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Volumn 93, Issue , 2013, Pages 40-49

Proteomics-based allergen analysis in plants

Author keywords

Allergenomics; Allergens; Genetically modified foods; IgE; Plant proteomics

Indexed keywords

ALLERGEN; AMINE; AMYLASE INHIBITOR; ARA H 2 PROTEIN; ARA H PROTEIN; AVENIN; BETA AMYLASE; ELONGATION FACTOR 2; ENOLASE; FRUCTOSE BISPHOSPHATE ALDOLASE; GLIADIN; GLUTENIN; HEAT SHOCK PROTEIN; IMMUNOGLOBULIN E; ISOFLAVONE; MALATE DEHYDROGENASE; OVOMUCOID; PEPTIDYLPROLYL ISOMERASE; POLYGALACTURONASE; POLYVINYLIDENE FLUORIDE; PROFILIN; PROTEINASE; PROTEINASE INHIBITOR; SERINE PROTEINASE INHIBITOR; THIOREDOXIN; THIOREDOXIN H; TRYPSIN INHIBITOR; UNCLASSIFIED DRUG; UNINDEXED DRUG; VEGETABLE PROTEIN; VICILIN;

EID: 84888022500     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.03.018     Document Type: Review
Times cited : (43)

References (91)
  • 2
    • 0029977729 scopus 로고    scopus 로고
    • Antigen-mediated IgE receptor aggregation and signaling
    • Holowka D., Baird B. Antigen-mediated IgE receptor aggregation and signaling. Annu Rev Biophys Biomol Struct 1996, 25:79-112.
    • (1996) Annu Rev Biophys Biomol Struct , vol.25 , pp. 79-112
    • Holowka, D.1    Baird, B.2
  • 5
    • 80053304692 scopus 로고    scopus 로고
    • The frontiers of mass spectrometry-based techniques in food allergenomics
    • Picariello G., Mamone G., Addeo F., Ferranti P. The frontiers of mass spectrometry-based techniques in food allergenomics. J Chromatogr A 2011, 1218:7386-7398.
    • (2011) J Chromatogr A , vol.1218 , pp. 7386-7398
    • Picariello, G.1    Mamone, G.2    Addeo, F.3    Ferranti, P.4
  • 6
    • 38149102307 scopus 로고    scopus 로고
    • Naturally occurring hypoallergenic Bet v 1 isoforms fail to induce IgE responses in individuals with birch pollen allergy
    • Wagner S., Radauer C., Bublin M., Hoffmann-Sommergruber K., Kopp T., Greisenegger E.K., et al. Naturally occurring hypoallergenic Bet v 1 isoforms fail to induce IgE responses in individuals with birch pollen allergy. J Allergy Clin Immunol 2008, 121:246-252.
    • (2008) J Allergy Clin Immunol , vol.121 , pp. 246-252
    • Wagner, S.1    Radauer, C.2    Bublin, M.3    Hoffmann-Sommergruber, K.4    Kopp, T.5    Greisenegger, E.K.6
  • 7
    • 84856378156 scopus 로고    scopus 로고
    • Proteomics of cypress pollen allergens using double and triple one-dimensional electrophoresis
    • Shahali Y., Sutra J.P., Haddad I., Vinh J., Guilloux L., Peltre G., et al. Proteomics of cypress pollen allergens using double and triple one-dimensional electrophoresis. Electrophoresis 2012, 33:462-469.
    • (2012) Electrophoresis , vol.33 , pp. 462-469
    • Shahali, Y.1    Sutra, J.P.2    Haddad, I.3    Vinh, J.4    Guilloux, L.5    Peltre, G.6
  • 8
    • 33645310636 scopus 로고    scopus 로고
    • Detection of low-molecular weight allergens resolved on two-dimensional electrophoresis with acid-urea polyacrylamide gel
    • Kitta K., Ohnishi-Kameyama M., Moriyama T., Ogawa T., Kawamoto S. Detection of low-molecular weight allergens resolved on two-dimensional electrophoresis with acid-urea polyacrylamide gel. Anal Biochem 2006, 351:290-297.
