomarkers of oxidative stress: a comparative study of river Yamuna fish Wallago attu (Bl. & Schn.). Sci Total Environ 309:105-115
    • (2003) Sci Total Environ , vol.309 , pp. 105-115
    • Pandey, S.1    Parvez, S.2    Sayeed, I.3    Haque, R.4    Bin-Hafeez, B.5    Raisuddin, S.6
  • 138
    • 0142075876 scopus 로고    scopus 로고
    • Molecular chaperones, stress proteins and redox homeostasis
    • Papp E, Nardai G, Soti C, Csermely P (2003) Molecular chaperones, stress proteins and redox homeostasis. Biofactors 17:249-257
    • (2003) Biofactors , vol.17 , pp. 249-257
    • Papp, E.1    Nardai, G.2    Soti, C.3    Csermely, P.4
  • 139
    • 0030835535 scopus 로고    scopus 로고
    • Responses of superoxide dismutase, glutathione peroxidase and reduced glutathione antioxidant defenses in gills of the freshwater catfish (Heteropneustes fossilis) to short-term elevated temperature
    • Parihar MS, Javeri T, Hemnani T, Dubey AK, Prakash P (1997) Responses of superoxide dismutase, glutathione peroxidase and reduced glutathione antioxidant defenses in gills of the freshwater catfish (Heteropneustes fossilis) to short-term elevated temperature. J Therm Biol 22:151-156
    • (1997) J Therm Biol , vol.22 , pp. 151-156
    • Parihar, M.S.1    Javeri, T.2    Hemnani, T.3    Dubey, A.K.4    Prakash, P.5
  • 140
  • 141
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell DA, Lindquist S (1993) The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu Rev Genet 27:437-496
    • (1993) Annu Rev Genet , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 142
    • 0000675009 scopus 로고
    • Heat shock proteins and stress tolerance
    • Morimoto RI, Tissieres A, Georgopoulos C (eds). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Parsell DA, Lindquist S (1994) Heat shock proteins and stress tolerance. In: Morimoto RI, Tissieres A, Georgopoulos C (eds) Biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp 457-494
    • (1994) Biology of Heat Shock Proteins and Molecular Chaperones , pp. 457-494
    • Parsell, D.A.1    Lindquist, S.2
  • 143
    • 0029875028 scopus 로고    scopus 로고
    • Cloning and characterization of a cDNA encoding the collagen-binding stress proteins Hsp47 in zebrafish
    • Pearson DS, Kulyk WM, Kelly GM, Krone PH (1996) Cloning and characterization of a cDNA encoding the collagen-binding stress proteins Hsp47 in zebrafish. DNA Cell Biol 15:263-271
    • (1996) DNA Cell Biol , vol.15 , pp. 263-271
    • Pearson, D.S.1    Kulyk, W.M.2    Kelly, G.M.3    Krone, P.H.4
  • 144
    • 0037023741 scopus 로고    scopus 로고
    • Requirement for a hsp90 chaperone-dependent MEK1/2-ERK pathway for B cell antigen receptor-induced cyclin D2 expression in mature B lymphocytes
    • Piatelli MJ, Doughty C, Chiles TC (2002) Requirement for a hsp90 chaperone-dependent MEK1/2-ERK pathway for B cell antigen receptor-induced cyclin D2 expression in mature B lymphocytes. J Biol Chem 277:12144-12150
    • (2002) J Biol Chem , vol.277 , pp. 12144-12150
    • Piatelli, M.J.1    Doughty, C.2    Chiles, T.C.3
  • 145
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • Picard D (2002) Heat-shock protein 90, a chaperone for folding and regulation. Cell Mol Life Sci 59:1640-1648
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 146
    • 17744372861 scopus 로고    scopus 로고
    • Roles of the heat shock transcription factors in regulation of the heat shock response and beyond
