메뉴 건너뛰기




Volumn 78, Issue , 2013, Pages 447-460

Comparative proteomic analysis for assessment of the ecological significance of maize and peanut intercropping

Author keywords

Ecological significance; Iron nutrition; Peanut maize intercropping; Proteomic analysis; Rhizosphere interaction

Indexed keywords

12 OXO PHYTODIENOIC ACID REDUCTASE; ALLENE OXIDE SYNTHASE; CARBON; JASMONIC ACID; NITROGEN; OXIDOREDUCTASE; SYNTHETASE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 84872766612     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.10.013     Document Type: Article
Times cited : (55)

References (87)
  • 1
    • 33745513063 scopus 로고
    • China Agricultural University Press, Beijing
    • Liu X.H. The farming systems 1994, China Agricultural University Press, Beijing.
    • (1994) The farming systems
    • Liu, X.H.1
  • 3
    • 77954655895 scopus 로고    scopus 로고
    • Rhizosphere processes and management for improving nutrient use efficiency and crop productivity: Implications for China
    • Zhang F., Shen J., Zhang J., Zuo Y., Li L., Chen X. Rhizosphere processes and management for improving nutrient use efficiency and crop productivity: Implications for China. Adv Agron 2010, 107:2-28.
    • (2010) Adv Agron , vol.107 , pp. 2-28
    • Zhang, F.1    Shen, J.2    Zhang, J.3    Zuo, Y.4    Li, L.5    Chen, X.6
  • 4
    • 34547427284 scopus 로고    scopus 로고
    • Diversity enhances agricultural productivity via rhizosphere phosphorus facilitation on phosphorus-deficient soils
    • Li L., Li S.M., Sun J.H., Zhou L.L., Bao X.G., Zhang H.G., et al. Diversity enhances agricultural productivity via rhizosphere phosphorus facilitation on phosphorus-deficient soils. Proc Natl Acad Sci U S A 2007, 104:11192-11196.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 11192-11196
    • Li, L.1    Li, S.M.2    Sun, J.H.3    Zhou, L.L.4    Bao, X.G.5    Zhang, H.G.6
  • 5
    • 0034121613 scopus 로고    scopus 로고
    • Studies on the improvement in iron nutrition of peanut by intercropping with maize on a calcareous soil
    • Zuo Y., Zhang F., Li X., Cao Y. Studies on the improvement in iron nutrition of peanut by intercropping with maize on a calcareous soil. Plant Soil 2000, 220:13-25.
    • (2000) Plant Soil , vol.220 , pp. 13-25
    • Zuo, Y.1    Zhang, F.2    Li, X.3    Cao, Y.4
  • 6
    • 41949086069 scopus 로고    scopus 로고
    • Effect of peanut mixed cropping with gramineous species on micronutrient concentrations and iron chlorosis of peanut plants grown in a calcareous soil
    • Zuo Y., Zhang F. Effect of peanut mixed cropping with gramineous species on micronutrient concentrations and iron chlorosis of peanut plants grown in a calcareous soil. Plant Soil 2008, 306:23-36.
    • (2008) Plant Soil , vol.306 , pp. 23-36
    • Zuo, Y.1    Zhang, F.2
  • 8
    • 0002286083 scopus 로고
    • Evidence for a specific uptake system for iron phytosiderophores in roots of grasses
    • Römheld V., Marschner H. Evidence for a specific uptake system for iron phytosiderophores in roots of grasses. Plant Physiol 1986, 80:175-180.
    • (1986) Plant Physiol , vol.80 , pp. 175-180
    • Römheld, V.1    Marschner, H.2
  • 10
    • 68749092956 scopus 로고    scopus 로고
    • Dissecting iron deficiency-induced proton extrusion in Arabidopsis roots
    • Santi S., Schmidt W. Dissecting iron deficiency-induced proton extrusion in Arabidopsis roots. New Phytol 2009, 183:1072-1084.
    • (2009) New Phytol , vol.183 , pp. 1072-1084
    • Santi, S.1    Schmidt, W.2
  • 11
    • 78549247422 scopus 로고    scopus 로고
    • Recent insights into iron homeostasis and their application in graminaceous crops
    • Kobayashi T., Nakanishi H., Nishizawa N.K. Recent insights into iron homeostasis and their application in graminaceous crops. Proc Jpn Acad Ser B Phys Biol Sci 2010, 86:900-913.
    • (2010) Proc Jpn Acad Ser B Phys Biol Sci , vol.86 , pp. 900-913
    • Kobayashi, T.1    Nakanishi, H.2    Nishizawa, N.K.3
  • 12
    • 65349103592 scopus 로고    scopus 로고
    • Iron and zinc biofortification strategies in dicot plants by intercropping with gramineous species. A review
    • Zuo Y., Zhang F. Iron and zinc biofortification strategies in dicot plants by intercropping with gramineous species. A review. Agron Sustain Dev 2009, 29:63-71.
