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Volumn 1798, Issue 9, 2010, Pages 1812-1820

Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state

Author keywords

Desiccation; FTIR spectroscopy; Intrinsically disordered proteins; LEA proteins; Lipid phase transitions; Protein secondary structure

Indexed keywords

CARBONYL DERIVATIVE; FATTY ACID; GALACTOSE; GALACTOSYLDIACYLGLYCEROL; HEAT SHOCK PROTEIN; LIPOSOME; PROTEIN COR15A; PROTEIN COR15B; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; ARABIDOPSIS PROTEIN; COR15 PROTEIN, ARABIDOPSIS; MEMBRANE LIPID;

EID: 77954658735     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.05.015     Document Type: Article
Times cited : (94)

References (76)
  • 2
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., Wright P.E. 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
  • 3
    • 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, 579:3346-3354.
    • (2005) FEBS Lett. , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 4
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • Tompa P., Csermely P. The role of structural disorder in the function of RNA and protein chaperones. FASEB J. 2004, 18:1169-1175.
    • (2004) FASEB J. , vol.18 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 7
    • 0019874708 scopus 로고
    • Developmental biochemistry of cottonseed embryogenesis and germination: changing messenger ribonucleic acid populations as shown by in vitro and in vivo protein synthesis
    • Dure L., Greenway S.C., Galau G.A. Developmental biochemistry of cottonseed embryogenesis and germination: changing messenger ribonucleic acid populations as shown by in vitro and in vivo protein synthesis. Biochemistry 1981, 20:4162-4168.
    • (1981) Biochemistry , vol.20 , pp. 4162-4168
    • Dure, L.1    Greenway, S.C.2    Galau, G.A.3
  • 8
    • 34548460796 scopus 로고    scopus 로고
    • The continuing conundrum of LEA proteins
    • Tunnacliffe A., Wise M.J. The continuing conundrum of LEA proteins. Naturwissenschaften 2007, 94:791-812.
    • (2007) Naturwissenschaften , vol.94 , pp. 791-812
    • Tunnacliffe, A.1    Wise, M.J.2
  • 9
    • 0033498862 scopus 로고    scopus 로고
    • Plant cold acclimation: freezing tolerance genes and regulatory mechanisms
    • Thomashow M.F. Plant cold acclimation: freezing tolerance genes and regulatory mechanisms. Annu. Rev. Plant Physiol. Plant Mol. Biol. 1999, 50:571-599.
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 571-599
    • Thomashow, M.F.1
  • 10
    • 34648834403 scopus 로고    scopus 로고
    • Cold stress regulation of gene expression in plants
    • Chinnusamy V., Zhu J., Zhu J.-K. Cold stress regulation of gene expression in plants. Trends Plant Sci. 2007, 12:444-451.
    • (2007) Trends Plant Sci. , vol.12 , pp. 444-451
    • Chinnusamy, V.1    Zhu, J.2    Zhu, J.-K.3
  • 11
    • 33645100080 scopus 로고    scopus 로고
    • Arabidopsis transcription factors regulating cold acclimation
    • van Buskirk H.A., Thomashow M.F. Arabidopsis transcription factors regulating cold acclimation. Physiol. Plant. 2006, 126:72-80.
    • (2006) Physiol. Plant. , vol.126 , pp. 72-80
    • van Buskirk, H.A.1    Thomashow, M.F.2
  • 12
    • 12844280128 scopus 로고    scopus 로고
    • Roles of the CBF2 and ZAT12 transcription factors in configuring the low temperature transcriptome of Arabidopsis
    • Vogel J.T., Zarka D.G., van Buskirk H.A., Fowler S.G., Thomashow M.F. Roles of the CBF2 and ZAT12 transcription factors in configuring the low temperature transcriptome of Arabidopsis. Plant J. 2005, 41:195-211.
    • (2005) Plant J. , vol.41 , pp. 195-211
    • Vogel, J.T.1    Zarka, D.G.2    van Buskirk, H.A.3    Fowler, S.G.4    Thomashow, M.F.5
  • 13
    • 0001695165 scopus 로고
    • Molecular cloning and expression of cor (cold-regulated) genes in Arabidopsis thaliana
    • Hajela R.K., Horvath D.P., Gilmour S.J., Thomashow M.F. Molecular cloning and expression of cor (cold-regulated) genes in Arabidopsis thaliana. Plant Physiol. 1990, 93:1246-1252.
