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Volumn 5, Issue 5, 2010, Pages 503-508

The multifunctionality of dehydrins: An overview

Author keywords

Dehydrin; Environmental stress; Intrinsically unstructured proteins; Late embryogenesis abundant proteins; Water stress

Indexed keywords

DEHYDRIN PROTEINS, PLANT; INTRINSICALLY DISORDERED PROTEIN; MACROMOLECULE; PROTEIN BINDING; VEGETABLE PROTEIN;

EID: 77954949426     PISSN: 15592316     EISSN: 15592324     Source Type: Journal    
DOI: 10.4161/psb.11085     Document Type: Review
Times cited : (123)

References (70)
  • 2
    • 0033498862 scopus 로고    scopus 로고
    • Plant cold acclimation: Freezing tolerance genes and regulatory mechanisms
    • Thomashow MF. Plant cold acclimation: Freezing tolerance genes and regulatory mechanisms. Annu Rev Plant Physiol Plant Mol Biol 1999; 50:571-99.
    • (1999) Annu Rev Plant Physiol Plant Mol Biol , vol.50 , pp. 571-599
    • Thomashow, M.F.1
  • 3
    • 0141725442 scopus 로고    scopus 로고
    • Regulatory network of gene expression in the drought and cold stress responses
    • Shinozaki K, Yamaguchi-Shinozaki K, Seki M. Regulatory network of gene expression in the drought and cold stress responses. Curr Opin Plant Biol 2003; 6:410-7.
    • (2003) Curr Opin Plant Biol , vol.6 , pp. 410-417
    • Shinozaki, K.1    Yamaguchi-Shinozaki, K.2    Seki, M.3
  • 4
    • 8444230584 scopus 로고    scopus 로고
    • Genes commonly regulated by water-deficit stress in Arabidopsis thaliana
    • Bray EA. Genes commonly regulated by water-deficit stress in Arabidopsis thaliana. J Exp Bot 2004; 55:2331-41.
    • (2004) J Exp Bot , vol.55 , pp. 2331-2341
    • Bray, E.A.1
  • 5
    • 0002663990 scopus 로고
    • Structural motifs in Lea proteins
    • Current Topics in Plant Physiology, Close TJ, Bray EA, eds., (Rockville: American Society of Plant Physiologists)
    • Dure L, III. Structural motifs in Lea proteins. In: Plant Responses to Cellular Dehydration during Environmental Stress. Current Topics in Plant Physiology, Close TJ, Bray EA, eds., (Rockville: American Society of Plant Physiologists) 1993; 10:91-103.
    • (1993) Plant Responses to Cellular Dehydration During Environmental Stress , vol.10 , pp. 91-103
    • Dure III, L.1
  • 6
    • 34548460796 scopus 로고    scopus 로고
    • The continuing conundrum of the LEA proteins
    • Tunnacliffe A, Wise MJ. The continuing conundrum of the LEA proteins. Naturwissenschaften 2007; 94:791-812.
    • (2007) Naturwissenschaften , vol.94 , pp. 791-812
    • Tunnacliffe, A.1    Wise, M.J.2
  • 8
    • 42149115630 scopus 로고    scopus 로고
    • LEA (late embryogenesis abundant) proteins and their encoding genes in Arabidopsis thaliana
    • Hundertmark M, Hincha DK. LEA (late embryogenesis abundant) proteins and their encoding genes in Arabidopsis thaliana. BMC Genomics 2008; 9:118.
    • (2008) BMC Genomics , vol.9 , pp. 118
    • Hundertmark, M.1    Hincha, D.K.2
  • 9
    • 42149111687 scopus 로고    scopus 로고
    • Inventory, evolution and expression profiling diversity of the LEA (late embryogenesis abundant) protein gene family in Arabidopsis thaliana
    • Bies-Ethève N, Gaubier-Comella P, Debures A, Lasserre E, Jobet E, Raynal M, et al. Inventory, evolution and expression profiling diversity of the LEA (late embryogenesis abundant) protein gene family in Arabidopsis thaliana. Plant Mol Biol 2008; 67:107-24.