    • (2009) Agron Sustain Dev , vol.29 , pp. 63-71
    • Zuo, Y.1    Zhang, F.2
  • 13
    • 34249869535 scopus 로고    scopus 로고
    • Peanut/maize intercropping induced changes in rhizosphere and nutrient concentrations in shoots
    • Inal A., Gunes A., Zhang F., Cakmak I. Peanut/maize intercropping induced changes in rhizosphere and nutrient concentrations in shoots. Plant Physiol Biochem 2007, 45:350-356.
    • (2007) Plant Physiol Biochem , vol.45 , pp. 350-356
    • Inal, A.1    Gunes, A.2    Zhang, F.3    Cakmak, I.4
  • 14
    • 11144302961 scopus 로고    scopus 로고
    • Studies on the improvement iron nutrition of peanut intercropping with maize on nitrogen fixation at early stages of growth of peanut on a calcareous soil
    • Zuo Y.M., Liu Y.X., Zhang F.S., Peter C. Studies on the improvement iron nutrition of peanut intercropping with maize on nitrogen fixation at early stages of growth of peanut on a calcareous soil. Soil Sci Plant Nutr 2004, 50:1071-1078.
    • (2004) Soil Sci Plant Nutr , vol.50 , pp. 1071-1078
    • Zuo, Y.M.1    Liu, Y.X.2    Zhang, F.S.3    Peter, C.4
  • 15
    • 79960971804 scopus 로고    scopus 로고
    • Plant proteome changes under abiotic stress - contribution of proteomics studies to understanding plant stress response
    • Kosová K., Vítámvás P., Prášil I.T., Renaut J. Plant proteome changes under abiotic stress - contribution of proteomics studies to understanding plant stress response. J Proteomics 2011, 74:1301-1322.
    • (2011) J Proteomics , vol.74 , pp. 1301-1322
    • Kosová, K.1    Vítámvás, P.2    Prášil, I.T.3    Renaut, J.4
  • 16
    • 41849137251 scopus 로고    scopus 로고
    • A proteomic study showing differential regulation of stress, redox regulation and peroxidase proteins by iron supply and the transcription factor FER
    • Brumbarova T., Matros A., Mock H.P., Bauer P. A proteomic study showing differential regulation of stress, redox regulation and peroxidase proteins by iron supply and the transcription factor FER. Plant J 2008, 54:321-334.
    • (2008) Plant J , vol.54 , pp. 321-334
    • Brumbarova, T.1    Matros, A.2    Mock, H.P.3    Bauer, P.4
  • 17
    • 46049119887 scopus 로고    scopus 로고
    • Proteomic response to iron deficiency in tomato root
    • Li J., Wu X.D., Hao S.T., Wang X.J., Ling H.Q. Proteomic response to iron deficiency in tomato root. Proteomics 2008, 8:2299-2311.
    • (2008) Proteomics , vol.8 , pp. 2299-2311
    • Li, J.1    Wu, X.D.2    Hao, S.T.3    Wang, X.J.4    Ling, H.Q.5
  • 18
    • 78649521637 scopus 로고    scopus 로고
    • Proteomic characterization of iron deficiency responses in Cucumis sativus L. roots
    • Donnini S., Prinsi B., Negri A.S., Vigani G., Espen L., Zocchi G. Proteomic characterization of iron deficiency responses in Cucumis sativus L. roots. BMC Plant Biol 2010, 10:268.
    • (2010) BMC Plant Biol , vol.10 , pp. 268
    • Donnini, S.1    Prinsi, B.2    Negri, A.S.3    Vigani, G.4    Espen, L.5    Zocchi, G.6
  • 20
    • 79955870864 scopus 로고    scopus 로고
    • Root responses of Medicago truncatula plants grown in two different iron deficiency conditions: changes in root protein profile and riboflavin biosynthesis
    • Rodríguez-Celma J., Lattanzio G., Grusak M.A., Abadía A., Abadía J., López-Millán A.F. Root responses of Medicago truncatula plants grown in two different iron deficiency conditions: changes in root protein profile and riboflavin biosynthesis. J Proteome Res 2011, 10:2590-2601.
    • (2011) J Proteome Res , vol.10 , pp. 2590-2601
    • Rodríguez-Celma, J.1    Lattanzio, G.2    Grusak, M.A.3    Abadía, A.4    Abadía, J.5    López-Millán, A.F.6
  • 22
    • 36849035455 scopus 로고    scopus 로고
    • Proteomics, pigment composition, and organization of thylakoid membranes in iron-deficient spinach leaves
    • Timperio A.M., D'Amici G.M., Barta C., Loreto F., Zolla L. Proteomics, pigment composition, and organization of thylakoid membranes in iron-deficient spinach leaves. J Exp Bot 2007, 58:3695-3710.
    • (2007) J Exp Bot , vol.58 , pp. 3695-3710
    • Timperio, A.M.1    D'Amici, G.M.2    Barta, C.3    Loreto, F.4    Zolla, L.5
  • 23
    • 84857632275 scopus 로고    scopus 로고
    • Proteomics in evolutionary ecology: linking the genotype with the phenotype
    • Diz A.P., Martínez-Fernández M., Rolán-Alvarez E. Proteomics in evolutionary ecology: linking the genotype with the phenotype. Mol Ecol 2012, 21:1060-1080.