    • (1990) Plant Physiol. , vol.93 , pp. 1246-1252
    • Hajela, R.K.1    Horvath, D.P.2    Gilmour, S.J.3    Thomashow, M.F.4
  • 14
    • 0000038789 scopus 로고
    • DNA sequence analysis of a complementary DNA for cold-regulated Arabidopsis gene cor15 and characterization of the COR15 polypeptide
    • Lin C., Thomashow M.F. DNA sequence analysis of a complementary DNA for cold-regulated Arabidopsis gene cor15 and characterization of the COR15 polypeptide. Plant Physiol. 1992, 99:519-525.
    • (1992) Plant Physiol. , vol.99 , pp. 519-525
    • Lin, C.1    Thomashow, M.F.2
  • 15
    • 34250683382 scopus 로고    scopus 로고
    • Arabidopsis Cor15am is a chloroplast stromal protein that has cryoprotective activity and forms oligomers
    • Nakayama K., Okawa K., Kakizaki T., Honma T., Itoh H., Inaba T. Arabidopsis Cor15am is a chloroplast stromal protein that has cryoprotective activity and forms oligomers. Plant Physiol. 2007, 144:513-523.
    • (2007) Plant Physiol. , vol.144 , pp. 513-523
    • Nakayama, K.1    Okawa, K.2    Kakizaki, T.3    Honma, T.4    Itoh, H.5    Inaba, T.6
  • 16
    • 0027750416 scopus 로고
    • Arabidopsis thaliana cor15b, an apparent homologue of cor15a, is strongly responsive to cold and ABA, but not drought
    • Wilhelm K.S., Thomashow M.F. Arabidopsis thaliana cor15b, an apparent homologue of cor15a, is strongly responsive to cold and ABA, but not drought. Plant Mol. Biol. 1993, 23:1073-1077.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 1073-1077
    • Wilhelm, K.S.1    Thomashow, M.F.2
  • 17
    • 42149115630 scopus 로고    scopus 로고
    • LEA (late embryogenesis abundant) proteins and their encoding genes in Arabidopsis thaliana
    • Hundertmark M., Hincha D.K. 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
  • 18
    • 0027140360 scopus 로고
    • Molecular responses to water deficit
    • Bray E.A. Molecular responses to water deficit. Plant Physiol. 1993, 103:1035-1040.
    • (1993) Plant Physiol. , vol.103 , pp. 1035-1040
    • Bray, E.A.1
  • 19
    • 0029825615 scopus 로고    scopus 로고
    • Constitutive expression of the cold-regulated Arabidopsis thaliana COR15a gene affects both chloroplast and protoplast freezing tolerance
    • Artus N.N., Uemura M., Steponkus P.L., Gilmour S.J., Lin C., Thomashow M.F. Constitutive expression of the cold-regulated Arabidopsis thaliana COR15a gene affects both chloroplast and protoplast freezing tolerance. Proc. Natl Acad. Sci. USA 1996, 93:13404-13409.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13404-13409
    • Artus, N.N.1    Uemura, M.2    Steponkus, P.L.3    Gilmour, S.J.4    Lin, C.5    Thomashow, M.F.6
  • 21
    • 0030137088 scopus 로고    scopus 로고
    • Purification and properties of Arabidopsis thaliana COR (Cold-Regulated) gene polypeptides COR15am and COR6.6 expressed in Escherichia coli
    • Gilmour S.J., Lin C., Thomashow M.F. Purification and properties of Arabidopsis thaliana COR (Cold-Regulated) gene polypeptides COR15am and COR6.6 expressed in Escherichia coli. Plant Physiol. 1996, 111:293-299.
    • (1996) Plant Physiol. , vol.111 , pp. 293-299
    • Gilmour, S.J.1    Lin, C.2    Thomashow, M.F.3
  • 22
    • 0026684471 scopus 로고
    • A cold-regulated Arabidopsis gene encodes a polypeptide having potent cryoprotective activity
    • Lin C., Thomashow M.F. A cold-regulated Arabidopsis gene encodes a polypeptide having potent cryoprotective activity. Biochem. Biophys. Res. Comm. 1992, 183:1103-1108.
