메뉴 건너뛰기




Volumn 9, Issue 5, 2004, Pages 244-252

Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; VEGETABLE PROTEIN;

EID: 2442445139     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tplants.2004.03.006     Document Type: Review
Times cited : (2208)

References (95)
  • 1
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist S. The heat-shock response. Annu. Rev. Biochem. 55:1986;1151-1191
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 3
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • Waters E.R., et al. Evolution, structure and function of the small heat shock proteins in plants. J. Exp. Bot. 47:1996;325-338
    • (1996) J. Exp. Bot. , vol.47 , pp. 325-338
    • Waters, E.R.1
  • 4
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • Boston R.S., et al. Molecular chaperones and protein folding in plants. Plant Mol. Biol. 32:1996;191-222
    • (1996) Plant Mol. Biol. , vol.32 , pp. 191-222
    • Boston, R.S.1
  • 6
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B., Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell. 92:1998;351-366
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 7
    • 0347300280 scopus 로고    scopus 로고
    • Plant responses to drought, salinity and extreme temperatures: Towards genetic engineering for stress tolerance
    • Wang W.X., et al. Plant responses to drought, salinity and extreme temperatures: towards genetic engineering for stress tolerance. Planta. 218:2003;1-14
    • (2003) Planta , vol.218 , pp. 1-14
    • Wang, W.X.1
  • 8
    • 0034088275 scopus 로고    scopus 로고
    • Isolation of Arabidopsis mutants lacking components of acquired thermotolerance
    • Burke J.J., et al. Isolation of Arabidopsis mutants lacking components of acquired thermotolerance. Plant Physiol. 123:2000;575-587
    • (2000) Plant Physiol. , vol.123 , pp. 575-587
    • Burke, J.J.1
  • 9
    • 0034986489 scopus 로고    scopus 로고
    • Identification of genetic diversity and mutations in higher plant acquired thermotolerance
    • Burke J.J. Identification of genetic diversity and mutations in higher plant acquired thermotolerance. Physiol. Plant. 112:2001;167-170
    • (2001) Physiol. Plant. , vol.112 , pp. 167-170
    • Burke, J.J.1
  • 10
    • 0034636040 scopus 로고    scopus 로고
    • Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress
    • Hong S.W., Vierling E. Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress. Proc. Natl. Acad. Sci. U. S. A. 97:2000;4392-4397
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 4392-4397
    • Hong, S.W.1    Vierling, E.2
  • 11
    • 0034895977 scopus 로고    scopus 로고
    • Hsp101 is necessary for heat tolerance but dispensable for development and germination in the absence of stress
    • Hong S.W., Vierling E. Hsp101 is necessary for heat tolerance but dispensable for development and germination in the absence of stress. Plant J. 27:2001;25-35
    • (2001) Plant J. , vol.27 , pp. 25-35
    • Hong, S.W.1    Vierling, E.2
  • 12
    • 0038797062 scopus 로고    scopus 로고
    • Arabidopsis hot mutants define multiple functions required for acclimation to high temperatures
    • Hong S.W., et al. Arabidopsis hot mutants define multiple functions required for acclimation to high temperatures. Plant Physiol. 132:2003;757-767
    • (2003) Plant Physiol. , vol.132 , pp. 757-767
    • Hong, S.W.1
  • 13
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F.U. Molecular chaperones in cellular protein folding. Nature. 381:1996;571-580
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 14
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70:2001;603-647
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 15
    • 0032924953 scopus 로고    scopus 로고
    • Hsp90 & Co. - A holding for folding
    • Buchner J. Hsp90 & Co. - a holding for folding. Trends Biochem. Sci. 24:1999;136-141
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 136-141