    • (2012) Mol Ecol , vol.21 , pp. 1060-1080
    • Diz, A.P.1    Martínez-Fernández, M.2    Rolán-Alvarez, E.3
  • 24
    • 0030433923 scopus 로고    scopus 로고
    • Enhanced leaf chlorophyll levels in plants treated with seaweed extract
    • Blunden G., Jenkins T., Liu Y.W. Enhanced leaf chlorophyll levels in plants treated with seaweed extract. J Appl Phycol 1997, 8:535-543.
    • (1997) J Appl Phycol , vol.8 , pp. 535-543
    • Blunden, G.1    Jenkins, T.2    Liu, Y.W.3
  • 25
    • 43049142644 scopus 로고    scopus 로고
    • Determination of optimal nitrogen rate for rice varieties using a chlorophyll meter
    • Huang J.L., He F., Cui K.H., Buresh R.J., Xu B., Gong W.H., et al. Determination of optimal nitrogen rate for rice varieties using a chlorophyll meter. Field Crops Res 2008, 105:70-80.
    • (2008) Field Crops Res , vol.105 , pp. 70-80
    • Huang, J.L.1    He, F.2    Cui, K.H.3    Buresh, R.J.4    Xu, B.5    Gong, W.H.6
  • 26
    • 0002081284 scopus 로고
    • 2+ estimation to resolve iron chlorosis in plants
    • 2+ estimation to resolve iron chlorosis in plants. J Plant Nutr 1984, 7:81-90.
    • (1984) J Plant Nutr , vol.7 , pp. 81-90
    • Takkar, P.N.1    Kaur, N.P.2
  • 27
    • 51649116399 scopus 로고    scopus 로고
    • Acoustic technology for high-performance disruption and extraction of plant proteins
    • Toorchi M., Nouri M.Z., Tsumura M., Komatsu S. Acoustic technology for high-performance disruption and extraction of plant proteins. J Proteome Res 2008, 7:3035-3041.
    • (2008) J Proteome Res , vol.7 , pp. 3035-3041
    • Toorchi, M.1    Nouri, M.Z.2    Tsumura, M.3    Komatsu, S.4
  • 28
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: a practical and powerful approach to multiple testing
    • Benjamini Y., Hochberg Y. Controlling the false discovery rate: a practical and powerful approach to multiple testing. J R Stat Soc B 1995, 57:289-300.
    • (1995) J R Stat Soc B , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 29
    • 39749169200 scopus 로고    scopus 로고
    • Interspecific root interactions and rhizosphere effects on salt ions and nutrient uptake between mixed grown peanut/maize and peanut/barley in original saline-sodic-boron toxic soil
    • Inal A., Gunes A. Interspecific root interactions and rhizosphere effects on salt ions and nutrient uptake between mixed grown peanut/maize and peanut/barley in original saline-sodic-boron toxic soil. J Plant Physiol 2008, 165:490-503.
    • (2008) J Plant Physiol , vol.165 , pp. 490-503
    • Inal, A.1    Gunes, A.2
  • 30
    • 0141676134 scopus 로고    scopus 로고
    • Iron nutrition of peanut enhanced by mixed cropping with maize: possible role of root morphology and rhizosphere microflora
    • Zuo Y., Li X., Cao Y., Zhang F., Christie P. Iron nutrition of peanut enhanced by mixed cropping with maize: possible role of root morphology and rhizosphere microflora. J Plant Nutr 2003, 26:2093-2110.
    • (2003) J Plant Nutr , vol.26 , pp. 2093-2110
    • Zuo, Y.1    Li, X.2    Cao, Y.3    Zhang, F.4    Christie, P.5
  • 31
    • 44649145983 scopus 로고    scopus 로고
    • Rubisco gene expression in C4 plants
    • Patel M., Berry J.O. Rubisco gene expression in C4 plants. J Exp Bot 2008, 59:1625-1634.
    • (2008) J Exp Bot , vol.59 , pp. 1625-1634
    • Patel, M.1    Berry, J.O.2
  • 32
    • 44649135348 scopus 로고    scopus 로고
    • Regulation of Rubisco activase and its interaction with Rubisco
    • Portis A.R., Li C., Wang D., Salvucci M.E. Regulation of Rubisco activase and its interaction with Rubisco. J Exp Bot 2008, 59:1597-1604.
    • (2008) J Exp Bot , vol.59 , pp. 1597-1604
    • Portis, A.R.1    Li, C.2    Wang, D.3    Salvucci, M.E.4
  • 33
    • 0029347125 scopus 로고
    • Early iron deficiency stress response in leaves of sugar beet
    • Winder T.L., Nishio J.N. Early iron deficiency stress response in leaves of sugar beet. Plant Physiol 1995, 108:1487-1494.
