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Volumn 12, Issue 11, 2013, Pages 4670-4684

Soybean proteomics for unraveling abiotic stress response mechanism

Author keywords

abiotic stresses; methodology; proteomics; review; soybean

Indexed keywords

HEAT SHOCK PROTEIN; HEAVY METAL; REGULATOR PROTEIN;

EID: 84887234901     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr400604b     Document Type: Review
Times cited : (79)

References (111)
  • 2
    • 0020458787 scopus 로고
    • Plant productivity and environment
    • Boyer, J. S. Plant productivity and environment Science 1982, 218 (4571) 443-448
    • (1982) Science , vol.218 , Issue.4571 , pp. 443-448
    • Boyer, J.S.1
  • 3
    • 84855523412 scopus 로고    scopus 로고
    • Plant cell organelle proteomics in response to abiotic stress
    • Hossain, Z.; Nouri, M. Z.; Komatsu, S. Plant cell organelle proteomics in response to abiotic stress J. Proteome Res. 2012, 11 (1) 37-48
    • (2012) J. Proteome Res. , vol.11 , Issue.1 , pp. 37-48
    • Hossain, Z.1    Nouri, M.Z.2    Komatsu, S.3
  • 4
    • 84855521319 scopus 로고    scopus 로고
    • Proteomics techniques for the development of flood tolerant crops
    • Komatsu, S.; Hiraga, S.; Yanagawa, Y. Proteomics techniques for the development of flood tolerant crops J. Proteome Res. 2012, 11, 68-78
    • (2012) J. Proteome Res. , vol.11 , pp. 68-78
    • Komatsu, S.1    Hiraga, S.2    Yanagawa, Y.3
  • 5
    • 84866179240 scopus 로고    scopus 로고
    • Organ-specific proteomics analysis for response mechanism in soybean seedlings under flooding stress
    • Khatoon, A.; Rehman, S.; Hiraga, S.; Makino, T.; Komatsu, S. Organ-specific proteomics analysis for response mechanism in soybean seedlings under flooding stress J. Proteomics 2012, 75, 5706-5723
    • (2012) J. Proteomics , vol.75 , pp. 5706-5723
    • Khatoon, A.1    Rehman, S.2    Hiraga, S.3    Makino, T.4    Komatsu, S.5
  • 6
    • 84857651754 scopus 로고    scopus 로고
    • Organ-specific proteomic analysis of drought-stressed soybean seedlings
    • Mohammadi, P. P.; Moieni, A.; Hiraga, S.; Komatsu, S. Organ-specific proteomic analysis of drought-stressed soybean seedlings J. Proteomics 2012, 75 (6) 1906-1923
    • (2012) J. Proteomics , vol.75 , Issue.6 , pp. 1906-1923
    • Mohammadi, P.P.1    Moieni, A.2    Hiraga, S.3    Komatsu, S.4
  • 8
    • 84872675844 scopus 로고    scopus 로고
    • Comparative proteome analysis of high and low cadmium accumulating soybeans under cadmium stress
    • Hossain, Z.; Hajika, M.; Komatsu, S. Comparative proteome analysis of high and low cadmium accumulating soybeans under cadmium stress Amino Acids 2012, 43 (6) 2393-2416
    • (2012) Amino Acids , vol.43 , Issue.6 , pp. 2393-2416
    • Hossain, Z.1    Hajika, M.2    Komatsu, S.3
  • 9
    • 70349970273 scopus 로고    scopus 로고
    • A comprehensive analysis of the soybean genes and proteins expressed under flooding stress using transcriptome and proteome techniques
    • Komatsu, S.; Yamamoto, R.; Nanjo, Y.; Mikami, Y.; Yunokawa, H.; Sakata, K. A comprehensive analysis of the soybean genes and proteins expressed under flooding stress using transcriptome and proteome techniques J. Proteome Res. 2009, 8, 4766-4778
    • (2009) J. Proteome Res. , vol.8 , pp. 4766-4778
    • Komatsu, S.1    Yamamoto, R.2    Nanjo, Y.3    Mikami, Y.4    Yunokawa, H.5    Sakata, K.6
  • 11
    • 78449275495 scopus 로고    scopus 로고
    • Comparative proteomics analysis of differentially expressed proteins in soybean cell wall during flooding stress
    • Komatsu, S.; Kobayashi, Y.; Nishizawa, K.; Nanjo, Y.; Furukawa, K. Comparative proteomics analysis of differentially expressed proteins in soybean cell wall during flooding stress Amino Acids 2010, 39 (5) 1435-1449
    • (2010) Amino Acids , vol.39 , Issue.5 , pp. 1435-1449
    • Komatsu, S.1    Kobayashi, Y.2    Nishizawa, K.3    Nanjo, Y.4    Furukawa, K.5
  • 12
    • 77951667995 scopus 로고    scopus 로고
    • Identification of flooding stress responsible cascades in root and hypocotyl of soybean using proteome analysis
    • Komatsu, S.; Sugimoto, T.; Hoshino, T.; Nanjo, Y.; Furukawa, K. Identification of flooding stress responsible cascades in root and hypocotyl of soybean using proteome analysis Amino Acids 2010, 38 (3) 729-738
    • (2010) Amino Acids , vol.38 , Issue.3 , pp. 729-738
    • Komatsu, S.1    Sugimoto, T.2    Hoshino, T.3    Nanjo, Y.4    Furukawa, K.5
  • 13
    • 80052511115 scopus 로고    scopus 로고
    • Comprehensive analysis of mitochondria in roots and hypocotyls of soybean under flooding stress using proteomics and metabolomics techniques
    • Komatsu, S.; Yamamoto, A.; Nakamura, T.; Nouri, M. Z.; Nanjo, Y.; Nishizawa, K.; Furukawa, K. Comprehensive analysis of mitochondria in roots and hypocotyls of soybean under flooding stress using proteomics and metabolomics techniques J. Proteome Res. 2011, 10 (9) 3993-4004
    • (2011) J. Proteome Res. , vol.10 , Issue.9 , pp. 3993-4004
    • Komatsu, S.1    Yamamoto, A.2    Nakamura, T.3    Nouri, M.Z.4    Nanjo, Y.5    Nishizawa, K.6    Furukawa, K.7
  • 15
    • 84872961657 scopus 로고    scopus 로고
    • Proteomic analysis of the flooding tolerance mechanism in mutant soybean
    • Komatsu, S.; Nanjo, Y.; Nishimura, M. Proteomic analysis of the flooding tolerance mechanism in mutant soybean J. Proteomics 2013, 79, 231-250
    • (2013) J. Proteomics , vol.79 , pp. 231-250
    • Komatsu, S.1    Nanjo, Y.2    Nishimura, M.3
  • 16
    • 84875532484 scopus 로고    scopus 로고
    • Proteomic analysis of response to long-term continuous stress in roots of germinating soybean seeds
