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Volumn 41, Issue 4, 2013, Pages 683-693

Expression of heat shock protein 90 genes during early development and infection in Megalobrama amblycephala and evidence for adaptive evolution in teleost

Author keywords

Adaptive selection; Aeromonas hydrophila; Heat shock protein 90; Megalobrama amblycephala; Teleost

Indexed keywords

COMPLEMENTARY DNA; HEAT SHOCK PROTEIN 90; MESSENGER RNA;

EID: 84883413551     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2013.08.007     Document Type: Article
Times cited : (22)

References (63)
  • 2
    • 0038325738 scopus 로고    scopus 로고
    • Migratory history of the three spine stickleback Gasterosteus aculeatus
    • Arial T., Goto A., Miyazaki N. Migratory history of the three spine stickleback Gasterosteus aculeatus. Ichthyol. Res. 2003, 50:9-14.
    • (2003) Ichthyol. Res. , vol.50 , pp. 9-14
    • Arial, T.1    Goto, A.2    Miyazaki, N.3
  • 3
    • 27844464029 scopus 로고    scopus 로고
    • Food-deprivation induces HSP70 and Hsp90 protein expression in larval gilthead sea bream and rainbow trout
    • Cara J.B., Aluru N., Moyano F.J., Vijayan M.M. Food-deprivation induces HSP70 and Hsp90 protein expression in larval gilthead sea bream and rainbow trout. Comp. Biochem. Physiol. B 2005, 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
  • 4
    • 33746269654 scopus 로고    scopus 로고
    • HSP70 gene expression in Mytilus galloprovincialis hemocytes is triggered by moderate heat shock and Vibrio anguillarum, but not by V-splendidus or Micrococcus lysodeikticus
    • Cellura C., Toubiana M., Parrinello N., Roch P. HSP70 gene expression in Mytilus galloprovincialis hemocytes is triggered by moderate heat shock and Vibrio anguillarum, but not by V-splendidus or Micrococcus lysodeikticus. Dev. Comp. Immunol. 2006, 30:984-997.
    • (2006) Dev. Comp. Immunol. , vol.30 , pp. 984-997
    • Cellura, C.1    Toubiana, M.2    Parrinello, N.3    Roch, P.4
  • 5
    • 0034027266 scopus 로고    scopus 로고
    • Expression of heat shock proteins in turtle and mammal hearts: relationship to anoxia tolerance
    • Chang J., Knowlton A.A., Wasser J.S. Expression of heat shock proteins in turtle and mammal hearts: relationship to anoxia tolerance. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2000, 278:R209-R214.
    • (2000) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.278
    • Chang, J.1    Knowlton, A.A.2    Wasser, J.S.3
  • 6
    • 28644443855 scopus 로고    scopus 로고
    • The Hsp90 family of genes in the human genome: insights into their divergence and evolution
    • Chen B., Piel W.H., Gui L., Bruford E., Momteiro A. The Hsp90 family of genes in the human genome: insights into their divergence and evolution. Genomics 2005, 86:627-637.
    • (2005) Genomics , vol.86 , pp. 627-637
    • Chen, B.1    Piel, W.H.2    Gui, L.3    Bruford, E.4    Momteiro, A.5
  • 7
    • 33746660802 scopus 로고    scopus 로고
    • Comparative genomics and evolution of the Hsp90 family of genes across all kingdoms of organisms
    • Chen B., Zhong D., Monteiro A. Comparative genomics and evolution of the Hsp90 family of genes across all kingdoms of organisms. BMC Genom. 2006, 7:156.
    • (2006) BMC Genom. , vol.7 , pp. 156
    • Chen, B.1    Zhong, D.2    Monteiro, A.3
  • 8
    • 77951123244 scopus 로고    scopus 로고
    • Cloning of an orange-spotted grouper Epinephelus coioidesheat shock protein90AB (HSP90AB) and characterization of its expression in response to nodavirus
    • Chen Y.M., Kuo C.E., Wang T.Y., Shie P.S., Wang W.C., Huang S.L., Tsai T.J., Chen P.P., Chen J.C., Chen T.Y. Cloning of an orange-spotted grouper Epinephelus coioidesheat shock protein90AB (HSP90AB) and characterization of its expression in response to nodavirus. Fish Shellfish Immunol. 2010, 28:895-904.