    • (1995) Plant Physiol , vol.108 , pp. 1487-1494
    • Winder, T.L.1    Nishio, J.N.2
  • 34
    • 84958319104 scopus 로고
    • Leaf responses to Fe deficiency: a review
    • Abadía J. Leaf responses to Fe deficiency: a review. J Plant Nutr 1992, 15:1699-1713.
    • (1992) J Plant Nutr , vol.15 , pp. 1699-1713
    • Abadía, J.1
  • 35
    • 0001618202 scopus 로고
    • Limiting factors of photosynthesis II: iron stress diminishes photochemical capacity by reducing the number of photosynthetic units
    • Spiller S.C., Terry N. Limiting factors of photosynthesis II: iron stress diminishes photochemical capacity by reducing the number of photosynthetic units. Plant Physiol 1980, 65:121-125.
    • (1980) Plant Physiol , vol.65 , pp. 121-125
    • Spiller, S.C.1    Terry, N.2
  • 36
    • 0000058570 scopus 로고
    • Specific mRNA and rRNA levels in greening pea leaves during recovery from iron stress
    • Spiller S.C., Kaufman L.S., Thompson W.F., Briggs W.R. Specific mRNA and rRNA levels in greening pea leaves during recovery from iron stress. Plant Physiol 1987, 84:409-414.
    • (1987) Plant Physiol , vol.84 , pp. 409-414
    • Spiller, S.C.1    Kaufman, L.S.2    Thompson, W.F.3    Briggs, W.R.4
  • 37
    • 0037021444 scopus 로고    scopus 로고
    • The HCF136 protein is essential for assembly of the photosystem II reaction center in Arabidopsis thaliana
    • Plücken H., Müller B., Grohmann D., Westhoff P., Eichacker L.A. The HCF136 protein is essential for assembly of the photosystem II reaction center in Arabidopsis thaliana. FEBS Lett 2002, 532:85-90.
    • (2002) FEBS Lett , vol.532 , pp. 85-90
    • Plücken, H.1    Müller, B.2    Grohmann, D.3    Westhoff, P.4    Eichacker, L.A.5
  • 38
    • 0031444519 scopus 로고    scopus 로고
    • Thioredoxins: structure and function in plant cells
    • Jacquot J.P., Lancelin J.M., Meyer Y. Thioredoxins: structure and function in plant cells. New Phytol 1997, 136:543-570.
    • (1997) New Phytol , vol.136 , pp. 543-570
    • Jacquot, J.P.1    Lancelin, J.M.2    Meyer, Y.3
  • 39
    • 0032922625 scopus 로고    scopus 로고
    • Regulation of chloroplast enzyme activities by thioredoxins: activation or relief from inhibition?
    • Ruelland E., Miginiac-Maslow M. Regulation of chloroplast enzyme activities by thioredoxins: activation or relief from inhibition?. Trends Plant Sci 1999, 4:136-141.
    • (1999) Trends Plant Sci , vol.4 , pp. 136-141
    • Ruelland, E.1    Miginiac-Maslow, M.2
  • 41
    • 0011187463 scopus 로고
    • The rubisco subunit binding protein
    • Ellis R.J., Van der Vies S.M. The rubisco subunit binding protein. Photosynth Res 1988, 16:101-115.
    • (1988) Photosynth Res , vol.16 , pp. 101-115
    • Ellis, R.J.1    Van der Vies, S.M.2
  • 42
    • 44649175852 scopus 로고    scopus 로고
    • Association of activase with chaperonin-60b: a possible mechanism for protecting photosynthesis during heat stress
    • Salvucci M.E. Association of activase with chaperonin-60b: a possible mechanism for protecting photosynthesis during heat stress. J Exp Bot 2008, 59:1923-1934.
    • (2008) J Exp Bot , vol.59 , pp. 1923-1934
    • Salvucci, M.E.1
  • 43
    • 12244262259 scopus 로고    scopus 로고
    • Adaptation to Fe-deficiency requires remodeling of the photosynthetic apparatus
    • Moseley J.L., Allinger T., Herzog S., Hoerth P., et al. Adaptation to Fe-deficiency requires remodeling of the photosynthetic apparatus. EMBO J 2002, 21:6709-6720.
    • (2002) EMBO J , vol.21 , pp. 6709-6720
    • Moseley, J.L.1    Allinger, T.2    Herzog, S.3    Hoerth, P.4
  • 44
    • 20144382680 scopus 로고    scopus 로고
    • N-terminal processing of Lhca3 Is a key step in remodeling of the photosystem I-light-harvesting complex under iron deficiency in Chlamydomonas reinhardtii
    • Naumann B., Stauber E.J., Busch A., Sommer F., Hippler M. N-terminal processing of Lhca3 Is a key step in remodeling of the photosystem I-light-harvesting complex under iron deficiency in Chlamydomonas reinhardtii. J Biol Chem 2005, 280:20431-20441.
    • (2005) J Biol Chem , vol.280 , pp. 20431-20441
    • Naumann, B.1    Stauber, E.J.2    Busch, A.3    Sommer, F.4    Hippler, M.5
  • 45
    • 33750967667 scopus 로고    scopus 로고
    • A pathogenesis related protein, AhPR10 from peanut: an insight of its mode of antifungal activity
    • Chadha P., Das R.H. A pathogenesis related protein, AhPR10 from peanut: an insight of its mode of antifungal activity. Planta 2006, 225:213-222.
