메뉴 건너뛰기




Volumn 193-194, Issue , 2012, Pages 120-129

Comparative proteomic study between tuberous roots of light orange- and purple-fleshed sweetpotato cultivars

Author keywords

Comparative proteomics; Light orange fleshed cultivar; Purple fleshed cultivar; Sweetpotato; Tuberous root

Indexed keywords

PIGMENT; VEGETABLE PROTEIN;

EID: 84862988280     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2012.06.003     Document Type: Article
Times cited : (30)

References (64)
  • 1
    • 66549117021 scopus 로고    scopus 로고
    • Characterization of full-length enriched expressed sequence tags of dehydration-treated white fibrous roots of sweetpotato
    • Kim S.H., Song W.K., Kim Y.H., Kwon S.Y., Lee H.S., Lee I.C., Kwak S.S. Characterization of full-length enriched expressed sequence tags of dehydration-treated white fibrous roots of sweetpotato. BMB Reports 2009, 42:271-276.
    • (2009) BMB Reports , vol.42 , pp. 271-276
    • Kim, S.H.1    Song, W.K.2    Kim, Y.H.3    Kwon, S.Y.4    Lee, H.S.5    Lee, I.C.6    Kwak, S.S.7
  • 2
    • 34047103986 scopus 로고    scopus 로고
    • Sweetpotato: a review of its past, present, and future role in human nutrition
    • Bovell-Benjamin A.C. Sweetpotato: a review of its past, present, and future role in human nutrition. Advances in Food and Nutrition Research 2007, 52:1-59.
    • (2007) Advances in Food and Nutrition Research , vol.52 , pp. 1-59
    • Bovell-Benjamin, A.C.1
  • 3
    • 33645094371 scopus 로고    scopus 로고
    • The cassava (Manihot esculenta Crantz) root proteome: protein identification and differential expression
    • Sheffield J., Taylor N., Fauquet C., Chen S. The cassava (Manihot esculenta Crantz) root proteome: protein identification and differential expression. Proteomics 2006, 6:1588-1598.
    • (2006) Proteomics , vol.6 , pp. 1588-1598
    • Sheffield, J.1    Taylor, N.2    Fauquet, C.3    Chen, S.4
  • 4
    • 55249117526 scopus 로고    scopus 로고
    • Comparative proteomics of tuber induction, development and maturation reveal the complexity of tuberization tuberization process in potato (Solanum tuberosum L.)
    • Agrawal L., Chakraborty S., Jaiswal D.K., Gupta S., Datta A., Chakraborty N. Comparative proteomics of tuber induction, development and maturation reveal the complexity of tuberization tuberization process in potato (Solanum tuberosum L.). Journal of Proteome Research 2008, 7:3803-3817.
    • (2008) Journal of Proteome Research , vol.7 , pp. 3803-3817
    • Agrawal, L.1    Chakraborty, S.2    Jaiswal, D.K.3    Gupta, S.4    Datta, A.5    Chakraborty, N.6
  • 6
    • 84855206976 scopus 로고    scopus 로고
    • Analysis of natural variation of the potato tuber proteome reveals novel candidate genes for tuber bruising
    • Urbany C., Colby T., Stich B., Schmidt L., Schmidt J., Gebhardt C. Analysis of natural variation of the potato tuber proteome reveals novel candidate genes for tuber bruising. Journal of Proteome Research 2012, 11:703-716.
    • (2012) Journal of Proteome Research , vol.11 , pp. 703-716
    • Urbany, C.1    Colby, T.2    Stich, B.3    Schmidt, L.4    Schmidt, J.5    Gebhardt, C.6
  • 8
    • 33750588336 scopus 로고    scopus 로고
    • Advances in plant proteomics
    • Chen S., Harmon A.C. Advances in plant proteomics. Proteomics 2006, 6:5504-5516.
    • (2006) Proteomics , vol.6 , pp. 5504-5516
    • Chen, S.1    Harmon, A.C.2
  • 9
    • 33644848361 scopus 로고    scopus 로고
    • Rice proteomics: a cornerstone for cereal food crop proteomes
    • Agrawal G.K., Rakwal R. Rice proteomics: a cornerstone for cereal food crop proteomes. Mass Spectrometry Reviews 2006, 25:1-53.