    • Swigonska, S.; Weidner, S. Proteomic analysis of response to long-term continuous stress in roots of germinating soybean seeds J. Plant Physiol. 2013, 170 (5) 470-479
    • (2013) J. Plant Physiol. , vol.170 , Issue.5 , pp. 470-479
    • Swigonska, S.1    Weidner, S.2
  • 17
    • 77954690166 scopus 로고    scopus 로고
    • Proteome analysis of soybean roots subjected to short-term drought stress
    • Alam, I.; Sharmin, S. A.; Kim, K. H.; Yang, J. K.; Choi, M. S.; Lee, B. H. Proteome analysis of soybean roots subjected to short-term drought stress Plant Soil 2010, 333, 491-505
    • (2010) Plant Soil , vol.333 , pp. 491-505
    • Alam, I.1    Sharmin, S.A.2    Kim, K.H.3    Yang, J.K.4    Choi, M.S.5    Lee, B.H.6
  • 18
    • 77951711549 scopus 로고    scopus 로고
    • Proteome analysis of soybean roots under waterlogging stress at an early vegetative stage
    • Alam, I.; Lee, D. G.; Kim, K. H.; Park, C. H.; Sharmin, S. A.; Lee, H.; Oh, K. W.; Yun, B. W.; Lee, B. H. Proteome analysis of soybean roots under waterlogging stress at an early vegetative stage J. Biosci. 2010, 35 (1) 49-62
    • (2010) J. Biosci. , vol.35 , Issue.1 , pp. 49-62
    • Alam, I.1    Lee, D.G.2    Kim, K.H.3    Park, C.H.4    Sharmin, S.A.5    Lee, H.6    Oh, K.W.7    Yun, B.W.8    Lee, B.H.9
  • 19
    • 85027944991 scopus 로고    scopus 로고
    • Analysis of response mechanism in soybean under low oxygen and flooding stresses using gel-base proteomics technique
    • Khatoon, A.; Rehman, S.; Oh, M. W.; Woo, S. H.; Komatsu, S. Analysis of response mechanism in soybean under low oxygen and flooding stresses using gel-base proteomics technique Mol. Biol. Rep. 2012, 39 (12) 10581-10594
    • (2012) Mol. Biol. Rep. , vol.39 , Issue.12 , pp. 10581-10594
    • Khatoon, A.1    Rehman, S.2    Oh, M.W.3    Woo, S.H.4    Komatsu, S.5
  • 20
    • 80051668746 scopus 로고    scopus 로고
    • Comparative proteomic approach to identify proteins involved in flooding combined with salinity stress in soybean
    • Alam, I.; Sharmin, S. A.; Kim, K.-H.; Kim, Y.-G.; Lee, J. J.; Bahk, J. D.; Lee, B.-H. Comparative proteomic approach to identify proteins involved in flooding combined with salinity stress in soybean Plant Soil 2011, 346, 45-62
    • (2011) Plant Soil , vol.346 , pp. 45-62
    • Alam, I.1    Sharmin, S.A.2    Kim, K.-H.3    Kim, Y.-G.4    Lee, J.J.5    Bahk, J.D.6    Lee, B.-H.7
  • 21
    • 77952389740 scopus 로고    scopus 로고
    • Comparative analysis of soybean plasma membrane proteins under osmotic stress using gel-based and LC MS/MS-based proteomics approaches
    • Nouri, M. Z.; Komatsu, S. Comparative analysis of soybean plasma membrane proteins under osmotic stress using gel-based and LC MS/MS-based proteomics approaches Proteomics 2010, 10 (10) 1930-1945
    • (2010) Proteomics , vol.10 , Issue.10 , pp. 1930-1945
    • Nouri, M.Z.1    Komatsu, S.2
  • 22
    • 70449622771 scopus 로고    scopus 로고
    • Proteomics approach for identifying osmotic-stress-related proteins in soybean roots
    • Toorchi, M.; Yukawa, K.; Nouri, M. Z.; Komatsu, S. Proteomics approach for identifying osmotic-stress-related proteins in soybean roots Peptides 2009, 30 (12) 2108-2117
    • (2009) Peptides , vol.30 , Issue.12 , pp. 2108-2117
    • Toorchi, M.1    Yukawa, K.2    Nouri, M.Z.3    Komatsu, S.4
  • 23
    • 84860255322 scopus 로고    scopus 로고
    • Differential responses of microsomal proteins and metabolites in two contrasting cadmium (Cd)-accumulating soybean cultivars under Cd stress
    • Ahsan, N.; Nakamura, T.; Komatsu, S. Differential responses of microsomal proteins and metabolites in two contrasting cadmium (Cd)-accumulating soybean cultivars under Cd stress Amino Acids 2012, 42 (1) 317-327
    • (2012) Amino Acids , vol.42 , Issue.1 , pp. 317-327
    • Ahsan, N.1    Nakamura, T.2    Komatsu, S.3
  • 24
    • 33749431711 scopus 로고    scopus 로고
    • Proteins induced by cadmium in soybean cells
    • Sobkowiak, R.; Deckert, J. Proteins induced by cadmium in soybean cells J. Plant Physiol. 2006, 163 (11) 1203-1206
    • (2006) J. Plant Physiol. , vol.163 , Issue.11 , pp. 1203-1206
    • Sobkowiak, R.1    Deckert, J.2
  • 25
    • 35948983064 scopus 로고    scopus 로고
    • Comparative proteome analysis of differentially expressed proteins induced by Al toxicity in soybean
    • Zhen, Y.; Qi, J. L.; Wang, S. S.; Su, J.; Xu, G. H.; Zhang, M. S.; Miao, L.; Peng, X. X.; Tian, D.; Yang, Y. H. Comparative proteome analysis of differentially expressed proteins induced by Al toxicity in soybean Physiol. Plant 2007, 131 (4) 542-554
    • (2007) Physiol. Plant , vol.131 , Issue.4 , pp. 542-554
    • Zhen, Y.1    Qi, J.L.2    Wang, S.S.3    Su, J.4    Xu, G.H.5    Zhang, M.S.6    Miao, L.7    Peng, X.X.8    Tian, D.9    Yang, Y.H.10
  • 26
    • 84857451367 scopus 로고    scopus 로고
    • From climate change to molecular response: Redox proteomics of ozone-induced responses in soybean
    • Galant, A.; Koester, R. P.; Ainsworth, E. A.; Hicks, L. M.; Jez, J. M. From climate change to molecular response: redox proteomics of ozone-induced responses in soybean New Phytol. 2012, 194 (1) 220-229
    • (2012) New Phytol. , vol.194 , Issue.1 , pp. 220-229
    • Galant, A.1    Koester, R.P.2    Ainsworth, E.A.3    Hicks, L.M.4    Jez, J.M.5
  • 27
    • 77954711265 scopus 로고    scopus 로고
    • Ozone stress-induced proteomic changes in leaf total soluble and chloroplast proteins of soybean reveal that carbon allocation is involved in adaptation in the early developmental stage