    • (2006) Planta , vol.225 , pp. 213-222
    • Chadha, P.1    Das, R.H.2
  • 46
    • 0027551362 scopus 로고
    • Isolation of an asparagus intracellular PR-gene (AoPR1) wound-responsive promoter by the inverse polymerase chain reaction and its characterization in transgenic tobacco
    • Warner S., Scott R., Draper J. Isolation of an asparagus intracellular PR-gene (AoPR1) wound-responsive promoter by the inverse polymerase chain reaction and its characterization in transgenic tobacco. Plant J 1993, 3:191-201.
    • (1993) Plant J , vol.3 , pp. 191-201
    • Warner, S.1    Scott, R.2    Draper, J.3
  • 47
    • 0031412446 scopus 로고    scopus 로고
    • Antagonistic effects of abscisic acid and jasmonates on salt stress-inducible transcripts in rice roots
    • Moons A., Prinsen E., Bauw G., Van Montagu M. Antagonistic effects of abscisic acid and jasmonates on salt stress-inducible transcripts in rice roots. Plant Cell 1997, 9:2243-2259.
    • (1997) Plant Cell , vol.9 , pp. 2243-2259
    • Moons, A.1    Prinsen, E.2    Bauw, G.3    Van Montagu, M.4
  • 48
    • 0001390371 scopus 로고
    • Plant lectins: molecular and biological aspects
    • Etzler M.E. Plant lectins: molecular and biological aspects. Ann Rev Plant Physiol 1985, 36:209-234.
    • (1985) Ann Rev Plant Physiol , vol.36 , pp. 209-234
    • Etzler, M.E.1
  • 49
  • 50
    • 0037018936 scopus 로고    scopus 로고
    • Structure of a tau class glutathione S-transferase from wheat active in herbicide detoxification
    • Thom R., Cummins I., Dixon D.P., Edwards R., Cole D.J., Lapthorn A.J. Structure of a tau class glutathione S-transferase from wheat active in herbicide detoxification. Biochemistry 2002, 41:7008-7020.
    • (2002) Biochemistry , vol.41 , pp. 7008-7020
    • Thom, R.1    Cummins, I.2    Dixon, D.P.3    Edwards, R.4    Cole, D.J.5    Lapthorn, A.J.6
  • 51
    • 0035983888 scopus 로고    scopus 로고
    • Probing the diversity of the Arabidopsis glutathione S-transferase gene family
    • Wagner U., Edwards R., Dixon D.P., Mauch F. Probing the diversity of the Arabidopsis glutathione S-transferase gene family. Plant Mol Biol 2002, 49:515-532.
    • (2002) Plant Mol Biol , vol.49 , pp. 515-532
    • Wagner, U.1    Edwards, R.2    Dixon, D.P.3    Mauch, F.4
  • 52
    • 1942501777 scopus 로고    scopus 로고
    • Mechanism of gene expression of Arabidopsis glutathione S-transferase, AtGST1, and AtGST11 in response to aluminum stress
    • Ezaki B., Suzuki M., Motoda H., Kawamura M., Nakashima S., Matsumoto H. Mechanism of gene expression of Arabidopsis glutathione S-transferase, AtGST1, and AtGST11 in response to aluminum stress. Plant Physiol 2004, 134:1672-1682.
    • (2004) Plant Physiol , vol.134 , pp. 1672-1682
    • Ezaki, B.1    Suzuki, M.2    Motoda, H.3    Kawamura, M.4    Nakashima, S.5    Matsumoto, H.6
  • 53
    • 75649127974 scopus 로고    scopus 로고
    • Extensive functional diversification of the Populus glutathione S-transferase supergene family
    • Lan T., Yang Z.L., Yang X., Liu Y.J., Wang X.R., Zeng Q.Y. Extensive functional diversification of the Populus glutathione S-transferase supergene family. Plant Cell 2009, 21:3749-3766.
    • (2009) Plant Cell , vol.21 , pp. 3749-3766
    • Lan, T.1    Yang, Z.L.2    Yang, X.3    Liu, Y.J.4    Wang, X.R.5    Zeng, Q.Y.6
  • 54
    • 77349084674 scopus 로고    scopus 로고
    • Comprehensive expression analysis suggests overlapping and specific roles of rice glutathione S-transferase genes during development and stress responses
    • Jain M., Ghanashyam C., Bhattacharjee A. Comprehensive expression analysis suggests overlapping and specific roles of rice glutathione S-transferase genes during development and stress responses. BMC Genomics 2010, 11:73.
    • (2010) BMC Genomics , vol.11 , pp. 73
    • Jain, M.1    Ghanashyam, C.2    Bhattacharjee, A.3
  • 55
    • 79951821140 scopus 로고    scopus 로고
    • Expansion mechanisms and functional divergence of the glutathione s-transferase family in sorghum and other higher plants
    • Chi Y., Cheng Y., Vanitha J., Kumar N., Ramamoorthy R., Ramachandran S., et al. Expansion mechanisms and functional divergence of the glutathione s-transferase family in sorghum and other higher plants. DNA Res 2011, 18:1-16.