    • Buchner, J.1
  • 16
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shook transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto R.I. Regulation of the heat shook transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev. 12:1998;3788-3796
    • (1998) Genes Dev. , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 17
    • 0032527735 scopus 로고    scopus 로고
    • Chaperonins
    • Ranson N.A., et al. Chaperonins. Biochem. J. 333:1998;233-242
    • (1998) Biochem. J. , vol.333 , pp. 233-242
    • Ranson, N.A.1
  • 18
    • 0031000773 scopus 로고    scopus 로고
    • The 70kDa stress-related proteins as molecular chaperones
    • Miernyk J.A. The 70kDa stress-related proteins as molecular chaperones. Trends Plant Sci. 2:1997;180-187
    • (1997) Trends Plant Sci. , vol.2 , pp. 180-187
    • Miernyk, J.A.1
  • 19
    • 0033625965 scopus 로고    scopus 로고
    • The Hsp110 and Grp170 stress proteins: Newly recognized relatives of the Hsp70s
    • Easton D.P., et al. The Hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s. Cell Stress Chaperones. 5:2000;276-290
    • (2000) Cell Stress Chaperones , vol.5 , pp. 276-290
    • Easton, D.P.1
  • 20
    • 0027445375 scopus 로고
    • Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family
    • Mukai H., et al. Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family. Gene. 132:1993;57-66
    • (1993) Gene , vol.132 , pp. 57-66
    • Mukai, H.1
  • 21
    • 0029079045 scopus 로고
    • Identification of a major subfamily of large Hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein
    • Lee-Yoon D., et al. Identification of a major subfamily of large Hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein. J. Biol. Chem. 270:1995;15725-15733
    • (1995) J. Biol. Chem. , vol.270 , pp. 15725-15733
    • Lee-Yoon, D.1
  • 22
    • 0030052105 scopus 로고    scopus 로고
    • The 170 kDa glucose regulated stress protein is a large HSP70-, HSP110-like protein of the endoplasmic reticulum
    • Chen X., et al. The 170 kDa glucose regulated stress protein is a large HSP70-, HSP110-like protein of the endoplasmic reticulum. FEBS Lett. 380:1996;68-72
    • (1996) FEBS Lett. , vol.380 , pp. 68-72
    • Chen, X.1
  • 23
    • 0035681414 scopus 로고    scopus 로고
    • Plant Hsp70 molecular chaperones: Protein structure, gene family, expression and function
    • Sung D.Y., et al. Plant Hsp70 molecular chaperones: protein structure, gene family, expression and function. Physiol. Plant. 113:2001;443-451
    • (2001) Physiol. Plant. , vol.113 , pp. 443-451
    • Sung, D.Y.1
  • 24
    • 0033950443 scopus 로고    scopus 로고
    • 14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants
    • May T., Soll J. 14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants. Plant Cell. 12:2000;53-64
    • (2000) Plant Cell , vol.12 , pp. 53-64
    • May, T.1    Soll, J.2
  • 25
    • 0034804490 scopus 로고    scopus 로고
    • Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana
    • Lin B.L., et al. Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana. Cell Stress Chaperones. 6:2001;201-208
    • (2001) Cell Stress Chaperones , vol.6 , pp. 201-208
    • Lin, B.L.1
  • 26
    • 0034978496 scopus 로고    scopus 로고
    • Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family
    • Sung D.Y., et al. Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family. Plant Physiol. 126:2001;789-800
    • (2001) Plant Physiol. , vol.126 , pp. 789-800
    • Sung, D.Y.1
  • 27
    • 0032051742 scopus 로고    scopus 로고
    • The organization and evolution of the spinach stress 70 molecular chaperone gene family
    • Guy C.L., Li Q.B. The organization and evolution of the spinach stress 70 molecular chaperone gene family. Plant Cell. 10:1998;539-556
    • (1998) Plant Cell , vol.10 , pp. 539-556
    • Guy, C.L.1    Li, Q.B.2
  • 28