    • (2006) Mass Spectrometry Reviews , vol.25 , pp. 1-53
    • Agrawal, G.K.1    Rakwal, R.2
  • 10
    • 0036325578 scopus 로고    scopus 로고
    • Involvement of anthocyanins and other phenolic compounds in radical-scavenging activity of purple-fleshed sweetpotato cultivars
    • Oki T., Masuda M., Furuta S., Nishiba Y., Terahara N., Suda I. Involvement of anthocyanins and other phenolic compounds in radical-scavenging activity of purple-fleshed sweetpotato cultivars. Journal of Food Science 2002, 67:1752-1756.
    • (2002) Journal of Food Science , vol.67 , pp. 1752-1756
    • Oki, T.1    Masuda, M.2    Furuta, S.3    Nishiba, Y.4    Terahara, N.5    Suda, I.6
  • 11
    • 34250663876 scopus 로고    scopus 로고
    • Isolation of a regulatory gene of anthocyanin biosynthesis in tuberous roots of purple-fleshed sweetpotato
    • Mano H., Ogasawara F., Sato K., Higo H., Minobe Y. Isolation of a regulatory gene of anthocyanin biosynthesis in tuberous roots of purple-fleshed sweetpotato. Plant Physiology 2007, 143:1252-1268.
    • (2007) Plant Physiology , vol.143 , pp. 1252-1268
    • Mano, H.1    Ogasawara, F.2    Sato, K.3    Higo, H.4    Minobe, Y.5
  • 12
    • 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 Physiology 1986, 81:802-806.
    • (1986) Plant Physiology , vol.81 , pp. 802-806
    • Hurkman, W.J.1    Tanaka, C.K.2
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976, 72:248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 14
  • 15
    • 34948843692 scopus 로고    scopus 로고
    • A proteomic approach in analyzing heat-responsive proteins in rice leaves
    • Lee D.G., Ahsan N., Lee S.H., Kang K.Y., Back J.D., Lee I.J., Lee B.H. A proteomic approach in analyzing heat-responsive proteins in rice leaves. Proteomics 2007, 7:3369-3383.
    • (2007) Proteomics , vol.7 , pp. 3369-3383
    • Lee, D.G.1    Ahsan, N.2    Lee, S.H.3    Kang, K.Y.4    Back, J.D.5    Lee, I.J.6    Lee, B.H.7
  • 17
    • 13244258357 scopus 로고    scopus 로고
    • Proteomic analysis of salt stress-responsive protein in rice roots
    • Yan S., Tang Z., Su W., Sun W. Proteomic analysis of salt stress-responsive protein in rice roots. Proteomics 2005, 5:235-244.
    • (2005) Proteomics , vol.5 , pp. 235-244
    • Yan, S.1    Tang, Z.2    Su, W.3    Sun, W.4
  • 20
    • 0001139394 scopus 로고
    • Effects of acifluorfen on endogenous antioxidants and protective enzymes in cucumber (Cucumis sativus L.) cotyledons
    • Kenyon W.H., Duke S.O. Effects of acifluorfen on endogenous antioxidants and protective enzymes in cucumber (Cucumis sativus L.) cotyledons. Plant Physiology 1985, 79:862-866.
    • (1985) Plant Physiology , vol.79 , pp. 862-866
    • Kenyon, W.H.1    Duke, S.O.2
  • 21
    • 7344235754 scopus 로고
    • Developmental effects of Sandoz 6706 on activities of enzymes of phenolic acid general metabolism in barley shoots grown in the dark or under low or high intensity light
    • Blume D.E., McClure J.W. Developmental effects of Sandoz 6706 on activities of enzymes of phenolic acid general metabolism in barley shoots grown in the dark or under low or high intensity light. Plant Physiology 1980, 65:238-244.
    • (1980) Plant Physiology , vol.65 , pp. 238-244
    • Blume, D.E.1    McClure, J.W.2
  • 22
    • 0001662170 scopus 로고
    • Ascorbate free radical reductase, a key enzyme of the ascorbic acid system
    • Arrigoni O., Dipierro S., Borraccino G. Ascorbate free radical reductase, a key enzyme of the ascorbic acid system. FEBS Letters 1981, 125:242-244.
    • (1981) FEBS Letters , vol.125 , pp. 242-244
    • Arrigoni, O.1    Dipierro, S.2    Borraccino, G.3
  • 24
    • 0036708430 scopus 로고    scopus 로고
    • Localization and physiological implication of aldose reductase and sorbitol dehydrogenase in reproductive tracts and spermatozoa of male rats
    • Kobayshi T., Kaneko T., Iuchi Y., Matsuki S., Takahashi M., Sasagawa I., Nakada T., Fujii J. Localization and physiological implication of aldose reductase and sorbitol dehydrogenase in reproductive tracts and spermatozoa of male rats. Journal of Andrology 2002, 23:674-683.