    • Pirkkala L, Nykanen P, Sistonen L (2001) Roles of the heat shock transcription factors in regulation of the heat shock response and beyond. FASEB J 15:1118-1131
    • (2001) FASEB J , vol.15 , pp. 1118-1131
    • Pirkkala, L.1    Nykanen, P.2    Sistonen, L.3
  • 147
    • 38449086073 scopus 로고    scopus 로고
    • Quantitative RT-PCR analysis and immunohistochemical localization of HSP70 in sea bass Dicentrarchus labrax exposed to transport stress
    • Poltronieri C, Maccatrozzo L, Simontacchi C, Bertotto D, Funkenstein B, Patruno M, Radaelli G (2007) Quantitative RT-PCR analysis and immunohistochemical localization of HSP70 in sea bass Dicentrarchus labrax exposed to transport stress. Eur J Histochem 51:125-135
    • (2007) Eur J Histochem , vol.51 , pp. 125-135
    • Poltronieri, C.1    MacCatrozzo, L.2    Simontacchi, C.3    Bertotto, D.4    Funkenstein, B.5    Patruno, M.6    Radaelli, G.7
  • 149
    • 33745749328 scopus 로고    scopus 로고
    • Chaperone network in the yeast cytosol: HSP110 is revealed as an HSP70 nucleotide exchange factor
    • Raviol H, Sadlish H, Rodriguez F, Mayer MP, Bukau B (2006) Chaperone network in the yeast cytosol: HSP110 is revealed as an HSP70 nucleotide exchange factor. EMBO J 25: 2510-2518
    • (2006) EMBO J , vol.25 , pp. 2510-2518
    • Raviol, H.1    Sadlish, H.2    Rodriguez, F.3    Mayer, M.P.4    Bukau, B.5
  • 150
    • 0027130806 scopus 로고
    • Biochemical indicators of oxidative stress in fish from polluted littoral areas
    • Rodriguez-Ariza A, Peinado J, Pueyo C, Lopez-Barea J (1993) Biochemical indicators of oxidative stress in fish from polluted littoral areas. Can J Fish Aquat Sci 50:2568-2573
    • (1993) Can J Fish Aquat Sci , vol.50 , pp. 2568-2573
    • Rodriguez-Ariza, A.1    Peinado, J.2    Pueyo, C.3    Lopez-Barea, J.4
  • 151
    • 14644435819 scopus 로고    scopus 로고
    • Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms
    • Rohde M, Daugaard M, Jensen MH, Helin K, Nylandsted J, Jattela M (2005) Members of the heat-shock protein 70 family promote cancer cell growth by distinct mechanisms. Genes Dev 19:570-582
    • (2005) Genes Dev , vol.19 , pp. 570-582
    • Rohde, M.1    Daugaard, M.2    Jensen, M.H.3    Helin, K.4    Nylandsted, J.5    Jattela, M.6
  • 152
    • 0030266991 scopus 로고    scopus 로고
    • Induction of tolerance to hyperthermia by previous heat shock using human fibroblasts in culture
    • Russotti G, Brieva TA, Toner M, Yarmush ML (1996) Induction of tolerance to hyperthermia by previous heat shock using human fibroblasts in culture. Cryobiology 33:567-580
    • (1996) Cryobiology , vol.33 , pp. 567-580
    • Russotti, G.1    Brieva, T.A.2    Toner, M.3    Yarmush, M.L.4
  • 153
    • 0028483991 scopus 로고
    • Evaluation of heavy-metal ion toxicity in fish cells using a combined stress protein and cytotoxicity assay
    • 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 13:1231-1240
    • (1994) Environ Toxicol Chem , vol.13 , pp. 1231-1240
    • Ryan, J.A.1    Hightower, L.E.2
  • 154
    • 0029681776 scopus 로고    scopus 로고
    • Stress proteins as molecular biomarkers for environmental toxicology
    • Feige U, Morimoto RI, Yahara I, Polla B (eds). Birkhauser Verlag, Basel
    • Ryan JA, Hightower LE (1996) Stress proteins as molecular biomarkers for environmental toxicology. In: Feige U, Morimoto RI, Yahara I, Polla B (eds) Stress-inducible cellular responses. Birkhauser Verlag, Basel, pp 411-424
    • (1996) Stress-inducible Cellular Responses , pp. 411-424
