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Volumn 126, Issue 1, 1996, Pages 65-75

Interspecific variation in thermal denaturation of proteins in the congeneric mussels Mytilus trossulus and M. galloprovincialis: Evidence from the heat-shock response and protein ubiquitination

Author keywords

[No Author keywords available]

Indexed keywords

MYTILUS EDULIS; MYTILUS GALLOPROVINCIALIS; MYTILUS TROSSULUS;

EID: 0029783164     PISSN: 00253162     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00571378     Document Type: Article
Times cited : (193)

References (72)
  • 1
    • 0022455603 scopus 로고
    • Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes
    • NY
    • Ananthan J, Goldberg AL, Voellmy R (1986) Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes. Science, NY 232: 522-524
    • (1986) Science , vol.232 , pp. 522-524
    • Ananthan, J.1    Goldberg, A.L.2    Voellmy, R.3
  • 2
    • 0027954495 scopus 로고
    • Heat-shock proteins as molecular chaperones
    • Becker J, Craig EA (1994) Heat-shock proteins as molecular chaperones. Eur J Biochem 219: 11-23
    • (1994) Eur J Biochem , vol.219 , pp. 11-23
    • Becker, J.1    Craig, E.A.2
  • 3
    • 0025303147 scopus 로고
    • Interaction of hsp70 with newly synthesized proteins: Implications for protein folding and assembly
    • NY
    • Beckmann RP, Mizzen LE, Welch WJ (1990) Interaction of hsp70 with newly synthesized proteins: implications for protein folding and assembly. Science, NY 248: 850-854
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.E.2    Welch, W.J.3
  • 4
    • 0022490771 scopus 로고
    • Catabolism of intracellular proteins: Molecular aspects
    • Beynon RJ, Bond JS (1986) Catabolism of intracellular proteins: molecular aspects. Am J Physiol 251: C141-C152
    • (1986) Am J Physiol , vol.251
    • Beynon, R.J.1    Bond, J.S.2
  • 6
    • 0024110459 scopus 로고
    • Thermotolerance and synthesis of heat shock proteins: These responses are present in Hydra attenuata but absent in Hydra oligactis
    • Bosch TCG, Krylow SM, Bode HR, Steele RE (1988) Thermotolerance and synthesis of heat shock proteins: these responses are present in Hydra attenuata but absent in Hydra oligactis. Proc natn Acad Sci USA 85: 7927-7931
    • (1988) Proc Natn Acad Sci USA , vol.85 , pp. 7927-7931
    • Bosch, T.C.G.1    Krylow, S.M.2    Bode, H.R.3    Steele, R.E.4
  • 7
    • 0025302387 scopus 로고
    • Accumulation, stability and localisation of a major chloroplast heat-shock protein
    • Chen Q, Lauzon LM, De Rocher AE, Vierling E (1990) Accumulation, stability and localisation of a major chloroplast heat-shock protein. J Cell Biol 110: 1873-1883
    • (1990) J Cell Biol , vol.110 , pp. 1873-1883
    • Chen, Q.1    Lauzon, L.M.2    De Rocher, A.E.3    Vierling, E.4
  • 8
    • 0023142971 scopus 로고
    • Microinjection of ubiquitin: Changes in protein degradation in HeLa cells subjected to heat-shock
    • Carlson N, Rogers S, Rechsteiner M (1987) Microinjection of ubiquitin: changes in protein degradation in HeLa cells subjected to heat-shock. J Cell Biol 104: 547-555
    • (1987) J Cell Biol , vol.104 , pp. 547-555
    • Carlson, N.1    Rogers, S.2    Rechsteiner, M.3
  • 10
    • 0027135040 scopus 로고
    • Kinetic and structural adaptations of cytoplasmic malate dehydrogenases of eastern Pacific abalone (genus Haliotts) from different thermal habitats: Biochemical correlates of biogeographical patterning
    • Dahlhoff E, Somero GN (1993) Kinetic and structural adaptations of cytoplasmic malate dehydrogenases of eastern Pacific abalone (genus Haliotts) from different thermal habitats: biochemical correlates of biogeographical patterning. J exp Biol 185: 137-150
    • (1993) J Exp Biol , vol.185 , pp. 137-150
    • Dahlhoff, E.1    Somero, G.N.2
  • 11
    • 0028395911 scopus 로고
    • Acclimation of the threshold induction temperatures for 70-kDa and 90-kDa heat shock proteins in the fish Gillichthys mirabilis
    • Dietz TJ (1994) Acclimation of the threshold induction temperatures for 70-kDa and 90-kDa heat shock proteins in the fish Gillichthys mirabilis. J exp Biol 188: 333-338
