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Volumn 6, Issue 12, 2011, Pages

The Gln32lys polymorphism in HSP22 of zhikong scallop chlamys farreri is associated with heat tolerance

Author keywords

[No Author keywords available]

Indexed keywords

CITRATE SYNTHASE; GLUTAMINE; HEAT SHOCK PROTEIN 22; HYBRID PROTEIN; LYSINE; CHAPERONE; RECOMBINANT PROTEIN; SMALL HEAT SHOCK PROTEIN;

EID: 82655189164     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0028564     Document Type: Article
Times cited : (13)

References (50)
  • 1
    • 0012608077 scopus 로고    scopus 로고
    • Analysis of the causes of mass mortality of farming Chlamys farreri in summer in coastal areas of Shandong
    • Zhang F, Yang H, (1999) Analysis of the causes of mass mortality of farming Chlamys farreri in summer in coastal areas of Shandong. China Mar Sci 1: 44-47.
    • (1999) China Mar Sci , vol.1 , pp. 44-47
    • Zhang, F.1    Yang, H.2
  • 2
    • 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
  • 3
  • 4
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU, (1996) Molecular chaperones in cellular protein folding. Nature 381: 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 5
    • 0032804190 scopus 로고    scopus 로고
    • Stress and the cell nucleus: dynamics of gene expression and structural reorganization
    • Jolly C, Morimoto R, (1999) Stress and the cell nucleus: dynamics of gene expression and structural reorganization. Gene Expression 7: 261.
    • (1999) Gene Expression , vol.7 , pp. 261
    • Jolly, C.1    Morimoto, R.2
  • 6
    • 3242776825 scopus 로고    scopus 로고
    • Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity
    • Chowdary TK, Raman B, Ramakrishna T, Rao CM, (2004) Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity. Biochem J 381: 379.
    • (2004) Biochem J , vol.381 , pp. 379
    • Chowdary, T.K.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 7
    • 0038797062 scopus 로고    scopus 로고
    • Arabidopsis hot mutants define multiple functions required for acclimation to high temperatures
    • Hong SW, Lee U, Vierling E, (2003) Arabidopsis hot mutants define multiple functions required for acclimation to high temperatures. Plant Physiol 132: 757.
    • (2003) Plant Physiol , vol.132 , pp. 757
    • Hong, S.W.1    Lee, U.2    Vierling, E.3
  • 8
    • 0031700092 scopus 로고    scopus 로고
    • Induced thermotolerance and associated expression of the heat©\shock protein Hsp70 in adult Drosophila melanogaster
    • Dahlgaard J, Loeschcke V, Michalak P, Justesen J, (1998) Induced thermotolerance and associated expression of the heat©\shock protein Hsp70 in adult Drosophila melanogaster. Funct Ecol 12: 786-793.
    • (1998) Funct Ecol , vol.12 , pp. 786-793
    • Dahlgaard, J.1    Loeschcke, V.2    Michalak, P.3    Justesen, J.4
  • 9
    • 0029964973 scopus 로고    scopus 로고
    • An Hsp70 antisense gene affects the expression of HSP70/HSC70, the regulation of HSF, and the acquisition of thermotolerance in transgenic Arabidopsis thaliana
    • Lee JH, Sch ffl F, (1996) An Hsp70 antisense gene affects the expression of HSP70/HSC70, the regulation of HSF, and the acquisition of thermotolerance in transgenic Arabidopsis thaliana. Molecular & general genetics: MGG 252: 11.
    • (1996) Molecular & General Genetics: MGG , vol.252 , pp. 11
    • Lee, J.H.1    Sch ffl, F.2
  • 10
    • 0037782281 scopus 로고    scopus 로고
    • Physiological and molecular assessment of altered expression of Hsc70-1 in Arabidopsis. Evidence for pleiotropic consequences
    • Sung DY, Guy CL, (2003) Physiological and molecular assessment of altered expression of Hsc70-1 in Arabidopsis. Evidence for pleiotropic consequences. Plant Physiol 132: 979.