    • Ryan, J.A.1    Hightower, L.E.2
  • 155
    • 0032440847 scopus 로고    scopus 로고
    • Heat shock proteins: Regulations of stress response and apoptosis
    • Samali A, Orrenius S (1998) Heat shock proteins: regulations of stress response and apoptosis. Cell Stress Chaperones 3:228-236
    • (1998) Cell Stress Chaperones , vol.3 , pp. 228-236
    • Samali, A.1    Orrenius, S.2
  • 157
    • 0030734660 scopus 로고    scopus 로고
    • Molecular characterization of a heat shock cognate cDNA of zebrafish, hsc70, and developmental expression of the corresponding transcripts
    • Santacruz H, Vriz S, Angelier N (1997) Molecular characterization of a heat shock cognate cDNA of zebrafish, hsc70, and developmental expression of the corresponding transcripts. Dev Genet 21:223-233
    • (1997) Dev Genet , vol.21 , pp. 223-233
    • Santacruz, H.1    Vriz, S.2    Angelier, N.3
  • 158
    • 0030029444 scopus 로고    scopus 로고
    • Specific localization of zebrafish hsp90α mRNA to myoD-expressing cells suggests a role for hsp90α during normal muscle development
    • Sass JB, Weinberg ES, Krone PH (1996) Specific localization of zebrafish hsp90α mRNA to myoD-expressing cells suggests a role for hsp90α during normal muscle development. Mech Dev 54:195-204
    • (1996) Mech Dev , vol.54 , pp. 195-204
    • Sass, J.B.1    Weinberg, E.S.2    Krone, P.H.3
  • 159
  • 160
    • 0038701730 scopus 로고    scopus 로고
    • Autoregulation of glucocorticoid receptor by cortisol in rainbow trout hepatocytes
    • Sathiyaa R, Vijayan MM (2003) Autoregulation of glucocorticoid receptor by cortisol in rainbow trout hepatocytes. Am J Physiol Cell Physiol 284:C1508-C1515
    • (2003) Am J Physiol Cell Physiol , vol.284
    • Sathiyaa, R.1    Vijayan, M.M.2
  • 165
    • 0031590456 scopus 로고    scopus 로고
    • Geldanamycin-induced destabilization of Raf-1 involves the proteasome
    • Schulte TW, AnWG, Neckers LM(1997) Geldanamycin-induced destabilization of Raf-1 involves the proteasome. Biochem Biophys Res Commun 239:655-659
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 655-659
    • Schulte, T.W.1    An, W.G.2    Neckers, L.M.3
  • 166
    • 0042330503 scopus 로고    scopus 로고
    • HSP10 and HSP60 modulate Bcl-2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells
    • Shan YX, Liu TJ, Su HF, Samsamshariat A, Mestril R, Wang PH (2003) HSP10 and HSP60 modulate Bcl-2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells. J Mol Cell Cardiol 35:1135-1143
    • (2003) J Mol Cell Cardiol , vol.35 , pp. 1135-1143
    • Shan, Y.X.1    Liu, T.J.2    Su, H.F.3    Samsamshariat, A.4    Mestril, R.5    Wang, P.H.6
  • 167
    • 33744939176 scopus 로고    scopus 로고
    • Oxidative stress response of European flounder (Platichthys flesus) to cadmium determined by a custom cDNA microarray
    • Sheader DL, Williams TD, Lyons BP, Chipman JK (2006) Oxidative stress response of European flounder (Platichthys flesus) to cadmium determined by a custom cDNA microarray. Mar Environ Res 62:33-44
    • (2006) Mar Environ Res , vol.62 , pp. 33-44
    • Sheader, D.L.1    Williams, T.D.2    Lyons, B.P.3    Chipman, J.K.4
  • 168
    • 0346401425 scopus 로고    scopus 로고
    • The role of biomarkers in the health assessment of aquatic ecosystems
    • Sherry JP (2003) The role of biomarkers in the health assessment of aquatic ecosystems. Aquat Ecosys Health Manage 6:423-440
    • (2003) Aquat Ecosys Health Manage , vol.6 , pp. 423-440