    • (2010) Fish Shellfish Immunol. , vol.28 , pp. 895-904
    • Chen, Y.M.1    Kuo, C.E.2    Wang, T.Y.3    Shie, P.S.4    Wang, W.C.5    Huang, S.L.6    Tsai, T.J.7    Chen, P.P.8    Chen, J.C.9    Chen, T.Y.10
  • 9
    • 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., Prohászka Z., Nardai G. The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol. Ther. 1998, 79:129-168.
    • (1998) Pharmacol. Ther. , vol.79 , pp. 129-168
    • Csermely, P.1    Schnaider, T.2    Soti, C.3    Prohászka, Z.4    Nardai, G.5
  • 10
    • 38649104452 scopus 로고    scopus 로고
    • Heat-shock protein 90α1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos
    • Du S.J., Li H., Bian Y., Zhong Y. Heat-shock protein 90α1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:554-559.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 554-559
    • Du, S.J.1    Li, H.2    Bian, Y.3    Zhong, Y.4
  • 12
    • 0031255704 scopus 로고    scopus 로고
    • Muscle fatigue and induction of stress protein genes: a dual function of reactive oxygen species?
    • Essig D.A., Nosek T.M. Muscle fatigue and induction of stress protein genes: a dual function of reactive oxygen species?. Can. J. Appl. Physiol. 1997, 22:409-428.
    • (1997) Can. J. Appl. Physiol. , vol.22 , pp. 409-428
    • Essig, D.A.1    Nosek, T.M.2
  • 13
    • 77956183479 scopus 로고    scopus 로고
    • FBMA,China Agriculture Press, Beijing, China, pp. 8-10
    • FBMA Chinese Fisheries Year Book 2008, China Agriculture Press, Beijing, China, pp. 8-10.
    • (2008) Chinese Fisheries Year Book
  • 14
    • 0033057848 scopus 로고    scopus 로고
    • Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology
    • Feder M.E., Hofmann G.E. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu. Rev. Physiol. 1999, 61:243-282.
    • (1999) Annu. Rev. Physiol. , vol.61 , pp. 243-282
    • Feder, M.E.1    Hofmann, G.E.2
  • 15
    • 84859121194 scopus 로고    scopus 로고
    • Expression analysis of heat shock genes in skin, spleen and blood of common carp (Cyprinus carpio) after cadmium exposure and hypothermia
    • Ferencz A., Juhász R., Butnariu M., Deér A.K., Varga I.S., Nemcsók J. Expression analysis of heat shock genes in skin, spleen and blood of common carp (Cyprinus carpio) after cadmium exposure and hypothermia. Acta Biol. Hung. 2012, 63:15-25.
    • (2012) Acta Biol. Hung. , vol.63 , pp. 15-25
    • Ferencz, A.1    Juhász, R.2    Butnariu, M.3    Deér, A.K.4    Varga, I.S.5    Nemcsók, J.6
  • 16
    • 79957871514 scopus 로고    scopus 로고
    • Cloning and expression of a heat shock protein (Hsp) 90 gene in the haemocytes of Crassostrea hongkongensis under osmotic stress and bacterial challenge
    • Fu D.K., Chen J.H., Zhang Y., Yu Z.N. Cloning and expression of a heat shock protein (Hsp) 90 gene in the haemocytes of Crassostrea hongkongensis under osmotic stress and bacterial challenge. Fish Shellfish Immunol. 2011, 31:118-125.
    • (2011) Fish Shellfish Immunol. , vol.31 , pp. 118-125
    • Fu, D.K.1    Chen, J.H.2    Zhang, Y.3    Yu, Z.N.4
  • 17
    • 40149107404 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression of heat shock protein 90 gene in the haemocytes of bay scallop Argopecten irradians
    • Gao Q., Zhao J.M., Song L.S., Qiu L.M., Yu Y.D., Zhang H., Ni D.J. Molecular cloning, characterization and expression of heat shock protein 90 gene in the haemocytes of bay scallop Argopecten irradians. Fish Shellfish Immunol. 2008, 24:379-385.
