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Volumn 267, Issue 8, 2000, Pages 2156-2165

A pea nuclear protein that is induced by dehydration belongs to the vicilin superfamily

Author keywords

Chromatin; Desiccation; Nuclei; Pea embryo; Vicilins

Indexed keywords

COMPLEMENTARY DNA; MESSENGER RNA; NUCLEAR PROTEIN; VICILIN;

EID: 0242436115     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01229.x     Document Type: Article
Times cited : (30)

References (59)
  • 1
  • 2
    • 0026914537 scopus 로고
    • Pea dehydrins: Identification, characterisation and expression
    • 2. Roberton, M. & Chandler, P.M. (1992) Pea dehydrins: identification, characterisation and expression. Plant Mol. Biol. 19, 1031-1044.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 1031-1044
    • Roberton, M.1    Chandler, P.M.2
  • 3
    • 0000243386 scopus 로고
    • Abscisic acid induction of cloned cotton late embryogenesis-abundant (Lea) mRNAs
    • 3. Galau, G.A., Hughes, D.W. & Dure, L.S. III (1986) Abscisic acid induction of cloned cotton late embryogenesis-abundant (Lea) mRNAs. Plant Mol. Biol. 7, 155-170.
    • (1986) Plant Mol. Biol. , vol.7 , pp. 155-170
    • Galau, G.A.1    Hughes, D.W.2    Dure L.S. III3
  • 4
    • 0025443920 scopus 로고
    • Gene expression in response to abscisic acid and osmotic stress
    • 4. Skriver, K. & Mundy, J. (1990) Gene expression in response to abscisic acid and osmotic stress. Plant Cell 2, 503-512.
    • (1990) Plant Cell , vol.2 , pp. 503-512
    • Skriver, K.1    Mundy, J.2
  • 6
    • 0024698889 scopus 로고
    • A cDNA-based comparison of dehydration-induced proteins (dehydrins) in barley and corn
    • 6. Close, T.J., Kortt, A.A. & Chandler, P.M. (1989) A cDNA-based comparison of dehydration-induced proteins (dehydrins) in barley and corn. Plant Mol. Biol. 13, 95-108.
    • (1989) Plant Mol. Biol. , vol.13 , pp. 95-108
    • Close, T.J.1    Kortt, A.A.2    Chandler, P.M.3
  • 8
    • 0025719084 scopus 로고
    • Cellular desiccation and hydration: Developmentally regulated proteins, and the maturation and germination of seed embryos
    • 8. Lane, B.G. (1991) Cellular desiccation and hydration: developmentally regulated proteins, and the maturation and germination of seed embryos. FASEB J. 5, 2893-2901.
    • (1991) FASEB J. , vol.5 , pp. 2893-2901
    • Lane, B.G.1
  • 9
    • 0024638573 scopus 로고
    • Temporally modular gene expression during cotyledon development
    • 9. Hughes, D.W. & Galau, G.A. (1989) Temporally modular gene expression during cotyledon development. Genes Dev. 3, 358-369.
    • (1989) Genes Dev. , vol.3 , pp. 358-369
    • Hughes, D.W.1    Galau, G.A.2
  • 10
    • 0030498675 scopus 로고    scopus 로고
    • Dehydrins: Emergence of a biochemical role of a family of plant dehydration proteins
    • 10. Close, T.J. (1996) Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiol. Plant. 97, 795-803.
    • (1996) Physiol. Plant. , vol.97 , pp. 795-803
    • Close, T.J.1
  • 11
    • 0000955291 scopus 로고
    • Cloning, characterization and expression of a cDNA encoding a 50-kilodalton protein specifically induced by cold acclimation in wheat
    • 11. Houde, M., Danyluk, J., LaLiberte, J.-F., Rassart, E., Dhindsa, R.S. & Sarhan, F. (1992) Cloning, characterization and expression of a cDNA encoding a 50-kilodalton protein specifically induced by cold acclimation in wheat. Plant Physiol. 99, 1381-1387.
