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Volumn 12, Issue 4, 2000, Pages 479-492

Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

DEVELOPMENTAL GENETICS; GENETIC CONSERVATION; GENETIC REGULATION; GERMINATION; GROWTH RATE; HEAT SHOCK PROTEIN; HEAT TOLERANCE; PLANT GROWTH; PROTEIN EXPRESSION; SURVIVAL; TRANSGENIC PLANT;

EID: 0034119621     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.12.4.479     Document Type: Article
Times cited : (573)

References (51)
  • 1
    • 0031624102 scopus 로고    scopus 로고
    • In planta Agrobacterium-mediated transformation of adult Arabidopsis thaliana plants by vacuum infiltration
    • Bechtold, N., and Pelletier, G. (1998). In planta Agrobacterium-mediated transformation of adult Arabidopsis thaliana plants by vacuum infiltration. Methods Mol. Biol. 82, 259-266.
    • (1998) Methods Mol. Biol. , vol.82 , pp. 259-266
    • Bechtold, N.1    Pelletier, G.2
  • 2
    • 0028890566 scopus 로고
    • Adaptations to environmental stresses
    • Bohnert, H.J., Nelson, D.E., and Jensen, R.G. (1995). Adaptations to environmental stresses. Plant Cell 7, 1099-1111.
    • (1995) Plant Cell , vol.7 , pp. 1099-1111
    • Bohnert, H.J.1    Nelson, D.E.2    Jensen, R.G.3
  • 3
    • 0030267627 scopus 로고    scopus 로고
    • Molecular chaperones and protein folding in plants
    • Boston, R.S., Viitanen, P.V., and Vierling, E. (1996). Molecular chaperones and protein folding in plants. Plant Mol. Biol. 32, 191-222.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 191-222
    • Boston, R.S.1    Viitanen, P.V.2    Vierling, E.3
  • 4
    • 0027764695 scopus 로고
    • Protective role of trehalose during heat stress in Saccharomyces cerevisiae
    • Eleutherio, E.C., Araujo, P.S., and Panek, A.D. (1993). Protective role of trehalose during heat stress in Saccharomyces cerevisiae. Cryobiology 30, 591-596.
    • (1993) Cryobiology , vol.30 , pp. 591-596
    • Eleutherio, E.C.1    Araujo, P.S.2    Panek, A.D.3
  • 5
    • 0029785532 scopus 로고    scopus 로고
    • The heat shock protein ClpB mediates the development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942
    • Eriksson, M.J., and Clarke, A.K. (1996). The heat shock protein ClpB mediates the development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942. J. Bacteriol. 178, 4839-4846.
    • (1996) J. Bacteriol. , vol.178 , pp. 4839-4846
    • Eriksson, M.J.1    Clarke, A.K.2
  • 6
    • 0346800265 scopus 로고    scopus 로고
    • Genetic dissection of thermotolerance in maize
    • S. Grillo and A. Leone, eds (New York: Springer-Verlag)
    • Frova, C. (1997). Genetic dissection of thermotolerance in maize. In Physical Stress in Plants, S. Grillo and A. Leone, eds (New York: Springer-Verlag), pp. 31-38.
    • (1997) Physical Stress in Plants , pp. 31-38
    • Frova, C.1
  • 7
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover, J.R., and Lindquist, S. (1998). Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins. Cell 94, 73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 9
    • 0034636040 scopus 로고    scopus 로고
    • Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress
    • in press
    • Hong, S.-W., and Vierling, E. (2000). Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress. Proc. Natl. Acad. Sci. USA, in press.
    • (2000) Proc. Natl. Acad. Sci. USA
    • Hong, S.-W.1    Vierling, E.2
  • 10
    • 0342326361 scopus 로고
    • Detailed characterization of heat shock protein synthesis and induced thermotolerance in seedlings of Sorghum bicolor L
    • Howarth, C.J., and Skot, K.P. (1994). Detailed characterization of heat shock protein synthesis and induced thermotolerance in seedlings of Sorghum bicolor L. J. Exp. Bot. 45, 1353-1363.