    • Ahsan, N.; Nanjo, Y.; Sawada, H.; Kohno, Y.; Komatsu, S. Ozone stress-induced proteomic changes in leaf total soluble and chloroplast proteins of soybean reveal that carbon allocation is involved in adaptation in the early developmental stage Proteomics 2010, 10, 2605-2619
    • (2010) Proteomics , vol.10 , pp. 2605-2619
    • Ahsan, N.1    Nanjo, Y.2    Sawada, H.3    Kohno, Y.4    Komatsu, S.5
  • 28
    • 37149054654 scopus 로고    scopus 로고
    • Impact of solar ultraviolet-B on the proteome in soybean lines differing in flavonoid contents
    • Xu, C.; Sullivan, J. H.; Garrett, W. M.; Caperna, T. J.; Natarajan, S. Impact of solar ultraviolet-B on the proteome in soybean lines differing in flavonoid contents Phytochemistry 2008, 69 (1) 38-48
    • (2008) Phytochemistry , vol.69 , Issue.1 , pp. 38-48
    • Xu, C.1    Sullivan, J.H.2    Garrett, W.M.3    Caperna, T.J.4    Natarajan, S.5
  • 29
    • 79960471828 scopus 로고    scopus 로고
    • Proteomic analysis of seed germination under salt stress in soybeans
    • Xu, X. Y.; Fan, R.; Zheng, R.; Li, C. M.; Yu, D. Y. Proteomic analysis of seed germination under salt stress in soybeans J. Zhejiang Univ., Sci., B 2011, 12 (7) 507-517
    • (2011) J. Zhejiang Univ., Sci., B , vol.12 , Issue.7 , pp. 507-517
    • Xu, X.Y.1    Fan, R.2    Zheng, R.3    Li, C.M.4    Yu, D.Y.5
  • 30
    • 58149235243 scopus 로고    scopus 로고
    • Proteome analysis of soybean hypocotyl and root under salt stress
    • Aghaei, K.; Ehsanpour, A. A.; Shah, A. H.; Komatsu, S. Proteome analysis of soybean hypocotyl and root under salt stress Amino Acids 2009, 36, 91-98
    • (2009) Amino Acids , vol.36 , pp. 91-98
    • Aghaei, K.1    Ehsanpour, A.A.2    Shah, A.H.3    Komatsu, S.4
  • 31
    • 77955459485 scopus 로고    scopus 로고
    • Tissue-specific defense and thermo-adaptive mechanisms of soybean seedlings under heat stress revealed by proteomic approach
    • Ahsan, N.; Donnart, T.; Nouri, M. Z.; Komatsu, S. Tissue-specific defense and thermo-adaptive mechanisms of soybean seedlings under heat stress revealed by proteomic approach J. Proteome Res. 2010, 9, 4189-4204
    • (2010) J. Proteome Res. , vol.9 , pp. 4189-4204
    • Ahsan, N.1    Donnart, T.2    Nouri, M.Z.3    Komatsu, S.4
  • 32
    • 63349106787 scopus 로고    scopus 로고
    • Soybean proteomics and its application to functional analysis
    • Komatsu, S.; Ahsan, N. Soybean proteomics and its application to functional analysis J. Proteomics 2009, 72 (3) 325-336
    • (2009) J. Proteomics , vol.72 , Issue.3 , pp. 325-336
    • Komatsu, S.1    Ahsan, N.2
  • 34
    • 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 (7) 3035-3041
    • (2008) J. Proteome Res. , vol.7 , Issue.7 , pp. 3035-3041
    • Toorchi, M.1    Nouri, M.Z.2    Tsumura, M.3    Komatsu, S.4
  • 35
    • 33645046883 scopus 로고    scopus 로고
    • Reduction of proteins during sample preparation and two-dimensional gel electrophoresis of woody plant samples
    • Valcu, C.-M.; Schlink, K. Reduction of proteins during sample preparation and two-dimensional gel electrophoresis of woody plant samples Proteomics 2006, 6, 1599-1605
    • (2006) Proteomics , vol.6 , pp. 1599-1605
    • Valcu, C.-M.1    Schlink, K.2
  • 36
    • 22044456721 scopus 로고    scopus 로고
    • Preparation of protein extracts from recalcitrant plant tissues: An evaluation of different methods for two-dimensional gel electrophoresis analysis
    • Carpentier, S. C.; Witters, E.; Laukens, K.; Deckers, P.; Swennen, R.; Panis, B. Preparation of protein extracts from recalcitrant plant tissues: an evaluation of different methods for two-dimensional gel electrophoresis analysis Proteomics 2005, 5, 2497-2507
    • (2005) Proteomics , vol.5 , pp. 2497-2507
    • Carpentier, S.C.1    Witters, E.2    Laukens, K.3    Deckers, P.4    Swennen, R.5    Panis, B.6
  • 37
    • 67649184776 scopus 로고    scopus 로고
    • A rapid and simple procedure for the depletion of abundant storage proteins from legume seeds to advance proteome analysis: A case study using Glycine max
    • Krishnan, H. B.; Oehrle, N. W.; Natarajan, S. S. A rapid and simple procedure for the depletion of abundant storage proteins from legume seeds to advance proteome analysis: a case study using Glycine max Proteomics 2009, 9 (11) 3174-3188
    • (2009) Proteomics , vol.9 , Issue.11 , pp. 3174-3188
    • Krishnan, H.B.1    Oehrle, N.W.2    Natarajan, S.S.3
  • 38
    • 69949097289 scopus 로고    scopus 로고
    • An efficient extraction method to enhance analysis of low abundant proteins from soybean seed
    • Natarajan, S. S.; Krishnan, H. B.; Lakshman, S.; Garrett, W. M. An efficient extraction method to enhance analysis of low abundant proteins from soybean seed Anal. Biochem. 2009, 394 (2) 259-268
    • (2009) Anal. Biochem. , vol.394 , Issue.2 , pp. 259-268
    • Natarajan, S.S.1    Krishnan, H.B.2    Lakshman, S.3    Garrett, W.M.4
  • 39
    • 21244455506 scopus 로고    scopus 로고
    • Comparison of protein solubilization methods suitable for proteomic analysis of soybean seed proteins
    • Natarajan, S.; Xu, C.; Caperna, T. J.; Garrett, W. M. Comparison of protein solubilization methods suitable for proteomic analysis of soybean seed proteins Anal. Biochem. 2005, 342, 214-220
    • (2005) Anal. Biochem. , vol.342 , pp. 214-220
    • Natarajan, S.1    Xu, C.2    Caperna, T.J.3    Garrett, W.M.4
  • 40
    • 70350448007 scopus 로고    scopus 로고
    • Comparative analyses of the proteomes of leaves and flowers at various stages of development reveal organ-specific functional differentiation of proteins in soybean
