메뉴 건너뛰기




Volumn 3, Issue 3, 2013, Pages 550-570

The cysteine protease–cysteine protease inhibitor system explored in soybean nodule development

Author keywords

Cystatins; Cysteine proteases; Glycine max; Nodule development; Senescence; Soybean nodules

Indexed keywords


EID: 84905646685     PISSN: None     EISSN: 20734395     Source Type: Journal    
DOI: 10.3390/agronomy3030550     Document Type: Article
Times cited : (10)

References (63)
  • 1
    • 48849115719 scopus 로고
    • Department of Agriculture Cooperating, New Mexico State University, (accessed on 12 July 2013)
    • Lindemann, W.C.; Glover, C.R. Nitrogen Fixation by Legumes. Department of Agriculture Cooperating, New Mexico State University, 1990. Available online: http://www.csun.edu/~hcbio027/biotechnology/lec10/lindemann.html (accessed on 12 July 2013).
    • (1990) Nitrogen Fixation by Legumes
    • Lindemann, W.C.1    Glover, C.R.2
  • 2
    • 0037043689 scopus 로고    scopus 로고
    • Agricultural sustainability and intensive production practices
    • Tilman, D.; Cassman, K.G.; Matson, P.A.; Naylor, R.; Polasky, S. Agricultural sustainability and intensive production practices. Nature 2002, 418, 671–677.
    • (2002) Nature , vol.418 , pp. 671-677
    • Tilman, D.1    Cassman, K.G.2    Matson, P.A.3    Naylor, R.4    Polasky, S.5
  • 6
    • 0038607583 scopus 로고    scopus 로고
    • Molecular genetics of leaf senescence in Arabidopsis
    • Lim, P.O.; Woo, H.R.; Nam, H.G. Molecular genetics of leaf senescence in Arabidopsis. Trends Sci. 2003, 8, 272–278.
    • (2003) Trends Sci , vol.8 , pp. 272-278
    • Lim, P.O.1    Woo, H.R.2    Nam, H.G.3
  • 7
    • 34247186321 scopus 로고    scopus 로고
    • Vacuolar cysteine proteases of wheat (Triticum aestivum L.) are common to leaf senescence induced by different factors
    • Martinez, D.E.; Bartoli, C.G.; Grbic, V.; Guiamet, J.J. Vacuolar cysteine proteases of wheat (Triticum aestivum L.) are common to leaf senescence induced by different factors. J. Exp. Bot. 2007, 58, 1099–1107.
    • (2007) J. Exp. Bot , vol.58 , pp. 1099-1107
    • Martinez, D.E.1    Bartoli, C.G.2    Grbic, V.3    Guiamet, J.J.4
  • 8
    • 0030298354 scopus 로고    scopus 로고
    • Expression of cysteine protease genes in pea nodule development and senescence
    • Kardailsky, I.V.; Brewin, N.J. Expression of cysteine protease genes in pea nodule development and senescence. Mol. Plant Microbe Inter. 1996, 9, 689–695.
    • (1996) Mol. Plant Microbe Inter , vol.9 , pp. 689-695
    • Kardailsky, I.V.1    Brewin, N.J.2
  • 9
    • 0033101490 scopus 로고    scopus 로고
    • The involvement of cysteine proteases and protease inhibitor genes in the regulation of programmed cell death in plants
    • Solomon, M.; Belenghi, B.; Delledonne, M.; Menachem, E.; Levine, A. The involvement of cysteine proteases and protease inhibitor genes in the regulation of programmed cell death in plants. Plant Cell 1999, 11, 431–443.
    • (1999) Plant Cell , vol.11 , pp. 431-443
    • Solomon, M.1    Belenghi, B.2    Delledonne, M.3    Menachem, E.4    Levine, A.5
  • 10
    • 0035047106 scopus 로고    scopus 로고
    • Proteases and cellular regulation in plants
    • Estelle, M. Proteases and cellular regulation in plants. Curr. Opin. Plant Biol. 2001, 4, 254–260.