    • Sherry, J.P.1
  • 169
    • 0000375530 scopus 로고    scopus 로고
    • Characterization of the heat shock protein response of Atlantic salmon (Salmo salar)
    • Smith TR, Tremblay GC, Bradley TM (1999) Characterization of the heat shock protein response of Atlantic salmon (Salmo salar). Fish Physiol Biochem 20:279-292
    • (1999) Fish Physiol Biochem , vol.20 , pp. 279-292
    • Smith, T.R.1    Tremblay, G.C.2    Bradley, T.M.3
  • 172
    • 0242574386 scopus 로고    scopus 로고
    • The evolutionary and ecological role of heat shock proteins
    • Sorensen JG, Kristensen TN, Loeschcke V (2003) The evolutionary and ecological role of heat shock proteins. Ecol Lett 6:1025-1037
    • (2003) Ecol Lett , vol.6 , pp. 1025-1037
    • Sorensen, J.G.1    Kristensen, T.N.2    Loeschcke, V.3
  • 173
    • 34248171100 scopus 로고    scopus 로고
    • Studying stress responses in the post-genomic era: Its ecological and evolutionary role
    • Sorensen JG, Loeschcke V (2007) Studying stress responses in the post-genomic era: its ecological and evolutionary role. J Biosci 32:447-456
    • (2007) J Biosci , vol.32 , pp. 447-456
    • Sorensen, J.G.1    Loeschcke, V.2
  • 175
    • 1542718628 scopus 로고    scopus 로고
    • Heat shock proteins in the regulation of apoptosis: New strategies in tumor therapy. A comprehensive review
    • Sreedhar AS, Csermely P (2004) Heat shock proteins in the regulation of apoptosis: new strategies in tumor therapy. A comprehensive review. Pharmacol Ther 101:227-257
    • (2004) Pharmacol Ther , vol.101 , pp. 227-257
    • Sreedhar, A.S.1    Csermely, P.2
  • 176
    • 0036468510 scopus 로고    scopus 로고
    • A cross talk between cellular signaling and cellular redox state during heat-induced apoptosis in a rat histiocytoma
    • Sreedhar AS, Pardhasaradhi BV, Khar A, Srinivas UK (2002) A cross talk between cellular signaling and cellular redox state during heat-induced apoptosis in a rat histiocytoma. Free Radic Biol Med 32:221-227
    • (2002) Free Radic Biol Med , vol.32 , pp. 221-227
    • Sreedhar, A.S.1    Pardhasaradhi, B.V.2    Khar, A.3    Srinivas, U.K.4
  • 177
    • 1642268986 scopus 로고    scopus 로고
    • HSP90 isoforms: Functions, expression and clinical importance
    • Sreedhar AS, Kalmar E, Csermely P, Shen YF (2004) HSP90 isoforms: functions, expression and clinical importance. FEBS Lett 562:11-15
    • (2004) FEBS Lett , vol.562 , pp. 11-15
    • Sreedhar, A.S.1    Kalmar, E.2    Csermely, P.3    Shen, Y.F.4
  • 179
    • 0001273770 scopus 로고    scopus 로고
    • Biomarkers of marine pollution observed in species of mullet living in two eastern Mediterranean harbours
    • Telli Karakoc F, Hewer A, Phillips DH, Gaines AF, Yuregir G (1997) Biomarkers of marine pollution observed in species of mullet living in two eastern Mediterranean harbours. Biomarkers 2:303-309
    • (1997) Biomarkers , vol.2 , pp. 303-309
    • Telli Karakoc, F.1    Hewer, A.2    Phillips, D.H.3    Gaines, A.F.4    Yuregir, G.5
  • 180
    • 0032059117 scopus 로고    scopus 로고
    • Oxidative stress and antioxidants in intestinal disease
    • Thomson A, Hemphill D, Jeejeebhoy KN (1998) Oxidative stress and antioxidants in intestinal disease. Dig Dis 16:152-158
    • (1998) Dig Dis , vol.16 , pp. 152-158
    • Thomson, A.1    Hemphill, D.2    Jeejeebhoy, K.N.3
  • 181
    • 33846879160 scopus 로고    scopus 로고
    • Chemotherapy: Induction of stress responses
    • Tiligada E (2006) Chemotherapy: induction of stress responses. Endocr Relat Cancer 13: S115-S124
