References
- Plant Mol Biol v.43 Isolation and characterization of a dehydrin gene from white spruce induced upon wounding, drought and cold stresses Armand.S. https://doi.org/10.1023/A:1006453811911
- Plant Physiol v.105 Cold acclimation in genetically related delicious and evegreen peach (Prunus persica [L.] Batsh). Ⅱ. A 60-kilodalton bark protein in cold-acclimated tissues of peach is heat stable and related to the dehydrin family of proteins Arora,R.;Wisniewski,M.E. https://doi.org/10.1104/pp.105.1.95
- Plant Mol. Biol. v.33 Seasonal expression of a dehydrin gene in sibling delicious and everagreen genotypes of peach(Prunus persica [L.] Batsh) Artlip,T.S.;Callahan,A.M.;Brassett.C.L.;Wisniewski,M.E. https://doi.org/10.1023/A:1005787909506
- Trends Plant Sci v.2 Plant responses to water deficit Bray,E.A. https://doi.org/10.1016/S1360-1385(97)82562-9
- a pictorial book of the Korean flora Lee,C.B.
- J. Korean SOC. FOOD NUTR. v.14 no.3 Screening test for antitumor activity of Codonopsis lanceolata and C. pilosula Park,B.D.;Park,Y.G.;Choi,K.S.
- Kor. J. Plant Pathol v.14 no.6 Incidence of disease in Codonopsis lanceolata with different ultivation method Kim,J.H.;Choi,J.S.
- Physiol. Plant. v.97 Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins Close,T.J. https://doi.org/10.1111/j.1399-3054.1996.tb00546.x
- Physiol. Plant v.100 Dehydrins: a commonality in the response of plants to the dehydration and low temperature Close,T.J. https://doi.org/10.1111/j.1399-3054.1997.tb04785.x
- FEBS Lett v.344 Differential expression of a gene encoding an acidic dehydrin in chilling sensitive and freezing tolerant gramineae speacies Danyluk,J.;Houde,M.;Rassart,E.;Sarhan,F. https://doi.org/10.1016/0014-5793(94)00353-X
- Plant Mol. Biol. v.12 Common amino acid sequence domains among the LEA proteins of higher plants Dure,L.I. https://doi.org/10.1007/BF00036962
- Plant Physiol v.98 The expression of proteinase inhibitor genes by methyl jasmonate and jamonic acid Finch-Savage,W.E.;Pramanik,S.K.;Bewley,J.D. https://doi.org/10.1104/pp.98.3.995
- Plant Cell v.6 The maiza abscisic acid-resposive protein Rab17 is located in the nucleus and interacts with nuclear localization signals Goday,A.;Jensen,A.B.;Culianez-Macia,F.A.;Alva,M.M.;Figueras,M.;Seeratosa,J.;Torrent,M.;Pages,M. https://doi.org/10.1105/tpc.6.3.351
- Plant Mol Biol. v.26 Expression, tissue distribution and subcellular localization of dehydrin TAS14 in salt-stressed tomato plants Goday,J.;Lunar,R.;Torres-Schumann,S.;Moreno,J.;Rodrigo,R.M;Pintor-Torro,J.A.. https://doi.org/10.1007/BF00019503
- fir.J.Plant Physiol v.147 Cloning and characterization of cDNA clones of three genes that are differentially expressed during dormancy-breaking in the seeds of Douglas Jarvis,s.B.;Taylor,M.A.;Macleod,M.R.;Davis,H.V. https://doi.org/10.1016/S0176-1617(96)80046-0
- J. Biol. Chem. v.267 Characterization of the gene family encoding abscisic acid and environmental stressinducible proteins of Alfalfa Luo,M.
- GeneDoc : analysis and visualization of genetic variation Nicholas,K.B.;Nicholas,H.B.
- Curr. Opi. Biotechnol v.7 Molecular responses to drought and cold stress Shinozaki,K.;Yamaguchi-Shinozaki,K. https://doi.org/10.1016/S0958-1669(96)80007-3
- Nucleic Acids Research v.22 CLUSTALW : improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-secific gap penalties and weight matrix choice Thompson,J.D.;Higgins.D.G.;Gilbson,T.J. https://doi.org/10.1093/nar/22.22.4673