    • (2001) Curr. Opin. Plant Biol , vol.4 , pp. 254-260
    • Estelle, M.1
  • 12
    • 20744438554 scopus 로고    scopus 로고
    • Isolation and characterization of a root nodule-specific cysteine proteinase cDNA from soybean
    • Oh, C.J.; Lee, H.; Kim, H.B.; An, C.S. Isolation and characterization of a root nodule-specific cysteine proteinase cDNA from soybean. J. Plant Biol. 2004, 47, 216–220.
    • (2004) J. Plant Biol , vol.47 , pp. 216-220
    • Oh, C.J.1    Lee, H.2    Kim, H.B.3    An, C.S.4
  • 13
    • 0034476852 scopus 로고    scopus 로고
    • Plant proteolytic enzymes: Possible roles during programmed cell death
    • Beers, E.P.; Woffenden, B.J.; Zhao, C. Plant proteolytic enzymes: Possible roles during programmed cell death. Plant Mol. Biol. 2000, 44, 399–415.
    • (2000) Plant Mol. Biol , vol.44 , pp. 399-415
    • Beers, E.P.1    Woffenden, B.J.2    Zhao, C.3
  • 14
    • 77954542512 scopus 로고    scopus 로고
    • A distinct subfamily of papain-like cystein proteinases regulated by senescence and stresses in Glycine max
    • Esteban-García, B.; Garrido-Cárdenas, J.A.; Alonso, D.L.; García-Maroto, F. A distinct subfamily of papain-like cystein proteinases regulated by senescence and stresses in Glycine max. J. Plant Physiol. 2010, 167, 1101–1108.
    • (2010) J. Plant Physiol , vol.167 , pp. 1101-1108
    • Esteban-García, B.1    Garrido-Cárdenas, J.A.2    Alonso, D.L.3    García-Maroto, F.4
  • 15
    • 6344278694 scopus 로고    scopus 로고
    • Analysis of the root nodule-enhanced transcriptome in soybean
    • Lee, H.; Hur, C.G.; Oh, C.J.; Kim, H.B.; Pakr, S.Y.; An, C.S. Analysis of the root nodule-enhanced transcriptome in soybean. Mol. Cells 2004, 18, 53–62.
    • (2004) Mol. Cells , vol.18 , pp. 53-62
    • Lee, H.1    Hur, C.G.2    Oh, C.J.3    Kim, H.B.4    Pakr, S.Y.5    An, C.S.6
  • 16
    • 2542450034 scopus 로고    scopus 로고
    • Molecular cloning, functional expression in Escherichia coli and enzymatic characterisation of a cysteine protease from white clover Trifolium repens
    • Asp, T.; Bowra, S.; Borg, S.; Holm, P.B. Molecular cloning, functional expression in Escherichia coli and enzymatic characterisation of a cysteine protease from white clover Trifolium repens. Biochim. Biophys. Acta Proteins Proteomics 2004, 1699, 111–122.
    • (2004) Biochim. Biophys. Acta Proteins Proteomics , vol.1699 , pp. 111-122
    • Asp, T.1    Bowra, S.2    Borg, S.3    Holm, P.B.4
  • 17
    • 0001684713 scopus 로고
    • Proteolytic activity in soybean root nodules: Activity in host cell cytosol and bacteroids throughout physiological development and senescence
    • Pfeiffer, N.E.; Torres, C.M.; Wagner, F.W. Proteolytic activity in soybean root nodules: Activity in host cell cytosol and bacteroids throughout physiological development and senescence. Plant Physiol. 1983, 71, 797.
    • (1983) Plant Physiol , vol.71 , pp. 797
    • Pfeiffer, N.E.1    Torres, C.M.2    Wagner, F.W.3
  • 18
    • 0027144231 scopus 로고
    • Proteolysis during development and senescence of effective and plant gene-controlled ineffective alfalfa nodules
    • Pladys, D.; Vance, C.P. Proteolysis during development and senescence of effective and plant gene-controlled ineffective alfalfa nodules. Plant Physiol. 1993, 103, 379–384.