    • (2006) Endocr Relat Cancer , vol.13
    • Tiligada, E.1
  • 182
    • 0036330635 scopus 로고    scopus 로고
    • Interspecific- and acclimation-induced variation in levels of heat shock proteins 70 (HSP70) and 90 (HSP90) and heat-shock transcription factor-1 (HSF1) in congeneric marine snails (genus Tegula): Implications for regulation of HSP gene expression
    • Tomanek L, Somero G (2002) Interspecific- and acclimation-induced variation in levels of heat shock proteins 70 (HSP70) and 90 (HSP90) and heat-shock transcription factor-1 (HSF1) in congeneric marine snails (genus Tegula): implications for regulation of HSP gene expression. J Exp Biol 205:677-685
    • (2002) J Exp Biol , vol.205 , pp. 677-685
    • Tomanek, L.1    Somero, G.2
  • 183
    • 0030456796 scopus 로고    scopus 로고
    • Biomonitoring of aquatic pollution with feral eel (Anguilla anguilla). II. Biomarkers: Pollution-induced biochemical responses
    • Van der Oost R, Goksoyr A, Celander M, Heida H, Vermeulen NPE (1996) Biomonitoring of aquatic pollution with feral eel (Anguilla anguilla). II. Biomarkers: pollution-induced biochemical responses. Aquat Toxicol 36:189-222
    • (1996) Aquat Toxicol , vol.36 , pp. 189-222
    • Van Der Oost, R.1    Goksoyr, A.2    Celander, M.3    Heida, H.4    Npe, V.5
  • 184
    • 0028109828 scopus 로고
    • The effects of cortisol on hepatocyte metabolism in rainbow trout: A study using the steroid analogue RU486
    • Vijayan MM, Reddy PK, Leatherland JF, Moon TW (1994) The effects of cortisol on hepatocyte metabolism in rainbow trout: a study using the steroid analogue RU486. Gen Comp Endocrinol 96:75-84
    • (1994) Gen Comp Endocrinol , vol.96 , pp. 75-84
    • Vijayan, M.M.1    Reddy, P.K.2    Leatherland, J.F.3    Moon, T.W.4
  • 185
    • 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 β-naphthoflavone
    • 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 β-naphthoflavone. Life Sci 61:117-127
    • (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
  • 186
    • 0031904901 scopus 로고    scopus 로고
    • Sublethal concentrations of contaminant induce the expression of hepatic heat shock protein 70 in 2 salmonids
    • Vijayan MM, Pereira C, Kruzynski G, Iwama GK (1998) Sublethal concentrations of contaminant induce the expression of hepatic heat shock protein 70 in 2 salmonids. Aquat Toxicol 40: 101-108
    • (1998) Aquat Toxicol , vol.40 , pp. 101-108
    • Vijayan, M.M.1    Pereira, C.2    Kruzynski, G.3    Iwama, G.K.4
  • 188
    • 25844519550 scopus 로고    scopus 로고
    • HSP90 and the chaperoning of cancer
    • Whitesell L, Lindquist SL (2005) HSP90 and the chaperoning of cancer. Nat Rev Cancer 5: 761-772
    • (2005) Nat Rev Cancer , vol.5 , pp. 761-772
    • Whitesell, L.1    Lindquist, S.L.2
  • 189
    • 0035380741 scopus 로고    scopus 로고
    • Influence of season and pollution on the antioxidant defenses of the cichlid fish acara (Geophagus brasiliensis)
    • Wilhelm Filho D, Torres MA, Tribess TB, Pedrosa RC, Soares CH (2001) Influence of season and pollution on the antioxidant defenses of the cichlid fish acara (Geophagus brasiliensis). Braz J Med Biol Res 34:719-726
    • (2001) Braz J Med Biol Res , vol.34 , pp. 719-726
    • Wilhelm Filho, D.1    Torres, M.A.2    Tribess, T.B.3    Pedrosa, R.C.4    Soares, C.H.5
  • 191
    • 33750295388 scopus 로고    scopus 로고