    • (2006) Anal Biochem , vol.351 , pp. 290-297
    • Kitta, K.1    Ohnishi-Kameyama, M.2    Moriyama, T.3    Ogawa, T.4    Kawamoto, S.5
  • 9
    • 53049102637 scopus 로고    scopus 로고
    • Introduction of the disulfide proteome: application of a technique for the analysis of plant storage proteins as well as allergens
    • Yano H., Kuroda S. Introduction of the disulfide proteome: application of a technique for the analysis of plant storage proteins as well as allergens. J Proteome Res 2008, 7:3071-3079.
    • (2008) J Proteome Res , vol.7 , pp. 3071-3079
    • Yano, H.1    Kuroda, S.2
  • 12
    • 34548248211 scopus 로고    scopus 로고
    • Evolutionary biology of plant food allergens
    • Radauer C., Breiteneder H. Evolutionary biology of plant food allergens. J Allergy Clin Immunol 2007, 120:518-525.
    • (2007) J Allergy Clin Immunol , vol.120 , pp. 518-525
    • Radauer, C.1    Breiteneder, H.2
  • 13
  • 14
    • 0036673739 scopus 로고    scopus 로고
    • Allergies to cross-reactive plant proteins. Latex-fruit syndrome is comparable with pollen-food allergy syndrome
    • Yagami T. Allergies to cross-reactive plant proteins. Latex-fruit syndrome is comparable with pollen-food allergy syndrome. Int Arch Allergy Immunol 2002, 128:271-279.
    • (2002) Int Arch Allergy Immunol , vol.128 , pp. 271-279
    • Yagami, T.1
  • 15
    • 75449095500 scopus 로고    scopus 로고
    • Oral allergy syndrome
    • Kondo Y., Urisu A. Oral allergy syndrome. Allergol Int 2009, 58:485-491.
    • (2009) Allergol Int , vol.58 , pp. 485-491
    • Kondo, Y.1    Urisu, A.2
  • 17
    • 0023626482 scopus 로고
    • Isolation and identification of pollen allergens of Artemisia scoparia
    • Jaggi K.S., Gangal S.V. Isolation and identification of pollen allergens of Artemisia scoparia. J Allergy Clin Immunol 1987, 80:562-572.
    • (1987) J Allergy Clin Immunol , vol.80 , pp. 562-572
    • Jaggi, K.S.1    Gangal, S.V.2
  • 18
    • 0018822435 scopus 로고
    • Widespread IgE-mediated hypersensitivity in the Sudan to the 'green nimitti' midge, Cladotanytarsus lewisi (Diptera: Chironomidae) II. Identification of a major allergen
    • Gad El Rab M.O., Thatcher D.R., Kay A.B. Widespread IgE-mediated hypersensitivity in the Sudan to the 'green nimitti' midge, Cladotanytarsus lewisi (Diptera: Chironomidae) II. Identification of a major allergen. Clin Exp Immunol 1980, 41:389-396.
    • (1980) Clin Exp Immunol , vol.41 , pp. 389-396
    • Gad El Rab, M.O.1    Thatcher, D.R.2    Kay, A.B.3
  • 19
    • 0013990809 scopus 로고
    • Studies on the atopic allergen in ripe tomato fruits. I. Isolation and identification of the allergen
    • Bleumink E., Berrens L., Young E. Studies on the atopic allergen in ripe tomato fruits. I. Isolation and identification of the allergen. Int Arch Allergy Appl Immunol 1966, 30:132-145.
    • (1966) Int Arch Allergy Appl Immunol , vol.30 , pp. 132-145
    • Bleumink, E.1    Berrens, L.2    Young, E.3
  • 20
    • 0036740044 scopus 로고    scopus 로고
    • Identification of an 11S globulin as a major hazelnut food allergen in hazelnut-induced systemic reactions
    • Beyer K., Grishina G., Bardina L., Grishin A., Sampson H.A. Identification of an 11S globulin as a major hazelnut food allergen in hazelnut-induced systemic reactions. J Allergy Clin Immunol 2002, 110:517-523.
    • (2002) J Allergy Clin Immunol , vol.110 , pp. 517-523
    • Beyer, K.1    Grishina, G.2    Bardina, L.3    Grishin, A.4    Sampson, H.A.5
  • 21
    • 14644394893 scopus 로고    scopus 로고
    • Analysis of the composition of an immunoglobulin E reactive high molecular weight protein complex of peanut extract containing Ara h 1 and Ara h 3/4
    • Boldt A., Fortunato D., Conti A., Petersen A., Ballmer-Weber B., Lepp U., et al. Analysis of the composition of an immunoglobulin E reactive high molecular weight protein complex of peanut extract containing Ara h 1 and Ara h 3/4. Proteomics 2005, 5:675-686.