    • (2003) Plant Physiol , vol.132 , pp. 979
    • Sung, D.Y.1    Guy, C.L.2
  • 11
    • 36348982737 scopus 로고    scopus 로고
    • A heat shock protein gene (hsp22. 4) from Chaetomium globosum confers heat and Na 2 CO 3 tolerance to yeast
    • Liu Z, Yang Q, Ma J, (2007) A heat shock protein gene (hsp22. 4) from Chaetomium globosum confers heat and Na 2 CO 3 tolerance to yeast. Appl Microbiol Biotechnol 77: 901-908.
    • (2007) Appl Microbiol Biotechnol , vol.77 , pp. 901-908
    • Liu, Z.1    Yang, Q.2    Ma, J.3
  • 13
    • 77953160263 scopus 로고    scopus 로고
    • The involvement of HSP22 from bay scallop Argopecten irradians in response to heavy metal stress
    • Zhang L, Wang L, Song L, Zhao J, Qiu L, et al. (2010) The involvement of HSP22 from bay scallop Argopecten irradians in response to heavy metal stress. Mol Biol Rep 37: 1763-1771.
    • (2010) Mol Biol Rep , vol.37 , pp. 1763-1771
    • Zhang, L.1    Wang, L.2    Song, L.3    Zhao, J.4    Qiu, L.5
  • 14
    • 33745642911 scopus 로고    scopus 로고
    • The cDNA cloning and mRNA expression of heat shock protein 70 gene in the haemocytes of bay scallop (Argopecten irradians, Lamarck 1819) responding to bacteria challenge and naphthalin stress
    • Song L, Wu L, Ni D, Chang Y, Xu W, et al. (2006) The cDNA cloning and mRNA expression of heat shock protein 70 gene in the haemocytes of bay scallop (Argopecten irradians, Lamarck 1819) responding to bacteria challenge and naphthalin stress. Fish Shellfish Immunol 21: 335-345.
    • (2006) Fish Shellfish Immunol , vol.21 , pp. 335-345
    • Song, L.1    Wu, L.2    Ni, D.3    Chang, Y.4    Xu, W.5
  • 15
    • 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, Song L, Qiu L, Yu Y, et al. (2008) Molecular cloning, characterization and expression of heat shock protein 90 gene in the haemocytes of bay scallop Argopecten irradians. Fish Shellfish Immunol 24: 379-385.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 379-385
    • Gao, Q.1    Zhao, J.2    Song, L.3    Qiu, L.4    Yu, Y.5
  • 16
    • 74349111346 scopus 로고    scopus 로고
    • The responsive expression of heat shock protein 22 gene in Zhikong scallop Chlamys farreri against a bacterial challenge
    • Zhang L, Wang L, Zhao J, Qiu L, Song L, et al. (2010) The responsive expression of heat shock protein 22 gene in Zhikong scallop Chlamys farreri against a bacterial challenge. Aquacult Res 41: 257-266.
    • (2010) Aquacult Res , vol.41 , pp. 257-266
    • Zhang, L.1    Wang, L.2    Zhao, J.3    Qiu, L.4    Song, L.5
  • 17
    • 0348222269 scopus 로고    scopus 로고
    • Identification and cloning of heat shock protein 70 gene from scallop Chlamys farreri
    • Wu LT, Song LS, Xu W, Qiu LH, Li HL, et al. (2003) Identification and cloning of heat shock protein 70 gene from scallop Chlamys farreri. High technol lett 13: 75-79.
    • (2003) High Technol Lett , vol.13 , pp. 75-79
    • Wu, L.T.1    Song, L.S.2    Xu, W.3    Qiu, L.H.4    Li, H.L.5
  • 19
    • 33748436681 scopus 로고    scopus 로고
    • Reduced heat shock response in human mononuclear cells during aging and its association with polymorphisms in HSP70 genes
    • Singh R, K lvraa S, Bross P, Jensen UB, Gregersen N, et al. (2006) Reduced heat shock response in human mononuclear cells during aging and its association with polymorphisms in HSP70 genes. Cell Stress Chaperones 11: 208.