    • 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 J.H., Schöffl F. An Hsp70 antisense gene affects the expression of HSP70/HSC70, the regulation of HSF and the acquisition of thermotolerance in transgenic Arabidopsis thaliana. Mol. Gen. Genet. 252:1996;11-19
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 11-19
    • Lee, J.H.1    Schöffl, F.2
  • 29
    • 0034952995 scopus 로고    scopus 로고
    • Enhanced accumulation of BiP in transgenic plants confers tolerance to water stress
    • Alvim F.C., et al. Enhanced accumulation of BiP in transgenic plants confers tolerance to water stress. Plant Physiol. 126:2001;1042-1054
    • (2001) Plant Physiol. , vol.126 , pp. 1042-1054
    • Alvim, F.C.1
  • 30
    • 0037782281 scopus 로고    scopus 로고
    • Physiological and molecular assessment of altered expression of Hsc70-1 in Arabidopsis. Evidence for pleiotropic consequences
    • Sung D.Y., Guy C.L. Physiological and molecular assessment of altered expression of Hsc70-1 in Arabidopsis. Evidence for pleiotropic consequences. Plant Physiol. 132:2003;979-987
    • (2003) Plant Physiol. , vol.132 , pp. 979-987
    • Sung, D.Y.1    Guy, C.L.2
  • 31
    • 0033618864 scopus 로고    scopus 로고
    • Overexpression of DnaK from a halotolerant cyanobacterium Aphanothece halophytice acquires resistance to salt stress in transgenic tobacco plants
    • Sugino M., et al. Overexpression of DnaK from a halotolerant cyanobacterium Aphanothece halophytice acquires resistance to salt stress in transgenic tobacco plants. Plant Sci. 146:1999;81-88
    • (1999) Plant Sci. , vol.146 , pp. 81-88
    • Sugino, M.1
  • 32
    • 0035809015 scopus 로고    scopus 로고
    • Overexpression of DnaK from a halotolerant cyanobacterium Aphanothece halophytica enhances the high-temperature tolerance of tobacco during germination and early growth
    • Ono K., et al. Overexpression of DnaK from a halotolerant cyanobacterium Aphanothece halophytica enhances the high-temperature tolerance of tobacco during germination and early growth. Plant Sci. 160:2001;455-461
    • (2001) Plant Sci. , vol.160 , pp. 455-461
    • Ono, K.1
  • 33
    • 0033101899 scopus 로고    scopus 로고
    • Overexpression of BiP in tobacco alleviates endoplasmic reticulum stress
    • Leborgne-Castel N., et al. Overexpression of BiP in tobacco alleviates endoplasmic reticulum stress. Plant Cell. 11:1999;459-470
    • (1999) Plant Cell , vol.11 , pp. 459-470
    • Leborgne-Castel, N.1
  • 34
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman R.J. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13:1999;1211-1233
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 35
    • 0032708369 scopus 로고    scopus 로고
    • Mitochondrial unfold precursor proteins by unraveling them from their N-termini
    • Huang S., et al. Mitochondrial unfold precursor proteins by unraveling them from their N-termini. Nat. Struct. Biol. 6:1999;1132-1138
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 1132-1138
    • Huang, S.1
  • 36
    • 0037059015 scopus 로고    scopus 로고
    • A subclass of plant heat shock cognate 70 chaperones carries a motif that facilitates trafficking through plasmodesmata
    • Aoki K., et al. A subclass of plant heat shock cognate 70 chaperones carries a motif that facilitates trafficking through plasmodesmata. Proc. Natl. Acad. Sci. U. S. A. 10:2002;16342-16347
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.10 , pp. 16342-16347
    • Aoki, K.1
  • 37
    • 0036007390 scopus 로고    scopus 로고
    • Interaction of plant mitochondrial and chloroplast signal peptides with the Hsp70 molecular chaperone
    • Zhang X.P., Glaser E. Interaction of plant mitochondrial and chloroplast signal peptides with the Hsp70 molecular chaperone. Trends Plant Sci. 7:2002;14-21
    • (2002) Trends Plant Sci. , vol.7 , pp. 14-21
    • Zhang, X.P.1    Glaser, E.2
  • 38
    • 0036007905 scopus 로고    scopus 로고