    • (2005) Proteomics , vol.5 , pp. 675-686
    • Boldt, A.1    Fortunato, D.2    Conti, A.3    Petersen, A.4    Ballmer-Weber, B.5    Lepp, U.6
  • 25
    • 79952708666 scopus 로고    scopus 로고
    • Proteomic analysis of known and candidate rice allergens between non-transgenic and transgenic plants
    • Satoh R., Nakamura R., Komatsu A., Oshima M., Teshima R. Proteomic analysis of known and candidate rice allergens between non-transgenic and transgenic plants. Regul Toxicol Pharmacol 2011, 59:437-444.
    • (2011) Regul Toxicol Pharmacol , vol.59 , pp. 437-444
    • Satoh, R.1    Nakamura, R.2    Komatsu, A.3    Oshima, M.4    Teshima, R.5
  • 26
    • 47249101589 scopus 로고    scopus 로고
    • Proteomic analysis of peanut seed storage proteins and genetic variation in a potential peanut allergen
    • Guo B., Liang X., Chung S.Y., Holbrook C.C., Maleki S.J. Proteomic analysis of peanut seed storage proteins and genetic variation in a potential peanut allergen. Protein Pept Lett 2008, 15:567-577.
    • (2008) Protein Pept Lett , vol.15 , pp. 567-577
    • Guo, B.1    Liang, X.2    Chung, S.Y.3    Holbrook, C.C.4    Maleki, S.J.5
  • 27
    • 24044487380 scopus 로고    scopus 로고
    • Mass spectrometric analysis of electrophoretically separated allergens and proteases in grass pollen diffusates
    • Raftery M.J., Saldanha R.G., Geczy C.L., Kumar R.K. Mass spectrometric analysis of electrophoretically separated allergens and proteases in grass pollen diffusates. Respir Res 2003, 4:10.
    • (2003) Respir Res , vol.4 , pp. 10
    • Raftery, M.J.1    Saldanha, R.G.2    Geczy, C.L.3    Kumar, R.K.4
  • 28
    • 36849082003 scopus 로고    scopus 로고
    • Proteomic analysis of tomato (Lycopersicon esculentum) pollen
    • Sheoran I.S., Ross A.R., Olson D.J., Sawhney V.K. Proteomic analysis of tomato (Lycopersicon esculentum) pollen. J Exp Bot 2007, 58:3525-3535.
    • (2007) J Exp Bot , vol.58 , pp. 3525-3535
    • Sheoran, I.S.1    Ross, A.R.2    Olson, D.J.3    Sawhney, V.K.4
  • 29
    • 70349923628 scopus 로고    scopus 로고
    • Novel IgE recognized components of Lolium perenne pollen extract: comparative proteomics evaluation of allergic patients sensitization profiles
    • De Canio M., D'Aguanno S., Sacchetti C., Petrucci F., Cavagni G., Nuccetelli M., et al. Novel IgE recognized components of Lolium perenne pollen extract: comparative proteomics evaluation of allergic patients sensitization profiles. J Proteome Res 2009, 8:4383-4391.
    • (2009) J Proteome Res , vol.8 , pp. 4383-4391
    • De Canio, M.1    D'Aguanno, S.2    Sacchetti, C.3    Petrucci, F.4    Cavagni, G.5    Nuccetelli, M.6
  • 30
    • 25844477996 scopus 로고    scopus 로고
    • Sub-proteome analysis of novel IgE-binding proteins from Bermuda grass pollen
    • Kao S.H., Su S.N., Huang S.W., Tsai J.J., Chow L.P. Sub-proteome analysis of novel IgE-binding proteins from Bermuda grass pollen. Proteomics 2005, 5:3805-3813.
    • (2005) Proteomics , vol.5 , pp. 3805-3813
    • Kao, S.H.1    Su, S.N.2    Huang, S.W.3    Tsai, J.J.4    Chow, L.P.5
  • 31
    • 33645065565 scopus 로고    scopus 로고
    • Down-regulation of the strawberry Bet v 1-homologous allergen in concert with the flavonoid biosynthesis pathway in colorless strawberry mutant
    • Hjernø K., Alm R., Canbäck B., Matthiesen R., Trajkovski K., Björk L., et al. Down-regulation of the strawberry Bet v 1-homologous allergen in concert with the flavonoid biosynthesis pathway in colorless strawberry mutant. Proteomics 2006, 6:1574-1587.
