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Volumn 12, Issue 1, 2014, Pages

Maize IgE binding proteins: Each plant a different profile?

Author keywords

2D gel electrophoresis; Maize allergens; Maize proteins; Western blot

Indexed keywords

ALBUMIN; ALLERGEN; BINDING PROTEIN; GLOBULIN; IMMUNOGLOBULIN E; IMMUNOGLOBULIN E BINDING PROTEIN; PROTEOME; UNCLASSIFIED DRUG;

EID: 84899078969     PISSN: None     EISSN: 14775956     Source Type: Journal    
DOI: 10.1186/1477-5956-12-17     Document Type: Article
Times cited : (14)

References (46)
  • 2
    • 68949155552 scopus 로고    scopus 로고
    • Maize food allergy: lipid-transfer proteins, endochitinases, and alpha-zein precursor are relevant maize allergens in double-blind placebo-controlled maize-challenge-positive patients
    • 10.1007/s00216-009-2945-z, 19669736
    • Pastorello EA, Farioli L, Pravettoni V, Scibilia J, Conti A, Fortunato D, Borgonovo L, Bonomi S, Primavesi L, Ballmer-Weber B. Maize food allergy: lipid-transfer proteins, endochitinases, and alpha-zein precursor are relevant maize allergens in double-blind placebo-controlled maize-challenge-positive patients. Anal Bioanal Chem 2009, 395:93-102. 10.1007/s00216-009-2945-z, 19669736.
    • (2009) Anal Bioanal Chem , vol.395 , pp. 93-102
    • Pastorello, E.A.1    Farioli, L.2    Pravettoni, V.3    Scibilia, J.4    Conti, A.5    Fortunato, D.6    Borgonovo, L.7    Bonomi, S.8    Primavesi, L.9    Ballmer-Weber, B.10
  • 4
    • 84858748677 scopus 로고    scopus 로고
    • Characterization of maize allergens - MON810 vs. its non-transgenic counterpart
    • 10.1016/j.jprot.2012.01.005, 22270010
    • Fonseca C, Planchon S, Renaut J, Oliveira MM, Batista R. Characterization of maize allergens - MON810 vs. its non-transgenic counterpart. J Proteomics 2012, 75:2027-2037. 10.1016/j.jprot.2012.01.005, 22270010.
    • (2012) J Proteomics , vol.75 , pp. 2027-2037
    • Fonseca, C.1    Planchon, S.2    Renaut, J.3    Oliveira, M.M.4    Batista, R.5
  • 5
    • 47749091255 scopus 로고    scopus 로고
    • Proteomics analysis of mature seed of four peanut cultivars using two-dimensional gel electrophoresis reveals distinct differential expression of storage, anti-nutritional, and allergenic proteins
    • Kottapalli KR, Payton P, Rakwal R, Agrawal GK, Shibato J, Burow M, Puppala N. Proteomics analysis of mature seed of four peanut cultivars using two-dimensional gel electrophoresis reveals distinct differential expression of storage, anti-nutritional, and allergenic proteins. Plant Sci 2008, 175:321-329.
    • (2008) Plant Sci , vol.175 , pp. 321-329
    • Kottapalli, K.R.1    Payton, P.2    Rakwal, R.3    Agrawal, G.K.4    Shibato, J.5    Burow, M.6    Puppala, N.7
  • 6
    • 35148838143 scopus 로고    scopus 로고
    • Proteomic analysis of the distribution of the major seed allergens in wild, landrace, ancestral, and modern soybean genotypes
    • Xu C, Caperna TJ, Garrett WM, Cregan P, Bae H, Luthria DL, Natarajan S. Proteomic analysis of the distribution of the major seed allergens in wild, landrace, ancestral, and modern soybean genotypes. J Sci Food Agric 2007, 87:2511-2518.