    • (1993) Plant Physiol , vol.103 , pp. 379-384
    • Pladys, D.1    Vance, C.P.2
  • 19
    • 0028134248 scopus 로고
    • Molecular analysis of natural leaf senescence in Arabidopsis thaliana
    • Lohman, K.N.; Gan, S.; John, M.C.; Amasino, R.M. Molecular analysis of natural leaf senescence in Arabidopsis thaliana. Physiol. Plant. 1994, 92, 322–328.
    • (1994) Physiol. Plant , vol.92 , pp. 322-328
    • Lohman, K.N.1    Gan, S.2    John, M.C.3    Amasino, R.M.4
  • 21
    • 47649106761 scopus 로고    scopus 로고
    • The origin and evolution of plant cystatins and their target cysteine proteinases indicate a complex functional relationship
    • Martinez, M.; Diaz, I. The origin and evolution of plant cystatins and their target cysteine proteinases indicate a complex functional relationship. BMC Evol. Biol. 2008, 8, 198.
    • (2008) BMC Evol. Biol , vol.8 , pp. 198
    • Martinez, M.1    Diaz, I.2
  • 22
    • 2442610018 scopus 로고    scopus 로고
    • Structure-function relationships in class CA1 cysteine peptidase propeptides
    • Wiederanders, B. Structure-function relationships in class CA1 cysteine peptidase propeptides. Acta Biochim. Pol. 2003, 50, 691–713.
    • (2003) Acta Biochim. Pol , vol.50 , pp. 691-713
    • Wiederanders, B.1
  • 23
    • 0036676947 scopus 로고    scopus 로고
    • Legumains and their functions in plants
    • Müntz, K.; Shutov, A.D. Legumains and their functions in plants. Trends Plant Sci. 2002, 7, 340–344.
    • (2002) Trends Plant Sci , vol.7 , pp. 340-344
    • Müntz, K.1    Shutov, A.D.2
  • 27
    • 51249094499 scopus 로고    scopus 로고
    • A nodule-specific plant cysteine proteinase, AsNODF32, is involved in nodule senescence and nitrogen fixation activity of the green manure legume Astragalus sinicus
    • Li, Y.; Zhou, L.; Li, Y.; Chen, D.; Tan, X.; Lei, L.; Zhou, J. A nodule-specific plant cysteine proteinase, AsNODF32, is involved in nodule senescence and nitrogen fixation activity of the green manure legume Astragalus sinicus. New Phytol. 2008, 180, 185–192.
    • (2008) New Phytol , vol.180 , pp. 185-192
    • Li, Y.1    Zhou, L.2    Li, Y.3    Chen, D.4    Tan, X.5    Lei, L.6    Zhou, J.7
  • 28
    • 0033729778 scopus 로고    scopus 로고
    • The involvement of a cysteine proteinase in the nodule development in Chinese milk vetch infected with Mesorhizobium huakuii subsp. rengei
    • Naito, Y.; Fujie, M.; Usami, S.; Murooka, Y.; Yamada, T. The involvement of a cysteine proteinase in the nodule development in Chinese milk vetch infected with Mesorhizobium huakuii subsp. rengei. Plant Physiol. 2000, 124, 1087–1096.
    • (2000) Plant Physiol , vol.124 , pp. 1087-1096
    • Naito, Y.1    Fujie, M.2    Usami, S.3    Murooka, Y.4    Yamada, T.5
  • 29
    • 0347948397 scopus 로고    scopus 로고
    • Nodule‐Enhanced protease inhibitor gene: Emerging patterns of gene expression in nodule development on Sesbania rostrata
    • Lievens, S.; Goormachtig, S.; Holsters, M. Nodule‐Enhanced protease inhibitor gene: Emerging patterns of gene expression in nodule development on Sesbania rostrata. J. Exp. Bot. 2004, 55, 89–97.