    • (2006) Cell Stress Chaperones , vol.11 , pp. 208
    • Singh, R.1    K lvraa, S.2    Bross, P.3    Jensen, U.B.4    Gregersen, N.5
  • 20
    • 77449121568 scopus 로고    scopus 로고
    • A SNP in the HSP90AA1 gene 5′ flanking region is associated with the adaptation to differential thermal conditions in the ovine species
    • Marcos-Carcavilla A, Mutikainen M, González C, Calvo J, Kantanen J, et al. (2010) A SNP in the HSP90AA1 gene 5′ flanking region is associated with the adaptation to differential thermal conditions in the ovine species. Cell Stress Chaperones 15: 67-81.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 67-81
    • Marcos-Carcavilla, A.1    Mutikainen, M.2    González, C.3    Calvo, J.4    Kantanen, J.5
  • 21
    • 0029848501 scopus 로고    scopus 로고
    • Response of two heat shock genes to selection for knockdown heat resistance in Drosophila melanogaster
    • McColl G, Hoffmann AA, McKechnie SW, (1996) Response of two heat shock genes to selection for knockdown heat resistance in Drosophila melanogaster. Genetics 143: 1615.
    • (1996) Genetics , vol.143 , pp. 1615
    • McColl, G.1    Hoffmann, A.A.2    McKechnie, S.W.3
  • 22
    • 0037303384 scopus 로고    scopus 로고
    • Thermal tolerance trade-offs associated with the right arm of chromosome 3 and marked by the hsr-omega gene in Drosophila melanogaster
    • Anderson A, Collinge J, Hoffmann A, Kellett M, McKechnie S, (2003) Thermal tolerance trade-offs associated with the right arm of chromosome 3 and marked by the hsr-omega gene in Drosophila melanogaster. Heredity 90: 195-202.
    • (2003) Heredity , vol.90 , pp. 195-202
    • Anderson, A.1    Collinge, J.2    Hoffmann, A.3    Kellett, M.4    McKechnie, S.5
  • 23
    • 0034613387 scopus 로고    scopus 로고
    • The small heat shock protein Hsp22 of Drosophila melanogaster is a mitochondrial protein displaying oligomeric organization
    • Morrow G, Inaguma Y, Kato K, Tanguay RM, (2000) The small heat shock protein Hsp22 of Drosophila melanogaster is a mitochondrial protein displaying oligomeric organization. J Biol Chem 275: 31204.
    • (2000) J Biol Chem , vol.275 , pp. 31204
    • Morrow, G.1    Inaguma, Y.2    Kato, K.3    Tanguay, R.M.4
  • 24
    • 0034682806 scopus 로고    scopus 로고
    • A novel human gene similar to the protein kinase (PK) coding domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) codes for a serine-threonine PK and is expressed in melanoma cells
    • Smith CC, Yu YX, Kulka M, Aurelian L, (2000) A novel human gene similar to the protein kinase (PK) coding domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) codes for a serine-threonine PK and is expressed in melanoma cells. J Biol Chem 275: 25690.
    • (2000) J Biol Chem , vol.275 , pp. 25690
    • Smith, C.C.1    Yu, Y.X.2    Kulka, M.3    Aurelian, L.4
  • 25
    • 0035920143 scopus 로고    scopus 로고
    • HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 (3DHSP27)
    • Benndorf R, Sun X, Gilmont RR, Biederman KJ, Molloy MP, et al. (2001) HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 (3DHSP27). J Biol Chem 276: 26753.
    • (2001) J Biol Chem , vol.276 , pp. 26753
    • Benndorf, R.1    Sun, X.2    Gilmont, R.R.3    Biederman, K.J.4    Molloy, M.P.5
  • 26
    • 0242407366 scopus 로고    scopus 로고
    • Expression of small heat shock proteins HspB2, HspB8, Hsp20 and cvHsp in different tissues of the perinatal developing pig
    • Verschuure P, Tatard C, Boelens WC, Grongnet JF, David JC, (2003) Expression of small heat shock proteins HspB2, HspB8, Hsp20 and cvHsp in different tissues of the perinatal developing pig. Eur J Cell Biol 82: 523-530.