    • (2006) Proteomics , vol.6 , pp. 1574-1587
    • Hjernø, K.1    Alm, R.2    Canbäck, B.3    Matthiesen, R.4    Trajkovski, K.5    Björk, L.6
  • 32
    • 34548162709 scopus 로고    scopus 로고
    • Proteomic variation is as large within as between strawberry varieties
    • Alm R., Ekefjärd A., Krogh M., Häkkinen J., Emanuelsson C. Proteomic variation is as large within as between strawberry varieties. J Proteome Res 2007, 6:3011-3020.
    • (2007) J Proteome Res , vol.6 , pp. 3011-3020
    • Alm, R.1    Ekefjärd, A.2    Krogh, M.3    Häkkinen, J.4    Emanuelsson, C.5
  • 33
    • 13244262678 scopus 로고    scopus 로고
    • Novel isoforms of Pru av 1 with diverging immunoglobulin E binding properties identified by a synergistic combination of molecular biology and proteomics
    • Reuter A., Fortunato D., Garoffo L.P., Napolitano L., Scheurer S., Giuffrida M.G., et al. Novel isoforms of Pru av 1 with diverging immunoglobulin E binding properties identified by a synergistic combination of molecular biology and proteomics. Proteomics 2005, 5:282-289.
    • (2005) Proteomics , vol.5 , pp. 282-289
    • Reuter, A.1    Fortunato, D.2    Garoffo, L.P.3    Napolitano, L.4    Scheurer, S.5    Giuffrida, M.G.6
  • 34
    • 77953643849 scopus 로고    scopus 로고
    • Proteome from lemon fruit flavedo reveals that this tissue produces high amounts of the Cit s1 germin-like isoforms
    • Pignataro V., Canton C., Spadafora A., Mazzuca S. Proteome from lemon fruit flavedo reveals that this tissue produces high amounts of the Cit s1 germin-like isoforms. J Agric Food Chem 2010, 58:7239-7244.
    • (2010) J Agric Food Chem , vol.58 , pp. 7239-7244
    • Pignataro, V.1    Canton, C.2    Spadafora, A.3    Mazzuca, S.4
  • 35
    • 77956445142 scopus 로고    scopus 로고
    • A convenient and sensitive allergy test: IgE crosslinking-induced luciferase expression in cultured mast cells
    • Nakamura R., Uchida Y., Higuchi M., Nakamura R., Tsuge I., Urisu A., et al. A convenient and sensitive allergy test: IgE crosslinking-induced luciferase expression in cultured mast cells. Allergy 2010, 65:1266-1273.
    • (2010) Allergy , vol.65 , pp. 1266-1273
    • Nakamura, R.1    Uchida, Y.2    Higuchi, M.3    Nakamura, R.4    Tsuge, I.5    Urisu, A.6
  • 36
    • 77950917155 scopus 로고    scopus 로고
    • In-depth exploration of Hevea brasiliensis latex proteome and "hidden allergens" via combinatorial peptide ligand libraries
    • D'Amato A., Bachi A., Fasoli E., Boschetti E., Peltre G., Sénéchal H., et al. In-depth exploration of Hevea brasiliensis latex proteome and "hidden allergens" via combinatorial peptide ligand libraries. J Proteomics 2010, 73:1368-1380.
    • (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
  • 37
    • 80052850750 scopus 로고    scopus 로고
    • IgE recognition patterns of profilin, PR-10, and tropomyosin panallergens tested in 3,113 allergic patients by allergen microarray-based technology
    • Scala E., Alessandri C., Palazzo P., Pomponi D., Liso M., Bernardi M.L., et al. IgE recognition patterns of profilin, PR-10, and tropomyosin panallergens tested in 3,113 allergic patients by allergen microarray-based technology. PLoS One 2011, 6:e24912.
    • (2011) PLoS One , vol.6
    • Scala, E.1    Alessandri, C.2    Palazzo, P.3    Pomponi, D.4    Liso, M.5    Bernardi, M.L.6
  • 39
    • 77956320456 scopus 로고    scopus 로고
    • A protein allergen microarray detects specific IgE to pollen surface, cytoplasmic, and commercial allergen extracts
    • Vigh-Conrad K.A., Conrad D.F., Preuss D. A protein allergen microarray detects specific IgE to pollen surface, cytoplasmic, and commercial allergen extracts. PLoS One 2010, 5:e10174.