    • (2008) Plant Mol Biol , vol.67 , pp. 107-124
    • Bies-Ethève, N.1    Gaubier-Comella, P.2    Debures, A.3    Lasserre, E.4    Jobet, E.5    Raynal, M.6
  • 10
    • 0033539557 scopus 로고    scopus 로고
    • Allelic variation of a dehydrin gene cosegregates with chilling tolerance during seedling emergence
    • Ismail AM, Hall AE, Close TJ. Allelic variation of a dehydrin gene cosegregates with chilling tolerance during seedling emergence. Proc Natl Acad Sci USA 1999; 96:13566-70.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13566-13570
    • Ismail, A.M.1    Hall, A.E.2    Close, T.J.3
  • 11
    • 33644913648 scopus 로고    scopus 로고
    • A dehydrin gene in Physcomitrella patens is required for salt and osmotic stress tolerance
    • Saavedra L, Svensson J, Carballo V, Izmendi D, Welin B, Vidal S. A dehydrin gene in Physcomitrella patens is required for salt and osmotic stress tolerance. Plant J 2006; 45:237-49.
    • (2006) Plant J , vol.45 , pp. 237-249
    • Saavedra, L.1    Svensson, J.2    Carballo, V.3    Izmendi, D.4    Welin, B.5    Vidal, S.6
  • 12
    • 0036380564 scopus 로고    scopus 로고
    • Wheat LEA genes, PMA80 and PMA1959 enhance dehydration tolerance of transgenic rice (Oryza sativa L.)
    • Cheng Z, Targolli J, Huang X, Wu R. Wheat LEA genes, PMA80 and PMA1959 enhance dehydration tolerance of transgenic rice (Oryza sativa L.). Mol Breed 2002; 10:71-82.
    • (2002) Mol Breed , vol.10 , pp. 71-82
    • Cheng, Z.1    Targolli, J.2    Huang, X.3    Wu, R.4
  • 13
    • 0038758836 scopus 로고    scopus 로고
    • Enhancement of cold tolerance and inhibition of lipid peroxidation by citrus dehydrin in transgenic tobacco
    • Hara M, Terashima S, Fukaya T, Kuboi T. Enhancement of cold tolerance and inhibition of lipid peroxidation by citrus dehydrin in transgenic tobacco. Planta 2003; 217:290-8.
    • (2003) Planta , vol.217 , pp. 290-298
    • Hara, M.1    Terashima, S.2    Fukaya, T.3    Kuboi, T.4
  • 14
    • 16544387856 scopus 로고    scopus 로고
    • Overexpression of multiple dehydrin genes enhances tolerance to freezing stress in Arabidopsis
    • Puhakainen T, Hess MW, Mäkelä P, Svensson J, Heino P, Palva ET. Overexpression of multiple dehydrin genes enhances tolerance to freezing stress in Arabidopsis. Plant Mol Biol 2004; 54:743-53.
    • (2004) Plant Mol Biol , vol.54 , pp. 743-753
    • Puhakainen, T.1    Hess, M.W.2    Mäkelä, P.3    Svensson, J.4    Heino, P.5    Palva, E.T.6
  • 15
    • 13444310781 scopus 로고    scopus 로고
    • Overexpression of the acidic dehydrin WCOR410 improves freezing tolerance in transgenic strawberry leaves
    • Houde M, Dallaire S, N'Dong D, Sarhan F. Overexpression of the acidic dehydrin WCOR410 improves freezing tolerance in transgenic strawberry leaves. Plant Biotech J 2004; 2:381-7.
    • (2004) Plant Biotech J , vol.2 , pp. 381-387
    • Houde, M.1    Dallaire, S.2    N'Dong, D.3    Sarhan, F.4
  • 16
    • 28144461633 scopus 로고    scopus 로고
    • Maize Rabl7 overexpression in Arabidopsis plants promotes osmotic stress tolerance
    • Figueras M, Pujal J, Saleh A, Save R, Pages M, Goday A. Maize Rabl7 overexpression in Arabidopsis plants promotes osmotic stress tolerance. Ann Appl Biol 2004; 144:251-7.
    • (2004) Ann Appl Biol , vol.144 , pp. 251-257
    • Figueras, M.1    Pujal, J.2    Saleh, A.3    Save, R.4    Pages, M.5    Goday, A.6
  • 17
    • 33748255935 scopus 로고    scopus 로고
    • Expression of a Solanum sogarandinum SK3-type dehydrin enhances cold tolerance in transgenic cucumber seedlings
    • Yin Z, Rorat T, Szabala BM, Ziólkowska A, Malepszy S. Expression of a Solanum sogarandinum SK3-type dehydrin enhances cold tolerance in transgenic cucumber seedlings. Plant Sci 2006; 170:1164-72.