    • Interaction between Arabidopsis heat shock transcription factor 1 and 70 kDa heat shock proteins
    • Kim B.H., Schoffl F. Interaction between Arabidopsis heat shock transcription factor 1 and 70 kDa heat shock proteins. J. Exp. Bot. 53:2002;371-375
    • (2002) J. Exp. Bot. , vol.53 , pp. 371-375
    • Kim, B.H.1    Schoffl, F.2
  • 39
    • 0031895617 scopus 로고    scopus 로고
    • Overexpression of HSP-70 inhibits the phosphorylation of HSF1 by activating protein phosphatase and inhibiting protein kinase C activity
    • Ding X.Z., et al. Overexpression of HSP-70 inhibits the phosphorylation of HSF1 by activating protein phosphatase and inhibiting protein kinase C activity. FASEB J. 12:1998;451-459
    • (1998) FASEB J. , vol.12 , pp. 451-459
    • Ding, X.Z.1
  • 40
    • 0023900525 scopus 로고
    • Homologous plant and bacterial proteins chaperone oligomeric protein assembly
    • Hemmingsen S.M., et al. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature. 26:1988;330-334
    • (1988) Nature , vol.26 , pp. 330-334
    • Hemmingsen, S.M.1
  • 41
    • 0032701797 scopus 로고    scopus 로고
    • Group II chaperonins: New TriC(k)s and turns of a protein folding machine
    • Gutsche I., et al. Group II chaperonins: new TriC(k)s and turns of a protein folding machine. J. Mol. Biol. 293:1999;295-312
    • (1999) J. Mol. Biol. , vol.293 , pp. 295-312
    • Gutsche, I.1
  • 42
    • 0037010181 scopus 로고    scopus 로고
    • Type I chaperonins: Not all are created equal
    • Levy-Rimler G., et al. Type I chaperonins: not all are created equal. FEBS Lett. 529:2002;1-5
    • (2002) FEBS Lett. , vol.529 , pp. 1-5
    • Levy-Rimler, G.1
  • 43
    • 0026744722 scopus 로고
    • Identification, characterization, and DNA sequence of a functional 'double' GroES-like chaperonin from chloroplasts of higher plants
    • Bertsch U., et al. Identification, characterization, and DNA sequence of a functional 'double' GroES-like chaperonin from chloroplasts of higher plants. Proc. Natl. Acad. Sci. U. S. A. 89:1992;8696-8700
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 8696-8700
    • Bertsch, U.1
  • 44
    • 0034809742 scopus 로고    scopus 로고
    • Arabidopsis thaliana type I and II chaperonins
    • Hill J.E., Hemmingsen S.M. Arabidopsis thaliana type I and II chaperonins. Cell Stress Chaperones. 6:2001;190-200
    • (2001) Cell Stress Chaperones , vol.6 , pp. 190-200
    • Hill, J.E.1    Hemmingsen, S.M.2
  • 45
    • 0034979913 scopus 로고    scopus 로고
    • The Arabidopsis embryo mutant schlepperless has a defect in the chaperonin-60 gene
    • Apuya N.R., et al. The Arabidopsis embryo mutant schlepperless has a defect in the chaperonin-60 gene. Plant Physiol. 126:2001;717-730
    • (2001) Plant Physiol. , vol.126 , pp. 717-730
    • Apuya, N.R.1
  • 46
    • 0028057089 scopus 로고
    • Antisense expression of chaperonin 60β in transgenic tobacco plants leads to abnormal phenotypes and altered distribution of photoassimilates
    • Zabaleta E., et al. Antisense expression of chaperonin 60β in transgenic tobacco plants leads to abnormal phenotypes and altered distribution of photoassimilates. Plant J. 6:1994;425-432
    • (1994) Plant J. , vol.6 , pp. 425-432
    • Zabaleta, E.1
  • 47
    • 0037364978 scopus 로고    scopus 로고
    • Deletion of a chaperonin 60 β gene leads to cell death in the Arabidopsis lesion initiation 1 mutant
    • Ishikawa A., et al. Deletion of a chaperonin 60 β gene leads to cell death in the Arabidopsis lesion initiation 1 mutant. Plant Cell Physiol. 44:2003;255-261
    • (2003) Plant Cell Physiol. , vol.44 , pp. 255-261
    • Ishikawa, A.1
  • 48
    • 0036707664 scopus 로고    scopus 로고
    • The role of plant CCTα in salt- and osmotic-stress tolerance
    • Yamada A., et al. The role of plant CCTα in salt- and osmotic-stress tolerance. Plant Cell Physiol. 43:2002;1043-1048
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1043-1048