    • (2010) PLoS One , vol.5
    • Vigh-Conrad, K.A.1    Conrad, D.F.2    Preuss, D.3
  • 40
    • 66749123071 scopus 로고    scopus 로고
    • Micro-arrayed wheat seed and grass pollen allergens for component-resolved diagnosis
    • Constantin C., Quirce S., Poorafshar M., Touraev A., Niggemann B., Mari A., et al. Micro-arrayed wheat seed and grass pollen allergens for component-resolved diagnosis. Allergy 2009, 64:1030-1037.
    • (2009) Allergy , vol.64 , pp. 1030-1037
    • Constantin, C.1    Quirce, S.2    Poorafshar, M.3    Touraev, A.4    Niggemann, B.5    Mari, A.6
  • 42
    • 65349124697 scopus 로고    scopus 로고
    • Detection of allergen specific immunoglobulins by microarrays coupled to microfluidics
    • Cretich M., Di Carlo G., Giudici C., Pokoj S., Lauer I., Scheurer S., et al. Detection of allergen specific immunoglobulins by microarrays coupled to microfluidics. Proteomics 2009, 9:2098-2107.
    • (2009) Proteomics , vol.9 , pp. 2098-2107
    • Cretich, M.1    Di Carlo, G.2    Giudici, C.3    Pokoj, S.4    Lauer, I.5    Scheurer, S.6
  • 44
    • 84888063912 scopus 로고    scopus 로고
    • Validation of quantitative and qualitative methods for detecting allergenic ingredients in processed foods in Japan
    • [Epub ahead of print]
    • Sakai S., Adachi R., Akiyama H., Teshima R. Validation of quantitative and qualitative methods for detecting allergenic ingredients in processed foods in Japan. J Agric Food Chem Oct. 5 2012, [Epub ahead of print].
    • (2012) J Agric Food Chem
    • Sakai, S.1    Adachi, R.2    Akiyama, H.3    Teshima, R.4
  • 46
    • 77956135648 scopus 로고    scopus 로고
    • Determination of walnut protein in processed foods by enzyme-linked immunosorbent assay: interlaboratory study
    • Sakai S., Adachi R., Akiyama H., Teshima R., Doi H., Shibata H. Determination of walnut protein in processed foods by enzyme-linked immunosorbent assay: interlaboratory study. J AOAC Int 2010, 93:1255-1261.
    • (2010) J AOAC Int , vol.93 , pp. 1255-1261
    • Sakai, S.1    Adachi, R.2    Akiyama, H.3    Teshima, R.4    Doi, H.5    Shibata, H.6
  • 47
    • 0037048737 scopus 로고    scopus 로고
    • Detection of potentially allergenic hazelnut (Corylus avellana) residues in food: a comparative study with DNA PCR-ELISA and protein sandwich-ELISA
    • Holzhauser T., Stephan O., Vieths S. Detection of potentially allergenic hazelnut (Corylus avellana) residues in food: a comparative study with DNA PCR-ELISA and protein sandwich-ELISA. J Agric Food Chem 2002, 50:5808-5815.
    • (2002) J Agric Food Chem , vol.50 , pp. 5808-5815
    • Holzhauser, T.1    Stephan, O.2    Vieths, S.3
  • 48
    • 0029865002 scopus 로고    scopus 로고
    • Applications of liquid chromatography-mass spectrometry interfacing systems in food analysis: pesticide, drug and toxic substance residues
    • Careri M., Mangia A., Musci M. Applications of liquid chromatography-mass spectrometry interfacing systems in food analysis: pesticide, drug and toxic substance residues. J Chromatogr A 1996, 727:153-184.
    • (1996) J Chromatogr A , vol.727 , pp. 153-184
    • Careri, M.1    Mangia, A.2    Musci, M.3
  • 49
    • 36849082932 scopus 로고    scopus 로고
    • Use of specific peptide biomarkers for quantitative confirmation of hidden allergenic peanut proteins Ara h 2 and Ara h 3/4 for food control by liquid chromatography-tandem mass spectrometry
    • Careri M., Costa A., Elviri L., Lagos J.B., Mangia A., Terenghi M., et al. Use of specific peptide biomarkers for quantitative confirmation of hidden allergenic peanut proteins Ara h 2 and Ara h 3/4 for food control by liquid chromatography-tandem mass spectrometry. Anal Bioanal Chem 2007, 389:1901-1907.