    • (2006) Plant Sci , vol.170 , pp. 1164-1172
    • Yin, Z.1    Rorat, T.2    Szabala, B.M.3    Ziólkowska, A.4    Malepszy, S.5
  • 18
    • 35248855455 scopus 로고    scopus 로고
    • Overexpression of wheat dehydrin DHN-5 enhances tolerance to salt and osmotic stress in Arabidopsis thaliana
    • Brini F, Hanin M, Lumbreras V, Amara I, Khoudi H, Hassairi A, et al. Overexpression of wheat dehydrin DHN-5 enhances tolerance to salt and osmotic stress in Arabidopsis thaliana. Plant Cell Rep 2007; 26:2017-26.
    • (2007) Plant Cell Rep , vol.26 , pp. 2017-2026
    • Brini, F.1    Hanin, M.2    Lumbreras, V.3    Amara, I.4    Khoudi, H.5    Hassairi, A.6
  • 20
    • 0030498675 scopus 로고    scopus 로고
    • Dehydrins: Emergence of a biochemical role of a family of plant dehydration proteins
    • Close TJ. Dehydrins: Emergence of a biochemical role of a family of plant dehydration proteins. Physiol Plant 1996; 97:795-803.
    • (1996) Physiol Plant , vol.97 , pp. 795-803
    • Close, T.J.1
  • 21
    • 0031007034 scopus 로고    scopus 로고
    • Dehydrins: A commonalty in the response of plants to dehydration and low temperature
    • Close TJ. Dehydrins: A commonalty in the response of plants to dehydration and low temperature. Physiol Plant 1997; 100:291-6.
    • (1997) Physiol Plant , vol.100 , pp. 291-296
    • Close, T.J.1
  • 22
    • 0030729290 scopus 로고    scopus 로고
    • Dehydrins: Genes, proteins and associations with phenotypic traits
    • Campbell SA, Close TJ. Dehydrins: genes, proteins and associations with phenotypic traits. New Phytol 1997; 137:61-74.
    • (1997) New Phytol , vol.137 , pp. 61-74
    • Campbell, S.A.1    Close, T.J.2
  • 25
    • 33847140438 scopus 로고    scopus 로고
    • Plant dehydrins: Tissue location, structure and function
    • Rorat T. Plant dehydrins: tissue location, structure and function. Cell Mol Biol Lett 2006; 11:536-56.
    • (2006) Cell Mol Biol Lett , vol.11 , pp. 536-556
    • Rorat, T.1
  • 28
    • 0029805280 scopus 로고    scopus 로고
    • The recombinant dehydrin-like desiccation stress protein from the resurrection plant Craterostigma plantagineum displays no defined three-dimensional structure in its native state
    • Lisse T, Bartels D, Kalbitzer HR, Jaenicke R. The recombinant dehydrin-like desiccation stress protein from the resurrection plant Craterostigma plantagineum displays no defined three-dimensional structure in its native state. Biol Chem 1996; 377:555-61.
    • (1996) Biol Chem , vol.377 , pp. 555-561
    • Lisse, T.1    Bartels, D.2    Kalbitzer, H.R.3    Jaenicke, R.4
  • 29
    • 0033134023 scopus 로고    scopus 로고
    • Purification and partial characterization of a dehydrin involved in chilling tolerance during seedling emergence of cowpea
    • Ismail AM, Hall AE, Close TJ. Purification and partial characterization of a dehydrin involved in chilling tolerance during seedling emergence of cowpea. Plant Physiol 1999; 120:237-44.
    • (1999) Plant Physiol , vol.120 , pp. 237-244
    • Ismail, A.M.1    Hall, A.E.2    Close, T.J.3
  • 30
    • 0034781789 scopus 로고    scopus 로고
    • Characterization and cryoprotective activity of cold-responsive dehydrin from Citrus unshiu
    • Hara M, Terashima S, Kuboi T. Characterization and cryoprotective activity of cold-responsive dehydrin from Citrus unshiu. J Plant Physiol 2001; 158:1333-9.