    • (2002) Journal of Andrology , vol.23 , pp. 674-683
    • Kobayshi, T.1    Kaneko, T.2    Iuchi, Y.3    Matsuki, S.4    Takahashi, M.5    Sasagawa, I.6    Nakada, T.7    Fujii, J.8
  • 25
    • 0002629092 scopus 로고
    • A technique for screening peanut for resistance to Meloidogyne arenaria
    • Holbrook C.C., Knauft D.A., Dickson D.W. A technique for screening peanut for resistance to Meloidogyne arenaria. Plant Disease 1983, 57:957-958.
    • (1983) Plant Disease , vol.57 , pp. 957-958
    • Holbrook, C.C.1    Knauft, D.A.2    Dickson, D.W.3
  • 26
  • 28
    • 33845603029 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the polyphenol oxidase gene from sweetpotato
    • Liao Z., Chen R., Chen M., Yang Y., Fu Y., Zhang Q., Lan X. Molecular cloning and characterization of the polyphenol oxidase gene from sweetpotato. Molecular Biology 2006, 40:907-913.
    • (2006) Molecular Biology , vol.40 , pp. 907-913
    • Liao, Z.1    Chen, R.2    Chen, M.3    Yang, Y.4    Fu, Y.5    Zhang, Q.6    Lan, X.7
  • 29
    • 51249105120 scopus 로고    scopus 로고
    • Proteome changes in the skin of the grape cultivar Barbera among different stages of ripening
    • Negri A.S., Prinsi B., Rossoni M., Failla O., Scienza A., Cocucci M., Espen L. Proteome changes in the skin of the grape cultivar Barbera among different stages of ripening. BMC Genomics 2008, 9:378-396.
    • (2008) BMC Genomics , vol.9 , pp. 378-396
    • Negri, A.S.1    Prinsi, B.2    Rossoni, M.3    Failla, O.4    Scienza, A.5    Cocucci, M.6    Espen, L.7
  • 30
    • 29244469942 scopus 로고    scopus 로고
    • Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-Co A decarboxylase by adenosine diphosphate
    • Berthold C.L., Moussatche P., Richards N.G.J., Lindqvist Y. Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-Co A decarboxylase by adenosine diphosphate. Journal of Biological Chemistry 2005, 280:41645-41654.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 41645-41654
    • Berthold, C.L.1    Moussatche, P.2    Richards, N.G.J.3    Lindqvist, Y.4
  • 31
    • 5144229754 scopus 로고    scopus 로고
    • Recent developments in understanding the regulation of starch metabolism in higher plants
    • Tetlow I.J., Morell M.K., Emes M.J. Recent developments in understanding the regulation of starch metabolism in higher plants. Journal of Experimental Botany 2004, 55:2131-2145.
    • (2004) Journal of Experimental Botany , vol.55 , pp. 2131-2145
    • Tetlow, I.J.1    Morell, M.K.2    Emes, M.J.3
  • 32
    • 0033047006 scopus 로고    scopus 로고
    • Structure of aspartate-β-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis
    • Hadfield A., Kryger G., Ouyang J., Petsko G.A., Ringe D., Viola R. Structure of aspartate-β-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis. Journal of Molecular Biology 1999, 289:991-1002.
    • (1999) Journal of Molecular Biology , vol.289 , pp. 991-1002
    • Hadfield, A.1    Kryger, G.2    Ouyang, J.3    Petsko, G.A.4    Ringe, D.5    Viola, R.6
  • 33
    • 0035807937 scopus 로고    scopus 로고
    • Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase
    • Hadfield A., Shammas C., Kryger G., Ringe D., Petsko G.A., Ouyang J., Viola R.E. Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase. Biochemistry 2001, 40:14475-14483.
    • (2001) Biochemistry , vol.40 , pp. 14475-14483
    • Hadfield, A.1    Shammas, C.2    Kryger, G.3    Ringe, D.4    Petsko, G.A.5    Ouyang, J.6    Viola, R.E.7
  • 34
    • 33846455426 scopus 로고    scopus 로고
    • Protein disulfide isomerase family proteins involved in soybean protein biogenesis
    • Wadahama H., Kamauchi S., Ishimoto M., Kawada T., Urade R. Protein disulfide isomerase family proteins involved in soybean protein biogenesis. The FEBS Journal 2007, 274:687-703.