    • (1992) Plant Physiol. , vol.99 , pp. 1381-1387
    • Houde, M.1    Danyluk, J.2    LaLiberte, J.-F.3    Rassart, E.4    Dhindsa, R.S.5    Sarhan, F.6
  • 12
    • 0027349170 scopus 로고
    • Characterization of a spinach gene responsive to low temperature and water stress
    • 12. Neven, L.G., Haskell, D.W., Hofig, A., Li, Q.-B. & Guy, C.L. (1993) Characterization of a spinach gene responsive to low temperature and water stress. Plant Mol. Biol. 21, 291-305.
    • (1993) Plant Mol. Biol. , vol.21 , pp. 291-305
    • Neven, L.G.1    Haskell, D.W.2    Hofig, A.3    Li, Q.-B.4    Guy, C.L.5
  • 13
    • 0024066710 scopus 로고
    • Abscisic acid and water-stress induce the expression of a novel rice gene
    • 13. Mundy, J. & Chua, N.-H. (1988) Abscisic acid and water-stress induce the expression of a novel rice gene. EMBO J. 7, 2279-2286.
    • (1988) EMBO J. , vol.7 , pp. 2279-2286
    • Mundy, J.1    Chua, N.-H.2
  • 15
    • 0029170832 scopus 로고
    • Changes in chromatin structure associated with germination of maize and their relation with desiccation tolerance
    • 15. Leprince, O., Colson, P., Houssier, C. & Deltour, R. (1995) Changes in chromatin structure associated with germination of maize and their relation with desiccation tolerance. Plant Cell Environ. 18, 619-629.
    • (1995) Plant Cell Environ. , vol.18 , pp. 619-629
    • Leprince, O.1    Colson, P.2    Houssier, C.3    Deltour, R.4
  • 16
    • 0025837183 scopus 로고
    • The nucleosomal core histone octamer at 3.1 Å resolution: A tripartite protein assembly and a left-handed superhelix
    • 16. Arents, G., Burlingame, R.W., Wang, B.W., Love, W.E. & Moudrianakis, E.N. (1991) The nucleosomal core histone octamer at 3.1 Å resolution: a tripartite protein assembly and a left-handed superhelix. Proc. Natl Acad. Sci. USA 88, 10148-10152.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 10148-10152
    • Arents, G.1    Burlingame, R.W.2    Wang, B.W.3    Love, W.E.4    Moudrianakis, E.N.5
  • 17
    • 0027431478 scopus 로고
    • Topography of the histone octamer surface: Repeating structural motifs utilized in the docking of nucleosomal DNA
    • 17. Arents, G. & Moudrianakis, E.N. (1993) Topography of the histone octamer surface: repeating structural motifs utilized in the docking of nucleosomal DNA. Proc. Natl Acad. Sci. USA 90, 10489-10493.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10489-10493
    • Arents, G.1    Moudrianakis, E.N.2
  • 18
    • 0028867087 scopus 로고
    • The histone fold: A ubiquitous architectural motif utilized in DNA compaction and protein dimerization
    • 18. Arents, G. & Moudrianakis, E.N. (1995) The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization. Proc. Natl Acad. Sci. USA 92, 11170-11174.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11170-11174
    • Arents, G.1    Moudrianakis, E.N.2
  • 20
    • 0002910388 scopus 로고
    • The nucleosomal repeat length of pea (Pisum sativum) chromatin changes during germination
    • 20. Ull, M.A. & Franco, L. (1986) The nucleosomal repeat length of pea (Pisum sativum) chromatin changes during germination. Plant Mol. Biol. 7, 25-31.
    • (1986) Plant Mol. Biol. , vol.7 , pp. 25-31
    • Ull, M.A.1    Franco, L.2
  • 21
    • 0001434261 scopus 로고
    • Histone variants from pea (Pisum sativum): Their differential presence in fractions obtained by DNase I digestion of nuclei
    • 21. Rodrigo, M.I. & Franco, L. (1990) Histone variants from pea (Pisum sativum): their differential presence in fractions obtained by DNase I digestion of nuclei. Physiol. Plant. 78, 602-608.