    • (1994) J Exp Biol , vol.188 , pp. 333-338
    • Dietz, T.J.1
  • 12
    • 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 natn Acad Sci USA 89: 3389-3393
    • (1992) Proc Natn Acad Sci USA , vol.89 , pp. 3389-3393
    • Dietz, T.J.1    Somero, G.N.2
  • 14
    • 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
  • 16
    • 0000699069 scopus 로고
    • Molecular chaperone functions of hsp70 and hsp60 in protein folding
    • Morimoto RI, Tissieres A, Georgopoulos C (eds) Cold Spring Harbor Press, New York
    • Frydman J, Hartl FU (1994) Molecular chaperone functions of hsp70 and hsp60 in protein folding. In: Morimoto RI, Tissieres A, Georgopoulos C (eds) The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Press, New York, pp 251-283
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 251-283
    • Frydman, J.1    Hartl, F.U.2
  • 17
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • Frydman J, Nimmesgern E, Ohtsuka E, Hartl FU (1994) Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature, Lond 370: 111-117
    • (1994) Nature, Lond , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, E.3    Hartl, F.U.4
  • 18
    • 0028923827 scopus 로고
    • Heat shock protein synthesis and thermotolerance in Cataglyphis, an ant from the Sahara desert
    • Gehring WJ, Wehner R (1995) Heat shock protein synthesis and thermotolerance in Cataglyphis, an ant from the Sahara desert. Proc natn Acad Sci USA 92: 2994-2998
    • (1995) Proc Natn Acad Sci USA , vol.92 , pp. 2994-2998
    • Gehring, W.J.1    Wehner, R.2
  • 19
    • 0028066397 scopus 로고
    • PCR-based detection of mtDNA haplotypes of native and invading mussels on the northeastern Pacific coast: Latitudinal pattern of invasion
    • Geller JB, Carlton JT, Powers DA (1994) PCR-based detection of mtDNA haplotypes of native and invading mussels on the northeastern Pacific coast: latitudinal pattern of invasion. Mar Biol 119: 243-249
    • (1994) Mar Biol , vol.119 , pp. 243-249
    • Geller, J.B.1    Carlton, J.T.2    Powers, D.A.3
  • 20
    • 0022344755 scopus 로고
    • Production of abnormal proteins in E. coli stimulates transcription of Ion and other heat shock genes
    • Goff SA, Goldberg AL (1985) Production of abnormal proteins in E. coli stimulates transcription of Ion and other heat shock genes. Cell 41: 587-595
    • (1985) Cell , vol.41 , pp. 587-595
    • Goff, S.A.1    Goldberg, A.L.2
  • 21
    • 0001974942 scopus 로고
    • Systematics and geographic distribution of Mytilus
    • Gosling E (ed) Elsevier Science Publishers B.V., Amsterdam
    • Gosling EM (1992) Systematics and geographic distribution of Mytilus. In: Gosling E (ed) The mussel Mytilus: ecology, physiology, genetics and culture. Elsevier Science Publishers B.V., Amsterdam, pp 1-20
    • (1992) The Mussel Mytilus: Ecology, Physiology, Genetics and Culture , pp. 1-20
    • Gosling, E.M.1
  • 22
    • 0002771750 scopus 로고
    • Electrophoretic and functional enzymic evolution in four species of eastern Pacific barracudas from different thermal environments
    • Graves JE, Somero GN (1982) Electrophoretic and functional enzymic evolution in four species of eastern Pacific barracudas from different thermal environments. Evolution 36: 97-106
    • (1982) Evolution , vol.36 , pp. 97-106
    • Graves, J.E.1    Somero, G.N.2
  • 23
    • 0022379602 scopus 로고
    • The immunochemical detection and quantification of intracellular ubiquitin-protein conjugates
    • Haas AL, Bright PM (1985) The immunochemical detection and quantification of intracellular ubiquitin-protein conjugates. J biol Chem 260: 12464-12473
    • (1985) J Biol Chem , vol.260 , pp. 12464-12473
    • Haas, A.L.1    Bright, P.M.2
  • 24
    • 0000547891 scopus 로고
    • Protein turnover: A functional appraisal
    • Hawkins AJS (1991) Protein turnover: a functional appraisal. Funct Ecol 5: 222-233
    • (1991) Funct Ecol , vol.5 , pp. 222-233
    • Hawkins, A.J.S.1
  • 25
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko A, Ciechanover A (1992) The ubiquitin system for protein degradation. A Rev Biochem 61: 761-807