    • (2007) J Sci Food Agric , vol.87 , pp. 2511-2518
    • Xu, C.1    Caperna, T.J.2    Garrett, W.M.3    Cregan, P.4    Bae, H.5    Luthria, D.L.6    Natarajan, S.7
  • 8
    • 84872416161 scopus 로고    scopus 로고
    • Challenges in testing genetically modified crops for potential increases in endogenous allergen expression for safety
    • 10.1111/all.12076, 23205714
    • Panda R, Ariyarathna H, Amnuaycheewa P, Tetteh A, Pramod SN, Taylor SL, Ballmer-Weber BK, Goodman RE. Challenges in testing genetically modified crops for potential increases in endogenous allergen expression for safety. Allergy 2013, 68:142-151. 10.1111/all.12076, 23205714.
    • (2013) Allergy , vol.68 , pp. 142-151
    • Panda, R.1    Ariyarathna, H.2    Amnuaycheewa, P.3    Tetteh, A.4    Pramod, S.N.5    Taylor, S.L.6    Ballmer-Weber, B.K.7    Goodman, R.E.8
  • 9
    • 72449124198 scopus 로고    scopus 로고
    • Apple (Malus domestica L. Borkh.) allergen Mal d 1: effect of cultivar, cultivation system, and storage conditions
    • 10.1021/jf901938q, 19845340
    • Matthes A, Schmitz-Eiberger M. Apple (Malus domestica L. Borkh.) allergen Mal d 1: effect of cultivar, cultivation system, and storage conditions. J Agric Food Chem 2009, 57:10548-10553. 10.1021/jf901938q, 19845340.
    • (2009) J Agric Food Chem , vol.57 , pp. 10548-10553
    • Matthes, A.1    Schmitz-Eiberger, M.2
  • 10
    • 43549101122 scopus 로고    scopus 로고
    • Staining efficiency of specific proteins depends on the staining method: wheat gluten proteins
    • 10.1002/pmic.200700956, 18398878
    • Van den Broeck HC, America AHP, Smulders MJM, Gilissen LJWJ, Van der Meer IM. Staining efficiency of specific proteins depends on the staining method: wheat gluten proteins. Proteomics 2008, 8:1880-1884. 10.1002/pmic.200700956, 18398878.
    • (2008) Proteomics , vol.8 , pp. 1880-1884
    • Van den Broeck, H.C.1    America, A.H.P.2    Smulders, M.J.M.3    Gilissen, L.J.W.J.4    Van der Meer, I.M.5
  • 12
    • 33645993622 scopus 로고    scopus 로고
    • Allergenicity of 10 different apple varieties
    • 10.1016/S1081-1206(10)63551-X, 16680927
    • Carnés J, Ferrer A, Fernández-Caldas E. Allergenicity of 10 different apple varieties. Ann Allergy Asthma Immunol 2006, 96:564-570. 10.1016/S1081-1206(10)63551-X, 16680927.
    • (2006) Ann Allergy Asthma Immunol , vol.96 , pp. 564-570
    • Carnés, J.1    Ferrer, A.2    Fernández-Caldas, E.3
  • 13
    • 80054033254 scopus 로고    scopus 로고
    • Allergenic activity of different tomato cultivars in tomato allergic subjects
    • 10.1111/j.1365-2222.2011.03841.x, 21955222
    • Dölle S, Lehmann K, Schwarz D, Weckwert W, Scheler C, George E, Franken P, Worm M. Allergenic activity of different tomato cultivars in tomato allergic subjects. Clin Exp Allergy 2011, 41:1643-1652. 10.1111/j.1365-2222.2011.03841.x, 21955222.