    • (2011) DNA Res , vol.18 , pp. 1-16
    • Chi, Y.1    Cheng, Y.2    Vanitha, J.3    Kumar, N.4    Ramamoorthy, R.5    Ramachandran, S.6
  • 56
    • 0033082685 scopus 로고    scopus 로고
    • Glyoxalase I from Brassica juncea: molecular cloning, regulation and its over-expression confer tolerance in transgenic tobacco under stress
    • Reddy V.S., Sopory Sudhir K. Glyoxalase I from Brassica juncea: molecular cloning, regulation and its over-expression confer tolerance in transgenic tobacco under stress. Plant J 1999, 17:385-395.
    • (1999) Plant J , vol.17 , pp. 385-395
    • Reddy, V.S.1    Sopory Sudhir, K.2
  • 57
    • 25844456887 scopus 로고    scopus 로고
    • Methylglyoxal levels in plants under salinity stress are dependent on glyoxalase I and glutathione
    • Yadav S.K., Singla-Pareek S.L., Ray M., Reddy M.K., Sopory S.K. Methylglyoxal levels in plants under salinity stress are dependent on glyoxalase I and glutathione. Biochem Biophys Res Commun 2005, 337:61-67.
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 61-67
    • Yadav, S.K.1    Singla-Pareek, S.L.2    Ray, M.3    Reddy, M.K.4    Sopory, S.K.5
  • 58
    • 45749125984 scopus 로고    scopus 로고
    • Recent advances in ascorbate biosynthesis and the physiological significance of ascorbate peroxidase in photosynthesizing organisms
    • Ishikawa T., Shigeoka S. Recent advances in ascorbate biosynthesis and the physiological significance of ascorbate peroxidase in photosynthesizing organisms. Biosci Biotechnol Biochem 2008, 72:1143-1154.
    • (2008) Biosci Biotechnol Biochem , vol.72 , pp. 1143-1154
    • Ishikawa, T.1    Shigeoka, S.2
  • 59
    • 33645031084 scopus 로고    scopus 로고
    • Expression profiles of hot pepper (Capsicum annum) genes under cold stress conditions
    • Hwang E.W., Kim K.A., Park S.C., Jeong M.J., Byun M.O., Kwon H.B. Expression profiles of hot pepper (Capsicum annum) genes under cold stress conditions. J Biosci 2005, 30:657-667.
    • (2005) J Biosci , vol.30 , pp. 657-667
    • Hwang, E.W.1    Kim, K.A.2    Park, S.C.3    Jeong, M.J.4    Byun, M.O.5    Kwon, H.B.6
  • 60
    • 70350223958 scopus 로고    scopus 로고
    • Proteomic analysis of the cold stress response in the moss, Physcomitrella patens
    • Wang X., Yang P., Zhang X., Xu Y., Kuang T., Shen S., et al. Proteomic analysis of the cold stress response in the moss, Physcomitrella patens. Proteomics 2009, 9:4529-4538.
    • (2009) Proteomics , vol.9 , pp. 4529-4538
    • Wang, X.1    Yang, P.2    Zhang, X.3    Xu, Y.4    Kuang, T.5    Shen, S.6
  • 61
    • 79960986809 scopus 로고    scopus 로고
    • Changes in the plant proteome resulting from salt stress: toward the creation of salt-tolerant crops?
    • Sobhanian H., Aghaei K., Komatsu S. Changes in the plant proteome resulting from salt stress: toward the creation of salt-tolerant crops?. J Proteomics 2011, 74:1323-1337.
    • (2011) J Proteomics , vol.74 , pp. 1323-1337
    • Sobhanian, H.1    Aghaei, K.2    Komatsu, S.3
  • 63
    • 21344497174 scopus 로고
    • Plant chitinases and their roles in resistance to fungal diseases
    • Punja Z.K., Zhang Y.Y. Plant chitinases and their roles in resistance to fungal diseases. J Nematol 1993, 25:526-540.
    • (1993) J Nematol , vol.25 , pp. 526-540
    • Punja, Z.K.1    Zhang, Y.Y.2
  • 64
    • 0141645390 scopus 로고    scopus 로고
    • Plant chitinases-regulation and function
    • Kasprzewska A. Plant chitinases-regulation and function. Cell Mol Biol Lett 2003, 8:809-824.
    • (2003) Cell Mol Biol Lett , vol.8 , pp. 809-824
    • Kasprzewska, A.1
  • 65
    • 0041859735 scopus 로고    scopus 로고
    • Co-expression of a modified maize ribosome-inactivating protein and a rice basic chitinase gene in transgenic rice plants confers enhanced resistance to sheath blight
    • Kim J.K., Jang I.C., Wu R., Zuo W.N., Boston R.S., Lee Y.H., et al. Co-expression of a modified maize ribosome-inactivating protein and a rice basic chitinase gene in transgenic rice plants confers enhanced resistance to sheath blight. Transgenic Res 2003, 12:475-484.