    • (1992) A Rev Biochem , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 26
    • 0019258079 scopus 로고
    • Cultured animal cells exposed to amino acid analogues or puromycin rapidly synthesize several polypeptides
    • Hightower LE (1980) Cultured animal cells exposed to amino acid analogues or puromycin rapidly synthesize several polypeptides. J Cell Physiol 102: 407-424
    • (1980) J Cell Physiol , vol.102 , pp. 407-424
    • Hightower, L.E.1
  • 27
    • 0027953136 scopus 로고
    • Genetics of physiological differentiation within the marine mussel genus Mytilus
    • Hilbish TJ, Bayne BL, Day A (1994) Genetics of physiological differentiation within the marine mussel genus Mytilus. Evolution 48: 267-286
    • (1994) Evolution , vol.48 , pp. 267-286
    • Hilbish, T.J.1    Bayne, B.L.2    Day, A.3
  • 28
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser M (1995) Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr Opinion Cell Biol 7: 215-223
    • (1995) Curr Opinion Cell Biol , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 29
    • 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
  • 30
    • 0030466706 scopus 로고    scopus 로고
    • Protein ubiquitination and stress protein synthesis in Mytilus trossulus occurs during recovery from tidal emersion
    • in press
    • Hofmann GE, Somero GN (1996) Protein ubiquitination and stress protein synthesis in Mytilus trossulus occurs during recovery from tidal emersion. Molec mar Biol Biotechnol (in press)
    • (1996) Molec Mar Biol Biotechnol
    • Hofmann, G.E.1    Somero, G.N.2
  • 31
    • 0000346071 scopus 로고
    • Molecular responses of plants to an increased incidence of heat shock
    • Howarth CJ (1991) Molecular responses of plants to an increased incidence of heat shock. Pl. Cell Envir 14: 831-841
    • (1991) Pl. Cell Envir , vol.14 , pp. 831-841
    • Howarth, C.J.1
  • 32
    • 0002923619 scopus 로고
    • Physiological consequences of habitat selection
    • Huey RB (1991) Physiological consequences of habitat selection. Am Nat 137: S91-S115
    • (1991) Am Nat , vol.137
    • Huey, R.B.1
  • 33
    • 0029444959 scopus 로고
    • Interspecific variations in adhesive protein sequences of Mytilus edulis. M. galloprovincialis, and M. trossulus
    • Woods Hole
    • Inoue K, Waite JH, Matsuoka M, Odo S, Harayama S (1995) Interspecific variations in adhesive protein sequences of Mytilus edulis. M. galloprovincialis, and M. trossulus. Biol Bull mar biol Lab. Woods Hole 189: 370-375
    • (1995) Biol Bull Mar Biol Lab , vol.189 , pp. 370-375
    • Inoue, K.1    Waite, J.H.2    Matsuoka, M.3    Odo, S.4    Harayama, S.5
  • 34
    • 0001476257 scopus 로고
    • The genetics and taxonomy of species in the genus Mytilus
    • Amsterdam
    • Koehn RK (1991) The genetics and taxonomy of species in the genus Mytilus. Aquaculture, Amsterdam 94: 125-145
    • (1991) Aquaculture , vol.94 , pp. 125-145
    • Koehn, R.K.1
  • 35
    • 0028252932 scopus 로고
    • Costs and benefits of activation of the heat shock response in Drosophila melanogaster
    • Krebs RA, Loeschcke V (1994a) Costs and benefits of activation of the heat shock response in Drosophila melanogaster. Funct Ecol 8: 730-737
    • (1994) Funct Ecol , vol.8 , pp. 730-737
    • Krebs, R.A.1    Loeschcke, V.2
  • 36
    • 0028161619 scopus 로고
    • Effects of exposure to short-term heat stress on fitness components in Drosophila melanogaster
    • Krebs RA, Loeschcke V (1994b) Effects of exposure to short-term heat stress on fitness components in Drosophila melanogaster. J evolut Biol 7: 39-49
    • (1994) J Evolut Biol , vol.7 , pp. 39-49
    • Krebs, R.A.1    Loeschcke, V.2
  • 37
    • 0022462428 scopus 로고
    • An ancient developmental induction: Heat-shock proteins induced in sporulation and oogenesis
    • NY
    • Kurtz S, Rossi J, Petko L, Lindquist S (1986) An ancient developmental induction: heat-shock proteins induced in sporulation and oogenesis. Science, NY 231: 1154-1157
    • (1986) Science , vol.231 , pp. 1154-1157
    • Kurtz, S.1    Rossi, J.2    Petko, L.3    Lindquist, S.4
  • 38