    • (2007) Anal Bioanal Chem , vol.389 , pp. 1901-1907
    • Careri, M.1    Costa, A.2    Elviri, L.3    Lagos, J.B.4    Mangia, A.5    Terenghi, M.6
  • 50
    • 84857675315 scopus 로고    scopus 로고
    • Current challenges in detecting food allergens by shotgun and targeted proteomic approaches: a case study on traces of peanut allergens in baked cookies
    • Pedreschi R., Nørgaard J., Maquet A. Current challenges in detecting food allergens by shotgun and targeted proteomic approaches: a case study on traces of peanut allergens in baked cookies. Nutrients 2012, 4:132-150.
    • (2012) Nutrients , vol.4 , pp. 132-150
    • Pedreschi, R.1    Nørgaard, J.2    Maquet, A.3
  • 51
    • 34250652972 scopus 로고    scopus 로고
    • Proteomics-based approach to detect and identify major allergens in processed peanuts by capillary LC-Q-TOF (MS/MS)
    • Chassaigne H., Nørgaard J.V., Hengel A.J. Proteomics-based approach to detect and identify major allergens in processed peanuts by capillary LC-Q-TOF (MS/MS). J Agric Food Chem 2007, 55:4461-4473.
    • (2007) J Agric Food Chem , vol.55 , pp. 4461-4473
    • Chassaigne, H.1    Nørgaard, J.V.2    Hengel, A.J.3
  • 52
    • 84879407082 scopus 로고    scopus 로고
    • Quantification of allergenic bovine milk α(S1)-casein in baked goods using an intact (15)N-labeled protein internal standard
    • [in press]
    • Newsome G.A., Scholl P.F. Quantification of allergenic bovine milk α(S1)-casein in baked goods using an intact (15)N-labeled protein internal standard. J Agric Food Chem 2013, [in press].
    • (2013) J Agric Food Chem
    • Newsome, G.A.1    Scholl, P.F.2
  • 53
    • 79251620332 scopus 로고    scopus 로고
    • Selection of possible marker peptides for the detection of major ruminant milk proteins in food by liquid chromatography-tandem mass spectrometry
    • Ansari P., Stoppacher N., Rudolf J., Schuhmacher R., Baumgartner S. Selection of possible marker peptides for the detection of major ruminant milk proteins in food by liquid chromatography-tandem mass spectrometry. Anal Bioanal Chem 2011, 399:1105-1115.
    • (2011) Anal Bioanal Chem , vol.399 , pp. 1105-1115
    • Ansari, P.1    Stoppacher, N.2    Rudolf, J.3    Schuhmacher, R.4    Baumgartner, S.5
  • 54
    • 80054822113 scopus 로고    scopus 로고
    • Development and validation of a method for the quantification of milk proteins in food products based on liquid chromatography with mass spectrometric detection
    • Lutter P., Parisod V., Weymuth H. Development and validation of a method for the quantification of milk proteins in food products based on liquid chromatography with mass spectrometric detection. J AOAC Int 2011, 94:1043-1059.
    • (2011) J AOAC Int , vol.94 , pp. 1043-1059
    • Lutter, P.1    Parisod, V.2    Weymuth, H.3
  • 55
    • 77952773738 scopus 로고    scopus 로고
    • Determination of allergenic egg proteins in food by protein-, mass spectrometry-, and DNA-based methods
    • Lee J.Y., Kim C.J. Determination of allergenic egg proteins in food by protein-, mass spectrometry-, and DNA-based methods. J AOAC Int 2010, 93:462-477.
    • (2010) J AOAC Int , vol.93 , pp. 462-477
    • Lee, J.Y.1    Kim, C.J.2
  • 57
    • 80054820101 scopus 로고    scopus 로고
    • Application of a liquid chromatography tandem mass spectrometry method for the simultaneous detection of seven allergenic foods in flour and bread and comparison of the method with commercially available ELISA test kits
    • Heick J., Fischer M., Kerbach S., Tamm U., Popping B. Application of a liquid chromatography tandem mass spectrometry method for the simultaneous detection of seven allergenic foods in flour and bread and comparison of the method with commercially available ELISA test kits. J AOAC Int 2011, 94:1060-1068.