    • Ahsan, N.; Komatsu, S. Comparative analyses of the proteomes of leaves and flowers at various stages of development reveal organ-specific functional differentiation of proteins in soybean Proteomics 2009, 9, 4889-4907
    • (2009) Proteomics , vol.9 , pp. 4889-4907
    • Ahsan, N.1    Komatsu, S.2
  • 41
    • 0001510436 scopus 로고
    • Solubilization of plant membrane proteins for analysis by two-dimensional gel electrophoresis
    • Hurkman, W. J.; Tanaka, C. K. Solubilization of plant membrane proteins for analysis by two-dimensional gel electrophoresis Plant Physiol. 1986, 81, 802-806
    • (1986) Plant Physiol. , vol.81 , pp. 802-806
    • Hurkman, W.J.1    Tanaka, C.K.2
  • 42
    • 45849097589 scopus 로고    scopus 로고
    • Plant protein isolation and stabilization for enhanced resolution of two-dimensional polyacrylamide gel electrophoresis
    • Sarma, A. D.; Oehrle, N. W.; Emerich, D. W. Plant protein isolation and stabilization for enhanced resolution of two-dimensional polyacrylamide gel electrophoresis Anal. Biochem. 2008, 379 (2) 192-195
    • (2008) Anal. Biochem. , vol.379 , Issue.2 , pp. 192-195
    • Sarma, A.D.1    Oehrle, N.W.2    Emerich, D.W.3
  • 44
  • 45
    • 0042572096 scopus 로고    scopus 로고
    • Role of ubiquitination in the regulation of plant defense against pathogens
    • Devoto, A.; Muskett, P. R.; Shirasu, K. Role of ubiquitination in the regulation of plant defense against pathogens Curr. Opin. Plant Biol. 2003, 6, 307-311
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 307-311
    • Devoto, A.1    Muskett, P.R.2    Shirasu, K.3
  • 46
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. Mechanisms underlying ubiquitination Annu. Rev. Biochem. 2001, 70, 503-533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 47
    • 77950903984 scopus 로고    scopus 로고
    • GmRFP1 encodes a previously unknown RING-type E3 ubiquitin ligase in Soybean (Glycine max)
    • Du, Q. L.; Cui, W. Z.; Zhang, C. H.; Yu, D. Y. GmRFP1 encodes a previously unknown RING-type E3 ubiquitin ligase in Soybean (Glycine max) Mol. Biol. Rep. 2010, 37, 685-693
    • (2010) Mol. Biol. Rep. , vol.37 , pp. 685-693
    • Du, Q.L.1    Cui, W.Z.2    Zhang, C.H.3    Yu, D.Y.4
  • 48
    • 77955459998 scopus 로고    scopus 로고
    • Comparative proteomic analysis of early-stage soybean seedlings responses to flooding by using gel and gel-free techniques
    • Nanjo, Y.; Skultety, L.; Ashraf, Y.; Komatsu, S. Comparative proteomic analysis of early-stage soybean seedlings responses to flooding by using gel and gel-free techniques J. Proteome Res. 2010, 9, 3989-4002
    • (2010) J. Proteome Res. , vol.9 , pp. 3989-4002
    • Nanjo, Y.1    Skultety, L.2    Ashraf, Y.3    Komatsu, S.4
  • 49
    • 78649851541 scopus 로고    scopus 로고
    • Wheat mitochondrial proteome provide new links between antioxidant defense and plant salinity tolerance
    • Jacoby, R. P.; Millar, A. H.; Taylor, N. L. Wheat mitochondrial proteome provide new links between antioxidant defense and plant salinity tolerance J. Proteome Res. 2010, 9, 6595-6604
    • (2010) J. Proteome Res. , vol.9 , pp. 6595-6604
    • Jacoby, R.P.1    Millar, A.H.2    Taylor, N.L.3
  • 50
    • 24044461712 scopus 로고    scopus 로고
    • Differential impact of environmental stresses on the pea mitochondrial proteome
    • Taylor, N. L.; Heazlewood, J. L.; Days, D. A.; Millar, A. H. Differential impact of environmental stresses on the pea mitochondrial proteome Mol. Cell. Proteomics 2005, 4, 1122-1133
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1122-1133
    • Taylor, N.L.1    Heazlewood, J.L.2    Days, D.A.3    Millar, A.H.4
  • 51
    • 67651083574 scopus 로고    scopus 로고
    • Mitochondrial damage in the soybean seed axis during imbibitions at chilling temperatures
    • Yin, G.; Sun, H.; Xin, X.; Qin, G.; Liang, Z.; Jing, X. Mitochondrial damage in the soybean seed axis during imbibitions at chilling temperatures Plant Cell Physiol. 2009, 50, 1304-1318
    • (2009) Plant Cell Physiol. , vol.50 , pp. 1304-1318
    • Yin, G.1    Sun, H.2    Xin, X.3    Qin, G.4    Liang, Z.5    Jing, X.6
  • 52
    • 34447311067 scopus 로고    scopus 로고
    • Responses to flooding and drought stress by two citrus rootstock seedlings with different water-use efficiency
    • Garcia-Sanchez, F.; Syvertsen, J. P.; Gimeno, V.; Botía, P.; Perez-Perez, J. G. Responses to flooding and drought stress by two citrus rootstock seedlings with different water-use efficiency Physiol. Plant. 2007, 130 (4) 532-542
    • (2007) Physiol. Plant. , vol.130 , Issue.4 , pp. 532-542
    • Garcia-Sanchez, F.1    Syvertsen, J.P.2    Gimeno, V.3    Botía, P.4    Perez-Perez, J.G.5
  • 53
    • 58549116129 scopus 로고    scopus 로고
    • A PIP-family protein is required for biosynthesis of tobacco alkaloids
    • Kajikawa, M.; Hirai, N.; Hashimoto, T. A PIP-family protein is required for biosynthesis of tobacco alkaloids Plant Mol. Biol. 2009, 69, 287-298
    • (2009) Plant Mol. Biol. , vol.69 , pp. 287-298
    • Kajikawa, M.1    Hirai, N.2    Hashimoto, T.3
  • 55
    • 84355161587 scopus 로고    scopus 로고
    • Analysis of proteomic changes in roots of soybean seedlings during recovery after flooding
    • Salavati, A.; Khatoon, A.; Nanjo, Y.; Komatsu, S. Analysis of proteomic changes in roots of soybean seedlings during recovery after flooding J. Proteomics 2012, 75, 878-893
    • (2012) J. Proteomics , vol.75 , pp. 878-893
    • Salavati, A.1    Khatoon, A.2    Nanjo, Y.3    Komatsu, S.4
  • 59
    • 84855560266 scopus 로고    scopus 로고
    • Mass spectrometry-based analysis of proteomic changes in the root tips of flooded soybean seedlings