    • (1990) Physiol. Plant. , vol.78 , pp. 602-608
    • Rodrigo, M.I.1    Franco, L.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 22. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0029745606 scopus 로고    scopus 로고
    • Core histones are glutaminyl substrates for tissue transglutaminase
    • 23. Ballestar, E., Abad, C. & Franco, L. (1996) Core histones are glutaminyl substrates for tissue transglutaminase. J. Biol. Chem. 271, 18817-18824.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18817-18824
    • Ballestar, E.1    Abad, C.2    Franco, L.3
  • 25
    • 0028170560 scopus 로고
    • Removal of polysaccharides from plant DNA by ethanol precipitation
    • 25. Michaels, S.D., John, M.C. & Amasino, R.M. (1994) Removal of polysaccharides from plant DNA by ethanol precipitation. Biotechniques 17, 274-275.
    • (1994) Biotechniques , vol.17 , pp. 274-275
    • Michaels, S.D.1    John, M.C.2    Amasino, R.M.3
  • 26
    • 0019882018 scopus 로고
    • Silver staining of proteins in polyacrylamide gels
    • 26. Wray, W., Boulikas, T., Wray, V.P. & Hancock, R. (1981) Silver staining of proteins in polyacrylamide gels. Anal. Biochem. 118, 197-203.
    • (1981) Anal. Biochem. , vol.118 , pp. 197-203
    • Wray, W.1    Boulikas, T.2    Wray, V.P.3    Hancock, R.4
  • 27
    • 0021774173 scopus 로고
    • In vitro exchange of nucleosomal histones H2a and H2b
    • 27. Louters, L. & Chalkley, R. (1984) In vitro exchange of nucleosomal histones H2a and H2b. Biochemistry 23, 547-552.
    • (1984) Biochemistry , vol.23 , pp. 547-552
    • Louters, L.1    Chalkley, R.2
  • 28
    • 0001918350 scopus 로고
    • Putative HMG non-histone chromosomal proteins from pea (Pisum sativum)
    • 28. Ull, M.A., Herrero, M.E. & Franco, L. (1991) Putative HMG non-histone chromosomal proteins from pea (Pisum sativum). Plant Sci. 75, 55-62.
    • (1991) Plant Sci. , vol.75 , pp. 55-62
    • Ull, M.A.1    Herrero, M.E.2    Franco, L.3
  • 30
    • 0027493762 scopus 로고
    • Site specificity of pea histone acetyltransferase B in vitro
    • 30. Mingarro, I., Sendra, R., Salvador, M.L. & Franco, L. (1993) Site specificity of pea histone acetyltransferase B in vitro. J. Biol. Chem. 268, 13248-13252.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13248-13252
    • Mingarro, I.1    Sendra, R.2    Salvador, M.L.3    Franco, L.4
  • 31
    • 0001726374 scopus 로고
    • Abscisic acid and the developmental regulation of embryo storage proteins in maize
    • 31. Rivin, C.J. & Grudt, T. (1991) Abscisic acid and the developmental regulation of embryo storage proteins in maize. Plant Physiol. 95, 358-365.
    • (1991) Plant Physiol. , vol.95 , pp. 358-365
    • Rivin, C.J.1    Grudt, T.2
  • 33
    • 0029360329 scopus 로고
    • The formation of mRNA 3′-ends in plants
    • 33. Wu, L., Ueda, T. & Messing, J. (1995) The formation of mRNA 3′-ends in plants. Plant J. 8, 323-329.