    • (2011) J AOAC Int , vol.94 , pp. 1060-1068
    • Heick, J.1    Fischer, M.2    Kerbach, S.3    Tamm, U.4    Popping, B.5
  • 58
    • 77956636375 scopus 로고    scopus 로고
    • Effects of thermal processing on the enzyme-linked immunosorbent assay (ELISA) detection of milk residues in a model food matrix
    • Downs M.L., Taylor S.L. Effects of thermal processing on the enzyme-linked immunosorbent assay (ELISA) detection of milk residues in a model food matrix. J Agric Food Chem 2010, 58:10085-10091.
    • (2010) J Agric Food Chem , vol.58 , pp. 10085-10091
    • Downs, M.L.1    Taylor, S.L.2
  • 59
    • 69149110073 scopus 로고    scopus 로고
    • Aspects of food processing and its effect on allergen structure
    • Paschke A. Aspects of food processing and its effect on allergen structure. Mol Nutr Food Res 2009, 53:959-962.
    • (2009) Mol Nutr Food Res , vol.53 , pp. 959-962
    • Paschke, A.1
  • 60
    • 72449124198 scopus 로고    scopus 로고
    • Apple (Malus domestica L. Borkh.) allergen Mal d 1: effect of cultivar, cultivation system, and storage conditions
    • 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.
    • (2009) J Agric Food Chem , vol.57 , pp. 10548-10553
    • Matthes, A.1    Schmitz-Eiberger, M.2
  • 61
    • 33746566570 scopus 로고    scopus 로고
    • Maturity and storage influence on the apple (Malus domestica) allergen Mal d 3, a nonspecific lipid transfer protein
    • Sancho A.I., Foxall R., Rigby N.M., Browne T., Zuidmeer L., van Ree R., et al. Maturity and storage influence on the apple (Malus domestica) allergen Mal d 3, a nonspecific lipid transfer protein. J Agric Food Chem 2006, 54:5098-5104.
    • (2006) J Agric Food Chem , vol.54 , pp. 5098-5104
    • Sancho, A.I.1    Foxall, R.2    Rigby, N.M.3    Browne, T.4    Zuidmeer, L.5    van Ree, R.6
  • 62
    • 64549148525 scopus 로고    scopus 로고
    • Influence of the natural ripening stage, cold storage, and ethylene treatment on the protein and IgE-binding profiles of green and gold kiwi fruit extracts
    • Ciardiello M.A., Giangrieco I., Tuppo L., Tamburrini M., Buccheri M., Palazzo P., et al. Influence of the natural ripening stage, cold storage, and ethylene treatment on the protein and IgE-binding profiles of green and gold kiwi fruit extracts. J Agric Food Chem 2009, 57:1565-1571.
    • (2009) J Agric Food Chem , vol.57 , pp. 1565-1571
    • Ciardiello, M.A.1    Giangrieco, I.2    Tuppo, L.3    Tamburrini, M.4    Buccheri, M.5    Palazzo, P.6
  • 63
    • 11144245490 scopus 로고    scopus 로고
    • Presence of allergenic proteins in different peach (Prunus persica) cultivars and dependence of their content on fruit ripening
    • Brenna O.V., Pastorello E.A., Farioli L., Pravettoni V., Pompei C. Presence of allergenic proteins in different peach (Prunus persica) cultivars and dependence of their content on fruit ripening. J Agric Food Chem 2004, 52:7997-8000.
    • (2004) J Agric Food Chem , vol.52 , pp. 7997-8000
    • Brenna, O.V.1    Pastorello, E.A.2    Farioli, L.3    Pravettoni, V.4    Pompei, C.5
  • 64
    • 68249124846 scopus 로고    scopus 로고
    • Gel-based proteomics approach to the study of metabolic changes in pear tissue during storage
    • Pedreschi R., Hertog M., Robben J., Lilley K.S., Karp N.A., Baggerman G., et al. Gel-based proteomics approach to the study of metabolic changes in pear tissue during storage. J Agric Food Chem 2009, 57:6997-7004.