    • (2007) The FEBS Journal , vol.274 , pp. 687-703
    • Wadahama, H.1    Kamauchi, S.2    Ishimoto, M.3    Kawada, T.4    Urade, R.5
  • 37
    • 3042527700 scopus 로고    scopus 로고
    • Differential expression of 10 sweetpotato peroxidase genes in reponse to bacterial pathogen, Pectobacterium chrysanthemi
    • Jang I.C., Park S.Y., Kim K.Y., Kwon S.Y., Kim G.K., Kwak S.S. Differential expression of 10 sweetpotato peroxidase genes in reponse to bacterial pathogen, Pectobacterium chrysanthemi. Plant Physiology and Biochemistry 2004, 42:451-455.
    • (2004) Plant Physiology and Biochemistry , vol.42 , pp. 451-455
    • Jang, I.C.1    Park, S.Y.2    Kim, K.Y.3    Kwon, S.Y.4    Kim, G.K.5    Kwak, S.S.6
  • 38
    • 0028254268 scopus 로고
    • The physiology and molecular biology of plant 1,3-β-d-glucanases and 1,3;1,4-β-d-glucanases
    • Simmons C.R. The physiology and molecular biology of plant 1,3-β-d-glucanases and 1,3;1,4-β-d-glucanases. Critical Reviews in Plant Sciences 1994, 13:325-387.
    • (1994) Critical Reviews in Plant Sciences , vol.13 , pp. 325-387
    • Simmons, C.R.1
  • 48
    • 23644437138 scopus 로고    scopus 로고
    • Peroxidases have more functions than a swiss army knife
    • Passardi F., Cosio C., Penel C., Dunand C. Peroxidases have more functions than a swiss army knife. Plant Cell Reports 2005, 24:255-265.
    • (2005) Plant Cell Reports , vol.24 , pp. 255-265
    • Passardi, F.1    Cosio, C.2    Penel, C.3    Dunand, C.4
  • 49
    • 0030876351 scopus 로고    scopus 로고
    • A new nomenclature for the aldo-keto reductase superfamily
    • Zet J.M., Flynn T.G., Penning T.M. A new nomenclature for the aldo-keto reductase superfamily. Biochemical Pharmacology 1997, 54:639-647.
    • (1997) Biochemical Pharmacology , vol.54 , pp. 639-647
    • Zet, J.M.1    Flynn, T.G.2    Penning, T.M.3
  • 50
    • 0034541782 scopus 로고    scopus 로고
    • A novel aldose/aldehyde reductase protects transgenic plants against lipid peroxidation under chemical and drought stresses
    • Oberschall A., Deak M., Török K., Sass L., Vass I., Kovács I., Fehér A., Dudits D., Horváth G.V. A novel aldose/aldehyde reductase protects transgenic plants against lipid peroxidation under chemical and drought stresses. Plant Journal 2000, 24:437-446.
    • (2000) Plant Journal , vol.24 , pp. 437-446
    • Oberschall, A.1    Deak, M.2    Török, K.3    Sass, L.4    Vass, I.5    Kovács, I.6    Fehér, A.7    Dudits, D.8    Horváth, G.V.9
  • 51
    • 24044525249 scopus 로고    scopus 로고
    • Structural elucidation of chalcone reductase and implications for deoxychalcone biosynthesis
    • Bomati E.K., Austin M.B., Bowman M.E., Dixon R.A., Noel J.P. Structural elucidation of chalcone reductase and implications for deoxychalcone biosynthesis. Journal of Biological Chemistry 2005, 280:30496-30503.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 30496-30503
    • Bomati, E.K.1    Austin, M.B.2    Bowman, M.E.3    Dixon, R.A.4    Noel, J.P.5
  • 53
    • 0001903928 scopus 로고    scopus 로고
    • Environmental significance of anthocyanins in plant stress responses
    • Chalker-Scott L. Environmental significance of anthocyanins in plant stress responses. Photochemistry and Photobiology 1999, 70:1-9.
    • (1999) Photochemistry and Photobiology , vol.70 , pp. 1-9
    • Chalker-Scott, L.1
  • 54
    • 0036011081 scopus 로고    scopus 로고
    • Biosynthesis of flavonoids and effects of stress
    • Winkel-Shirley B. Biosynthesis of flavonoids and effects of stress. Current Opinion in Plant Biology 2002, 5:218-223.