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli EK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, Lond 227: 680-685
    • (1970) Nature, Lond , vol.227 , pp. 680-685
    • Laemmli, E.K.1
  • 39
    • 0020074070 scopus 로고
    • Synthesis and degradation of heat shock proteins during development and decay of thermotolerance
    • Landry J, Bernier D, Chretien P, Nicole LM, Tanguay RM, Marceau N (1982) Synthesis and degradation of heat shock proteins during development and decay of thermotolerance. Cancer Res 42: 2457-2461
    • (1982) Cancer Res , vol.42 , pp. 2457-2461
    • Landry, J.1    Bernier, D.2    Chretien, P.3    Nicole, L.M.4    Tanguay, R.M.5    Marceau, N.6
  • 40
    • 0026596223 scopus 로고
    • Successive action of Dnak, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer T, Lu C, Echols H, Flanagan J, Hayer MK (1992) Successive action of Dnak, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature, Lond 356: 683-689
    • (1992) Nature, Lond , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5
  • 41
    • 0026073457 scopus 로고
    • Thermal response of rat fibroblasts stably transfected with the human 70-kDa heat shock protein-encoding gene
    • Li GC, Li LG, Liu YK, Mak JY, Chen LL (1991) Thermal response of rat fibroblasts stably transfected with the human 70-kDa heat shock protein-encoding gene. Proc natn Acad Sci USA 88: 1681-1685
    • (1991) Proc Natn 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
  • 42
    • 0029138519 scopus 로고
    • Thermal adaptation of cytoplasmic malate dehydrogenases of eastern Pacific barracuda (Sphyraena spp): The role of differential isoenzyme expression
    • Lin JJ, Somero GN (1995) Thermal adaptation of cytoplasmic malate dehydrogenases of eastern Pacific barracuda (Sphyraena spp): the role of differential isoenzyme expression. J exp Biol 198: 551-560
    • (1995) J Exp Biol , vol.198 , pp. 551-560
    • Lin, J.J.1    Somero, G.N.2
  • 43
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist S (1986) The heat-shock response. A Rev Biochem 55: 1151-1191
    • (1986) A Rev Biochem , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 44
    • 0002971496 scopus 로고
    • Possible ecological responses to global climate change: Nearshore benthic biota of northeastern Pacific coastal ecosystems
    • Mooney HA, Fuentes ER, Kronberg BI (eds) Academic Press, New York
    • Lubchenco J, Navarrete SA, Tissot BN, Castilla JC (1993) Possible ecological responses to global climate change: nearshore benthic biota of northeastern Pacific coastal ecosystems. In: Mooney HA, Fuentes ER, Kronberg BI (eds) Earth system responses to global change. Academic Press, New York, pp 147-166
    • (1993) Earth System Responses to Global Change , pp. 147-166
    • Lubchenco, J.1    Navarrete, S.A.2    Tissot, B.N.3    Castilla, J.C.4
  • 45
    • 0000475320 scopus 로고
    • The mussels Mytilus galloprovincialis and M. trossulus on the Pacific coast of North America
    • McDonald JH, Koehn RK (1988) The mussels Mytilus galloprovincialis and M. trossulus on the Pacific coast of North America. Mar Biol 99: 111-118
    • (1988) Mar Biol , vol.99 , pp. 111-118
    • McDonald, J.H.1    Koehn, R.K.2
  • 46
    • 0001282088 scopus 로고
    • Allozymes and morphometric characters of three species of Mytilus in the Northern and Southern Hemispheres
    • McDonald JH, Seed R, Koehn RK (1991) Allozymes and morphometric characters of three species of Mytilus in the Northern and Southern Hemispheres. Mar Biol 111: 323-333
    • (1991) Mar Biol , vol.111 , pp. 323-333
    • McDonald, J.H.1    Seed, R.2    Koehn, R.K.3
  • 47
    • 0025369515 scopus 로고
    • A comparative study of the thermal stability of the vertebrate eye lens: Antarctic fish to the desert iguana
    • McFall-Ngai MJ, Horwitz J (1990) A comparative study of the thermal stability of the vertebrate eye lens: antarctic fish to the desert iguana. Expl Eye Res 50: 703-709
    • (1990) Expl Eye Res , vol.50 , pp. 703-709
    • McFall-Ngai, M.J.1    Horwitz, J.2
  • 48
    • 0023924166 scopus 로고