    • (2003) Eur J Cell Biol , vol.82 , pp. 523-530
    • Verschuure, P.1    Tatard, C.2    Boelens, W.C.3    Grongnet, J.F.4    David, J.C.5
  • 28
    • 10644284300 scopus 로고    scopus 로고
    • Cytokine genetics-polymorphisms, functional variations and disease associations
    • The Cytokine Handbook
    • Gallagher G, Eskdale J, Bidwell JL, (2003) Cytokine genetics-polymorphisms, functional variations and disease associations. The Cytokine Handbook.
    • (2003)
    • Gallagher, G.1    Eskdale, J.2    Bidwell, J.L.3
  • 29
    • 0141844530 scopus 로고    scopus 로고
    • Forced expression of the H11 heat shock protein can be regulated by DNA methylation and trigger apoptosis in human cells
    • Gober MD, Smith CC, Ueda K, Toretsky JA, Aurelian L, (2003) Forced expression of the H11 heat shock protein can be regulated by DNA methylation and trigger apoptosis in human cells. J Biol Chem 278: 37600.
    • (2003) J Biol Chem , vol.278 , pp. 37600
    • Gober, M.D.1    Smith, C.C.2    Ueda, K.3    Toretsky, J.A.4    Aurelian, L.5
  • 30
    • 33644862630 scopus 로고    scopus 로고
    • H11 kinase prevents myocardial infarction by preemptive preconditioning of the heart
    • Depre C, Wang L, Sui X, Qiu H, Hong C, et al. (2006) H11 kinase prevents myocardial infarction by preemptive preconditioning of the heart. Circul Res 98: 280-288.
    • (2006) Circul Res , vol.98 , pp. 280-288
    • Depre, C.1    Wang, L.2    Sui, X.3    Qiu, H.4    Hong, C.5
  • 31
    • 38849180142 scopus 로고    scopus 로고
    • Structure, properties, and functions of the human small heat©\shock protein HSP22 (HspB8, H11, E2IG1): A critical review
    • Shemetov AA, Seit-Nebi AS, Gusev NB, (2008) Structure, properties, and functions of the human small heat©\shock protein HSP22 (HspB8, H11, E2IG1): A critical review. J Neurosci Res 86: 264-269.
    • (2008) J Neurosci Res , vol.86 , pp. 264-269
    • Shemetov, A.A.1    Seit-Nebi, A.S.2    Gusev, N.B.3
  • 32
    • 2642539919 scopus 로고    scopus 로고
    • Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy
    • Irobi J, Van Impe K, Seeman P, Jordanova A, Dierick I, et al. (2004) Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy. Nat Genet 36: 597-601.
    • (2004) Nat Genet , vol.36 , pp. 597-601
    • Irobi, J.1    van Impe, K.2    Seeman, P.3    Jordanova, A.4    Dierick, I.5
  • 33
    • 19944433659 scopus 로고    scopus 로고
    • Small heat-shock protein 22 mutated in autosomal dominant Charcot-Marie-Tooth disease type 2L
    • Tang BS, Zhao GH, Luo W, Xia K, Cai F, et al. (2005) Small heat-shock protein 22 mutated in autosomal dominant Charcot-Marie-Tooth disease type 2L. Hum Genet 116: 222-224.
    • (2005) Hum Genet , vol.116 , pp. 222-224
    • Tang, B.S.1    Zhao, G.H.2    Luo, W.3    Xia, K.4    Cai, F.5
  • 34
    • 20444478694 scopus 로고    scopus 로고
    • The small heat shock proteins and their role in human disease
    • Sun Y, MacRae TH, (2005) The small heat shock proteins and their role in human disease. FEBS J 272: 2613-2627.