    • (2004) J. Exp. Bot , vol.55 , pp. 89-97
    • Lievens, S.1    Goormachtig, S.2    Holsters, M.3
  • 30
    • 0034119995 scopus 로고    scopus 로고
    • Immunolocalization of a cysteine protease in vacuoles, vesicles, and symbiosomes of pea nodule cells
    • Vincent, J.L.; Brewin, N.J. Immunolocalization of a cysteine protease in vacuoles, vesicles, and symbiosomes of pea nodule cells. Plant Physiol. 2000, 123, 521–530.
    • (2000) Plant Physiol , vol.123 , pp. 521-530
    • Vincent, J.L.1    Brewin, N.J.2
  • 31
    • 24044517545 scopus 로고    scopus 로고
    • Modified expression of cysteine protease affects seed germination, vegetative growth and nodule development in transgenic lines of Medicago truncatula
    • Sheokand, S.; Dahiya, P.; Vincent, J.; Brewin, N. Modified expression of cysteine protease affects seed germination, vegetative growth and nodule development in transgenic lines of Medicago truncatula. Plant Sci. 2005, 169, 966–975.
    • (2005) Plant Sci , vol.169 , pp. 966-975
    • Sheokand, S.1    Dahiya, P.2    Vincent, J.3    Brewin, N.4
  • 32
    • 70350686335 scopus 로고    scopus 로고
    • Characterization of the entire cystatin gene family in barley and their target cathepsin l-like cysteine-proteases, partners in the hordein mobilization during seed germination
    • Martinez, M.; Cambra, I.; Carrillo, L.; Diaz-Mendoza, M.; Diaz, I. Characterization of the entire cystatin gene family in barley and their target cathepsin l-like cysteine-proteases, partners in the hordein mobilization during seed germination. Plant Physiol. 2009, 151, 1531–1545.
    • (2009) Plant Physiol , vol.151 , pp. 1531-1545
    • Martinez, M.1    Cambra, I.2    Carrillo, L.3    Diaz-Mendoza, M.4    Diaz, I.5
  • 33
    • 59349098502 scopus 로고    scopus 로고
    • Differential proteomic analysis of soluble extracellular proteins reveals the cysteine protease and cystatin involved in suspension-cultured cell proliferation in rice
    • Tian, L.; Zhang, L.; Zhang, J.; Song, Y.; Guo, Y. Differential proteomic analysis of soluble extracellular proteins reveals the cysteine protease and cystatin involved in suspension-cultured cell proliferation in rice. Biochim. Biophys. Acta 2009, 1794, 459–467.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 459-467
    • Tian, L.1    Zhang, L.2    Zhang, J.3    Song, Y.4    Guo, Y.5
  • 34
    • 4644253630 scopus 로고    scopus 로고
    • Multifunctional role of plant cysteine proteinases
    • Grudkowska, M.; Zagdanska, B. Multifunctional role of plant cysteine proteinases. Acta Biochim. Pol. 2004, 51, 609–624.
    • (2004) Acta Biochim. Pol , vol.51 , pp. 609-624
    • Grudkowska, M.1    Zagdanska, B.2
  • 35
    • 0036008857 scopus 로고    scopus 로고
    • Is a cysteine proteinase inhibitor involved in the regulation of petal wilting in senescing carnation (Dianthus caryophyllus L.) flowers?
    • Sugawara, H.; Shibuya, K.; Yoshioka, T.; Hashiba, T.; Satoh, S. Is a cysteine proteinase inhibitor involved in the regulation of petal wilting in senescing carnation (Dianthus caryophyllus L.) flowers? J. Exp. Bot. 2002, 53, 407–413.