    • Nanjo, Y.; Skultety, L.; Uváčková, L.; Klubicová, K.; Hajduch, M.; Komatsu, S. Mass spectrometry-based analysis of proteomic changes in the root tips of flooded soybean seedlings J. Proteome Res. 2012, 11 (1) 372-385
    • (2012) J. Proteome Res. , vol.11 , Issue.1 , pp. 372-385
    • Nanjo, Y.1    Skultety, L.2    Uváčková, L.3    Klubicová, K.4    Hajduch, M.5    Komatsu, S.6
  • 60
    • 33646241061 scopus 로고    scopus 로고
    • Apoptosis-like programmed cell death occurs in procambium and ground meristem of pea (Pisum sativum) root tips exposed to sudden flooding
    • Gladish, D. K.; Xu, J.; Niki, T. Apoptosis-like programmed cell death occurs in procambium and ground meristem of pea (Pisum sativum) root tips exposed to sudden flooding Ann. Bot. 2006, 97 (5) 895-902
    • (2006) Ann. Bot. , vol.97 , Issue.5 , pp. 895-902
    • Gladish, D.K.1    Xu, J.2    Niki, T.3
  • 61
    • 33751001355 scopus 로고    scopus 로고
    • Yeast complementation reveals a role for an Arabidopsis thaliana late embryogenesis abundant (LEA)-like protein in oxidative stress tolerance
    • Mowla, S. B.; Cuypers, A.; Driscoll, S. P.; Kiddle, G.; Thomson, J.; Foyer, C. H.; Theodoulou, F. L. Yeast complementation reveals a role for an Arabidopsis thaliana late embryogenesis abundant (LEA)-like protein in oxidative stress tolerance Plant J. 2006, 48, 743-756
    • (2006) Plant J. , vol.48 , pp. 743-756
    • Mowla, S.B.1    Cuypers, A.2    Driscoll, S.P.3    Kiddle, G.4    Thomson, J.5    Foyer, C.H.6    Theodoulou, F.L.7
  • 62
    • 20444472040 scopus 로고    scopus 로고
    • Water deficits affect caffeate O-methyltransferase, lignification, and related enzymes in maize leaves. A proteomic investigation
    • Vincent, D.; Lapierre, C.; Pollet, B.; Cornic, G.; Negroni, L.; Zivy, M. Water deficits affect caffeate O-methyltransferase, lignification, and related enzymes in maize leaves. A proteomic investigation Plant Physiol. 2005, 137 (3) 949-960
    • (2005) Plant Physiol. , vol.137 , Issue.3 , pp. 949-960
    • Vincent, D.1    Lapierre, C.2    Pollet, B.3    Cornic, G.4    Negroni, L.5    Zivy, M.6
  • 64
    • 79956369680 scopus 로고    scopus 로고
    • Transformation of tomato with a bacterial codA gene enhances tolerance to salt and water stresses
    • Goel, D.; Singh, A. K.; Yadav, V.; Babbar, S. B.; Murata, N.; Bansal, K. C. Transformation of tomato with a bacterial codA gene enhances tolerance to salt and water stresses J. Plant Physiol. 2011, 168 (11) 1286-1294
    • (2011) J. Plant Physiol. , vol.168 , Issue.11 , pp. 1286-1294
    • Goel, D.1    Singh, A.K.2    Yadav, V.3    Babbar, S.B.4    Murata, N.5    Bansal, K.C.6
  • 65
    • 0000219790 scopus 로고    scopus 로고
    • In vitro salt tolerance and proline accumulation in Andean potato (Solanum spp.) differing in frost resistance
    • Martienz, C. A.; Maestri, M.; Lani, E. G. In vitro salt tolerance and proline accumulation in Andean potato (Solanum spp.) differing in frost resistance Plant Sci. 1996, 116, 177-184
    • (1996) Plant Sci. , vol.116 , pp. 177-184
    • Martienz, C.A.1    Maestri, M.2    Lani, E.G.3
  • 66
    • 33750963981 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel salt inducible gene encoding an acidic isoform of PR-5 protein in soybean (Glycine max [L.] Merr)
    • Onishi, M.; Tachi, H.; Kojima, T.; Shiraiwa, M.; Takahara, H. Molecular cloning and characterization of a novel salt inducible gene encoding an acidic isoform of PR-5 protein in soybean (Glycine max [L.] Merr) Plant Physiol. Biochem. 2006, 44, 573-580
    • (2006) Plant Physiol. Biochem. , vol.44 , pp. 573-580
    • Onishi, M.1    Tachi, H.2    Kojima, T.3    Shiraiwa, M.4    Takahara, H.5
  • 67
    • 23844545649 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel soybean gene encoding a leucine-zipper-like protein induced to salt stress
    • Aoki, A.; Kanegami, A.; Mihara, M.; Kojima, T.; Shiraiwa, M.; Takahara, H. Molecular cloning and characterization of a novel soybean gene encoding a leucine-zipper-like protein induced to salt stress Gene 2005, 356, 135-145
    • (2005) Gene , vol.356 , pp. 135-145
    • Aoki, A.1    Kanegami, A.2    Mihara, M.3    Kojima, T.4    Shiraiwa, M.5    Takahara, H.6
  • 68
    • 0025925472 scopus 로고
    • The impact of heavy metals on lowland rivers and the implications for man and the environment
    • Bubb, J. M.; Lester, J. N. The impact of heavy metals on lowland rivers and the implications for man and the environment Sci. Total Environ. 1991, 100, 207-233
    • (1991) Sci. Total Environ. , vol.100 , pp. 207-233
    • Bubb, J.M.1    Lester, J.N.2
  • 69
    • 0037772259 scopus 로고    scopus 로고
    • Heavy metal toxicity: Cadmium permeates through calcium channels and disturbs the plant water status
    • Perfus-Barbeoch, L.; Leonhardt, N.; Vavasseur, A.; Forestier, C. Heavy metal toxicity: cadmium permeates through calcium channels and disturbs the plant water status Plant J. 2002, 32, 539-548
    • (2002) Plant J. , vol.32 , pp. 539-548
    • Perfus-Barbeoch, L.1    Leonhardt, N.2    Vavasseur, A.3    Forestier, C.4
  • 70
    • 58149510121 scopus 로고    scopus 로고
    • The relationship between metal toxicity and cellular redox imbalance
    • Sharma, S. S.; Dietz, K. J. The relationship between metal toxicity and cellular redox imbalance Trends Plant Sci. 2009, 14, 43-50
    • (2009) Trends Plant Sci. , vol.14 , pp. 43-50
    • Sharma, S.S.1    Dietz, K.J.2
  • 71
    • 66949176994 scopus 로고    scopus 로고
    • Mechanisms to cope with arsenic or cadmium excess in plants
    • Verbruggen, N.; Hermans, C.; Schat, H. Mechanisms to cope with arsenic or cadmium excess in plants Curr. Opin. Plant Biol. 2009, 12, 364-372