    • (2005) FEBS J , vol.272 , pp. 2613-2627
    • Sun, Y.1    MacRae, T.H.2
  • 35
    • 33748892808 scopus 로고    scopus 로고
    • Structure and properties of K141E mutant of small heat shock protein HSP22 (HspB8, H11) that is expressed in human neuromuscular disorders
    • Kim MV, Kasakov AS, Seit-Nebi AS, Marston SB, Gusev NB, (2006) Structure and properties of K141E mutant of small heat shock protein HSP22 (HspB8, H11) that is expressed in human neuromuscular disorders. Arch Biochem Biophys 454: 32-41.
    • (2006) Arch Biochem Biophys , vol.454 , pp. 32-41
    • Kim, M.V.1    Kasakov, A.S.2    Seit-Nebi, A.S.3    Marston, S.B.4    Gusev, N.B.5
  • 36
    • 34748911724 scopus 로고    scopus 로고
    • Genome-wide analysis and expression profiling of the small heat shock proteins in zebrafish
    • Elicker KS, Hutson LD, (2007) Genome-wide analysis and expression profiling of the small heat shock proteins in zebrafish. Gene 403: 60-69.
    • (2007) Gene , vol.403 , pp. 60-69
    • Elicker, K.S.1    Hutson, L.D.2
  • 37
    • 67650488922 scopus 로고    scopus 로고
    • The polymorphism of lysozyme gene in Zhikong scallop (Chlamys farreri) and its association with susceptibility/resistance to Listonella anguillarum
    • Li L, Zhao JM, Wang LL, Qiu LM, Zhang H, et al. (2009) The polymorphism of lysozyme gene in Zhikong scallop (Chlamys farreri) and its association with susceptibility/resistance to Listonella anguillarum. Fish Shellfish Immunol 27: 136-142.
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 136-142
    • Li, L.1    Zhao, J.M.2    Wang, L.L.3    Qiu, L.M.4    Zhang, H.5
  • 38
    • 18944381751 scopus 로고    scopus 로고
    • SHEsis, a powerful software platform for analyses of linkage disequilibrium, haplotype construction, and genetic association at polymorphism loci
    • Shi YY, He L, (2005) SHEsis, a powerful software platform for analyses of linkage disequilibrium, haplotype construction, and genetic association at polymorphism loci. Cell Res 15: 97-98.
    • (2005) Cell Res , vol.15 , pp. 97-98
    • Shi, Y.Y.1    He, L.2
  • 40
    • 0029442314 scopus 로고
    • Assaying proteins for molecular chaperone activity
    • Lee GJ, (1995) Assaying proteins for molecular chaperone activity. Methods Cell Biol 50: 325-334.
    • (1995) Methods Cell Biol , vol.50 , pp. 325-334
    • Lee, G.J.1
  • 41
    • 0031890821 scopus 로고    scopus 로고
    • Identification of two QTL influencing upper temperature tolerance in three rainbow trout (Oncorhynchus mykiss) half-sib families
    • Jackson TR, Ferguson MM, Danzmann RG, Fishback AG, Ihssen PE, et al. (1998) Identification of two QTL influencing upper temperature tolerance in three rainbow trout (Oncorhynchus mykiss) half-sib families. Heredity 80: 143-151.
    • (1998) Heredity , vol.80 , pp. 143-151
    • Jackson, T.R.1    Ferguson, M.M.2    Danzmann, R.G.3    Fishback, A.G.4    Ihssen, P.E.5
  • 42
    • 50849120027 scopus 로고    scopus 로고
    • Using fluorous amino acids to probe the effects of changing hydrophobicity on the physical and biological properties of the beta-hairpin antimicrobial peptide protegrin-1
    • Gottler LM, Bea RD, Shelburne CE, Ramamoorthy A, Marsh ENG, (2008) Using fluorous amino acids to probe the effects of changing hydrophobicity on the physical and biological properties of the beta-hairpin antimicrobial peptide protegrin-1. Biochemistry (Mosc) 47: 9243-9250.