    • (2011) Clin Exp Allergy , vol.41 , pp. 1643-1652
    • Dölle, S.1    Lehmann, K.2    Schwarz, D.3    Weckwert, W.4    Scheler, C.5    George, E.6    Franken, P.7    Worm, M.8
  • 14
    • 33745655602 scopus 로고    scopus 로고
    • Regulations of granule-bound starch synthase I gene expression in rice leaves by temperature and drought stress
    • Wang SJ, Liu LF, Chen CK, Chen LW. Regulations of granule-bound starch synthase I gene expression in rice leaves by temperature and drought stress. Biol Plant 2006, 50:537-541.
    • (2006) Biol Plant , vol.50 , pp. 537-541
    • Wang, S.J.1    Liu, L.F.2    Chen, C.K.3    Chen, L.W.4
  • 15
    • 33847416642 scopus 로고    scopus 로고
    • Alanine aminotransferase catalyses the breakdown of alanine after hypoxia in Arabidopsis thaliana
    • 10.1111/j.1365-313X.2006.03023.x, 17319845
    • Miyashita Y, Dolferus R, Ismond KP, Good AG. Alanine aminotransferase catalyses the breakdown of alanine after hypoxia in Arabidopsis thaliana. Plant J 2007, 49:1108-1121. 10.1111/j.1365-313X.2006.03023.x, 17319845.
    • (2007) Plant J , vol.49 , pp. 1108-1121
    • Miyashita, Y.1    Dolferus, R.2    Ismond, K.P.3    Good, A.G.4
  • 17
    • 0039002154 scopus 로고    scopus 로고
    • Characterization of two fungal-elicitor-induced rice cDNAs encoding functional homologues of the rab-specific GDP-dissociation inhibitor
    • 10.1007/s004250050663, 10592042
    • Kim WY, Kim CY, Cheong NE, Choi YO, Lee KO, Lee S-H, Park JB, Nakano A, Bahk JD, Cho MJ, Lee SY. Characterization of two fungal-elicitor-induced rice cDNAs encoding functional homologues of the rab-specific GDP-dissociation inhibitor. Planta 1999, 210:143-149. 10.1007/s004250050663, 10592042.
    • (1999) Planta , vol.210 , pp. 143-149
    • Kim, W.Y.1    Kim, C.Y.2    Cheong, N.E.3    Choi, Y.O.4    Lee, K.O.5    Lee, S.-H.6    Park, J.B.7    Nakano, A.8    Bahk, J.D.9    Cho, M.J.10    Lee, S.Y.11
  • 18
    • 0033895244 scopus 로고    scopus 로고
    • Enhanced tolerance to salt stress in transgenic rice that overexpresses chloroplast glutamine synthetase
    • 10.1023/A:1006408712416, 10949377
    • Hoshida H, Tanaka Y, Hibino T, Hayashi Y, Tanaka A, Takabe T. Enhanced tolerance to salt stress in transgenic rice that overexpresses chloroplast glutamine synthetase. Plant Mol Biol 2000, 43:103-111. 10.1023/A:1006408712416, 10949377.
    • (2000) Plant Mol Biol , vol.43 , pp. 103-111
    • Hoshida, H.1    Tanaka, Y.2    Hibino, T.3    Hayashi, Y.4    Tanaka, A.5    Takabe, T.6
  • 20
    • 64049092155 scopus 로고    scopus 로고
    • Proteomic study for responses to cadmium stress in rice seedlings
    • Ge C, Wang Z, Wan D, Ding Y, Wang Y, Shang Q, Luo S. Proteomic study for responses to cadmium stress in rice seedlings. Rice Sci 2009, 16:33-44.
    • (2009) Rice Sci , vol.16 , pp. 33-44
    • Ge, C.1    Wang, Z.2    Wan, D.3    Ding, Y.4    Wang, Y.5    Shang, Q.6    Luo, S.7
  • 21
    • 77951525154 scopus 로고    scopus 로고
    • Arabidopsis AtSerpin1, crystal structure and in vivo interaction with its target protease RESPONSIVE TO DESICCATION-21 (RD21)
    • 10.1074/jbc.M109.095075, 2859516, 20181955
    • Lampl N, Budai-Hadrian O, Davydov O, Joss T, Harrop S, Curmi P, Roberts T, Fluhr R. Arabidopsis AtSerpin1, crystal structure and in vivo interaction with its target protease RESPONSIVE TO DESICCATION-21 (RD21). J Biol Chem 2010, 285:13550-13560. 10.1074/jbc.M109.095075, 2859516, 20181955.