    • (2008) Fish Shellfish Immunol. , vol.24 , pp. 379-385
    • Gao, Q.1    Zhao, J.M.2    Song, L.S.3    Qiu, L.M.4    Yu, Y.D.5    Zhang, H.6    Ni, D.J.7
  • 18
    • 84864697201 scopus 로고    scopus 로고
    • Transcriptome analysis and SSR/SNP markers information of the blunt snout bream (Megalobrama amblycephala)
    • Gao Z.X., Luo W., Liu H., Zeng C., Liu X.L., Yi S.K., Wang W.M. Transcriptome analysis and SSR/SNP markers information of the blunt snout bream (Megalobrama amblycephala). PLoS One 2012, 7:e42637.
    • (2012) PLoS One , vol.7
    • Gao, Z.X.1    Luo, W.2    Liu, H.3    Zeng, C.4    Liu, X.L.5    Yi, S.K.6    Wang, W.M.7
  • 21
    • 0028785298 scopus 로고
    • Phylogenetic analysis of the 90kD heat shock family of protein sequences and an examination of the relationship among animals, plants, and fungi species
    • Gupta R.S. Phylogenetic analysis of the 90kD heat shock family of protein sequences and an examination of the relationship among animals, plants, and fungi species. Mol. Biol. Evol. 1995, 12:1063-1073.
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 1063-1073
    • Gupta, R.S.1
  • 22
    • 33750983940 scopus 로고    scopus 로고
    • The middle domain of Hsp90 acts as a discriminator between different types of client proteins
    • Hawle P., Siepmann M., Harst A., Siderius M., Reusch H.P., Obermann W.M. The middle domain of Hsp90 acts as a discriminator between different types of client proteins. Mol. Cell. Biol. 2006, 26:8385-8395.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8385-8395
    • Hawle, P.1    Siepmann, M.2    Harst, A.3    Siderius, M.4    Reusch, H.P.5    Obermann, W.M.6
  • 24
    • 0034849408 scopus 로고    scopus 로고
    • MRBAYES: Bayesian inference of phylogenetic trees
    • Huelsenbeck J.P., Ronquist F. MRBAYES: Bayesian inference of phylogenetic trees. Bioinformatics 2001, 17:754-755.
    • (2001) Bioinformatics , vol.17 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 25
    • 0034000070 scopus 로고    scopus 로고
    • Regulation of heat shock protein 72kDa and 90kDa in human breast cancer MCA-MB-231 cells
    • Kiang J.G., Gist I.D., Tsokos G.C. Regulation of heat shock protein 72kDa and 90kDa in human breast cancer MCA-MB-231 cells. Mol. Cell. Biochem. 2000, 204:169-178.
    • (2000) Mol. Cell. Biochem. , vol.204 , pp. 169-178
    • Kiang, J.G.1    Gist, I.D.2    Tsokos, G.C.3
  • 26
    • 0017368336 scopus 로고
    • Preponderance of synonymous changes as evidence for the neutral theory of molecular evolution
    • Kimura M. Preponderance of synonymous changes as evidence for the neutral theory of molecular evolution. Nature 1977, 267:275-276.
    • (1977) Nature , vol.267 , pp. 275-276
    • Kimura, M.1
  • 27
    • 0028171452 scopus 로고
    • Hsp90 alpha and Hsp90 beta genes are present in the zebrafish and are differentially regulated in developing embryos
    • Krone P.H., Sass J.B. Hsp90 alpha and Hsp90 beta genes are present in the zebrafish and are differentially regulated in developing embryos. Biochem. Biophys. Res. Commun. 1994, 204:746-752.
    • (1994) Biochem. Biophys. Res. Commun. , vol.204 , pp. 746-752
    • Krone, P.H.1    Sass, J.B.2
  • 28
    • 0024548919 scopus 로고
    • Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are hosphorylated in vitro by casein kinase II
    • Lees-Miller S.P., Anderson C.W. Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are hosphorylated in vitro by casein kinase II. J. Biol. Chem. 1989, 264:2431-2437.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2431-2437
    • Lees-Miller, S.P.1    Anderson, C.W.2
  • 30
    • 84860881643 scopus 로고    scopus 로고
    • Cloning and characterization of the Hsp90 beta gene from Tanichthys albonubes Lin (Cyprinidae): effect of copper and cadmium exposure
    • Liu H.C., Chen H.H., Jing J., Ma X.F. Cloning and characterization of the Hsp90 beta gene from Tanichthys albonubes Lin (Cyprinidae): effect of copper and cadmium exposure. Fish. Physiol. Biochem. 2012, 38:745-756.