    • (2001) J Plant Physiol , vol.158 , pp. 1333-1339
    • Hara, M.1    Terashima, S.2    Kuboi, T.3
  • 31
    • 0348150694 scopus 로고    scopus 로고
    • The binding of maize DHN1 to lipid vesicles. Gain of structure and lipid specificity
    • Koag MC, Fenton RD, Wilkens S, Close TJ. The binding of maize DHN1 to lipid vesicles. Gain of structure and lipid specificity. Plant Physiol 2003; 131:309-16.
    • (2003) Plant Physiol , vol.131 , pp. 309-316
    • Koag, M.C.1    Fenton, R.D.2    Wilkens, S.3    Close, T.J.4
  • 32
    • 0346034535 scopus 로고    scopus 로고
    • Conformation of a group 2 late embryogenesis abundant protein from soybean. Evidence of poly (L-proline)-type II structure
    • Soulages JL, Kim K, Arrese EL, Walters C, Cushman JC. Conformation of a group 2 late embryogenesis abundant protein from soybean. Evidence of poly (L-proline)-type II structure. Plant Physiol 2003; 131:963-75.
    • (2003) Plant Physiol , vol.131 , pp. 963-975
    • Soulages, J.L.1    Kim, K.2    Arrese, E.L.3    Walters, C.4    Cushman, J.C.5
  • 33
    • 33745655415 scopus 로고    scopus 로고
    • Structural investigation of disordered stress proteins: Comparison of full-length dehydrins with isolated peptides of their conserved segments
    • Mouillon JM, Gustafsson P, Harryson P. Structural investigation of disordered stress proteins: comparison of full-length dehydrins with isolated peptides of their conserved segments. Plant Physiol 2006; 141:638-50.
    • (2006) Plant Physiol , vol.141 , pp. 638-650
    • Mouillon, J.M.1    Gustafsson, P.2    Harryson, P.3
  • 34
    • 57749111581 scopus 로고    scopus 로고
    • Mimicking the plant cell interior under water stress by macromolecular crowding: Disordered dehydrin proteins are highly resistant to structural collapse
    • Mouillon JM, Eriksson SK, Harryson P. Mimicking the plant cell interior under water stress by macromolecular crowding: disordered dehydrin proteins are highly resistant to structural collapse. Plant Physiol 2008; 148:1925-37.
    • (2008) Plant Physiol , vol.148 , pp. 1925-1937
    • Mouillon, J.M.1    Eriksson, S.K.2    Harryson, P.3
  • 35
    • 50649098927 scopus 로고    scopus 로고
    • Chaperone activity of ERD10 and ERD14, two disordered stressrelated plant proteins
    • Kovacs D, Kalmar E, Torok Z, Tompa P. Chaperone activity of ERD10 and ERD14, two disordered stressrelated plant proteins. Plant Physiol 2008; 147:381-90.
    • (2008) Plant Physiol , vol.147 , pp. 381-390
    • Kovacs, D.1    Kalmar, E.2    Torok, Z.3    Tompa, P.4
  • 37
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 2005; 6:197-208.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 38
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa P. The interplay between structure and function in intrinsically unstructured proteins. FEBS Lett 2005; 579:3346-54.
    • (2005) FEBS Lett , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 39
    • 67650175436 scopus 로고    scopus 로고
    • The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes
    • Koag MC, Wilkens S, Fenton RD, Resnik J, Vo E, Close TJ. The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes. Plant Physiol 2009; 150:1503-14.
    • (2009) Plant Physiol , vol.150 , pp. 1503-1514
    • Koag, M.C.1    Wilkens, S.2    Fenton, R.D.3    Resnik, J.4    Vo, E.5    Close, T.J.6
  • 40
  • 41
    • 0036802435 scopus 로고    scopus 로고
    • The calcium-binding activity of a vacuole-associated, dehydrin-like protein is regulated by phosphorylation
    • Heyen BJ, Alsheikh MK, Smith EA, Torvik CF, Seals DF, Randall SK. The calcium-binding activity of a vacuole-associated, dehydrin-like protein is regulated by phosphorylation. Plant Physiol 2002; 130:675-87.
    • (2002) Plant Physiol , vol.130 , pp. 675-687
    • Heyen, B.J.1    Alsheikh, M.K.2    Smith, E.A.3    Torvik, C.F.4    Seals, D.F.5    Randall, S.K.6
  • 42
    • 0142103428 scopus 로고    scopus 로고
    • Ion binding properties of the dehydrin ERD14 are dependent upon phosphorylation
    • Alsheikh MK, Heyen BJ, Randall SK. Ion binding properties of the dehydrin ERD14 are dependent upon phosphorylation. J Biol Chem 2003; 278:40882-9.