    • (1995) Plant J. , vol.8 , pp. 323-329
    • Wu, L.1    Ueda, T.2    Messing, J.3
  • 34
    • 0021760521 scopus 로고
    • Compilation of published signal sequences
    • 34. Watson, M.E. (1984) Compilation of published signal sequences. Nucleic Acids Res. 12, 5145-5159.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 5145-5159
    • Watson, M.E.1
  • 35
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • 35. von Heijne, G. (1986) A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14, 4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 36
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • 36. Pearson, W.R. & Lipman, D.J. (1988) Improved tools for biological sequence comparison. Proc. Natl Acad. Sci. USA 85, 2444-2448.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 38
    • 0027022498 scopus 로고
    • A 62-kD sucrose binding protein is expressed and localized in tissues actively engaged in sucrose transport
    • 38. Grimes, H.D., Overvoorde, P.J., Ripp, K., Franceschi, V. & Hitz, W.D. (1992) A 62-kD sucrose binding protein is expressed and localized in tissues actively engaged in sucrose transport. Plant Cell 4, 1561-1574.
    • (1992) Plant Cell , vol.4 , pp. 1561-1574
    • Grimes, H.D.1    Overvoorde, P.J.2    Ripp, K.3    Franceschi, V.4    Hitz, W.D.5
  • 39
    • 0026043040 scopus 로고
    • Molecular basis for allelic polymorphism of the maize Globulin-1 gene
    • 39. Belanger, F.C. & Kriz, A.L. (1991) Molecular basis for allelic polymorphism of the maize Globulin-1 gene. Genetics 129, 863-872.
    • (1991) Genetics , vol.129 , pp. 863-872
    • Belanger, F.C.1    Kriz, A.L.2
  • 40
    • 0000720759 scopus 로고
    • Developmental biochemistry of cotton seed embryogenesis and germination. XVIII. cDNA and amino acid sequences of members of the storage protein families
    • 40. Chlan, C.A., Pyle, J.B., Legocki, A.B. & Dure, L. III (1986) Developmental biochemistry of cotton seed embryogenesis and germination. XVIII. cDNA and amino acid sequences of members of the storage protein families. Plant Mol. Biol. 7, 475-489.
    • (1986) Plant Mol. Biol. , vol.7 , pp. 475-489
    • Chlan, C.A.1    Pyle, J.B.2    Legocki, A.B.3    Dure L. III4
  • 41
    • 0000149283 scopus 로고
    • Developmental biochemistry of cotton seed embryogenesis and germination. XIX. Sequences and genomic organization of the α-globulin (vicilin) genes of cotton seed
    • 41. Chlan, C.A., Borroto, K., Kamalay, J.A. & Dure, L. III (1987) Developmental biochemistry of cotton seed embryogenesis and germination. XIX. Sequences and genomic organization of the α-globulin (vicilin) genes of cotton seed. Plant Mol. Biol. 9, 533-546.
    • (1987) Plant Mol. Biol. , vol.9 , pp. 533-546
    • Chlan, C.A.1    Borroto, K.2    Kamalay, J.A.3    Dure L. III4
  • 42
    • 0000220088 scopus 로고
    • The sequence of a pea vicilin gene and its expression in transgenic tobacco plants
    • 42. Higgins, T.J.V., Newbigin, E.J., Spencer, D., Llewellyn, D.J. & Craig, S. (1988) The sequence of a pea vicilin gene and its expression in transgenic tobacco plants. Plant Mol. Biol. 11, 683-695.
    • (1988) Plant Mol. Biol. , vol.11 , pp. 683-695
    • Higgins, T.J.V.1    Newbigin, E.J.2    Spencer, D.3    Llewellyn, D.J.4    Craig, S.5
  • 43
    • 0023650392 scopus 로고
    • Nucleotide sequence of a field bean (Vicia faba L. var. minor) vicilin gene
    • 43. Weschke, W., Baumlein, H. & Wobus, U. (1987) Nucleotide sequence of a field bean (Vicia faba L. var. minor) vicilin gene. Nucleic Acids Res. 15, 10065.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 10065
    • Weschke, W.1    Baumlein, H.2    Wobus, U.3
  • 44
    • 0025974147 scopus 로고
    • Sequence and genetic analysis of NHP2: A moderately abundant high mobility group-like nuclear protein with an essential function in Saccharomyces cerevisiae
    • 44. Kolodrubetz, D. & Burgum, A. (1991) Sequence and genetic analysis of NHP2: a moderately abundant high mobility group-like nuclear protein with an essential function in Saccharomyces cerevisiae. Yeast 7, 79-90.