    • (2002) J. Exp. Bot , vol.53 , pp. 407-413
    • Sugawara, H.1    Shibuya, K.2    Yoshioka, T.3    Hashiba, T.4    Satoh, S.5
  • 36
    • 0037336595 scopus 로고    scopus 로고
    • Identification of dehydration-responsive cysteine proteases during post-harvest senescence of broccoli florets
    • Coupe, S.A.; Sinclair, B.K.; Watson, L.M.; Heyes, J.A.; Eason, J.R. Identification of dehydration-responsive cysteine proteases during post-harvest senescence of broccoli florets. J. Exp. Bot. 2003, 54, 1045–1056.
    • (2003) J. Exp. Bot , vol.54 , pp. 1045-1056
    • Coupe, S.A.1    Sinclair, B.K.2    Watson, L.M.3    Heyes, J.A.4    Eason, J.R.5
  • 38
    • 0032547704 scopus 로고    scopus 로고
    • Gel electrophoresis of proteolytic enzymes
    • Michaud, D. Gel electrophoresis of proteolytic enzymes. Anal. Chim. Acta 1998, 372, 173–185.
    • (1998) Anal. Chim. Acta , vol.372 , pp. 173-185
    • Michaud, D.1
  • 39
    • 0019948262 scopus 로고
    • L-Trans-epoxysuccinyl-leucylamido(4-guanidino) butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
    • Barrett, A.J.; Kembhavi, A.A.; Brown, M.A.; Kirschke, H.; Knight, C.G.; Tamai, M.; Hanada, K. L-Trans-epoxysuccinyl-leucylamido(4-guanidino) butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem. J. 1982, 201, 189–198.
    • (1982) Biochem. J , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3    Kirschke, H.4    Knight, C.G.5    Tamai, M.6    Hanada, K.7
  • 40
    • 36248964645 scopus 로고    scopus 로고
    • Metabolism of reactive oxygen species is attenuated in leghemoglobin-deficient nodules of Lotus japonicus
    • Gunther, C.; Schlereth, A.; Udvardi, M.; Ott, T. Metabolism of reactive oxygen species is attenuated in leghemoglobin-deficient nodules of Lotus japonicus. Mol. Plant Microbe Inter. 2007, 20, 1596–1603.
    • (2007) Mol. Plant Microbe Inter , vol.20 , pp. 1596-1603
    • Gunther, C.1    Schlereth, A.2    Udvardi, M.3    Ott, T.4
  • 41
    • 0000524370 scopus 로고    scopus 로고
    • Physiological and biochemical basis of nodule senescence in legumes: A review
    • Swaraj, K.; Bishnoi, N. Physiological and biochemical basis of nodule senescence in legumes: A review. Plant Physiol. Biochem. 1996, 23, 105–116.
    • (1996) Plant Physiol. Biochem , vol.23 , pp. 105-116
    • Swaraj, K.1    Bishnoi, N.2
  • 42
    • 0000870242 scopus 로고
    • Leghemoglobin and Rhizobium respiration
    • Appleby, C.A. Leghemoglobin and Rhizobium respiration. Ann. Rev. Plant Physiol. 1984, 33, 443–478.
    • (1984) Ann. Rev. Plant Physiol , vol.33 , pp. 443-478
    • Appleby, C.A.1
  • 43
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680–685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 44
    • 0004268863 scopus 로고
    • Inhibition of proteolytic enzymes
    • Beynon, R.J., Bond, J.S., Eds.; IRL Press at Oxford University Press: Oxford, UK
    • Salvesen, G.; Nagase, H. Inhibition of proteolytic enzymes. In Proteolytic Enzymes: A Practical Approach; Beynon, R.J., Bond, J.S., Eds.; IRL Press at Oxford University Press: Oxford, UK, 1989; pp. 83–104.