    • (2009) Curr. Opin. Plant Biol. , vol.12 , pp. 364-372
    • Verbruggen, N.1    Hermans, C.2    Schat, H.3
  • 72
    • 84862666002 scopus 로고    scopus 로고
    • Proteomic study of β-aminobutyric acid-mediated cadmium stress alleviation in soybean
    • Hossain, Z.; Makino, T.; Komatsu, S. Proteomic study of β-aminobutyric acid-mediated cadmium stress alleviation in soybean J. Proteomics 2012, 75 (13) 4151-4164
    • (2012) J. Proteomics , vol.75 , Issue.13 , pp. 4151-4164
    • Hossain, Z.1    Makino, T.2    Komatsu, S.3
  • 74
    • 48249085699 scopus 로고    scopus 로고
    • Quantitative changes in protein expression of cadmium-exposed poplar plants
    • Kieffer, P.; Dommes, J.; Hoffmann, L.; Hausman, J. F.; Renaut, J. Quantitative changes in protein expression of cadmium-exposed poplar plants Proteomics 2008, 8 (12) 2514-2530
    • (2008) Proteomics , vol.8 , Issue.12 , pp. 2514-2530
    • Kieffer, P.1    Dommes, J.2    Hoffmann, L.3    Hausman, J.F.4    Renaut, J.5
  • 75
    • 2442445139 scopus 로고    scopus 로고
    • Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response
    • Wang, W.; Vinocur, B.; Shoseyov, O.; Altman, A. Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response Trends Plant Sci. 2004, 9 (5) 244-252
    • (2004) Trends Plant Sci. , vol.9 , Issue.5 , pp. 244-252
    • Wang, W.1    Vinocur, B.2    Shoseyov, O.3    Altman, A.4
  • 77
    • 0017804407 scopus 로고
    • Reactions of radicals with lecithin bilayers
    • Barber, D. J. W.; Thomas, J. K. Reactions of radicals with lecithin bilayers Radiat. Res. 1978, 74, 51-65
    • (1978) Radiat. Res. , vol.74 , pp. 51-65
    • Barber, D.J.W.1    Thomas, J.K.2
  • 78
    • 84865084967 scopus 로고    scopus 로고
    • Oxidative Response and Antioxidative Mechanism in Germinating Soybean Seeds Exposed to Cadmium
    • Yang, S.; Xie, J.; Li, Q. Oxidative Response and Antioxidative Mechanism in Germinating Soybean Seeds Exposed to Cadmium Int. J. Environ. Res. Public Health 2012, 9, 2827-2838
    • (2012) Int. J. Environ. Res. Public Health , vol.9 , pp. 2827-2838
    • Yang, S.1    Xie, J.2    Li, Q.3
  • 80
    • 33845250983 scopus 로고    scopus 로고
    • Pathogenesis-related proteins. Research progress in the last 15 years
    • Edreva, A. Pathogenesis-related proteins. Research progress in the last 15 years Gen. Appl. Plant Physiol. 2005, 31, 105-124
    • (2005) Gen. Appl. Plant Physiol. , vol.31 , pp. 105-124
    • Edreva, A.1
  • 81
    • 72049107810 scopus 로고    scopus 로고
    • Comparative proteomic analysis of the short-term responses of rice roots and leaves to cadmium
    • Lee, K.; Bae, D. W.; Kim, S. H.; Han, H. J.; Liu, X.; Park, H. C.; Lim, C. O.; Lee, S. Y.; Chung, W. S. Comparative proteomic analysis of the short-term responses of rice roots and leaves to cadmium J. Plant Physiol. 2010, 167 (3) 161-168
    • (2010) J. Plant Physiol. , vol.167 , Issue.3 , pp. 161-168
    • Lee, K.1    Bae, D.W.2    Kim, S.H.3    Han, H.J.4    Liu, X.5    Park, H.C.6    Lim, C.O.7    Lee, S.Y.8    Chung, W.S.9
  • 82
    • 0034858234 scopus 로고    scopus 로고
    • High-resolution two-dimensional electrophoresis separation of proteins from metal-stressed rice (Oryza sativa L.) leaves: Drastic reductions/ fragmentation of ribulose-1,5-bisphosphate carboxylase/oxygenase and induction of stress-related proteins
    • Hajduch, M.; Rakwal, R.; Agrawal, G. K.; Yonekura, M.; Pretova, A. High-resolution two-dimensional electrophoresis separation of proteins from metal-stressed rice (Oryza sativa L.) leaves: drastic reductions/fragmentation of ribulose-1,5-bisphosphate carboxylase/oxygenase and induction of stress-related proteins Electrophoresis 2001, 22, 2824-2831
    • (2001) Electrophoresis , vol.22 , pp. 2824-2831
    • Hajduch, M.1    Rakwal, R.2    Agrawal, G.K.3    Yonekura, M.4    Pretova, A.5
  • 83
    • 79959228435 scopus 로고    scopus 로고
    • Proteomic analysis of soybean roots under aluminum stress
    • 282531
    • Duressa, D.; Soliman, K.; Taylor, R.; Senwo, Z. Proteomic analysis of soybean roots under aluminum stress Int. J. Plant Genomics 2011, 2011 (282531) 1-12
    • (2011) Int. J. Plant Genomics , vol.2011 , pp. 1-12
    • Duressa, D.1    Soliman, K.2    Taylor, R.3    Senwo, Z.4
  • 85
    • 61649110036 scopus 로고    scopus 로고
    • Is a short, sharp shock equivalent to longterm punishment? Contrasting the spatial pattern of acute and chronic ozone damage to soybean leaves via chlorophyll fluorescence imaging
    • Chen, C. P.; Frank, T. D.; Long, S. P. Is a short, sharp shock equivalent to longterm punishment? Contrasting the spatial pattern of acute and chronic ozone damage to soybean leaves via chlorophyll fluorescence imaging Plant Cell Environ. 2009, 32, 327-335
    • (2009) Plant Cell Environ. , vol.32 , pp. 327-335
    • Chen, C.P.1    Frank, T.D.2    Long, S.P.3
  • 86
    • 77955237485 scopus 로고    scopus 로고
    • Effects of chronic elevated ozone concentration on antioxidant capacity, photosynthesis and seed yield of 10 soybean cultivars
    • Betzelberger, A. M.; Gillespie, K. M.; McGrath, J. M.; Koester, R. P.; Nelson, R. L.; Ainsworth, E. A. Effects of chronic elevated ozone concentration on antioxidant capacity, photosynthesis and seed yield of 10 soybean cultivars Plant Cell Environ. 2010, 33, 1569-1581
    • (2010) Plant Cell Environ. , vol.33 , pp. 1569-1581
    • Betzelberger, A.M.1    Gillespie, K.M.2    McGrath, J.M.3    Koester, R.P.4    Nelson, R.L.5    Ainsworth, E.A.6
  • 87
    • 25444511285 scopus 로고    scopus 로고