    • (1992) Biochem. Biophys. Res. Comm. , vol.183 , pp. 1103-1108
    • Lin, C.1    Thomashow, M.F.2
  • 23
    • 45849096406 scopus 로고    scopus 로고
    • Evaluation of the protective activities of a late embryogenesis abundant (LEA) related protein, Cor15am, during various stresses in vitro
    • Nakayama K., Okawa K., Kakizaki T., Inaba T. Evaluation of the protective activities of a late embryogenesis abundant (LEA) related protein, Cor15am, during various stresses in vitro. Biosci. Biotechnol. Biochem. 2008, 72:1642-1645.
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 1642-1645
    • Nakayama, K.1    Okawa, K.2    Kakizaki, T.3    Inaba, T.4
  • 25
    • 17044405795 scopus 로고    scopus 로고
    • LEA proteins prevent protein aggregation due to water stress
    • Goyal K., Walton L.J., Tunnacliffe A. LEA proteins prevent protein aggregation due to water stress. Biochem. J. 2005, 388:151-157.
    • (2005) Biochem. J. , vol.388 , pp. 151-157
    • Goyal, K.1    Walton, L.J.2    Tunnacliffe, A.3
  • 29
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa
    • Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Anal. Biochem. 1987, 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 30
    • 77956741418 scopus 로고
    • Ultraviolet spectra of proteins and amino acids
    • Wetlaufer D.B. Ultraviolet spectra of proteins and amino acids. Adv. Protein Chem. 1962, 17:303-390.
    • (1962) Adv. Protein Chem. , vol.17 , pp. 303-390
    • Wetlaufer, D.B.1
  • 31
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis
    • Sreerama N., Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. Anal. Biochem. 2000, 287:243-251.
    • (2000) Anal. Biochem. , vol.287 , pp. 243-251
    • Sreerama, N.1    Woody, R.W.2
  • 33
    • 0036239562 scopus 로고    scopus 로고
    • Specific effects of fructo- and gluco-oligosaccharides in the preservation of liposomes during drying
    • Hincha D.K., Zuther E., Hellwege E.M., Heyer A.G. Specific effects of fructo- and gluco-oligosaccharides in the preservation of liposomes during drying. Glycobiology 2002, 12:103-110.
    • (2002) Glycobiology , vol.12 , pp. 103-110
    • Hincha, D.K.1    Zuther, E.2    Hellwege, E.M.3    Heyer, A.G.4
  • 34
    • 33646179170 scopus 로고    scopus 로고
    • Low amounts of sucrose are sufficient to depress the phase transition temperature of dry phosphatidylcholine, but not for lyoprotection of liposomes
    • Cacela C., Hincha D.K. Low amounts of sucrose are sufficient to depress the phase transition temperature of dry phosphatidylcholine, but not for lyoprotection of liposomes. Biophys. J. 2006, 90:2831-2842.
    • (2006) Biophys. J. , vol.90 , pp. 2831-2842
    • Cacela, C.1    Hincha, D.K.2
  • 35
    • 0041320844 scopus 로고    scopus 로고
    • Intermolecular interactions in dry and rehydrated pure and mixed bilayers of phosphatidylcholine and digalactosyldiacylglycerol: a Fourier-transform infrared spectroscopy study
    • Popova A.V., Hincha D.K. Intermolecular interactions in dry and rehydrated pure and mixed bilayers of phosphatidylcholine and digalactosyldiacylglycerol: a Fourier-transform infrared spectroscopy study. Biophys. J. 2003, 85:1682-1690.
    • (2003) Biophys. J. , vol.85 , pp. 1682-1690
    • Popova, A.V.1    Hincha, D.K.2
  • 36
    • 0031205005 scopus 로고    scopus 로고
    • Stabilization of dry membranes by mixtures of hydroxyethyl starch and glucose: the role of vitrification
    • Crowe J.H., Oliver A.E., Hoekstra F.A., Crowe L.M. Stabilization of dry membranes by mixtures of hydroxyethyl starch and glucose: the role of vitrification. Cryobiology 1997, 35:20-30.