    • (2003) Transgenic Res , vol.12 , pp. 475-484
    • Kim, J.K.1    Jang, I.C.2    Wu, R.3    Zuo, W.N.4    Boston, R.S.5    Lee, Y.H.6
  • 66
    • 0001596943 scopus 로고
    • The biochemistry and the physiological and molecular actions of jasmonates
    • Sembdner G., Parthier B. The biochemistry and the physiological and molecular actions of jasmonates. Annu Rev Plant Physiol Plant Mol Biol 1993, 44:569-589.
    • (1993) Annu Rev Plant Physiol Plant Mol Biol , vol.44 , pp. 569-589
    • Sembdner, G.1    Parthier, B.2
  • 67
    • 11944254202 scopus 로고
    • Interplant communication: airborne methyl jasmonate induces synthesis of proteinase inhibitors in plant leaves
    • Farmer E.E., Ryan C.A. Interplant communication: airborne methyl jasmonate induces synthesis of proteinase inhibitors in plant leaves. Proc Natl Acad Sci U S A 1990, 87:7713-7716.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 7713-7716
    • Farmer, E.E.1    Ryan, C.A.2
  • 68
    • 0030293867 scopus 로고    scopus 로고
    • An octadecanoid pathway mutant (JL5) of tomato is compromised in signaling for defense against insect attack
    • Howe G.A., Lightner J., Browse J., Ryan C.A. An octadecanoid pathway mutant (JL5) of tomato is compromised in signaling for defense against insect attack. Plant Cell 1996, 8:2067-2077.
    • (1996) Plant Cell , vol.8 , pp. 2067-2077
    • Howe, G.A.1    Lightner, J.2    Browse, J.3    Ryan, C.A.4
  • 69
    • 0030331042 scopus 로고    scopus 로고
    • Pathogen-induced systemic activation of a plant defensin gene in Arabidopsis follows a salicylic acid-independent pathway
    • Penninckx I.A.M.A., Eggermont K., Terras F.R.G., Thomma B.P.H.J., De Samblanx G.W., Buchala A., et al. Pathogen-induced systemic activation of a plant defensin gene in Arabidopsis follows a salicylic acid-independent pathway. Plant Cell 1996, 8:2309-2323.
    • (1996) Plant Cell , vol.8 , pp. 2309-2323
    • Penninckx, I.A.M.A.1    Eggermont, K.2    Terras, F.R.G.3    Thomma, B.P.H.J.4    De Samblanx, G.W.5    Buchala, A.6
  • 71
    • 0032167942 scopus 로고    scopus 로고
    • Jasmonate signaling mutants of Arabidopsis are susceptible to the soil fungus Pythium irregulare
    • Staswick P.E., Yuen G.Y., Lehman C.C. Jasmonate signaling mutants of Arabidopsis are susceptible to the soil fungus Pythium irregulare. Plant J 1998, 16:747-754.
    • (1998) Plant J , vol.16 , pp. 747-754
    • Staswick, P.E.1    Yuen, G.Y.2    Lehman, C.C.3
  • 73
    • 0028361976 scopus 로고
    • JIP60, a methyl jasmonate-induced ribosomeinactivating protein involved in plant stress reactions
    • Reinbothe S., Reinbothe C., Lehman J., Becker W., Apel K., Parthier B. JIP60, a methyl jasmonate-induced ribosomeinactivating protein involved in plant stress reactions. Proc Natl Acad Sci U S A 1994, 91:7012-7016.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 7012-7016
    • Reinbothe, S.1    Reinbothe, C.2    Lehman, J.3    Becker, W.4    Apel, K.5    Parthier, B.6
  • 75
    • 0033785117 scopus 로고    scopus 로고
    • Exploiting chemical ecology and species diversity: stemborer and striga control for maize and sorghum in Africa
    • Khan Z.R., Pickett J.A., van den Berg J., Wadhams L.J., Woodcock C.M. Exploiting chemical ecology and species diversity: stemborer and striga control for maize and sorghum in Africa. Pest Manag Sci 2000, 56:957-962.
    • (2000) Pest Manag Sci , vol.56 , pp. 957-962
    • Khan, Z.R.1    Pickett, J.A.2    van den Berg, J.3    Wadhams, L.J.4    Woodcock, C.M.5
  • 76
    • 0001309166 scopus 로고
    • The current status and prospects of multiline cultivars and variety mixtures for disease resistance
    • Wolfe M.S. The current status and prospects of multiline cultivars and variety mixtures for disease resistance. Annu Rev Phytopathol 1985, 23:251-273.
    • (1985) Annu Rev Phytopathol , vol.23 , pp. 251-273
    • Wolfe, M.S.1
  • 77
    • 0001839511 scopus 로고
    • Disease incidence and yield of different cereal cultivars in pure stands and mixtures. I. Spring barley (Hordeum vulgare L.)