    • Development of the GENIPOL European flounder (Platichthys flesus) microarray and determination of temporal transcriptional responses to cadmium at low dose
    • Williams TD, Diab AM, George SG, Godfrey RE, Sabine V, Conesa A, Minchin SD, Watts PC, Chipman JK (2006) Development of the GENIPOL European flounder (Platichthys flesus) microarray and determination of temporal transcriptional responses to cadmium at low dose. Environ Sci Technol 40:6479-6488
    • (2006) Environ Sci Technol , vol.40 , pp. 6479-6488
    • Williams, T.D.1    Diab, A.M.2    George, S.G.3    Godfrey, R.E.4    Sabine, V.5    Conesa, A.6    Minchin, S.D.7    Watts, P.C.8    Chipman, J.K.9
  • 192
    • 33846250858 scopus 로고    scopus 로고
    • Gene expression responses of European flounder (Platichthys flesus) to 17-beta estradiol
    • Williams TD, Diab AM, George SG, Sabine V, Chipman JK (2007) Gene expression responses of European flounder (Platichthys flesus) to 17-beta estradiol. Toxicol Lett 168:236-248
    • (2007) Toxicol Lett , vol.168 , pp. 236-248
    • Williams, T.D.1    Diab, A.M.2    George, S.G.3    Sabine, V.4    Chipman, J.K.5
  • 195
    • 0032875601 scopus 로고    scopus 로고
    • Identification of differentially expressed genes in Con A-activated carp (Cyprinus carpio L.) leucocytes
    • Yin Z, He JY, Gong Z, Lam TJ, Sin YM (1999) Identification of differentially expressed genes in Con A-activated carp (Cyprinus carpio L.) leucocytes. Comp Biochem Physiol B Biochem Mol Biol 124:41-50
    • (1999) Comp Biochem Physiol B Biochem Mol Biol , vol.124 , pp. 41-50
    • Yin, Z.1    He, J.Y.2    Gong, Z.3    Lam, T.J.4    Sin, Y.M.5
  • 196
    • 0035939668 scopus 로고    scopus 로고
    • HSP90: A specialized but essential protein-folding tool
    • Young JC, Moarefi I, Hartl FU (2001) HSP90: a specialized but essential protein-folding tool. J Cell Biol 154:267-273
    • (2001) J Cell Biol , vol.154 , pp. 267-273
    • Young, J.C.1    Moarefi, I.2    Hartl, F.U.3
  • 197
    • 0026518440 scopus 로고
    • Molecular cloning and characterization of a constitutively expressed heat shock cognate hsc71 gene from rainbow trout
    • Zafarullah M, Wisniewski J, Shworak NW, Schieman S, Misra S, Gedamu L (1992) Molecular cloning and characterization of a constitutively expressed heat shock cognate hsc71 gene from rainbow trout. Eur J Biochem 204:893-900
    • (1992) Eur J Biochem , vol.204 , pp. 893-900
    • Zafarullah, M.1    Wisniewski, J.2    Shworak, N.W.3    Schieman, S.4    Misra, S.5    Gedamu, L.6
  • 198
    • 20544446881 scopus 로고    scopus 로고
    • HSP90-Akt phosphorylates ASK1 and inhibits ASK1-mediated apoptosis
    • Zhang R, Luo D, Miao R, Bai L, Ge Q, Sessa WC, Min W (2005) HSP90-Akt phosphorylates ASK1 and inhibits ASK1-mediated apoptosis. Oncogene 24:3954-3963
    • (2005) Oncogene , vol.24 , pp. 3954-3963
    • Zhang, R.1    Luo, D.2    Miao, R.3    Bai, L.4    Ge, Q.5    Sessa, W.C.6    Min, W.7
  • 199
    • 0031868230 scopus 로고    scopus 로고
    • Correlation between glutathione oxidation and trimerization of heat shock factor 1, an early step in stress induction of the HSP response
    • Zou J, Salminien WF, Roberts SM, Voellmy R (1998) Correlation between glutathione oxidation and trimerization of heat shock factor 1, an early step in stress induction of the HSP response. Cell Stress Chaperones 3:130-141
    • (1998) Cell Stress Chaperones , vol.3 , pp. 130-141
    • Zou, J.1    Salminien, W.F.2    Roberts, S.M.3    Voellmy, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.