    • (1997) Cryobiology , vol.35 , pp. 20-30
    • Crowe, J.H.1    Oliver, A.E.2    Hoekstra, F.A.3    Crowe, L.M.4
  • 37
    • 34548290371 scopus 로고    scopus 로고
    • Effects of cholesterol on dry bilayers: interactions between phosphatidylcholine unsaturation and glycolopid or free sugar
    • Popova A.V., Hincha D.K. Effects of cholesterol on dry bilayers: interactions between phosphatidylcholine unsaturation and glycolopid or free sugar. Biophys. J. 2007, 93:1204-1214.
    • (2007) Biophys. J. , vol.93 , pp. 1204-1214
    • Popova, A.V.1    Hincha, D.K.2
  • 38
    • 33747818327 scopus 로고    scopus 로고
    • Kalign, Kalignvu and Mumsa: web servers for multiple sequence alignment
    • Lassmann T., Sonnhammer E.L.L. Kalign, Kalignvu and Mumsa: web servers for multiple sequence alignment. Nucleic Acids Res. 2006, 34:W596-W599.
    • (2006) Nucleic Acids Res. , vol.34
    • Lassmann, T.1    Sonnhammer, E.L.L.2
  • 39
  • 40
    • 0025334980 scopus 로고
    • Improvements in protein secondary structure prediction by an enhanced neural network
    • Kneller D.G., Cohen F.E., Langridge R. Improvements in protein secondary structure prediction by an enhanced neural network. J. Mol. Biol. 1990, 214:171-182.
    • (1990) J. Mol. Biol. , vol.214 , pp. 171-182
    • Kneller, D.G.1    Cohen, F.E.2    Langridge, R.3
  • 41
    • 0029595442 scopus 로고
    • SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
    • Geourjon C., Deleage G. SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Comput. Appl. Biosci. 1995, 11:681-684.
    • (1995) Comput. Appl. Biosci. , vol.11 , pp. 681-684
    • Geourjon, C.1    Deleage, G.2
  • 42
    • 0036568279 scopus 로고    scopus 로고
    • Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles
    • Pollastrii G., Przybyski D., Rost B., Baldi P. Improving the prediction of protein secondary structure in three and eight classes using recurrent neural networks and profiles. Proteins 2002, 47:228-235.
    • (2002) Proteins , vol.47 , pp. 228-235
    • Pollastrii, G.1    Przybyski, D.2    Rost, B.3    Baldi, P.4
  • 43
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole C., Barber J.D., Barton G.J. The Jpred 3 secondary structure prediction server. Nucleic Acids Res. 2008, 36:W197-W201.
    • (2008) Nucleic Acids Res. , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 44
    • 17844392864 scopus 로고    scopus 로고
    • Combining prediction of secondary structure and solvent accessibility in proteins
    • Adamczak R., Porollo A., Meller J. Combining prediction of secondary structure and solvent accessibility in proteins. Proteins 2005, 59:467-475.
    • (2005) Proteins , vol.59 , pp. 467-475
    • Adamczak, R.1    Porollo, A.2    Meller, J.3
  • 45
    • 84987288517 scopus 로고
    • Analysis of conformations of amino acid residues and prediction of backbone topography in proteins
    • Burgess A.W., Ponnuswamy P.K., Sheraga H.A. Analysis of conformations of amino acid residues and prediction of backbone topography in proteins. Israel J. Chem. 1974, 2:239-286.
    • (1974) Israel J. Chem. , vol.2 , pp. 239-286
    • Burgess, A.W.1    Ponnuswamy, P.K.2    Sheraga, H.A.3
  • 46
    • 0001040367 scopus 로고
    • An algorithm for secondary structure prediction based on class prediction
    • Deleage G., Roux B. An algorithm for secondary structure prediction based on class prediction. Protein Eng. 1987, 1:289-294.
    • (1987) Protein Eng. , vol.1 , pp. 289-294
    • Deleage, G.1    Roux, B.2
  • 47
    • 0029804192 scopus 로고    scopus 로고
    • Identification and application of the concepts important for accurate and reliable protein secondary structure prediction
    • King R.D., Sternberg M.J.E. Identification and application of the concepts important for accurate and reliable protein secondary structure prediction. Protein Sci. 1996, 5:2298-2310.
    • (1996) Protein Sci. , vol.5 , pp. 2298-2310
    • King, R.D.1    Sternberg, M.J.E.2
  • 48
    • 0029884694 scopus 로고    scopus 로고
    • GOR method for predicting protein secondary structure from amino acid sequence
    • Garnier J., Gibrat J.F., Robson B. GOR method for predicting protein secondary structure from amino acid sequence. Meth. Enzymol. 1996, 266:97-120.