    • (2003) J Biol Chem , vol.278 , pp. 40882-40889
    • Alsheikh, M.K.1    Heyen, B.J.2    Randall, S.K.3
  • 43
    • 33744495390 scopus 로고    scopus 로고
    • Phosphorylation regulated ion-binding is a property shared by the acidic subclass dehydrins
    • Alsheikh MK, Svensson JT, Randall SK. Phosphorylation regulated ion-binding is a property shared by the acidic subclass dehydrins. Plant Cell Environ 2005; 28:1114-22.
    • (2005) Plant Cell Environ , vol.28 , pp. 1114-1122
    • Alsheikh, M.K.1    Svensson, J.T.2    Randall, S.K.3
  • 44
    • 0742323272 scopus 로고    scopus 로고
    • POPP the question: What do LEA proteins do?
    • Wise MJ, Tunnacliffe A. POPP the question: What do LEA proteins do? Trends Plant Sci 2004; 9:13-7.
    • (2004) Trends Plant Sci , vol.9 , pp. 13-17
    • Wise, M.J.1    Tunnacliffe, A.2
  • 45
    • 24944438537 scopus 로고    scopus 로고
    • Metal binding by citrus dehydrin with histidine-rich domains
    • Hara M, Fujinaga M, Kuboi T. Metal binding by citrus dehydrin with histidine-rich domains. J Exp Bot 2005; 56:2695-703.
    • (2005) J Exp Bot , vol.56 , pp. 2695-2703
    • Hara, M.1    Fujinaga, M.2    Kuboi, T.3
  • 46
    • 0028291932 scopus 로고
    • KEKE motifs: Proposed roles in protein-protein association and presentation of peptides by MHC Class I receptors
    • Realini C, Rogers SW, Rechsteiner M. KEKE motifs: Proposed roles in protein-protein association and presentation of peptides by MHC Class I receptors. FEBS Lett 1994; 348:109-13.
    • (1994) FEBS Lett , vol.348 , pp. 109-113
    • Realini, C.1    Rogers, S.W.2    Rechsteiner, M.3
  • 47
    • 33749987806 scopus 로고    scopus 로고
    • Identification of plant cytoskeletoninteracting proteins by screening for actin stress fiber association in mammalian fibroblasts
    • Abu-Abied M, Golomb L, Belausov E, Huang S, Geiger B, Kam Z, et al. Identification of plant cytoskeletoninteracting proteins by screening for actin stress fiber association in mammalian fibroblasts. Plant J 2006; 48:367-79.
    • (2006) Plant J , vol.48 , pp. 367-379
    • Abu-Abied, M.1    Golomb, L.2    Belausov, E.3    Huang, S.4    Geiger, B.5    Kam, Z.6
  • 49
    • 33748489098 scopus 로고    scopus 로고
    • Desiccation of the resurrection plant Craterostigma plantagineum induces dynamic changes in protein phosphorylation
    • Röhrig H, Schmidt J, Colby T, Bräutigam A, Hufnagel P, Bartels D. Desiccation of the resurrection plant Craterostigma plantagineum induces dynamic changes in protein phosphorylation. Plant Cell Environ 2006; 29:1606-17.
    • (2006) Plant Cell Environ , vol.29 , pp. 1606-1617
    • Röhrig, H.1    Schmidt, J.2    Colby, T.3    Bräutigam, A.4    Hufnagel, P.5    Bartels, D.6
  • 50
    • 10644286555 scopus 로고    scopus 로고
    • β-Elimination coupled with tandem mass spectrometry for the identification of in vivo and in vitro phosphorylation sites in maize dehydrin DHN1 protein
    • Jiang X, Wang Y. β-Elimination coupled with tandem mass spectrometry for the identification of in vivo and in vitro phosphorylation sites in maize dehydrin DHN1 protein. Biochemistry 2004; 43:15567-76.
    • (2004) Biochemistry , vol.43 , pp. 15567-15576
    • Jiang, X.1    Wang, Y.2
  • 51
    • 0032033115 scopus 로고    scopus 로고
    • Phosphorylation mediates the nuclear targeting of the maize Rab17 protein
    • Jensen AB, Goday A, Figueras M, Jessop AC, Pagès M. Phosphorylation mediates the nuclear targeting of the maize Rab17 protein. Plant J 1998; 13:691-7.