    • (1991) Yeast , vol.7 , pp. 79-90
    • Kolodrubetz, D.1    Burgum, A.2
  • 45
    • 0030005821 scopus 로고    scopus 로고
    • Cloning and mapping of a human novel cDNA (NHP2L1) that encodes a protein highly homologous to yeast nuclear protein NHP2
    • 45. Saito, H., Fujiwara, T., Shin, S., Okui, K. & Nakamura, Y. (1996) Cloning and mapping of a human novel cDNA (NHP2L1) that encodes a protein highly homologous to yeast nuclear protein NHP2. Cytogenet. Cell Genet. 72, 191-196.
    • (1996) Cytogenet. Cell Genet. , vol.72 , pp. 191-196
    • Saito, H.1    Fujiwara, T.2    Shin, S.3    Okui, K.4    Nakamura, Y.5
  • 47
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • 47. Kyte, J. & Doolittle, R.F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 48
    • 0021104094 scopus 로고
    • Sequence specificity of the post-translational proteolytic cleavage of vicilin, a seed storage protein of pea (Pisum sativum L.)
    • 48. Gatehouse, J.A., Lycett, G.W., Delauney, A.J., Croy, R.D.R. & Boulter, D. (1983) Sequence specificity of the post-translational proteolytic cleavage of vicilin, a seed storage protein of pea (Pisum sativum L.). Biochem. J. 212, 427-432.
    • (1983) Biochem. J. , vol.212 , pp. 427-432
    • Gatehouse, J.A.1    Lycett, G.W.2    Delauney, A.J.3    Croy, R.D.R.4    Boulter, D.5
  • 49
    • 0021111891 scopus 로고
    • The vicilin gene family of pea (Pisum sativum L.): A complete cDNA coding sequence for preprovicilin
    • 49. Lycett, G.W., Delauney, A.J., Gatehouse, J.A., Gilroy, J., Croy, R.D.R. & Boulter, D. (1983) The vicilin gene family of pea (Pisum sativum L.): a complete cDNA coding sequence for preprovicilin. Nucleic Acids Res. 11, 2367-2380.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 2367-2380
    • Lycett, G.W.1    Delauney, A.J.2    Gatehouse, J.A.3    Gilroy, J.4    Croy, R.D.R.5    Boulter, D.6
  • 50
    • 0029240342 scopus 로고
    • Molecular characterization of proteins in protein-body membrane that disappear most rapidly during transformation of protein bodies into vacuoles
    • 50. Inoue, K., Motozaki, A., Takeuchi, Y., Nishimura, M. & HaraNishimura, I. (1995) Molecular characterization of proteins in protein-body membrane that disappear most rapidly during transformation of protein bodies into vacuoles. Plant J. 7, 235-243.
    • (1995) Plant J. , vol.7 , pp. 235-243
    • Inoue, K.1    Motozaki, A.2    Takeuchi, Y.3    Nishimura, M.4    Haranishimura, I.5
  • 51
    • 0030019538 scopus 로고    scopus 로고
    • Light-modulated abundance of an mRNA encoding a calmodulin-regulated, chromatin-associated NTPase in pea
    • 51. Hsieh, H.-L., Tong, C.-G., Thomas, C. & Roux, S.J. (1996) Light-modulated abundance of an mRNA encoding a calmodulin-regulated, chromatin-associated NTPase in pea. Plant Mol. Biol. 30, 135-147.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 135-147
    • Hsieh, H.-L.1    Tong, C.-G.2    Thomas, C.3    Roux, S.J.4
  • 52
    • 0025117557 scopus 로고
    • Evolution of a protein superfamily: Relationships between vertebrate lens crystallins and microorganism dormancy proteins
    • 52. Wistow, G. (1990) Evolution of a protein superfamily: Relationships between vertebrate lens crystallins and microorganism dormancy proteins. J. Mol. Evol. 30, 140-145.