    • (1994) J. Exp. Bot. , vol.45 , pp. 1353-1363
    • Howarth, C.J.1    Skot, K.P.2
  • 11
    • 0032993342 scopus 로고    scopus 로고
    • Improving plant drought, salt, and freezing tolerance by gene transfer of a single stress-inducible transcription factor
    • Kasuga, M., Liu, Q., Miura, S., Yamaguchi-Shinozaki, K., and Shinozaki, K. (1999). Improving plant drought, salt, and freezing tolerance by gene transfer of a single stress-inducible transcription factor. Nat. Biotechnol. 17, 287-291.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 287-291
    • Kasuga, M.1    Liu, Q.2    Miura, S.3    Yamaguchi-Shinozaki, K.4    Shinozaki, K.5
  • 12
    • 0002982078 scopus 로고
    • T-DNA transformation and insertion mutagenesis
    • C. Koncz, N.-H. Chua, and J. Schell, eds (Singapore: World Scientific Publishing)
    • Koncz, C., Schell, J., and Redei, G.P. (1992). T-DNA transformation and insertion mutagenesis. In Methods in Arabidopsis Research, C. Koncz, N.-H. Chua, and J. Schell, eds (Singapore: World Scientific Publishing), pp. 224-273.
    • (1992) Methods in Arabidopsis Research , pp. 224-273
    • Koncz, C.1    Schell, J.2    Redei, G.P.3
  • 13
    • 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., and Schöffl, 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. Mol. Gen. Genet. 252, 11-19.
    • (1996) Mol. Gen. Genet. , vol.252 , pp. 11-19
    • Lee, J.H.1    Schöffl, F.2
  • 14
    • 0029379547 scopus 로고
    • Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis
    • Lee, J.H., Hubel, A., and Schöffl, F. (1995). Derepression of the activity of genetically engineered heat shock factor causes constitutive synthesis of heat shock proteins and increased thermotolerance in transgenic Arabidopsis. Plant J. 8, 603-612.
    • (1995) Plant J. , vol.8 , pp. 603-612
    • Lee, J.H.1    Hubel, A.2    Schöffl, F.3
  • 15
    • 0028675574 scopus 로고
    • A soybean 101-kD heat shock protein complements a yeast HSP104 deletion mutant in acquiring thermotolerance
    • Lee, Y.R., Nagao, R.T., and Key, J.L. (1994). A soybean 101-kD heat shock protein complements a yeast HSP104 deletion mutant in acquiring thermotolerance. Plant Cell 6, 1889-1897.
    • (1994) Plant Cell , vol.6 , pp. 1889-1897
    • Lee, Y.R.1    Nagao, R.T.2    Key, J.L.3
  • 16
    • 0001866298 scopus 로고
    • Responses of plants to environmental stresses
    • T.T. Kozlowski, ed (New York: Academic Press)
    • Levitt, J. (1980). Responses of plants to environmental stresses. In Physiological Ecology, T.T. Kozlowski, ed (New York: Academic Press), pp. 347-448.
    • (1980) Physiological Ecology , pp. 347-448
    • Levitt, J.1
  • 17
    • 0029950703 scopus 로고    scopus 로고
    • Heat-shock protein 104 expression is sufficient for thermotolerance in yeast
    • Lindquist, S., and Kim, G. (1996). Heat-shock protein 104 expression is sufficient for thermotolerance in yeast. Proc. Natl. Acad. Sci. USA 93, 5301-5306.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5301-5306
    • Lindquist, S.1    Kim, G.2
  • 18
    • 0032697142 scopus 로고    scopus 로고
    • Modified expression of a carrot small heat shock protein gene, HSP17.7, results in increased or decreased thermotolerance
    • Malik, M.K., Slovin, J.P., Hwang, C.H., and Zimmerman, J.L. (1999). Modified expression of a carrot small heat shock protein gene, HSP17.7, results in increased or decreased thermotolerance. Plant J. 20, 1-11.
    • (1999) Plant J. , vol.20 , pp. 1-11
    • Malik, M.K.1    Slovin, J.P.2    Hwang, C.H.3    Zimmerman, J.L.4
  • 19
    • 0029102514 scopus 로고
    • How and why do plants inactivate homologous (trans)genes?
    • Matzke, M.A., and Matzke, A.J.M. (1995). How and why do plants inactivate homologous (trans)genes? Plant Physiol. 107, 679-685.
    • (1995) Plant Physiol. , vol.107 , pp. 679-685
    • Matzke, M.A.1    Matzke, A.J.M.2
  • 20
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile E. coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • Mogk, A., Tomoyasu, T., Goloubinoff, P., Rüdiger, S., Rôder, D., Langen, H., and Bukau, B. (1999). Identification of thermolabile E. coli proteins: Prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18, 6934-6949.