    • Crop responses to ozone: Uptake, models of action, carbon assimilation and partitioning
    • Fiscus, E. L.; Booker, F. L.; Burkey, K. O. Crop responses to ozone: uptake, models of action, carbon assimilation and partitioning Plant Cell Environ. 2005, 28, 997-1011
    • (2005) Plant Cell Environ. , vol.28 , pp. 997-1011
    • Fiscus, E.L.1    Booker, F.L.2    Burkey, K.O.3
  • 88
    • 0033220162 scopus 로고    scopus 로고
    • Short communication: Subcellular localization of ozone-induced hydrogen peroxide production in birch (Betula pendula) leaf cells
    • Pellinen, R.; Palva, T.; Kangasjärvi, J. Short communication: subcellular localization of ozone-induced hydrogen peroxide production in birch (Betula pendula) leaf cells Plant J. 1999, 20 (3) 349-356
    • (1999) Plant J. , vol.20 , Issue.3 , pp. 349-356
    • Pellinen, R.1    Palva, T.2    Kangasjärvi, J.3
  • 89
    • 33748937740 scopus 로고    scopus 로고
    • Heme oxygenase up-regulation in ultraviolet-B irradiated soybean plants involves reactive oxygen species
    • Yannarelli, G. G.; Noriega, G. O.; Batlle, A.; Tomaro, M. L. Heme oxygenase up-regulation in ultraviolet-B irradiated soybean plants involves reactive oxygen species Planta 2006, 224, 1154-1162
    • (2006) Planta , vol.224 , pp. 1154-1162
    • Yannarelli, G.G.1    Noriega, G.O.2    Batlle, A.3    Tomaro, M.L.4
  • 90
    • 0035112262 scopus 로고    scopus 로고
    • Effect of solar ultraviolet-B radiation during springtime ozone depletion on photosynthesis and biomass production of Antarctic vascular plants
    • Xiong, F. S.; Day, T. A. Effect of solar ultraviolet-B radiation during springtime ozone depletion on photosynthesis and biomass production of Antarctic vascular plants Plant Physiol. 2001, 125, 738-751
    • (2001) Plant Physiol. , vol.125 , pp. 738-751
    • Xiong, F.S.1    Day, T.A.2
  • 91
    • 0031401513 scopus 로고    scopus 로고
    • Evidence that heat and ultraviolet radiation activate a common stress-response program in plants that is altered in the uvh6 mutant of Arabidopsis thaliana
    • Jenkins, M. E.; Suzuki, T. C.; Mount, D. W. Evidence that heat and ultraviolet radiation activate a common stress-response program in plants that is altered in the uvh6 mutant of Arabidopsis thaliana Plant Physiol. 1997, 115 (4) 1351-1358
    • (1997) Plant Physiol. , vol.115 , Issue.4 , pp. 1351-1358
    • Jenkins, M.E.1    Suzuki, T.C.2    Mount, D.W.3
  • 92
    • 0034879874 scopus 로고    scopus 로고
    • Heat-shock responses in two leguminous plants: A comparative study
    • Ortiz, C.; Cardemil, L. Heat-shock responses in two leguminous plants: a comparative study J. Exp. Bot. 2001, 52, 1711-1719
    • (2001) J. Exp. Bot. , vol.52 , pp. 1711-1719
    • Ortiz, C.1    Cardemil, L.2
  • 93
    • 34548461256 scopus 로고    scopus 로고
    • Subcellular shotgun proteomics in plants: Looking beyond the usual suspects
    • Haynes, P. A.; Roberts, T. H. Subcellular shotgun proteomics in plants: looking beyond the usual suspects Proteomics 2007, 7 (16) 2963-2975
    • (2007) Proteomics , vol.7 , Issue.16 , pp. 2963-2975
    • Haynes, P.A.1    Roberts, T.H.2
  • 94
    • 31344434715 scopus 로고    scopus 로고
    • Host cell factor and an uncharacterized SANT domain protein are stable components of ATAC, a novel dAda2A/ dGcn5-containing histone acetyltransferase complex in Drosophila
    • Guelman, S.; Suganuma, T.; Florens, L.; Swanson, S. K. Host cell factor and an uncharacterized SANT domain protein are stable components of ATAC, a novel dAda2A/ dGcn5-containing histone acetyltransferase complex in Drosophila Mol. Cell. Biol. 2006, 26, 871-882
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 871-882
    • Guelman, S.1    Suganuma, T.2    Florens, L.3    Swanson, S.K.4
  • 95
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu, C. C.; MacCoss, M. J.; Howell, K. E.; Yates, J. R. A method for the comprehensive proteomic analysis of membrane proteins Nat. Biotechnol. 2003, 21, 532-538
    • (2003) Nat. Biotechnol. , vol.21 , pp. 532-538
    • Wu, C.C.1    Maccoss, M.J.2    Howell, K.E.3    Yates, J.R.4
  • 96
    • 33750117539 scopus 로고    scopus 로고
    • Analysis of the defence phosphoproteome of Arabidopsis thaliana using differential mass tagging
    • Jones, A. M.; Bennett, M. H.; Mansfield, J. W.; Grant, M. Analysis of the defence phosphoproteome of Arabidopsis thaliana using differential mass tagging Proteomics 2006, 6, 4155-4165
    • (2006) Proteomics , vol.6 , pp. 4155-4165
    • Jones, A.M.1    Bennett, M.H.2    Mansfield, J.W.3    Grant, M.4
  • 97
    • 79958135365 scopus 로고    scopus 로고
    • Quantitative proteomic analyses of crop seedlings subjected to stress conditions; A commentary
    • Nanjo, Y.; Nouri, M. Z.; Komatsu, S. Quantitative proteomic analyses of crop seedlings subjected to stress conditions; a commentary Phytochemistry 2011, 72 (10) 1263-1272
    • (2011) Phytochemistry , vol.72 , Issue.10 , pp. 1263-1272
    • Nanjo, Y.1    Nouri, M.Z.2    Komatsu, S.3
  • 98
    • 77955459998 scopus 로고    scopus 로고
    • Comparative proteome analysis of early-stage soybean seedlings responses to flooding by using gel and gel-free techniques
    • Nanjo, Y.; Skultety, L.; Ashraf, Y.; Komatsu, S. Comparative proteome analysis of early-stage soybean seedlings responses to flooding by using gel and gel-free techniques J. Proteome Res. 2010, 9, 3989-4002
    • (2010) J. Proteome Res. , vol.9 , pp. 3989-4002
    • Nanjo, Y.1    Skultety, L.2    Ashraf, Y.3    Komatsu, S.4
  • 99
    • 60249091270 scopus 로고    scopus 로고
    • Establishment of a protein reference map for soybean root hair cells