    • Yamada, A.1
  • 49
    • 0035939668 scopus 로고    scopus 로고
    • Hsp90: A specialized but essential protein-folding tool
    • Young J.C., et al. Hsp90: a specialized but essential protein-folding tool. J. Cell Biol. 154:2001;267-273
    • (2001) J. Cell Biol. , vol.154 , pp. 267-273
    • Young, J.C.1
  • 50
    • 0034892432 scopus 로고    scopus 로고
    • Hsp90: Chaperoning signal transduction
    • Richter K., Buchner J. Hsp90: chaperoning signal transduction. J. Cell. Physiol. 188:2001;281-290
    • (2001) J. Cell. Physiol. , vol.188 , pp. 281-290
    • Richter, K.1    Buchner, J.2
  • 51
    • 0035205522 scopus 로고    scopus 로고
    • Hsp90-binding immunophilins in plants: The protein movers
    • Pratt W.B., et al. Hsp90-binding immunophilins in plants: the protein movers. Trends Plant Sci. 6:2001;54-58
    • (2001) Trends Plant Sci. , vol.6 , pp. 54-58
    • Pratt, W.B.1
  • 52
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • Rutherford S.L., Lindquist S. Hsp90 as a capacitor for morphological evolution. Nature. 396:1998;336-342
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 53
    • 0037030713 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for phenotypic variation
    • Queitsch C., et al. Hsp90 as a capacitor for phenotypic variation. Nature. 417:2002;618-624
    • (2002) Nature , vol.417 , pp. 618-624
    • Queitsch, C.1
  • 54
    • 0042313977 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome
    • Imai J., et al. The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J. 22:2003;3557-3567
    • (2003) EMBO J. , vol.22 , pp. 3557-3567
    • Imai, J.1
  • 55
    • 0037320062 scopus 로고    scopus 로고
    • Characterization of a plant homolog of Hop, a co-chaperone of Hsp90
    • Zhang Z., et al. Characterization of a plant homolog of Hop, a co-chaperone of Hsp90. Plant Physiol. 131:2003;525-535
    • (2003) Plant Physiol. , vol.131 , pp. 525-535
    • Zhang, Z.1
  • 56
    • 0034817255 scopus 로고    scopus 로고
    • The Hsp90 family of proteins in Arabidopsis thaliana
    • Krishna P., Gloor G. The Hsp90 family of proteins in Arabidopsis thaliana. Cell Stress Chaperones. 6:2001;238-246
    • (2001) Cell Stress Chaperones , vol.6 , pp. 238-246
    • Krishna, P.1    Gloor, G.2
  • 57
    • 0031470696 scopus 로고    scopus 로고
    • Genomic organization of Hsp90 gene family in Arabidopsis
    • Milioni D., Hatzopoulos P. Genomic organization of Hsp90 gene family in Arabidopsis. Plant Mol. Biol. 35:1997;955-961
    • (1997) Plant Mol. Biol. , vol.35 , pp. 955-961
    • Milioni, D.1    Hatzopoulos, P.2
  • 58
    • 0030219939 scopus 로고    scopus 로고
    • Hsp100/Clp proteins: A common mechanism explains diverse functions
    • Schirmer E.C., et al. Hsp100/Clp proteins: a common mechanism explains diverse functions. Trends Biochem. Sci. 21:1996;289-296
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 289-296
    • Schirmer, E.C.1
  • 59
    • 0031973716 scopus 로고    scopus 로고
    • The AAA team: Related ATPases with diverse functions
    • Patel S., Latterich M. The AAA team: related ATPases with diverse functions. Trends Cell Biol. 8:1998;65-71
    • (1998) Trends Cell Biol. , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 60
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation and disassembly of protein complexes
    • Neuwald A.F., et al. AAA+: a class of chaperone-like ATPases associated with the assembly, operation and disassembly of protein complexes. Genome Res. 9:1999;27-43
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1
  • 61
    • 0034809744 scopus 로고    scopus 로고
    • Arabidopsis thaliana Hsp100 proteins: Kith and kin
    • Agarwal M., et al. Arabidopsis thaliana Hsp100 proteins: kith and kin. Cell Stress Chaperones. 6:2001;219-224
    • (2001) Cell Stress Chaperones , vol.6 , pp. 219-224
    • Agarwal, M.1
  • 62
    • 0025340973 scopus 로고
    • Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes
    • Gottesman S., et al. Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes. Proc. Natl. Acad. Sci. U. S. A. 87:1990;3513-3517
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 3513-3517
    • Gottesman, S.1
  • 63
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70 and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover J.R., Lindquist S. Hsp104, Hsp70 and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell. 94:1998;73-82
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 64
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff P., et al. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl. Acad. Sci. U. S. A. 96:1999;13732-13737
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1
  • 65
    • 0032215219 scopus 로고    scopus 로고
    • At sixes and sevens: Characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease
    • Beuron M.R., et al. At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease. J. Struct. Biol. 123:1998;248-259
    • (1998) J. Struct. Biol. , vol.123 , pp. 248-259
    • Beuron, M.R.1
  • 66
    • 0033517351 scopus 로고    scopus 로고
    • Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
    • Weber-Ban E.U., et al. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature. 401:1999;90-93
    • (1999) Nature , vol.401 , pp. 90-93
    • Weber-Ban, E.U.1
  • 67
    • 0035027728 scopus 로고    scopus 로고
    • Chloroplast and mitochondrial proteases in Arabidopsis. A proposed nomenclature
    • Adam Z., et al. Chloroplast and mitochondrial proteases in Arabidopsis. A proposed nomenclature. Plant Physiol. 125:2001;1912-1918
    • (2001) Plant Physiol. , vol.125 , pp. 1912-1918
    • Adam, Z.1
  • 68
    • 0033940993 scopus 로고    scopus 로고
    • Acquired thermotolerance and expression of the HSP100/ClpB genes of Lima bean
    • Keeler S., et al. Acquired thermotolerance and expression of the HSP100/ClpB genes of Lima bean. Plant Physiol. 123:2000;1121-1132
    • (2000) Plant Physiol. , vol.123 , pp. 1121-1132
    • Keeler, S.1
  • 69
    • 0034119621 scopus 로고    scopus 로고
    • Heat stress protein 101 plays a crucial role in thermotolerance in Arabidopsis
    • Queitsch C., et al. Heat stress protein 101 plays a crucial role in thermotolerance in Arabidopsis. Plant Cell. 12:2000;479-492
    • (2000) Plant Cell , vol.12 , pp. 479-492
    • Queitsch, C.1
  • 70
    • 0036776905 scopus 로고    scopus 로고
    • Cutting edge of chloroplast proteolysis
    • Adam Z., Clarke A.K. Cutting edge of chloroplast proteolysis. Trends Plant Sci. 7:2002;451-456
    • (2002) Trends Plant Sci. , vol.7 , pp. 451-456
    • Adam, Z.1    Clarke, A.K.2
  • 71
    • 0028675582 scopus 로고
    • An Arabidopsis heat shock protein complements a thermotolerance defect in yeast
    • Schirmer E.C., et al. An Arabidopsis heat shock protein complements a thermotolerance defect in yeast. Plant Cell. 6:1994;1899-1909
    • (1994) Plant Cell , vol.6 , pp. 1899-1909
    • Schirmer, E.C.1
  • 72
    • 0028675574 scopus 로고
    • A soybean 101-kD heat shock protein complements a yeast HSP 104 deletion mutant in acquiring thermotolerance
    • Lee Y.R.J., et al. A soybean 101-kD heat shock protein complements a yeast HSP 104 deletion mutant in acquiring thermotolerance. Plant Cell. 6:1994;1889-1897
    • (1994) Plant Cell , vol.6 , pp. 1889-1897
    • Lee, Y.R.J.1
  • 73
    • 0037342584 scopus 로고    scopus 로고
    • Molecular characterization of rice HSP101: Complementation of yeast hsp104 mutation by disaggregation of protein granules and differential expression in indica and japonica rice types
    • Agarwal M., et al. Molecular characterization of rice HSP101: complementation of yeast hsp104 mutation by disaggregation of protein granules and differential expression in indica and japonica rice types. Plant Mol. Biol. 51:2003;543-553
    • (2003) Plant Mol. Biol. , vol.51 , pp. 543-553