    • (1999) EMBO J. , vol.18 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rüdiger, S.4    Rôder, D.5    Langen, H.6    Bukau, B.7
  • 21
    • 0031825456 scopus 로고    scopus 로고
    • A search in the genome of Saccharomyces cerevisiae for genes regulated via stress
    • Moskvina, E., Schuller, C., Maurer, C.T., Mager, W.H., and Ruis, H. (1998). A search in the genome of Saccharomyces cerevisiae for genes regulated via stress. Yeast 14, 1041-1050.
    • (1998) Yeast , vol.14 , pp. 1041-1050
    • Moskvina, E.1    Schuller, C.2    Maurer, C.T.3    Mager, W.H.4    Ruis, H.5
  • 22
    • 0033594880 scopus 로고    scopus 로고
    • Heat-inactivated proteins are rescued by the DnaK/J-GrpE set and ClpB chaperones
    • Motohashi, K., Watanabe, Y., Yohda, M., and Yoshida, M. (1999). Heat-inactivated proteins are rescued by the DnaK/J-GrpE set and ClpB chaperones. Proc. Natl. Acad. Sci. USA 96, 7184-7189.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7184-7189
    • Motohashi, K.1    Watanabe, Y.2    Yohda, M.3    Yoshida, M.4
  • 23
    • 0031259651 scopus 로고    scopus 로고
    • A nuclear gene, erd1, encoding a chloroplast-targeted Clp protease regulatory subunit homolog is not only induced by water stress but also developmentally up-regulated during senescence in Arabidopsis thaliana
    • Nakashima, K., Kiyosue, T., Yamaguchi-Shinozaki, K., and Shinozaki, K. (1997). A nuclear gene, erd1, encoding a chloroplast-targeted Clp protease regulatory subunit homolog is not only induced by water stress but also developmentally up-regulated during senescence in Arabidopsis thaliana. Plant J. 12, 851-861.
    • (1997) Plant J. , vol.12 , pp. 851-861
    • Nakashima, K.1    Kiyosue, T.2    Yamaguchi-Shinozaki, K.3    Shinozaki, K.4
  • 24
    • 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., Aravind, L., Spouge, J.L., and Koonin, E.V. (1999). AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 25
    • 0031048279 scopus 로고    scopus 로고
    • Stable association of chloroplastic precursors with protein translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone
    • Nielsen, E., Akita, M., Davila-Aponte, J., and Keegstra, K. (1997). Stable association of chloroplastic precursors with protein translocation complexes that contain proteins from both envelope membranes and a stromal Hsp100 molecular chaperone. EMBO J. 16, 935-946.
    • (1997) EMBO J. , vol.16 , pp. 935-946
    • Nielsen, E.1    Akita, M.2    Davila-Aponte, J.3    Keegstra, K.4
  • 26
    • 0025121236 scopus 로고
    • Molecular cell biology of the heat stress response. I
    • Nover, L. (1990). Molecular cell biology of the heat stress response. I. Naturwissenschaften 77, 310-316.
    • (1990) Naturwissenschaften , vol.77 , pp. 310-316
    • Nover, L.1
  • 27
    • 0027154225 scopus 로고
    • Poly(A) tail length of a heat shock protein RNA is increased by severe heat stress, but intron splicing is unaffected
    • Osteryoung, K.W., Sundberg, H., and Vierling, E. (1993). Poly(A) tail length of a heat shock protein RNA is increased by severe heat stress, but intron splicing is unaffected. Mol. Gen. Genet. 239, 323-333.
    • (1993) Mol. Gen. Genet. , vol.239 , pp. 323-333
    • Osteryoung, K.W.1    Sundberg, H.2    Vierling, E.3
  • 28
    • 0024153226 scopus 로고
    • Temperature shock proteins in plants
    • Ougham, H.J., and Howarth, C.J. (1988). Temperature shock proteins in plants. Symp. Soc. Exp. Biol. 42, 259-280.
    • (1988) Symp. Soc. Exp. Biol. , vol.42 , pp. 259-280
    • Ougham, H.J.1    Howarth, C.J.2
  • 29
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell, D.A., and Lindquist, S. (1993). The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins. Annu. Rev. Genet. 27, 437-496.
    • (1993) Annu. Rev. Genet. , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 30
    • 0000675009 scopus 로고
    • Heat shock proteins and stress tolerance
    • R.I. Morimoto, A. Tissieres, and C. Georgopoulos, eds (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press)
    • Parsell, D.A., and Lindquist, S. (1994). Heat shock proteins and stress tolerance. In The Biology of Heat Shock Proteins and Molecular Chaperones, R.I. Morimoto, A. Tissieres, and C. Georgopoulos, eds (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press), pp. 457-494.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 457-494
    • Parsell, D.A.1    Lindquist, S.2
  • 31
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell, D.A., Kowal, A.S., Singer, M.A., and Lindquist, S. (1994). Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372, 475-478.