    • (1998) Plant J , vol.13 , pp. 691-697
    • Jensen, A.B.1    Goday, A.2    Figueras, M.3    Jessop, A.C.4    Pagès, M.5
  • 52
    • 3042709455 scopus 로고    scopus 로고
    • Protein kinase CK2 modulates developmental functions of the abscisic acid responsive protein Rab17 from maize
    • Riera M, Figueras M, Lopez C, Goday A, Pages M. Protein kinase CK2 modulates developmental functions of the abscisic acid responsive protein Rab17 from maize. Proc Natl Acad Sci USA 2004; 101:9879-84.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9879-9884
    • Riera, M.1    Figueras, M.2    Lopez, C.3    Goday, A.4    Pages, M.5
  • 53
    • 47249136621 scopus 로고    scopus 로고
    • A versatile strategy to define the phosphorylation preferences of plant protein kinases and screen for putative substrates
    • Vlad F, Turk BE, Peynot P, Leung J, Merlot S. A versatile strategy to define the phosphorylation preferences of plant protein kinases and screen for putative substrates. Plant J 2008; 55:104-17.
    • (2008) Plant J , vol.55 , pp. 104-117
    • Vlad, F.1    Turk, B.E.2    Peynot, P.3    Leung, J.4    Merlot, S.5
  • 54
    • 0033769133 scopus 로고    scopus 로고
    • Purification of recombinant Arabidopsis thaliana dehydrins by metal ion affinity chromatography
    • Svensson J, Palva ET, Welin B. Purification of recombinant Arabidopsis thaliana dehydrins by metal ion affinity chromatography. Protein Expr Purif 2000; 20:169-78.
    • (2000) Protein Expr Purif , vol.20 , pp. 169-178
    • Svensson, J.1    Palva, E.T.2    Welin, B.3
  • 55
    • 0037067730 scopus 로고    scopus 로고
    • A metalbinding member of the late embryogenesis abundant protein family transports iron in the phloem of Ricinus communis L
    • Kruger C, Berkowitz O, Stephan UW, Hell R. A metalbinding member of the late embryogenesis abundant protein family transports iron in the phloem of Ricinus communis L. J Biol Chem 2002; 277:25062-9.
    • (2002) J Biol Chem , vol.277 , pp. 25062-25069
    • Kruger, C.1    Berkowitz, O.2    Stephan, U.W.3    Hell, R.4
  • 57
    • 0035859817 scopus 로고    scopus 로고
    • Functional activity and role of cation-efflux family members in Ni hyperaccumulation in Thlaspi goesingense
    • Persans MW, Nieman K, Salt DE. Functional activity and role of cation-efflux family members in Ni hyperaccumulation in Thlaspi goesingense. Proc Natl Acad Sci USA 2001; 98:9995-10000.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9995-10000
    • Persans, M.W.1    Nieman, K.2    Salt, D.E.3
  • 58
    • 43749090437 scopus 로고    scopus 로고
    • Deletion of a histidine-rich loop of AtMTP1, a vacuolar Zn(2+)/H(+) antiporter of Arabidopsis thaliana, stimulates the transport activity
    • Kawachi M, Kobae Y, Mimura T, Maeshima M. Deletion of a histidine-rich loop of AtMTP1, a vacuolar Zn(2+)/H(+) antiporter of Arabidopsis thaliana, stimulates the transport activity. J Biol Chem 2008; 283:8374-83.
    • (2008) J Biol Chem , vol.283 , pp. 8374-8383
    • Kawachi, M.1    Kobae, Y.2    Mimura, T.3    Maeshima, M.4
  • 59
    • 33748510154 scopus 로고    scopus 로고
    • Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects
    • Tompa P, Bánki P, Bokor M, Kamasa P, Kovács D, Lasanda G, Tompa K. Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects. Biophys J 2006; 91:2243-9.
    • (2006) Biophys J , vol.91 , pp. 2243-2249
    • Tompa, P.1    Bánki, P.2    Bokor, M.3    Kamasa, P.4    Kovács, D.5    Lasanda, G.6    Tompa, K.7
  • 60
    • 0028150137 scopus 로고
    • Purification and characterization of COR85-oligomeric complex from cold-acclimated spinach
    • Kazuoka T, Oeda K. Purification and characterization of COR85-oligomeric complex from cold-acclimated spinach. Plant Cell Physiol 1994; 35:601-11.