    • Brechenmacher, L.; Lee, J.; Sachdev, S.; Song, Z.; Nguyen, T. H. Establishment of a protein reference map for soybean root hair cells Plant Physiol. 2009, 149 (2) 670-682
    • (2009) Plant Physiol. , vol.149 , Issue.2 , pp. 670-682
    • Brechenmacher, L.1    Lee, J.2    Sachdev, S.3    Song, Z.4    Nguyen, T.H.5
  • 100
    • 84855565348 scopus 로고    scopus 로고
    • Shotgun proteomic analysis of long-distance drought signaling in rice roots
    • Mirzaei, M.; Soltani, N.; Sarhadi, E.; Pascovici, D.; Keighley, T. Shotgun proteomic analysis of long-distance drought signaling in rice roots J. Proteome Res. 2012, 11 (1) 348-358
    • (2012) J. Proteome Res. , vol.11 , Issue.1 , pp. 348-358
    • Mirzaei, M.1    Soltani, N.2    Sarhadi, E.3    Pascovici, D.4    Keighley, T.5
  • 101
    • 0038523728 scopus 로고    scopus 로고
    • Genetic modification removes an immunodominant allergen from soybean
    • Herman, E. M.; Helm, R. M.; Jung, R.; Kinney, A. J. Genetic modification removes an immunodominant allergen from soybean Plant Physiol. 2003, 132, 36-43
    • (2003) Plant Physiol. , vol.132 , pp. 36-43
    • Herman, E.M.1    Helm, R.M.2    Jung, R.3    Kinney, A.J.4
  • 102
    • 48649107513 scopus 로고    scopus 로고
    • The effect of DTT in protein preparations for proteomic analysis: Removal of a highly abundant plant enzyme, ribulose bisphosphate carboxylase/oxygenase
    • Cho, J.-H.; Hwang, H.; Cho, M.-H.; Kwon, Y.-K.; Jeon, J.-S.; Bhoo, S. H.; Hahn, T.-R. The effect of DTT in protein preparations for proteomic analysis: removal of a highly abundant plant enzyme, ribulose bisphosphate carboxylase/oxygenase J. Plant Biol. 2008, 51, 297-301
    • (2008) J. Plant Biol. , vol.51 , pp. 297-301
    • Cho, J.-H.1    Hwang, H.2    Cho, M.-H.3    Kwon, Y.-K.4    Jeon, J.-S.5    Bhoo, S.H.6    Hahn, T.-R.7
  • 103
    • 59449111124 scopus 로고    scopus 로고
    • Combining subproteome enrichment and Rubisco depletion enables identification of low abundance proteins differentially regulated during plant defense
    • Widjaja, I.; Naumann, K.; Roth, U.; Wolf, N.; Mackey, D.; Dangl, J. L.; Scheel, D.; Lee, J. Combining subproteome enrichment and Rubisco depletion enables identification of low abundance proteins differentially regulated during plant defense Proteomics 2009, 9 (1) 138-147
    • (2009) Proteomics , vol.9 , Issue.1 , pp. 138-147
    • Widjaja, I.1    Naumann, K.2    Roth, U.3    Wolf, N.4    Mackey, D.5    Dangl, J.L.6    Scheel, D.7    Lee, J.8
  • 104
    • 70549101152 scopus 로고    scopus 로고
    • A rapid method for depletion of Rubisco from soybean (Glycine max) leaf for proteomic analysis of lower abundance proteins
    • Krishnan, H. B.; Natarajan, S. S. A rapid method for depletion of Rubisco from soybean (Glycine max) leaf for proteomic analysis of lower abundance proteins Phytochemistry 2009, 70 (17-18) 1958-1964
    • (2009) Phytochemistry , vol.70 , Issue.1718 , pp. 1958-1964
    • Krishnan, H.B.1    Natarajan, S.S.2
  • 106
    • 34248228084 scopus 로고    scopus 로고
    • Proteomic analysis of rice seedlings during cold stress
    • Hashimoto, M.; Komatsu, S. Proteomic analysis of rice seedlings during cold stress Proteomics 2007, 7 (8) 1293-1302
    • (2007) Proteomics , vol.7 , Issue.8 , pp. 1293-1302
    • Hashimoto, M.1    Komatsu, S.2
  • 107
    • 84872280883 scopus 로고    scopus 로고
    • An improved plant leaf protein extraction method for high resolution two-dimensional polyacrylamide gel electrophoresis and comparative proteomics
    • Alam, I.; Sharmin, S.; Kim, K. H.; Kim, Y. G.; Lee, J.; Lee, B. H. An improved plant leaf protein extraction method for high resolution two-dimensional polyacrylamide gel electrophoresis and comparative proteomics Biotech. Histochem. 2013, 88, 61-75
    • (2013) Biotech. Histochem. , vol.88 , pp. 61-75
    • Alam, I.1    Sharmin, S.2    Kim, K.H.3    Kim, Y.G.4    Lee, J.5    Lee, B.H.6
  • 108
    • 84861990380 scopus 로고    scopus 로고
    • Selected reaction monitoring-based proteomics: Workflows, potential, pitfalls and future directions
    • Picotti, P.; Aebersold, R. Selected reaction monitoring-based proteomics: workflows, potential, pitfalls and future directions Nat. Methods 2012, 9 (6) 555-566
    • (2012) Nat. Methods , vol.9 , Issue.6 , pp. 555-566
    • Picotti, P.1    Aebersold, R.2
  • 109
    • 84864356128 scopus 로고    scopus 로고
    • Acyl chains of phospholipase D transphosphatidylation products in Arabidopsis cells: A study using multiple reaction monitoring mass spectrometry
    • Rainteau, D.; Humbert, L.; Delage, E.; Vergnolle, C.; Cantrel, C. Acyl chains of phospholipase D transphosphatidylation products in Arabidopsis cells: a study using multiple reaction monitoring mass spectrometry PLoS One 2012, 7, e41985
    • (2012) PLoS One , vol.7 , pp. 41985
    • Rainteau, D.1    Humbert, L.2    Delage, E.3    Vergnolle, C.4    Cantrel, C.5
  • 110
  • 111
    • 79551490355 scopus 로고    scopus 로고
    • Lights and shadows of proteomic technologies for the study of protein species including isoforms, splicing variants and protein post-translational modifications
    • Casado-Vela, J.; Cebrián, A.; Gómez del Pulgar, M. T.; Sánchez-López, E.; Vilaseca, M. Lights and shadows of proteomic technologies for the study of protein species including isoforms, splicing variants and protein post-translational modifications Proteomics 2011, 11 (4) 590-603
    • (2011) Proteomics , vol.11 , Issue.4 , pp. 590-603
    • Casado-Vela, J.1    Cebrián, A.2    Gómez Del Pulgar, M.T.3    Sánchez-López, E.4    Vilaseca, M.5


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