    • (2012) Fish. Physiol. Biochem. , vol.38 , pp. 745-756
    • Liu, H.C.1    Chen, H.H.2    Jing, J.3    Ma, X.F.4
  • 32
    • 43149120646 scopus 로고    scopus 로고
    • Molecular characterization, gene expression and transcriptional regulation of cytosolic Hsp90 genes in the flat fish Senegalese sole (Solea senegalensis Kaup)
    • Manchado M., Salas-Leiton E., Infante C., Ponce M., Asensio E., Crespo A., Zuasti E., Cañavate J.P. Molecular characterization, gene expression and transcriptional regulation of cytosolic Hsp90 genes in the flat fish Senegalese sole (Solea senegalensis Kaup). Gene 2008, 416:77-84.
    • (2008) Gene , vol.416 , pp. 77-84
    • Manchado, M.1    Salas-Leiton, E.2    Infante, C.3    Ponce, M.4    Asensio, E.5    Crespo, A.6    Zuasti, E.7    Cañavate, J.P.8
  • 33
    • 38349118581 scopus 로고
    • Organ development of blunt snout bream
    • Meng Q.W., Tang Y.P. Organ development of blunt snout bream. J. Fisheries. China 1986, 10:395-406.
    • (1986) J. Fisheries. China , vol.10 , pp. 395-406
    • Meng, Q.W.1    Tang, Y.P.2
  • 34
    • 0027475243 scopus 로고
    • Hsp90 chaperonins possess ATPase activity and bind heat-shock transcription factors and peptidylprolyl isomerases
    • Nadeau K., Das A., Walsh C.T. Hsp90 chaperonins possess ATPase activity and bind heat-shock transcription factors and peptidylprolyl isomerases. J. Biol. Chem. 1993, 268:1479-1487.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1479-1487
    • Nadeau, K.1    Das, A.2    Walsh, C.T.3
  • 35
    • 0035934077 scopus 로고    scopus 로고
    • Is Aeromonas hydrophila the dominant motile Aeromonas species that causes disease outbreaks in aquaculture production in the Zhejiang Province of China?
    • Nielsen M.E., Hoi L., Schmidt A.S., Qian D., Shimada T., Shen J.Y., Larsen J.L. Is Aeromonas hydrophila the dominant motile Aeromonas species that causes disease outbreaks in aquaculture production in the Zhejiang Province of China?. Dis. Aquat. Organ. 2001, 46:23-29.
    • (2001) Dis. Aquat. Organ. , vol.46 , pp. 23-29
    • Nielsen, M.E.1    Hoi, L.2    Schmidt, A.S.3    Qian, D.4    Shimada, T.5    Shen, J.Y.6    Larsen, J.L.7
  • 37
    • 0033583771 scopus 로고    scopus 로고
    • Sequence features and phylogenetic analysis of the stress protein HSP90AA in chinook salmon (Oncorhynchus tshawytscha), a poikilothermic vertebrate
    • Palmisano A.N., Winton J.R., Dickhoff W.W. Sequence features and phylogenetic analysis of the stress protein HSP90AA in chinook salmon (Oncorhynchus tshawytscha), a poikilothermic vertebrate. Biochem. Biophys. Res. Commun. 1999, 258:784-791.
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 784-791
    • Palmisano, A.N.1    Winton, J.R.2    Dickhoff, W.W.3
  • 38
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou B., Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 1998, 17:4829-4836.
    • (1998) EMBO J. , vol.17 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3    O'Brien, R.4    Ladbury, J.E.5    Piper, P.W.6    Pearl, L.H.7
  • 39
    • 0034255940 scopus 로고    scopus 로고
    • Cloning and characterization of salmon hsp90 cDNA: upregulation by thermal and hyperosmotic stress
    • Pan F., Zarate J.M., Tremblay G.C., Bradley T.M. Cloning and characterization of salmon hsp90 cDNA: upregulation by thermal and hyperosmotic stress. J. Exp. Zool. 2000, 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
  • 40
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl L.H., Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 2006, 75:271-294.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 41
    • 0036810352 scopus 로고    scopus 로고
    • Heat-shock protein 90, a chaperone for folding and regulation
    • Picard D. Heat-shock protein 90, a chaperone for folding and regulation. Cell. Mol. Life Sci. 2002, 59:1640-1648.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1640-1648
    • Picard, D.1
  • 42
    • 45849154165 scopus 로고    scopus 로고
    • JModelTest: phylogenetic model averaging
    • Posada D. JModelTest: phylogenetic model averaging. Mol. Biol. Evol. 2008, 25:1253-1256.