    • (1994) Plant Cell Physiol , vol.35 , pp. 601-611
    • Kazuoka, T.1    Oeda, K.2
  • 61
    • 0029379706 scopus 로고
    • Immunolocalization of freezing-toleranceassociated proteins in the cytoplasm and nucleoplasm of wheat crown tissues
    • Houde M, Daniel C, Lachapelle M, Allard F, Laliberté S, Sarhan F. Immunolocalization of freezing-toleranceassociated proteins in the cytoplasm and nucleoplasm of wheat crown tissues. Plant J 1995; 8:583-93.
    • (1995) Plant J , vol.8 , pp. 583-593
    • Houde, M.1    Daniel, C.2    Lachapelle, M.3    Allard, F.4    Laliberté, S.5    Sarhan, F.6
  • 62
    • 0032701931 scopus 로고    scopus 로고
    • Dehydrins in cold-acclimated apices of birch (Betula pubescens Ehrh.): Production, localization and potential role in rescuing enzyme function during dehydration
    • Rinne PLH, Kaikuranta PLM, van der Plas LHW, van der Schoot C. Dehydrins in cold-acclimated apices of birch (Betula pubescens Ehrh.): production, localization and potential role in rescuing enzyme function during dehydration. Planta 1999; 209:377-88.
    • (1999) Planta , vol.209 , pp. 377-388
    • Rinne, P.L.H.1    Kaikuranta, P.L.M.2    van der Plas, L.H.W.3    van der Schoot, C.4
  • 65
    • 0033047676 scopus 로고    scopus 로고
    • Purification, immunolocalization, cryoprotective and antifreeze activity of PCA60: A dehydrin from peach (Prunus persica)
    • Wisniewski M, Webb R, Balsamo R, Close TJ, Yu XM, Griffith M. Purification, immunolocalization, cryoprotective and antifreeze activity of PCA60: A dehydrin from peach (Prunus persica). Physiol Plant 1999; 105:600-8.
    • (1999) Physiol Plant , vol.105 , pp. 600-608
    • Wisniewski, M.1    Webb, R.2    Balsamo, R.3    Close, T.J.4    Yu, X.M.5    Griffith, M.6
  • 67
    • 58149500610 scopus 로고    scopus 로고
    • Cold stability of intrinsically disordered proteins
    • Tantos A, Friedrich P, Tompa P. Cold stability of intrinsically disordered proteins. FEBS Lett 2009; 583:465-9.
    • (2009) FEBS Lett , vol.583 , pp. 465-469
    • Tantos, A.1    Friedrich, P.2    Tompa, P.3
  • 68
    • 4444293567 scopus 로고    scopus 로고
    • Radical scavenging activity and oxidative modification of citrus dehydrin
    • Hara M, Fujinaga M, Kuboi T. Radical scavenging activity and oxidative modification of citrus dehydrin. Plant Physiol Biochem 2004; 42:657-62.
    • (2004) Plant Physiol Biochem , vol.42 , pp. 657-662
    • Hara, M.1    Fujinaga, M.2    Kuboi, T.3
  • 69
    • 34247325590 scopus 로고    scopus 로고
    • ROS production and protein oxidation as a novel mechanism for seed dormancy alleviation
    • Oracz K, El-Maarouf Bouteau H, Farrant JM, Cooper K, Belghazi M, Job C, et al. ROS production and protein oxidation as a novel mechanism for seed dormancy alleviation. Plant J 2007; 50:452-65.
    • (2007) Plant J , vol.50 , pp. 452-465
    • Oracz, K.1    el-Maarouf Bouteau, H.2    Farrant, J.M.3    Cooper, K.4    Belghazi, M.5    Job, C.6
  • 70
    • 33344476927 scopus 로고    scopus 로고
    • Two different late embryogenesis abundant proteins from Arabidopsis thaliana contain specific domains that inhibit Escherichia coli growth
    • Campos F, Zamudio F, Covarrubias AA. Two different late embryogenesis abundant proteins from Arabidopsis thaliana contain specific domains that inhibit Escherichia coli growth. Biochem Biophys Res Commun 2006; 342:406-13.
    • (2006) Biochem Biophys Res Commun , vol.342 , pp. 406-413
    • Campos, F.1    Zamudio, F.2    Covarrubias, A.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.