    • (1996) Meth. Enzymol. , vol.266 , pp. 97-120
    • Garnier, J.1    Gibrat, J.F.2    Robson, B.3
  • 49
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • Garnier J., Osguthorpe D.J., Robson B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol. 1978, 120:97-120.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 50
    • 0000268209 scopus 로고
    • Protein secondary structure prediction with neural networks
    • Holley L.H., Karplus M. Protein secondary structure prediction with neural networks. Proc. Natl Acad. Sci. USA 1989, 86:152-156.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 152-156
    • Holley, L.H.1    Karplus, M.2
  • 51
    • 0025633838 scopus 로고
    • Machine learning approach for the prediction of protein secondary structure
    • King R.D., Sternberg M.J.E. Machine learning approach for the prediction of protein secondary structure. J. Mol. Biol. 1990, 216:441-457.
    • (1990) J. Mol. Biol. , vol.216 , pp. 441-457
    • King, R.D.1    Sternberg, M.J.E.2
  • 52
    • 51749085388 scopus 로고    scopus 로고
    • HELIQUEST: a web server to screen sequences with specific α-helical properties
    • Gautier R., Douguet D., Antonny B., Drin G. HELIQUEST: a web server to screen sequences with specific α-helical properties. Bioinformatics 2008, 15:2101-2102.
    • (2008) Bioinformatics , vol.15 , pp. 2101-2102
    • Gautier, R.1    Douguet, D.2    Antonny, B.3    Drin, G.4
  • 53
    • 50649098927 scopus 로고    scopus 로고
    • Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins
    • Kovacs D., Kalmar E., Torok Z., Tompa P. Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. Plant Physiol. 2008, 147:381-390.
    • (2008) Plant Physiol. , vol.147 , pp. 381-390
    • Kovacs, D.1    Kalmar, E.2    Torok, Z.3    Tompa, P.4
  • 54
    • 0030138097 scopus 로고    scopus 로고
    • Effects of COR6.6 and COR15am polypeptides encoded by cor (cold-regulated) genes of Arabidopsis thaliana on dehydration-induced phase transitions of phospholipid membranes
    • Webb M.S., Gilmour S.J., Thomashow M.F., Steponkus P.L. Effects of COR6.6 and COR15am polypeptides encoded by cor (cold-regulated) genes of Arabidopsis thaliana on dehydration-induced phase transitions of phospholipid membranes. Plant Physiol. 1996, 111:301-312.
    • (1996) Plant Physiol. , vol.111 , pp. 301-312
    • Webb, M.S.1    Gilmour, S.J.2    Thomashow, M.F.3    Steponkus, P.L.4
  • 55
    • 0026008797 scopus 로고
    • Biochemical and biophysical properties of thylakoid acyl lipids
    • Webb M.S., Green B.R. Biochemical and biophysical properties of thylakoid acyl lipids. Biochim. Biophys. Acta 1991, 1060:133-158.
    • (1991) Biochim. Biophys. Acta , vol.1060 , pp. 133-158
    • Webb, M.S.1    Green, B.R.2
  • 56
    • 0024460832 scopus 로고
    • Direct transition of dioleoylphosphatidylethanolamine from lamellar gel to inverted hexagonal phase caused by trehalose
    • Aurell Wistrom C., Rand R.P., Crowe L.M., Spargo B.J., Crowe J.H. Direct transition of dioleoylphosphatidylethanolamine from lamellar gel to inverted hexagonal phase caused by trehalose. Biochim. Biophys. Acta 1989, 984:238-242.
    • (1989) Biochim. Biophys. Acta , vol.984 , pp. 238-242
    • Aurell Wistrom, C.1    Rand, R.P.2    Crowe, L.M.3    Spargo, B.J.4    Crowe, J.H.5
  • 57
    • 0026070508 scopus 로고
    • Phospholipid phase transitions in model and biological membranes as studied by infrared spectroscopy
    • Mantsch H.H., McElhaney R.N. Phospholipid phase transitions in model and biological membranes as studied by infrared spectroscopy. Chem. Phys. Lipids 1991, 57:213-226.