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 1253-1256
    • Posada, D.1
  • 43
    • 21844432419 scopus 로고    scopus 로고
    • Anadromy and the marine migrations of pacific salmon and trout: Rounsefell revisited
    • Quinn T.P., Myers K.W. Anadromy and the marine migrations of pacific salmon and trout: Rounsefell revisited. Rev. Fish. Boil. Fisher. 2004, 14:421-442.
    • (2004) Rev. Fish. Boil. Fisher. , vol.14 , pp. 421-442
    • Quinn, T.P.1    Myers, K.W.2
  • 44
    • 84856531737 scopus 로고    scopus 로고
    • Ischaemia-induced protein ubiquitinylation is differentially accompanied with heat-shock protein 70 expression after naive and preconditioned ischaemia
    • Racay P. Ischaemia-induced protein ubiquitinylation is differentially accompanied with heat-shock protein 70 expression after naive and preconditioned ischaemia. Cell. Mol. Neurobiol. 2012, 32:107-119.
    • (2012) Cell. Mol. Neurobiol. , vol.32 , pp. 107-119
    • Racay, P.1
  • 45
  • 46
    • 0034892432 scopus 로고    scopus 로고
    • Hsp90: chaperoning signal trasduction
    • Richter K., Buchner J. Hsp90: chaperoning signal trasduction. J. Cell. Physiol. 2001, 188:281-290.
    • (2001) J. Cell. Physiol. , vol.188 , pp. 281-290
    • Richter, K.1    Buchner, J.2
  • 48
    • 0037409604 scopus 로고    scopus 로고
    • Evolution of heat shock protein and immunity
    • Robert J. Evolution of heat shock protein and immunity. Dev. Comp. Immunol. 2003, 27:449-464.
    • (2003) Dev. Comp. Immunol. , vol.27 , pp. 449-464
    • Robert, J.1
  • 49
    • 77955277737 scopus 로고    scopus 로고
    • Expression and distribution of three heat shock protein genes under heat shock stress and under exposure to vibrio harveyi in penaeus monodon
    • Rungrassamee W., Leelatanawit R., Jiravanichpaisal P., Klinbunga S., Karoonuthaisiri N. Expression and distribution of three heat shock protein genes under heat shock stress and under exposure to vibrio harveyi in penaeus monodon. Dev. Comp. Immunol. 2010, 34:1082-1089.
    • (2010) Dev. Comp. Immunol. , vol.34 , pp. 1082-1089
    • Rungrassamee, W.1    Leelatanawit, R.2    Jiravanichpaisal, P.3    Klinbunga, S.4    Karoonuthaisiri, N.5
  • 50
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., Hartl F.U., Moarefi I. Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 2000, 101:199-210.
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 51
    • 84871721498 scopus 로고    scopus 로고
    • Structure and functional studies of Leisgmania braziliensis Hsp90
    • Silva K.P., Seraphim T.V., Borges J.C. Structure and functional studies of Leisgmania braziliensis Hsp90. Biochem. Biophys. Acta 2012, 1834:351-361.
    • (2012) Biochem. Biophys. Acta , vol.1834 , pp. 351-361
    • Silva, K.P.1    Seraphim, T.V.2    Borges, J.C.3
  • 52
    • 1542718628 scopus 로고    scopus 로고
    • Heat shock proteins in the regulation of apoptosis: new strategies in tumor therapy. A comprehensive review
    • Sreedhar A.S., Csermely P. Heat shock proteins in the regulation of apoptosis: new strategies in tumor therapy. A comprehensive review. Pharmacol. Ther. 2004, 101:227-257.
    • (2004) Pharmacol. Ther. , vol.101 , pp. 227-257
    • Sreedhar, A.S.1    Csermely, P.2
  • 53
    • 1642268986 scopus 로고    scopus 로고
    • Hsp90 isoforms: functions, expression and clinical importance
    • Sreedhar A.S., Kalmár E., Csermely P., Shen Y.F. Hsp90 isoforms: functions, expression and clinical importance. FEBS Lett. 2004, 562:11-15.