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 32
    • 0031842946 scopus 로고    scopus 로고
    • HSF3, a new heat shock factor from Arabidopsis thaliana, derepresses the heat shock response and confers thermotolerance when overexpressed in transgenic plants
    • Prändl, R., Hinderhofer, K., Eggers-Schumacher, G., and Schöffl, F. (1998). HSF3, a new heat shock factor from Arabidopsis thaliana, derepresses the heat shock response and confers thermotolerance when overexpressed in transgenic plants. Mol. Gen. Genet. 258, 269-278.
    • (1998) Mol. Gen. Genet. , vol.258 , pp. 269-278
    • Prändl, R.1    Hinderhofer, K.2    Eggers-Schumacher, G.3    Schöffl, F.4
  • 33
    • 0029395010 scopus 로고
    • Stress signaling in yeast
    • Ruis, H., and Schuller, C. (1995). Stress signaling in yeast. Bioessays 17, 959-965.
    • (1995) Bioessays , vol.17 , pp. 959-965
    • Ruis, H.1    Schuller, C.2
  • 34
    • 0026523626 scopus 로고
    • Hsp104 is required for tolerance to many forms of stress
    • Sanchez, Y., Taulien, J., Borkovich, K.A., and Lindquist, S. (1992). Hsp104 is required for tolerance to many forms of stress. EMBO J. 11, 2357-2364.
    • (1992) EMBO J. , vol.11 , pp. 2357-2364
    • Sanchez, Y.1    Taulien, J.2    Borkovich, K.A.3    Lindquist, S.4
  • 35
    • 0028675582 scopus 로고
    • An Arabidopsis heat shock protein complements a thermotolerance defect in yeast
    • Schirmer, E.C., Lindquist, S., and Vierling, E. (1994). An Arabidopsis heat shock protein complements a thermotolerance defect in yeast. Plant Cell 6, 1899-1909.
    • (1994) Plant Cell , vol.6 , pp. 1899-1909
    • Schirmer, E.C.1    Lindquist, S.2    Vierling, E.3
  • 36
  • 37
    • 0029392885 scopus 로고
    • The stroma of higher plant plastids contain ClpP and ClpC, functional homologs of Escherichia coli ClpP and ClpA: An archetypal two-component ATP-dependent protease
    • Shanklin, J., DeWitt, N.D., and Flanagan, J.M. (1995). The stroma of higher plant plastids contain ClpP and ClpC, functional homologs of Escherichia coli ClpP and ClpA: An archetypal two-component ATP-dependent protease. Plant Cell 7, 1713-1722.
    • (1995) Plant Cell , vol.7 , pp. 1713-1722
    • Shanklin, J.1    DeWitt, N.D.2    Flanagan, J.M.3
  • 38
    • 0032908943 scopus 로고    scopus 로고
    • Multiple independent regulatory pathways control UB14 expression after heat shock in Saccharomyces cerevisiae
    • Simon, J.R., Treger, J.M., and McEntee, K. (1999). Multiple independent regulatory pathways control UB14 expression after heat shock in Saccharomyces cerevisiae. Mol. Microbiol. 31, 823-832.
    • (1999) Mol. Microbiol. , vol.31 , pp. 823-832
    • Simon, J.R.1    Treger, J.M.2    McEntee, K.3
  • 39
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effects of trehalose on protein folding in vitro and in vivo
    • Singer, M.A., and Lindquist, S. (1998). Multiple effects of trehalose on protein folding in vitro and in vivo. Mol. Cell 1, 639-648.
    • (1998) Mol. Cell , vol.1 , pp. 639-648
    • Singer, M.A.1    Lindquist, S.2
  • 40
    • 0031898169 scopus 로고    scopus 로고
    • Plant resistance to environmental stress
    • Smirnoff, N. (1998). Plant resistance to environmental stress. Curr. Opin. Biotechnol. 9, 214-219.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 214-219
    • Smirnoff, N.1
  • 41
    • 0033062218 scopus 로고    scopus 로고
    • DREB takes the stress out of growing up
    • Smirnoff, N., and Bryant, J.A. (1999). DREB takes the stress out of growing up. Nat. Biotechnol. 17, 229-230.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 229-230
    • Smirnoff, N.1    Bryant, J.A.2
  • 42
    • 0025787706 scopus 로고
    • Changes in hsp70 alter thermotolerance and heatshock regulation in Drosophila
    • Solomon, J.M., Rossi, J.M., Golic, K., McGarry, T., and Lindquist, S. (1991). Changes in hsp70 alter thermotolerance and heatshock 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
  • 43
    • 0020667551 scopus 로고
    • Is the major Drosophila heat shock protein present in cells that have not been heat shocked?