    • (2010) J Biol Chem , vol.285 , pp. 13550-13560
    • Lampl, N.1    Budai-Hadrian, O.2    Davydov, O.3    Joss, T.4    Harrop, S.5    Curmi, P.6    Roberts, T.7    Fluhr, R.8
  • 22
    • 0036095644 scopus 로고    scopus 로고
    • Drought stress affects chloroplast lipid metabolism in rape (Brassica napus) leaves
    • 10.1034/j.1399-3054.2002.1150207.x, 12060239
    • Benhassaine-Kesri G, Aid F, Demandre C, Kader J-C, Mazliak P. Drought stress affects chloroplast lipid metabolism in rape (Brassica napus) leaves. Physiol Plant 2002, 115:221-227. 10.1034/j.1399-3054.2002.1150207.x, 12060239.
    • (2002) Physiol Plant , vol.115 , pp. 221-227
    • Benhassaine-Kesri, G.1    Aid, F.2    Demandre, C.3    Kader, J.-C.4    Mazliak, P.5
  • 23
    • 33745800028 scopus 로고    scopus 로고
    • Plastoglobules are lipoprotein subcompartments of the chloroplast that are permanently coupled to thylakoid membranes and contain biosynthetic enzymes
    • 10.1105/tpc.105.039859, 1488921, 16731586
    • Aunstin JR, Frost E, Vidi P-A, Kessler F, Staehelin LA. Plastoglobules are lipoprotein subcompartments of the chloroplast that are permanently coupled to thylakoid membranes and contain biosynthetic enzymes. Plant Cell 2006, 18:1693-1703. 10.1105/tpc.105.039859, 1488921, 16731586.
    • (2006) Plant Cell , vol.18 , pp. 1693-1703
    • Aunstin, J.R.1    Frost, E.2    Vidi, P.-A.3    Kessler, F.4    Staehelin, L.A.5
  • 24
    • 84876695124 scopus 로고    scopus 로고
    • Overexpression of the Glyoxalase II Gene Leads to Enhanced Salinity Tolerance in Brassica Juncea
    • Saxena M, Roy SD, Singla-Pareek S-L, Sopory SK, Bhalla-Sarin N. Overexpression of the Glyoxalase II Gene Leads to Enhanced Salinity Tolerance in Brassica Juncea. Open Plant Sci J 2011, 5:23-28.
    • (2011) Open Plant Sci J , vol.5 , pp. 23-28
    • Saxena, M.1    Roy, S.D.2    Singla-Pareek, S.-L.3    Sopory, S.K.4    Bhalla-Sarin, N.5
  • 25
    • 70450173107 scopus 로고    scopus 로고
    • Proteasome regulation, plant growth and stress tolerance
    • 10.4161/psb.4.10.9469, 2801354, 19826220
    • Kurepa J, Wang S, Li Y, Smalle J. Proteasome regulation, plant growth and stress tolerance. Plant Signal Behav 2009, 4:924-927. 10.4161/psb.4.10.9469, 2801354, 19826220.
    • (2009) Plant Signal Behav , vol.4 , pp. 924-927
    • Kurepa, J.1    Wang, S.2    Li, Y.3    Smalle, J.4
  • 26
    • 0036007393 scopus 로고    scopus 로고
    • Complex regulation of ABA biosynthesis in plants
    • Seo M, Koshiba T. Complex regulation of ABA biosynthesis in plants. Trends Plant Sci 2002, 7:41-48.