    • (2004) FEBS Lett. , vol.562 , pp. 11-15
    • Sreedhar, A.S.1    Kalmár, E.2    Csermely, P.3    Shen, Y.F.4
  • 54
    • 84855220120 scopus 로고    scopus 로고
    • Quantification of heat shock protein mRNA expression in warm and cold anoxic turtles (Trachemys scripta) using an external RNA control for normalization
    • Stecyk J.A.W., Couturier C.S., Fagernes C.E., Ellefsen S., Nilsson G.E. Quantification of heat shock protein mRNA expression in warm and cold anoxic turtles (Trachemys scripta) using an external RNA control for normalization. Comp. Biochem. Physiol. D 2012, 7:59-72.
    • (2012) Comp. Biochem. Physiol. D , vol.7 , pp. 59-72
    • Stecyk, J.A.W.1    Couturier, C.S.2    Fagernes, C.E.3    Ellefsen, S.4    Nilsson, G.E.5
  • 55
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K., Peterson D., Peterson N., Stecher G., Nei M., Kumar S. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol. 2011, 28:2731-2739.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 56
    • 33845608851 scopus 로고    scopus 로고
    • CDNA cloning, heat shock regulation and development expression of the hsp83 gene in the Mediterranean fruit fly Ceratitis capitata
    • Theodoraki M.A., Mintzas A.C. CDNA cloning, heat shock regulation and development expression of the hsp83 gene in the Mediterranean fruit fly Ceratitis capitata. Insect. Mol. Biol. 2006, 15:839-852.
    • (2006) Insect. Mol. Biol. , vol.15 , pp. 839-852
    • Theodoraki, M.A.1    Mintzas, A.C.2
  • 57
    • 0344654820 scopus 로고    scopus 로고
    • Expression of the 72-kD heat shock protein is induced by ultraviolet A radiation in a human fibrosarcoma cell line
    • Trautinger F., Kokesch C., Klosner G., Knonbler R.M., Kinfas-Mügge I. Expression of the 72-kD heat shock protein is induced by ultraviolet A radiation in a human fibrosarcoma cell line. Exp. Dermatol. 1999, 8:187-192.
    • (1999) Exp. Dermatol. , vol.8 , pp. 187-192
    • Trautinger, F.1    Kokesch, C.2    Klosner, G.3    Knonbler, R.M.4    Kinfas-Mügge, I.5
  • 59
    • 33751004957 scopus 로고    scopus 로고
    • Postembryonic development of Megalobrama skolkovii
    • Wan C.Y., Lin Y.S., Huang D.M. Postembryonic development of Megalobrama skolkovii. J. Lake Sci. 1999, 11:357-362.
    • (1999) J. Lake Sci. , vol.11 , pp. 357-362
    • Wan, C.Y.1    Lin, Y.S.2    Huang, D.M.3
  • 61
    • 34547803197 scopus 로고    scopus 로고
    • PAML 4: phylogenetic analysis by maximum likelihood
    • Yang Z.H. PAML 4: phylogenetic analysis by maximum likelihood. Mol. Biol. Evol. 2007, 24:1586-1591.
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1586-1591
    • Yang, Z.H.1
  • 62
    • 16344378246 scopus 로고    scopus 로고
    • Bayes Empirical Bayes Inference of amino acid sites under positive selection
    • Yang Z.H., Wong W.S., Nielsen R. Bayes Empirical Bayes Inference of amino acid sites under positive selection. Mol. Biol. Evol. 2005, 22:1107-1118.
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 1107-1118
    • Yang, Z.H.1    Wong, W.S.2    Nielsen, R.3
  • 63
    • 84880043601 scopus 로고    scopus 로고
    • Observations on the embryonic development of Megalobrama amblycephala in the fishing areas of Poyang lake
    • Yu P.C., Zhang F.W. Observations on the embryonic development of Megalobrama amblycephala in the fishing areas of Poyang lake. J. Fishery. Sci. China 1998, 5:103-108.
    • (1998) J. Fishery. Sci. China , vol.5 , pp. 103-108
    • Yu, P.C.1    Zhang, F.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.