    • (1989) Proteolytic Enzymes: A Practical Approach , pp. 83-104
    • Salvesen, G.1    Nagase, H.2
  • 45
    • 0034095585 scopus 로고    scopus 로고
    • Morphological and yield traits of wild legume (Tetragonolobus palaestinus Boiss) populations
    • Al-Karaki, G.N. Morphological and yield traits of wild legume (Tetragonolobus palaestinus Boiss) populations. J. Agron. Crop Sci. 2000, 184, 267–270.
    • (2000) J. Agron. Crop Sci , vol.184 , pp. 267-270
    • Al-Karaki, G.N.1
  • 46
    • 26444513601 scopus 로고    scopus 로고
    • Drought stress induced changes in some organic substances in nodules and other plant parts of two potential legumes differing in salt tolerance
    • Ashraf, M.; Iram, A. Drought stress induced changes in some organic substances in nodules and other plant parts of two potential legumes differing in salt tolerance. Flora 2005, 200, 535–546.
    • (2005) Flora , vol.200 , pp. 535-546
    • Ashraf, M.1    Iram, A.2
  • 47
    • 0002859247 scopus 로고
    • Measurement of nitrogen fixation by indirect means
    • Bergersen, F.J., Ed.; John Wiley and Sons: New York, NY, USA
    • Turner, G.L.; Gibson, A.H. Measurement of nitrogen fixation by indirect means. In Methods for Evaluating Biological Nitrogen Fixation; Bergersen, F.J., Ed.; John Wiley and Sons: New York, NY, USA, 1980; pp. 111–138.
    • (1980) Methods for Evaluating Biological Nitrogen Fixation , pp. 111-138
    • Turner, G.L.1    Gibson, A.H.2
  • 49
    • 84964217690 scopus 로고    scopus 로고
    • Identification and Application of Phenotypic and Molecular Markers for Abiotic Stress Tolerance in Soybean
    • Krezhova, D., Ed.; InTech: Shanghai, China, (accessed on 12 July 2013)
    • Fenta, B.A.; Urte Schlüter, U.; Garcia, B.M.; DuPlessis, M.; Foyer, C.H.; Kunert, K.J. Identification and Application of Phenotypic and Molecular Markers for Abiotic Stress Tolerance in Soybean. In Soybean—Genetics and Novel Techniques for Yield Enhancement; Krezhova, D., Ed.; InTech: Shanghai, China, 2011; pp. 181–200. Available online: http://www.intechopen.com/books/soybean-genetics-and-novel-techniques-for-yield-enhancement/identification-and-application-of-phenotypic-and-molecular-markers-for-abiotic-stress-tolerance-in-s (accessed on 12 July 2013).
    • (2011) Soybean—Genetics and Novel Techniques for Yield Enhancement , pp. 181-200
    • Fenta, B.A.1    Urte Schlüter, U.2    Garcia, B.M.3    DuPlessis, M.4    Foyer, C.H.5    Kunert, K.J.6
  • 50
    • 85111470276 scopus 로고    scopus 로고
    • Phytozome, Version 9.1: Biomart; Joint Genome Institute, Center for Integrative Genomics and University of California Regents, USA, 2006–2013; (accessed on 12 July 2013)
    • Phytozome, Version 9.1: Biomart; Joint Genome Institute, Center for Integrative Genomics and University of California Regents, USA, 2006–2013; Available online: http://www.phytozome.net/biomart (accessed on 12 July 2013).
  • 51
    • 85111418131 scopus 로고    scopus 로고
    • USDA-ARS and IOWA State University, (accessed on 12 July 2013)
    • SoyBase and the Soybean Breeder’s Toolbox; USDA-ARS and IOWA State University, 2010. Available online: http://soybase.org (accessed on 12 July 2013).
    • (2010) SoyBase and the Soybean Breeder’s Toolbox
  • 52
    • 75549088763 scopus 로고    scopus 로고
    • SoyBase, the USDA-ARS soybean genetics and genomics database
    • Grant, D.; Nelson, R.T.; Cannon, S.B.; Shoemaker, R.C. SoyBase, the USDA-ARS soybean genetics and genomics database. Nucleic Acids Res. 2010, 38, 843–846.