    • (2008) Biochemistry (Mosc) , vol.47 , pp. 9243-9250
    • Gottler, L.M.1    Bea, R.D.2    Shelburne, C.E.3    Ramamoorthy, A.4    Marsh, E.N.G.5
  • 43
    • 77951258363 scopus 로고    scopus 로고
    • Characterization of the shsp genes in Drosophila buzzatii and association between the frequency of Valine mutations in hsp23 and climatic variables along a longitudinal gradient in Australia
    • Frydenberg J, Barker JSF, Loeschcke V, (2010) Characterization of the shsp genes in Drosophila buzzatii and association between the frequency of Valine mutations in hsp23 and climatic variables along a longitudinal gradient in Australia. Cell Stress Chaperones 15: 271-280.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 271-280
    • Frydenberg, J.1    Barker, J.S.F.2    Loeschcke, V.3
  • 44
    • 27644442375 scopus 로고    scopus 로고
    • Protein glycosylation - Chaperone mutation in Tn syndrome
    • Ju TZ, Cummings RD, (2005) Protein glycosylation- Chaperone mutation in Tn syndrome. Nature 437: 1252-1252.
    • (2005) Nature , vol.437 , pp. 1252
    • Ju, T.Z.1    Cummings, R.D.2
  • 45
    • 0344737954 scopus 로고    scopus 로고
    • Structural diversity in the small heat shock protein superfamily: control of aggregation by the N-terminal region
    • Salerno JC, Eifert CL, Salerno KM, Koretz JF, (2003) Structural diversity in the small heat shock protein superfamily: control of aggregation by the N-terminal region. Protein Eng 16: 847-851.
    • (2003) Protein Eng , vol.16 , pp. 847-851
    • Salerno, J.C.1    Eifert, C.L.2    Salerno, K.M.3    Koretz, J.F.4
  • 46
    • 1642524277 scopus 로고    scopus 로고
    • Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation - The N-terminal domain is important for oligomer assembly and the binding of unfolding proteins
    • Stromer T, Fischer E, Richter K, Haslbeck M, Buchner J, (2004) Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation- The N-terminal domain is important for oligomer assembly and the binding of unfolding proteins. J Biol Chem 279: 11222-11228.
    • (2004) J Biol Chem , vol.279 , pp. 11222-11228
    • Stromer, T.1    Fischer, E.2    Richter, K.3    Haslbeck, M.4    Buchner, J.5
  • 47
    • 14844355848 scopus 로고    scopus 로고
    • The essential role of the flexible termini in the temperature-responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli
    • Jiao WW, Qian MD, Li PL, Zhao L, Chang ZY, (2005) The essential role of the flexible termini in the temperature-responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli. J Mol Biol 347: 871-884.
    • (2005) J Mol Biol , vol.347 , pp. 871-884
    • Jiao, W.W.1    Qian, M.D.2    Li, P.L.3    Zhao, L.4    Chang, Z.Y.5
  • 49
    • 0027673091 scopus 로고
    • Comparison of the Homologous Carboxy-Terminal Domain and Tail of Alpha-Crystallin and Small Heat-Shock Protein
    • Merck KB, Horwitz J, Kersten M, Overkamp P, Gaestel M, et al. (1993) Comparison of the Homologous Carboxy-Terminal Domain and Tail of Alpha-Crystallin and Small Heat-Shock Protein. Mol Biol Rep 18: 209-215.
    • (1993) Mol Biol Rep , vol.18 , pp. 209-215
    • Merck, K.B.1    Horwitz, J.2    Kersten, M.3    Overkamp, P.4    Gaestel, M.5
  • 50
    • 0029956553 scopus 로고    scopus 로고
    • Effects of site-directed mutations on the chaperone-like activity of alpha B-crystallin
    • Plater ML, Goode D, Crabbe MJC, (1996) Effects of site-directed mutations on the chaperone-like activity of alpha B-crystallin. J Biol Chem 271: 28558-28566.
    • (1996) J Biol Chem , vol.271 , pp. 28558-28566
    • Plater, M.L.1    Goode, D.2    Crabbe, M.J.C.3


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