    • Agarwal, M.1
  • 74
    • 0035191639 scopus 로고    scopus 로고
    • Crystal structure and assembly of a eukaryotic small heat shock protein
    • Van Montfort R.L., et al. Crystal structure and assembly of a eukaryotic small heat shock protein. Nat. Struct. Biol. 8:2001;1025-1030
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 1025-1030
    • Van Montfort, R.L.1
  • 75
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger M.S., et al. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16:1997;221-229
    • (1997) EMBO J. , vol.16 , pp. 221-229
    • Ehrnsperger, M.S.1
  • 76
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee G.J., et al. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J. 16:1997;659-671
    • (1997) EMBO J. , vol.16 , pp. 659-671
    • Lee, G.J.1
  • 77
    • 0032079487 scopus 로고    scopus 로고
    • The small heat-shock protein IbpB from E. coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network
    • Veinger L., et al. The small heat-shock protein IbpB from E. coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network. J. Biol. Chem. 273:1998;11032-11037
    • (1998) J. Biol. Chem. , vol.273 , pp. 11032-11037
    • Veinger, L.1
  • 78
    • 0033765314 scopus 로고    scopus 로고
    • A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein
    • Lee G.J., Vierling E. A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein. Plant Physiol. 122:2000;189-198
    • (2000) Plant Physiol. , vol.122 , pp. 189-198
    • Lee, G.J.1    Vierling, E.2
  • 79
    • 0034681446 scopus 로고    scopus 로고
    • Temperature-dependent chaperone activity and structural properties of human αa- and αb-crystallins
    • Reddy G.B., et al. Temperature-dependent chaperone activity and structural properties of human αA- and αB-crystallins. J. Biol. Chem. 275:2000;4565-4570
    • (2000) J. Biol. Chem. , vol.275 , pp. 4565-4570
    • Reddy, G.B.1
  • 80
    • 0042733148 scopus 로고    scopus 로고
    • Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK
    • Mogk A., et al. Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J. Biol. Chem. 278:2003;31033-31042
    • (2003) J. Biol. Chem. , vol.278 , pp. 31033-31042
    • Mogk, A.1
  • 81
    • 0034815248 scopus 로고    scopus 로고
    • The expanding family of Arabidopsis thaliana small heat stress proteins and a new family of proteins containing α-crystallin domains (ACD proteins)
    • Scharf K.D., et al. The expanding family of Arabidopsis thaliana small heat stress proteins and a new family of proteins containing α-crystallin domains (ACD proteins). Cell Stress Chaperones. 6:2001;225-237
    • (2001) Cell Stress Chaperones , vol.6 , pp. 225-237
    • Scharf, K.D.1
  • 82
    • 0034958914 scopus 로고    scopus 로고
    • Mitochondrial adaptations to NaCl. Complex I is protected by anti-oxidants and small heat shock proteins, whereas complex II is protected by proline and betaine
    • Hamilton E.W. III, Heckathorn S.A. Mitochondrial adaptations to NaCl. Complex I is protected by anti-oxidants and small heat shock proteins, whereas complex II is protected by proline and betaine. Plant Physiol. 126:2001;1266-1274
    • (2001) Plant Physiol. , vol.126 , pp. 1266-1274
    • Hamilton III, E.W.1    Heckathorn, S.A.2
  • 83
    • 0141563540 scopus 로고    scopus 로고
    • Heat sensitivity in a bentgrass variant. Failure to accumulate a chloroplast heat shock protein isoform implicated in heat tolerance
    • Wang D., Luthe D.S. Heat sensitivity in a bentgrass variant. Failure to accumulate a chloroplast heat shock protein isoform implicated in heat tolerance. Plant Physiol. 133:2003;319-327
    • (2003) Plant Physiol. , vol.133 , pp. 319-327
    • Wang, D.1    Luthe, D.S.2
  • 84
    • 0036773161 scopus 로고    scopus 로고
    • Characterization of SP1, a stress-responsive, boiling-soluble, homo-oligomeric protein from Aspen (Populus tremula L.)