    • (1991) Chem. Phys. Lipids , vol.57 , pp. 213-226
    • Mantsch, H.H.1    McElhaney, R.N.2
  • 58
    • 0025134135 scopus 로고
    • II) phase, and non-lamellar phase transitions of lipids
    • II) phase, and non-lamellar phase transitions of lipids. Biochim. Biophys. Acta 1990, 1031:1-69.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 1-69
    • Seddon, J.M.1
  • 60
    • 0014062165 scopus 로고
    • Use of helical wheels to represent the structures of proteins and to identify segments with helical potential
    • Schiffer M., Edmundson A.B. Use of helical wheels to represent the structures of proteins and to identify segments with helical potential. Biophys. J. 1967, 7:121-135.
    • (1967) Biophys. J. , vol.7 , pp. 121-135
    • Schiffer, M.1    Edmundson, A.B.2
  • 61
    • 42149111687 scopus 로고    scopus 로고
    • Inventory, evolution and expression profiling diversity of the LEA (late embryogenesis abundant) protein gene family in Arabidopsis thaliana
    • Bies-Etheve N., Gaubier-Comella P., Debures A., Lasserre E., Jobet E., Raynal M., Cooke R., Delseny M. Inventory, evolution and expression profiling diversity of the LEA (late embryogenesis abundant) protein gene family in Arabidopsis thaliana. Plant Mol. Biol. 2008, 67:107-124.
    • (2008) Plant Mol. Biol. , vol.67 , pp. 107-124
    • Bies-Etheve, N.1    Gaubier-Comella, P.2    Debures, A.3    Lasserre, E.4    Jobet, E.5    Raynal, M.6    Cooke, R.7    Delseny, M.8
  • 62
    • 33745655415 scopus 로고    scopus 로고
    • Structural investigation of disordered stress proteins. Comparison of full-length dehydrins with isolated peptides of their conserved segments
    • Mouillon J.-M., 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, 141:638-650.
    • (2006) Plant Physiol. , vol.141 , pp. 638-650
    • Mouillon, J.-M.1    Gustafsson, P.2    Harryson, P.3
  • 63
    • 33745476713 scopus 로고    scopus 로고
    • Comparative analysis of the heat stable proteome of radicles of Medicago truncatula seeds during germination identifies late embryogenesis abundant proteins associated with desiccation tolerance
    • Boudet J., Buitink J., Hoekstra F.A., Rogniaux H., Larre C., Satour P., Leprince O. Comparative analysis of the heat stable proteome of radicles of Medicago truncatula seeds during germination identifies late embryogenesis abundant proteins associated with desiccation tolerance. Plant Physiol. 2006, 140:1418-1436.
    • (2006) Plant Physiol. , vol.140 , pp. 1418-1436
    • Boudet, J.1    Buitink, J.2    Hoekstra, F.A.3    Rogniaux, H.4    Larre, C.5    Satour, P.6    Leprince, O.7
  • 64
    • 0038305931 scopus 로고    scopus 로고
    • Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein
    • Goyal K., Tisi L., Basran A., Browne J., Burnell A., Zurdo J., Tunnacliffe A. Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. J. Biol. Chem. 2003, 278:12977-12984.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12977-12984
    • Goyal, K.1    Tisi, L.2    Basran, A.3    Browne, J.4    Burnell, A.5    Zurdo, J.6    Tunnacliffe, A.7
  • 65
    • 17844363270 scopus 로고    scopus 로고
    • Gene cloning and characterization of a soybean (Glycine max L.) LEA protein, GmPM16
    • Shih M., Lin S., Hsieh J., Tsou C., Chow T., Lin T., Hsing Y. Gene cloning and characterization of a soybean (Glycine max L.) LEA protein, GmPM16. Plant Mol. Biol. 2004, 56:689-703.
    • (2004) Plant Mol. Biol. , vol.56 , pp. 689-703
    • Shih, M.1    Lin, S.2    Hsieh, J.3    Tsou, C.4    Chow, T.5    Lin, T.6    Hsing, Y.7
  • 67
    • 0035847037 scopus 로고    scopus 로고
    • Isolation and characterization of a D-7 LEA protein from pollen that stabilizes glasses in vitro
    • Wolkers W.F., McCready S., Brandt W.F., Lindsey G.G., Hoekstra F.A. Isolation and characterization of a D-7 LEA protein from pollen that stabilizes glasses in vitro. Biochim. Biophys. Acta 2001, 1544:196-206.