    • Characterization of the thermotolerant cell. I. Effects on protein synthesis activity and the regulation of heat-shock protein 70 expression
    • Mizzen LA, Welch WJ (1988) Characterization of the thermotolerant cell. I. Effects on protein synthesis activity and the regulation of heat-shock protein 70 expression. J biol Chem 106: 1105-1116
    • (1988) J Biol Chem , vol.106 , pp. 1105-1116
    • Mizzen, L.A.1    Welch, W.J.2
  • 49
    • 0027522356 scopus 로고
    • Cells in stress: Transcriptional activation of heat shock genes
    • NY
    • Morimoto RI (1993) Cells in stress: transcriptional activation of heat shock genes. Science, NY 259: 1409-1410
    • (1993) Science , vol.259 , pp. 1409-1410
    • Morimoto, R.I.1
  • 52
    • 0026028987 scopus 로고
    • Synthesis of heat shock proteins in the isolated fin of the medaka, Oryzias latipes, acclimated to various temperatures
    • Oda S, Mitani H, Naruse K, Shima A (1991) Synthesis of heat shock proteins in the isolated fin of the medaka, Oryzias latipes, acclimated to various temperatures. Comp Biochem Physiol 98B: 587-591
    • (1991) Comp Biochem Physiol , vol.98 B , pp. 587-591
    • Oda, S.1    Mitani, H.2    Naruse, K.3    Shima, A.4
  • 53
    • 0023087430 scopus 로고
    • Effect of heat shock on protein degradation in mammalian cells: Involvement of the ubiquitin system
    • Parag HA, Raboy B, Kulka RG (1987) Effect of heat shock on protein degradation in mammalian cells: involvement of the ubiquitin system. EMBO J 6: 55-61
    • (1987) EMBO J , vol.6 , pp. 55-61
    • Parag, H.A.1    Raboy, B.2    Kulka, R.G.3
  • 54
  • 55
    • 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. A Rev Genet 27: 437-496
    • (1993) A Rev Genet , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 56
    • 0000675009 scopus 로고
    • Heat shock proteins and stress tolerance
    • Morimoto RI, Tissieres A, Georgopoulos C (eds) Cold Spring Harbor Press, New York
    • Parsell DA, Lindquist S (1994) Heat shock proteins and stress tolerance. In: Morimoto RI, Tissieres A, Georgopoulos C (eds) The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Press, New York, pp 457-494
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 457-494
    • Parsell, D.A.1    Lindquist, S.2
  • 57
    • 0027925666 scopus 로고
    • The role of heat-shock proteins in thermotolerance
    • Ser B
    • Parsell DA, Taulien J, Lindquist S (1993) The role of heat-shock proteins in thermotolerance. Phil Trans R Soc (Ser B) 339: 279-286
    • (1993) Phil Trans R Soc , vol.339 , pp. 279-286
    • Parsell, D.A.1    Taulien, J.2    Lindquist, S.3
  • 58
    • 0029809327 scopus 로고
    • Distribution of male and female mtDNA lineages in populations of blue mussels. Mytilus trossulus and M. galloprovincialis, along the Pacific coast of North America
    • Rawson PD, Hilbish TJ (1995) Distribution of male and female mtDNA lineages in populations of blue mussels. Mytilus trossulus and M. galloprovincialis, along the Pacific coast of North America. Mar Biol 124: 245-250
    • (1995) Mar Biol , vol.124 , pp. 245-250
    • Rawson, P.D.1    Hilbish, T.J.2
  • 59
    • 0023505078 scopus 로고
    • Ubiquitin-mediated pathways for intracellular proteolysis
    • Rechsteiner M (1987) Ubiquitin-mediated pathways for intracellular proteolysis. A Rev Cell Biol 3: 1-30
    • (1987) A Rev Cell Biol , vol.3 , pp. 1-30
    • Rechsteiner, M.1
  • 61
    • 0025193343 scopus 로고
    • Hsp104 required for induced thermotolerance
    • NY
    • Sanchez Y, Lindquist SL (1990) Hsp104 required for induced thermotolerance. Science, NY 248: 1112-1115
    • (1990) Science , vol.248 , pp. 1112-1115
    • Sanchez, Y.1    Lindquist, S.L.2
  • 62
    • 0000107718 scopus 로고
    • Characterization of the stress protein response in two species of Collisella limpets with different temperature tolerances
    • 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 Zoöl 64: 1471-1489
    • (1991) Physiol Zoöl , vol.64 , pp. 1471-1489
    • Sanders, B.M.1    Hope, C.2    Pascoe, V.M.3    Martin, L.S.4
  • 64
    • 0000890433 scopus 로고
    • Genetic population structure of a species' complex of blue mussels (Mytilus spp.)