    • (1990) J. Mol. Evol. , vol.30 , pp. 140-145
    • Wistow, G.1
  • 53
    • 0030941835 scopus 로고    scopus 로고
    • A plasma membrane sucrose-binding protein that mediates sucrose uptake shares structural and sequence similarity with seed storage proteins but remains functionally distinct
    • 53. Overvoorde, P.J., Chao, W.S. & Grimes, H.D. (1997) A plasma membrane sucrose-binding protein that mediates sucrose uptake shares structural and sequence similarity with seed storage proteins but remains functionally distinct. J. Biol. Chem. 272, 15898-15904.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15898-15904
    • Overvoorde, P.J.1    Chao, W.S.2    Grimes, H.D.3
  • 54
    • 0025773551 scopus 로고
    • Homologies between members of the germin gene family in hexaploid wheat and similarities between these wheat germins and certain Physarum spherulins
    • 54. Lane, B.G., Bernier, F., Dratewka-Kos, E., Shafai, R., Kennedy, T.D., Pyne, C., Munro, J.R., Vaughan, T., Walters, D. & Altomare, F. (1991) Homologies between members of the germin gene family in hexaploid wheat and similarities between these wheat germins and certain Physarum spherulins. J. Biol. Chem. 266, 10461-10469.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10461-10469
    • Lane, B.G.1    Bernier, F.2    Dratewka-Kos, E.3    Shafai, R.4    Kennedy, T.D.5    Pyne, C.6    Munro, J.R.7    Vaughan, T.8    Walters, D.9    Altomare, F.10
  • 56
    • 0027161641 scopus 로고
    • Germin, a protein marker of early plant development, is an oxalate oxidase
    • 56. Lane, B.G., Dunwell, J.M., Ray, J.A., Schmitt, M.R. & Cuming, A.G. (1993) Germin, a protein marker of early plant development, is an oxalate oxidase. J. Biol. Chem. 268, 12239-12242.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12239-12242
    • Lane, B.G.1    Dunwell, J.M.2    Ray, J.A.3    Schmitt, M.R.4    Cuming, A.G.5
  • 57
    • 0023461304 scopus 로고
    • Gene families encode the major encystment-specific proteins of Physarum polycephalum plasmodia
    • 57. Bernier, F., Lemieux, G. & Pallota, D. (1987) Gene families encode the major encystment-specific proteins of Physarum polycephalum plasmodia. Gene 59, 265-277.
    • (1987) Gene , vol.59 , pp. 265-277
    • Bernier, F.1    Lemieux, G.2    Pallota, D.3
  • 58
    • 0029666134 scopus 로고    scopus 로고
    • A vicilin-like seed protein of cycads: Similarity to sucrose-binding proteins
    • 58. Braun, H., Czihal, A., Shutov, A.D. & Bäumlein, H. (1996) A vicilin-like seed protein of cycads: similarity to sucrose-binding proteins. Plant Mol. Biol. 31, 35-44.
    • (1996) Plant Mol. Biol. , vol.31 , pp. 35-44
    • Braun, H.1    Czihal, A.2    Shutov, A.D.3    Bäumlein, H.4
  • 59
    • 0032519625 scopus 로고    scopus 로고
    • A gene encoding a vicilin-like protein is specifically expressed in fern spores. Evolutionary pathway of seed storage globulins
    • 59. Shutov, A.D., Braun, H., Chesnokov, Y.V. & Bäumlein, H. (1998) A gene encoding a vicilin-like protein is specifically expressed in fern spores. Evolutionary pathway of seed storage globulins. Eur. J. Biochem. 252, 79-89.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 79-89
    • Shutov, A.D.1    Braun, H.2    Chesnokov, Y.V.3    Bäumlein, H.4


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