    • (2001) Biochim. Biophys. Acta , vol.1544 , pp. 196-206
    • Wolkers, W.F.1    McCready, S.2    Brandt, W.F.3    Lindsey, G.G.4    Hoekstra, F.A.5
  • 68
    • 0033516703 scopus 로고    scopus 로고
    • An amphipathic α-helix at a membrane interface: a structural study using a novel X-ray diffraction method
    • Hristova K., Wimley W.C., Mishra V.K., Anantharamaiah G.M., Segrest J.P., White S.H. An amphipathic α-helix at a membrane interface: a structural study using a novel X-ray diffraction method. J. Mol. Biol. 1999, 290:99-117.
    • (1999) J. Mol. Biol. , vol.290 , pp. 99-117
    • Hristova, K.1    Wimley, W.C.2    Mishra, V.K.3    Anantharamaiah, G.M.4    Segrest, J.P.5    White, S.H.6
  • 69
    • 0028360934 scopus 로고
    • Interactions of synthetic peptide analogs of the class A amphipathic helix with lipids
    • Mishra V.K., Palgunachari M.N., Segrest J.P., Anantharamaiah G.M. Interactions of synthetic peptide analogs of the class A amphipathic helix with lipids. J. Biol. Chem. 1994, 289:7185-7191.
    • (1994) J. Biol. Chem. , vol.289 , pp. 7185-7191
    • Mishra, V.K.1    Palgunachari, M.N.2    Segrest, J.P.3    Anantharamaiah, G.M.4
  • 71
    • 0027564435 scopus 로고
    • A repeating 11-mer amino acid motif and plant desiccation
    • Dure L. A repeating 11-mer amino acid motif and plant desiccation. Plant J. 1993, 3:363-369.
    • (1993) Plant J. , vol.3 , pp. 363-369
    • Dure, L.1
  • 72
    • 67049098975 scopus 로고    scopus 로고
    • Desiccation induced structural alterations in a 66-amino acid fragment of an anhydrobiotic nematode late embryogenesis abundant (LEA) protein
    • Li D., He X. Desiccation induced structural alterations in a 66-amino acid fragment of an anhydrobiotic nematode late embryogenesis abundant (LEA) protein. Biomacromolecules 2009, 10:1469-1477.
    • (2009) Biomacromolecules , vol.10 , pp. 1469-1477
    • Li, D.1    He, X.2
  • 73
    • 47049119099 scopus 로고    scopus 로고
    • Effects of sugars on the stability of lipid membranes during drying
    • Elsevier, Amsterdam
    • Hincha D.K., Popova A.V., Cacela C. Effects of sugars on the stability of lipid membranes during drying. Advances in Planar Lipid Bilayers and Liposomes 2006, vol. 3:189-217. Elsevier, Amsterdam.
    • (2006) Advances in Planar Lipid Bilayers and Liposomes , vol.3 , pp. 189-217
    • Hincha, D.K.1    Popova, A.V.2    Cacela, C.3
  • 74
    • 0036181843 scopus 로고    scopus 로고
    • Looking beyond sugars: the role of amphiphilic solutes in preventing adventitious reactions in anhydrobiotes at low water contents
    • Oliver A.E., Hincha D.K., Crowe J.H. Looking beyond sugars: the role of amphiphilic solutes in preventing adventitious reactions in anhydrobiotes at low water contents. Comp. Biochem. Physiol. 2002, 131A:515-525.
    • (2002) Comp. Biochem. Physiol. , vol.131 A , pp. 515-525
    • Oliver, A.E.1    Hincha, D.K.2    Crowe, J.H.3
  • 75
    • 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 J.-M., Eriksson S.K., 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, 148:1925-1937.
    • (2008) Plant Physiol. , vol.148 , pp. 1925-1937
    • Mouillon, J.-M.1    Eriksson, S.K.2    Harryson, P.3
  • 76
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • Tompa P., Szasz C., Buday L. Structural disorder throws new light on moonlighting. Trends Biochem. Sci. 2005, 30:484-489.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 484-489
    • Tompa, P.1    Szasz, C.2    Buday, L.3


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