    • Wang W.X., et al. Characterization of SP1, a stress-responsive, boiling-soluble, homo-oligomeric protein from Aspen (Populus tremula L.). Plant Physiol. 130:2002;865-875
    • (2002) Plant Physiol. , vol.130 , pp. 865-875
    • Wang, W.X.1
  • 85
    • 0037136230 scopus 로고    scopus 로고
    • Small heat shock proteins and stress tolerance in plants
    • Sun W., et al. Small heat shock proteins and stress tolerance in plants. Biochim. Biophys. Acta. 1577:2002;1-9
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 1-9
    • Sun, W.1
  • 86
    • 0142125283 scopus 로고    scopus 로고
    • Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation
    • Mogk A., et al. Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol. Microbiol. 50:2003;585-595
    • (2003) Mol. Microbiol. , vol.50 , pp. 585-595
    • Mogk, A.1
  • 87
    • 0035783169 scopus 로고    scopus 로고
    • Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones
    • Peres Ben-Zvi A., Goloubinoff P. Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones. J. Biol. Chem. 135:2001;84-93
    • (2001) J. Biol. Chem. , vol.135 , pp. 84-93
    • Peres Ben-Zvi, A.1    Goloubinoff, P.2
  • 88
    • 0037888827 scopus 로고    scopus 로고
    • Biotechnology of plant osmotic stress tolerance: Physiological and molecular considerations
    • Wang W.X., et al. Biotechnology of plant osmotic stress tolerance: physiological and molecular considerations. Acta Hortic. 560:2001;285-292
    • (2001) Acta Hortic. , vol.560 , pp. 285-292
    • Wang, W.X.1
  • 89
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effects of trehalose on protein folding in vitro and in vivo
    • Singer M.A., Lindquist S. Multiple effects of trehalose on protein folding in vitro and in vivo. Mol. Cell. 1:1998;639-648
    • (1998) Mol. Cell , vol.1 , pp. 639-648
    • Singer, M.A.1    Lindquist, S.2
  • 90
    • 0035955743 scopus 로고    scopus 로고
    • Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses
    • Diamant S., et al. Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses. J. Biol. Chem. 276:2001;39586-39591
    • (2001) J. Biol. Chem. , vol.276 , pp. 39586-39591
    • Diamant, S.1
  • 91
    • 0034992527 scopus 로고    scopus 로고
    • Influence of trehalose on the molecular chaperone activity of p26, a small heat shock/α-crystallin protein
    • Viner R.I., Clegg J.S. Influence of trehalose on the molecular chaperone activity of p26, a small heat shock/α-crystallin protein. Cell Stress Chaperones. 6:2001;126-135
    • (2001) Cell Stress Chaperones , vol.6 , pp. 126-135
    • Viner, R.I.1    Clegg, J.S.2
  • 92
    • 0037099046 scopus 로고    scopus 로고
    • Chaperoning signaling pathways: Molecular chaperones as stress-sensing 'heat shock' proteins
    • Ellen A.A., et al. Chaperoning signaling pathways: molecular chaperones as stress-sensing 'heat shock' proteins. J. Cell Sci. 115:2002;2809-2816
    • (2002) J. Cell Sci. , vol.115 , pp. 2809-2816
    • Ellen, A.A.1
  • 93
    • 0031962486 scopus 로고    scopus 로고
    • Small stress proteins: Chaperones that act as regulators of intracellular redox state and programmed cell death
    • Arrigo A.P. Small stress proteins: chaperones that act as regulators of intracellular redox state and programmed cell death. Biol. Chem. 379:1998;19-26
    • (1998) Biol. Chem. , vol.379 , pp. 19-26
    • Arrigo, A.P.1
  • 94
    • 0035983670 scopus 로고    scopus 로고
    • Heat stress- and heat shock transcription factor-dependent expression and activity of ascorbate peroxidase in Arabidopsis
    • Panchuk I.I., et al. Heat stress- and heat shock transcription factor-dependent expression and activity of ascorbate peroxidase in Arabidopsis. Plant Physiol. 129:2002;838-853
    • (2002) Plant Physiol. , vol.129 , pp. 838-853
    • Panchuk, I.I.1
  • 95
    • 0036851187 scopus 로고    scopus 로고
    • Global changes in gene expression in response to high light in Arabidopsis
    • Rossel J.B., et al. Global changes in gene expression in response to high light in Arabidopsis. Plant Physiol. 130:2002;1109-1120
    • (2002) Plant Physiol. , vol.130 , pp. 1109-1120
    • Rossel, J.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.