    • Velazquez, J.M., Sonoda, S., Bugaisky, G., and Lindquist, S. (1983). Is the major Drosophila heat shock protein present in cells that have not been heat shocked? J. Cell Biol. 96, 286-290.
    • (1983) J. Cell Biol. , vol.96 , pp. 286-290
    • Velazquez, J.M.1    Sonoda, S.2    Bugaisky, G.3    Lindquist, S.4
  • 45
    • 0033117630 scopus 로고    scopus 로고
    • Chloroplast-targeted ERD1 protein declines but its mRNA increases during senescence in Arabidopsis
    • Weaver, L.M., Froehlich, J.E., and Amasino, R.M. (1999). Chloroplast-targeted ERD1 protein declines but its mRNA increases during senescence in Arabidopsis. Plant Physiol. 119, 1209-1216.
    • (1999) Plant Physiol. , vol.119 , pp. 1209-1216
    • Weaver, L.M.1    Froehlich, J.E.2    Amasino, R.M.3
  • 46
    • 0030265854 scopus 로고    scopus 로고
    • Synthesis of small heat-shock proteins is part of the developmental program of late seed maturation
    • Wehmeyer, N., Hernandez, L.D., Finkelstein, R.R., and Vierling, E. (1996). Synthesis of small heat-shock proteins is part of the developmental program of late seed maturation. Plant Physiol. 112, 747-757.
    • (1996) Plant Physiol. , vol.112 , pp. 747-757
    • Wehmeyer, N.1    Hernandez, L.D.2    Finkelstein, R.R.3    Vierling, E.4
  • 47
    • 0032532127 scopus 로고    scopus 로고
    • HSP101 functions as a specific translational regulatory protein whose activity is regulated by nutrient status
    • Wells, D.R., Tanguay, R.L., Le, H., and Gallie, D.R. (1998). HSP101 functions as a specific translational regulatory protein whose activity is regulated by nutrient status. Genes Dev. 12, 3236-3251.
    • (1998) Genes Dev. , vol.12 , pp. 3236-3251
    • Wells, D.R.1    Tanguay, R.L.2    Le, H.3    Gallie, D.R.4
  • 48
    • 0027144416 scopus 로고
    • A new method for manipulating transgenes: Engineering heat tolerance in a complex, multicellular organism
    • Weite, M.A., Tetrault, J.M., Dellavalle, R.P., and Lindquist, S. (1993). A new method for manipulating transgenes: Engineering heat tolerance in a complex, multicellular organism. Curr. Biol. 3, 842-853.
    • (1993) Curr. Biol. , vol.3 , pp. 842-853
    • Weite, M.A.1    Tetrault, J.M.2    Dellavalle, R.P.3    Lindquist, S.4
  • 49
    • 84982005535 scopus 로고
    • Plant low-molecular-mass heat-shock proteins: Their relationship to the acquisition of thermotolerance in plants
    • Yen, K.W., Jinn, T.L., Yen, C.H., Chen, Y.M., and Lin, C.Y. (1994). Plant low-molecular-mass heat-shock proteins: Their relationship to the acquisition of thermotolerance in plants. Biotechnol. Appl. Biochem. 19, 41-49.
    • (1994) Biotechnol. Appl. Biochem. , vol.19 , pp. 41-49
    • Yen, K.W.1    Jinn, T.L.2    Yen, C.H.3    Chen, Y.M.4    Lin, C.Y.5
  • 50
    • 0040342971 scopus 로고    scopus 로고
    • Neutral trehalase Nth1p of Saccharomyces cerevisiae encoded by the NTH1 gene is a multiple stress responsive protein
    • Zahringer, H., Burgert, M., Holzer, H., and Nwaka, S. (1997). Neutral trehalase Nth1p of Saccharomyces cerevisiae encoded by the NTH1 gene is a multiple stress responsive protein. FEBS Lett. 412, 615-620.
    • (1997) FEBS Lett. , vol.412 , pp. 615-620
    • Zahringer, H.1    Burgert, M.2    Holzer, H.3    Nwaka, S.4
  • 51
    • 0033214052 scopus 로고    scopus 로고
    • ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli
    • Zolkiewski, M. (1999). ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. J. Biol. Chem. 274, 28083-28086.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28083-28086
    • Zolkiewski, M.1


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