    • (2002) Current Opinion in Plant Biology , vol.5 , pp. 218-223
    • Winkel-Shirley, B.1
  • 56
    • 0031081795 scopus 로고    scopus 로고
    • Functional activity of sporamin from sweetpotato (Ipomoea batatas Lim.): a tuber storage protein with trypsin inhibitory activity
    • Yeh K.W., Chen J.C., Lin M.I., Chen Y.M., Lin C.Y. Functional activity of sporamin from sweetpotato (Ipomoea batatas Lim.): a tuber storage protein with trypsin inhibitory activity. Plant Molecular Biology 1997, 33:565-570.
    • (1997) Plant Molecular Biology , vol.33 , pp. 565-570
    • Yeh, K.W.1    Chen, J.C.2    Lin, M.I.3    Chen, Y.M.4    Lin, C.Y.5
  • 57
    • 0000445548 scopus 로고
    • Characterization of major proteins in sweetpotato tuberous roots
    • Maeshima M., Sasaki T., Asahi T. Characterization of major proteins in sweetpotato tuberous roots. Phytochemistry 1985, 24:1899-1902.
    • (1985) Phytochemistry , vol.24 , pp. 1899-1902
    • Maeshima, M.1    Sasaki, T.2    Asahi, T.3
  • 58
    • 0030750613 scopus 로고    scopus 로고
    • Sweetpotato (Ipomoea batatas) trypsin inhibitors expressed in transgenic tobacco plants confer resistance against Spodoptera litura
    • Yeh K.W., Lin M.I., Tuan S.J., Chen Y.M., Lin C.Y., Kao S.S. Sweetpotato (Ipomoea batatas) trypsin inhibitors expressed in transgenic tobacco plants confer resistance against Spodoptera litura. Plant Cell Reports 1997, 16:696-699.
    • (1997) Plant Cell Reports , vol.16 , pp. 696-699
    • Yeh, K.W.1    Lin, M.I.2    Tuan, S.J.3    Chen, Y.M.4    Lin, C.Y.5    Kao, S.S.6
  • 60
    • 0038057913 scopus 로고    scopus 로고
    • Sporamin-mediated resistance to beet cyst nematodes (Heterodera schachtii Schm.) is dependent on trypsin inhibitory activity in sugar beet (Beta vulgaris L.) hairy roots
    • Cai D., Thurau T., Tian Y., Lange T., Yeh K.W., Jung C. Sporamin-mediated resistance to beet cyst nematodes (Heterodera schachtii Schm.) is dependent on trypsin inhibitory activity in sugar beet (Beta vulgaris L.) hairy roots. Plant Molecular Biology 2003, 51:839-849.
    • (2003) Plant Molecular Biology , vol.51 , pp. 839-849
    • Cai, D.1    Thurau, T.2    Tian, Y.3    Lange, T.4    Yeh, K.W.5    Jung, C.6
  • 61
    • 23244451433 scopus 로고    scopus 로고
    • Isolation and expression of protein disulfide isomerase cDNA from sweetpotato (Ipomoea batatus [L.] Lam 'Tainong 57') storage roots
    • Haung D.J., Chen H.J., Lin Y.H. Isolation and expression of protein disulfide isomerase cDNA from sweetpotato (Ipomoea batatus [L.] Lam 'Tainong 57') storage roots. Plant Science 2005, 169:776-784.
    • (2005) Plant Science , vol.169 , pp. 776-784
    • Haung, D.J.1    Chen, H.J.2    Lin, Y.H.3
  • 62
    • 0030895921 scopus 로고    scopus 로고
    • A comparison of selected mRNA and protein abundances in human liver
    • Anderson L., Seilhamer J. A comparison of selected mRNA and protein abundances in human liver. Electrophoresis 1997, 18:533-537.
    • (1997) Electrophoresis , vol.18 , pp. 533-537
    • Anderson, L.1    Seilhamer, J.2
  • 64
    • 84862868321 scopus 로고    scopus 로고
    • De novo sequencing and a comprehensive analysis of purple sweet potato (Impomoea batatas L.) transcriptome, Planta. doi:10.1007/s00425-012-1591-4
    • F. Xie, C.E. Burklew, Y. Yang, M. Liu, P. Xiao, B. Zhang, D. Qiu, De novo sequencing and a comprehensive analysis of purple sweet potato (Impomoea batatas L.) transcriptome, Planta, 2012, doi:10.1007/s00425-012-1591-4.
    • (2012)
    • Xie, F.1    Burklew, C.E.2    Yang, Y.3    Liu, M.4    Xiao, P.5    Zhang, B.6    Qiu, D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.