    • Gieffers W., Hesselbach J. Disease incidence and yield of different cereal cultivars in pure stands and mixtures. I. Spring barley (Hordeum vulgare L.). Z Pflanzenkr Pflanzenschutz 1988, 95:46-62.
    • (1988) Z Pflanzenkr Pflanzenschutz , vol.95 , pp. 46-62
    • Gieffers, W.1    Hesselbach, J.2
  • 78
  • 80
    • 34247267003 scopus 로고    scopus 로고
    • Metabolic changes in iron-stressed dicotyledonous plants
    • Springer, Netherlands, L.L. Barton, J. Abadia (Eds.)
    • Zocchi G. Metabolic changes in iron-stressed dicotyledonous plants. Iron Nutrition in Plants and Rhizospheric Microorganisms 2006, 359-370. Springer, Netherlands. L.L. Barton, J. Abadia (Eds.).
    • (2006) Iron Nutrition in Plants and Rhizospheric Microorganisms , pp. 359-370
    • Zocchi, G.1
  • 81
    • 83355166798 scopus 로고    scopus 로고
    • Discovering the role of mitochondria in the iron deficiency-induced metabolic responses of plants
    • Vigani G. Discovering the role of mitochondria in the iron deficiency-induced metabolic responses of plants. J Plant Physiol 2012, 169:1-11.
    • (2012) J Plant Physiol , vol.169 , pp. 1-11
    • Vigani, G.1
  • 82
    • 0034536648 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase in cucumber (Cucumis sativus L.) roots under iron deficiency: activity and kinetic characterisation
    • De Nisi P., Zocchi G. Phosphoenolpyruvate carboxylase in cucumber (Cucumis sativus L.) roots under iron deficiency: activity and kinetic characterisation. J Exp Bot 2000, 352:1903-1909.
    • (2000) J Exp Bot , vol.352 , pp. 1903-1909
    • De Nisi, P.1    Zocchi, G.2
  • 83
    • 0000974248 scopus 로고
    • NAD-malic enzyme from plants
    • Artus N.N., Edwards G.E. NAD-malic enzyme from plants. FEBS Lett 1985, 182:225-233.
    • (1985) FEBS Lett , vol.182 , pp. 225-233
    • Artus, N.N.1    Edwards, G.E.2
  • 84
    • 0035148218 scopus 로고    scopus 로고
    • Iron-induced changes in pyruvate metabolism of Tritrichomonas foetus and involvement of iron in expression of hydrogenosomal proteins
    • Vanacova S., Rasoloson D., Razga J., Hrdy I., Kulda J., Tachezy J. Iron-induced changes in pyruvate metabolism of Tritrichomonas foetus and involvement of iron in expression of hydrogenosomal proteins. Microbiology 2001, 147:53-62.
    • (2001) Microbiology , vol.147 , pp. 53-62
    • Vanacova, S.1    Rasoloson, D.2    Razga, J.3    Hrdy, I.4    Kulda, J.5    Tachezy, J.6
  • 85
    • 34247183784 scopus 로고    scopus 로고
    • Expression of an NADP-malic enzyme gene in rice (Oryza sativa. L) is induced by environmental stresses; over-expression of the gene in Arabidopsis confers salt and osmotic stress tolerance
    • Liu S.K., Cheng Y.X., Zhang X.X., Guan Q.J., Nishiuchi S., Hase K., et al. Expression of an NADP-malic enzyme gene in rice (Oryza sativa. L) is induced by environmental stresses; over-expression of the gene in Arabidopsis confers salt and osmotic stress tolerance. Plant Mol Biol 2007, 64:49-58.
    • (2007) Plant Mol Biol , vol.64 , pp. 49-58
    • Liu, S.K.1    Cheng, Y.X.2    Zhang, X.X.3    Guan, Q.J.4    Nishiuchi, S.5    Hase, K.6
  • 86
    • 77953649564 scopus 로고    scopus 로고
    • Cloning and functional analysis of the peanut iron transporter AhIRT1 during iron deficiency stress and intercropping with maize
    • Ding H., Duan L., Li J., Yan H., Zhao M., Zhang F., et al. Cloning and functional analysis of the peanut iron transporter AhIRT1 during iron deficiency stress and intercropping with maize. J Plant Physiol 2010, 167:996-1002.
    • (2010) J Plant Physiol , vol.167 , pp. 996-1002
    • Ding, H.1    Duan, L.2    Li, J.3    Yan, H.4    Zhao, M.5    Zhang, F.6
  • 87
    • 67650581552 scopus 로고    scopus 로고
    • Regulation of AhFRO1, an Fe(III)-chelate reductase of peanut, during iron deficiency stress and intercropping with maize
    • Ding H., Duan L., Wu H., Yang R., Ling H., Li W.X., et al. Regulation of AhFRO1, an Fe(III)-chelate reductase of peanut, during iron deficiency stress and intercropping with maize. Physiol Plant 2009, 136:274-283.
    • (2009) Physiol Plant , vol.136 , pp. 274-283
    • Ding, H.1    Duan, L.2    Wu, H.3    Yang, R.4    Ling, H.5    Li, W.X.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.