    • (2010) Nucleic Acids Res , vol.38 , pp. 843-846
    • Grant, D.1    Nelson, R.T.2    Cannon, S.B.3    Shoemaker, R.C.4
  • 54
    • 85111451569 scopus 로고    scopus 로고
    • Legume Base; University of Miyazaki: Miyazaki, Japan, (accessed on 12 July 2013)
    • Legume Base; University of Miyazaki: Miyazaki, Japan, 2009. Available online: http://www. legumebase.brc.miyazaki-u.ac.jp (accessed on 12 July 2013).
    • (2009)
  • 57
    • 34247186321 scopus 로고    scopus 로고
    • Vacuolar cysteine proteases of wheat (Triticum aestivum L.) are common to leaf senescence induced by different factors
    • Martínez, D.E.; Bartoli, C.G.; Grbic, V.; Guiamet, J.J. Vacuolar cysteine proteases of wheat (Triticum aestivum L.) are common to leaf senescence induced by different factors. J. Exp. Bot. 2007, 58, 1099–1107.
    • (2007) J. Exp. Bot , vol.58 , pp. 1099-1107
    • Martínez, D.E.1    Bartoli, C.G.2    Grbic, V.3    Guiamet, J.J.4
  • 58
    • 83255189512 scopus 로고    scopus 로고
    • Advances in Omics and bioinformatics tools for systems analyses of plant functions
    • Mochida, K.; Shinozaki, K. Advances in Omics and bioinformatics tools for systems analyses of plant functions. Plant Cell Physiol. 2011, 52, 2017–2038.
    • (2011) Plant Cell Physiol , vol.52 , pp. 2017-2038
    • Mochida, K.1    Shinozaki, K.2
  • 59
    • 39649117755 scopus 로고    scopus 로고
    • The impact of next-generation sequencing technology on genetics
    • Mardis, E. The impact of next-generation sequencing technology on genetics. Trends Genet. 2008, 24, 133–141.
    • (2008) Trends Genet , vol.24 , pp. 133-141
    • Mardis, E.1
  • 60
    • 78650517886 scopus 로고    scopus 로고
    • Functional genomics of soybean for improvement of productivity in adverse conditions
    • Tran, L.S.; Mochida, K. Functional genomics of soybean for improvement of productivity in adverse conditions. Funct. Integr. Genomics 2010, 10, 447–462.
    • (2010) Funct. Integr. Genomics , vol.10 , pp. 447-462
    • Tran, L.S.1    Mochida, K.2
  • 62
    • 1542279127 scopus 로고    scopus 로고
    • Oryzacystatin I expression in transformed tobacco produces a conditional growth phenotype and enhances chilling tolerance
    • Van der Vyver, C.; Schneidereit, J.; Driscoll, S.; Turner, J.; Kunert, K.; Foyer, C.H. Oryzacystatin I expression in transformed tobacco produces a conditional growth phenotype and enhances chilling tolerance. Plant Biotech. J. 2003, 1, 101–112.
    • (2003) Plant Biotech. J , vol.1 , pp. 101-112
    • Van der Vyver, C.1    Schneidereit, J.2    Driscoll, S.3    Turner, J.4    Kunert, K.5    Foyer, C.H.6
  • 63
    • 34250357224 scopus 로고    scopus 로고
    • Carboxy terminal extended phytocystatins are bifunctional inhibitors of papain and legumain cysteine proteinases
    • Martinez, M.; Diaz-Mendoza, M.; Carrillo, L.; Diaz, I. Carboxy terminal extended phytocystatins are bifunctional inhibitors of papain and legumain cysteine proteinases. FEBS Lett. 2007, 581, 2914–2918.
    • (2007) FEBS Lett , vol.581 , pp. 2914-2918
    • Martinez, M.1    Diaz-Mendoza, M.2    Carrillo, L.3    Diaz, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.