    • (2002) Trends Plant Sci , vol.7 , pp. 41-48
    • Seo, M.1    Koshiba, T.2
  • 29
    • 34548757949 scopus 로고    scopus 로고
    • Proteomics-based dissection of stress-responsive pathways in plants
    • 10.1016/j.jplph.2007.01.013, 17662502
    • Qureshi MI, Qadir S, Zolla L. Proteomics-based dissection of stress-responsive pathways in plants. J Plant Physiol 2007, 164:1239-1260. 10.1016/j.jplph.2007.01.013, 17662502.
    • (2007) J Plant Physiol , vol.164 , pp. 1239-1260
    • Qureshi, M.I.1    Qadir, S.2    Zolla, L.3
  • 30
    • 38149018511 scopus 로고    scopus 로고
    • Metabolomics for plant stress response
    • 10.1111/j.1399-3054.2007.01025.x, 18251861
    • Shulaev V, Cortes D, Miller G, Mittler R. Metabolomics for plant stress response. Physiol Plant 2008, 132:199-208. 10.1111/j.1399-3054.2007.01025.x, 18251861.
    • (2008) Physiol Plant , vol.132 , pp. 199-208
    • Shulaev, V.1    Cortes, D.2    Miller, G.3    Mittler, R.4
  • 31
    • 33748324641 scopus 로고    scopus 로고
    • Transgeneration memory of stress in plants
    • 10.1038/nature05022, 16892047
    • Molinier J, Ries G, Zipfel C, Hohn B. Transgeneration memory of stress in plants. Nature 2006, 442:1046-1049. 10.1038/nature05022, 16892047.
    • (2006) Nature , vol.442 , pp. 1046-1049
    • Molinier, J.1    Ries, G.2    Zipfel, C.3    Hohn, B.4
  • 33
    • 0032840501 scopus 로고    scopus 로고
    • Increased allergen production in turnip (Brassica rapa) by treatments activating defense mechanisms
    • 10.1016/S0091-6749(99)70135-1, 10400861
    • Hänninen A, Mikkola JH, Kalkkinen N, Ylitalo L, Reunala T, Palosuo T. Increased allergen production in turnip (Brassica rapa) by treatments activating defense mechanisms. J Allergy Clin Immunol 1999, 104:194-201. 10.1016/S0091-6749(99)70135-1, 10400861.
    • (1999) J Allergy Clin Immunol , vol.104 , pp. 194-201
    • Hänninen, A.1    Mikkola, J.H.2    Kalkkinen, N.3    Ylitalo, L.4    Reunala, T.5    Palosuo, T.6
  • 36
    • 0034775074 scopus 로고    scopus 로고
    • Isolation and characterization of barley lipid transfer protein and protein Z as beer allergens
    • 10.1067/mai.2001.118793, 11590395
    • García-Casado G, Crespo JF, Rodríguez J, Salcedo G. Isolation and characterization of barley lipid transfer protein and protein Z as beer allergens. J Allergy Clin Immunol 2001, 108:647-649. 10.1067/mai.2001.118793, 11590395.
    • (2001) J Allergy Clin Immunol , vol.108 , pp. 647-649
    • García-Casado, G.1    Crespo, J.F.2    Rodríguez, J.3    Salcedo, G.4
  • 37
    • 0035815736 scopus 로고    scopus 로고
    • A 33-kDa allergen from rice (Oryza sativa L. Japonica). cDNA cloning, expression, and identification as a novel glyoxalase I
    • 10.1074/jbc.M010337200, 11139585
    • Usui Y, Nakase M, Hotta H, Urisu A, Aoki N, Kitajima K, Matsuda T. A 33-kDa allergen from rice (Oryza sativa L. Japonica). cDNA cloning, expression, and identification as a novel glyoxalase I. J Biol Chem 2001, 276:11376-11381. 10.1074/jbc.M010337200, 11139585.