    • Sarver SK, Foltz DW (1993) Genetic population structure of a species' complex of blue mussels (Mytilus spp.). Mar Biol 117: 105-112
    • (1993) Mar Biol , vol.117 , pp. 105-112
    • Sarver, S.K.1    Foltz, D.W.2
  • 65
    • 0242376218 scopus 로고
    • The genetics of California populations of the blue mussel: Further evidence for the existence of electrophoretically distinguishable species or subspecies
    • Sarver SK, Loudenslager EJ (1991) The genetics of California populations of the blue mussel: further evidence for the existence of electrophoretically distinguishable species or subspecies. Biochem Syst Ecol 19: 183-188
    • (1991) Biochem Syst Ecol , vol.19 , pp. 183-188
    • Sarver, S.K.1    Loudenslager, E.J.2
  • 66
    • 0027427986 scopus 로고
    • DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schröder H, Langer T, Hartl FU, Bukau B (1993) DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J 12: 4137-4144
    • (1993) EMBO J , vol.12 , pp. 4137-4144
    • Schröder, H.1    Langer, T.2    Hartl, F.U.3    Bukau, B.4
  • 67
    • 0000343345 scopus 로고
    • Systematics, evolution and distribution of mussels belonging to the genus Mytilus: An overview
    • Seed R (1992) Systematics, evolution and distribution of mussels belonging to the genus Mytilus: an overview. Am malac Bull 9: 123-137
    • (1992) Am Malac Bull , vol.9 , pp. 123-137
    • Seed, R.1
  • 68
    • 0028154168 scopus 로고
    • Expression of low molecular weight HSP 70 related polypeptides from the symbiotic sea anemone Anemonia viridis Forskall in response to heat shock
    • 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 Forskall in response to heat shock. J exp mar Biol Ecol 179: 179-193
    • (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
  • 69
    • 0025787706 scopus 로고
    • Changes in Hsp70 alter thermotolerance and heat-shock regulation in Drosophila
    • 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: 1106-1120
    • (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
  • 70
    • 0028949615 scopus 로고
    • Proteins and temperature
    • Somero GN (1995) Proteins and temperature. A Rev Physiol 57: 43-68
    • (1995) A Rev Physiol , vol.57 , pp. 43-68
    • Somero, G.N.1
  • 71
    • 0020359569 scopus 로고
    • Polymerization thermodynamics and structural stabilities of skeletal muscle actins from vertebrates adapted to different temperatures and pressures
    • Pa
    • Swezey RR, Somero GN (1982) Polymerization thermodynamics and structural stabilities of skeletal muscle actins from vertebrates adapted to different temperatures and pressures. Biochemistry (Am chem Soc) Easton, Pa 21: 4496-4503
    • (1982) Biochemistry (Am Chem Soc) Easton , vol.21 , pp. 4496-4503
    • Swezey, R.R.1    Somero, G.N.2
  • 72
    • 0000228567 scopus 로고
    • Latitudinal effects on physiological properties of animal populations
    • Vernberg FJ (1962) Latitudinal effects on physiological properties of animal populations. A Rev Physiol 24: 517-546
    • (1962) A Rev Physiol , vol.24 , pp. 517-546
    • Vernberg, F.J.1


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