    • (2001) J Biol Chem , vol.276 , pp. 11376-11381
    • Usui, Y.1    Nakase, M.2    Hotta, H.3    Urisu, A.4    Aoki, N.5    Kitajima, K.6    Matsuda, T.7
  • 38
    • 77950917155 scopus 로고    scopus 로고
    • In-depth exploration of Hevea brasiliensis latex proteome and " hidden allergens" via combinatorial peptide ligand libraries
    • 10.1016/j.jprot.2010.03.002, 20226888
    • D'Amato A, Bachi A, Fasoli E, Boschetti E, Peltre G, Sénéchal H, Sutra JP, Citterio A, Righetti PG. In-depth exploration of Hevea brasiliensis latex proteome and " hidden allergens" via combinatorial peptide ligand libraries. J Proteomics 2010, 73:1368-1380. 10.1016/j.jprot.2010.03.002, 20226888.
    • (2010) J Proteomics , vol.73 , pp. 1368-1380
    • D'Amato, A.1    Bachi, A.2    Fasoli, E.3    Boschetti, E.4    Peltre, G.5    Sénéchal, H.6    Sutra, J.P.7    Citterio, A.8    Righetti, P.G.9
  • 42
    • 67049155252 scopus 로고    scopus 로고
    • Taking advantage of nonspecific trypsin cleavages for the identification of seed storage proteins in cereals
    • 10.1021/pr801093f, 19382796
    • Sergeant K, Pinheiro C, Hausman J-F, Ricardo CP, Renaut J. Taking advantage of nonspecific trypsin cleavages for the identification of seed storage proteins in cereals. J Proteome Res 2009, 8:3182-3190. 10.1021/pr801093f, 19382796.
    • (2009) J Proteome Res , vol.8 , pp. 3182-3190
    • Sergeant, K.1    Pinheiro, C.2    Hausman, J.-F.3    Ricardo, C.P.4    Renaut, J.5
  • 43
    • 0032603137 scopus 로고    scopus 로고
    • Quantifying protein in 2D-PAGE solubilization buffers
    • Ramagli LS. Quantifying protein in 2D-PAGE solubilization buffers. Methods Mol Biol 1998, 112:99-103.
    • (1998) Methods Mol Biol , vol.112 , pp. 99-103
    • Ramagli, L.S.1
  • 44
    • 34547802296 scopus 로고    scopus 로고
    • A proteomic study to identify soya allergens - the human response to transgenic versus non-transgenic soya samples
    • 10.1159/000102611, 17496424
    • Batista R, Martins I, Jenö P, Ricardo CP, Oliveira MM. A proteomic study to identify soya allergens - the human response to transgenic versus non-transgenic soya samples. Int Arch Allergy Immunol 2007, 144:29-38. 10.1159/000102611, 17496424.
    • (2007) Int Arch Allergy Immunol , vol.144 , pp. 29-38
    • Batista, R.1    Martins, I.2    Jenö, P.3    Ricardo, C.P.4    Oliveira, M.M.5
  • 45
    • 0022262821 scopus 로고
    • Clear background and highly sensitive protein staining with Coomassie Blue dyes in polyacrylamide gels: a systematic analysis
    • Neuhoff V, Stamm R, Eibl H. Clear background and highly sensitive protein staining with Coomassie Blue dyes in polyacrylamide gels: a systematic analysis. Electrophoresis 1985, 6:427-448.
    • (1985) Electrophoresis , vol.6 , pp. 427-448
    • Neuhoff, V.1    Stamm, R.2    Eibl, H.3
  • 46
    • 0034690931 scopus 로고    scopus 로고
    • Use of mass spectrometry to study signaling pathways
    • Pandey A, Andersen JS, Mann M. Use of mass spectrometry to study signaling pathways. Sci STKE 2000, 2000:pl1.
    • (2000) Sci STKE , vol.2000
    • Pandey, A.1    Andersen, J.S.2    Mann, M.3


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