    • (2009) J Agric Food Chem , vol.57 , pp. 6997-7004
    • Pedreschi, R.1    Hertog, M.2    Robben, J.3    Lilley, K.S.4    Karp, N.A.5    Baggerman, G.6
  • 65
    • 67651233459 scopus 로고    scopus 로고
    • 2-D DIGE analysis of the proteome of extracts from peanut variants reveals striking differences in major allergen contents
    • Schmidt H., Gelhaus C., Latendorf T., Nebendahl M., Petersen A., Krause S., et al. 2-D DIGE analysis of the proteome of extracts from peanut variants reveals striking differences in major allergen contents. Proteomics 2009, 9:3507-3521.
    • (2009) Proteomics , vol.9 , pp. 3507-3521
    • Schmidt, H.1    Gelhaus, C.2    Latendorf, T.3    Nebendahl, M.4    Petersen, A.5    Krause, S.6
  • 66
    • 78650049978 scopus 로고    scopus 로고
    • Characterization of Phleum pratense pollen extracts by 2-D DIGE and allergen immunoreactivity
    • Schmidt H., Gelhaus C., Nebendahl M., Janssen O., Petersen A. Characterization of Phleum pratense pollen extracts by 2-D DIGE and allergen immunoreactivity. Proteomics 2010, 10:4352-4362.
    • (2010) Proteomics , vol.10 , pp. 4352-4362
    • Schmidt, H.1    Gelhaus, C.2    Nebendahl, M.3    Janssen, O.4    Petersen, A.5
  • 69
    • 79953687955 scopus 로고    scopus 로고
    • Proteomic profiling of birch (Betula verrucosa) pollen extracts from different origins
    • Erler A., Hawranek T., Krückemeier L., Asam C., Egger M., Ferreira F., et al. Proteomic profiling of birch (Betula verrucosa) pollen extracts from different origins. Proteomics 2011, 11:1486-1498.
    • (2011) Proteomics , vol.11 , pp. 1486-1498
    • Erler, A.1    Hawranek, T.2    Krückemeier, L.3    Asam, C.4    Egger, M.5    Ferreira, F.6
  • 70
    • 33750340111 scopus 로고    scopus 로고
    • Storage protein profiles in Spanish and runner market type peanuts and potential markers
    • Liang X.Q., Luo M., Holbrook C.C., Guo B.Z. Storage protein profiles in Spanish and runner market type peanuts and potential markers. BMC Plant Biol 2006, 6:24.
    • (2006) BMC Plant Biol , vol.6 , pp. 24
    • Liang, X.Q.1    Luo, M.2    Holbrook, C.C.3    Guo, B.Z.4
  • 71
    • 51649115314 scopus 로고    scopus 로고
    • Vegetable proteomics: the detection of Ole e 1 isoallergens by peptide matching of MALDI MS/MS spectra of underivatized and dansylated glycopeptides
    • Napoli A., Aiello D., Di Donna L., Moschidis P., Sindona G. Vegetable proteomics: the detection of Ole e 1 isoallergens by peptide matching of MALDI MS/MS spectra of underivatized and dansylated glycopeptides. J Proteome Res 2008, 7:2723-2732.
    • (2008) J Proteome Res , vol.7 , pp. 2723-2732
    • Napoli, A.1    Aiello, D.2    Di Donna, L.3    Moschidis, P.4    Sindona, G.5
  • 72
    • 1542316859 scopus 로고    scopus 로고
    • Two-dimensional IgE-binding spectrum of Japanese cedar (Cryptomeria japonica) pollen allergens
    • Fujimura T., Shigeta S., Kawamoto S., Aki T., Masubuchi M., Hayashi T., et al. Two-dimensional IgE-binding spectrum of Japanese cedar (Cryptomeria japonica) pollen allergens. Int Arch Allergy Immunol 2004, 133:125-135.
    • (2004) Int Arch Allergy Immunol , vol.133 , pp. 125-135
    • Fujimura, T.1    Shigeta, S.2    Kawamoto, S.3    Aki, T.4    Masubuchi, M.5    Hayashi, T.6
  • 73
    • 77953621468 scopus 로고    scopus 로고
    • Crucial roles of membrane stability and its related proteins in the tolerance of peach fruit to chilling injury
    • Zhang C., Ding Z., Xu X., Wang Q., Qin G., Tian S. Crucial roles of membrane stability and its related proteins in the tolerance of peach fruit to chilling injury. Amino Acids 2010, 39:181-194.
    • (2010) Amino Acids , vol.39 , pp. 181-194
    • Zhang, C.1    Ding, Z.2    Xu, X.3    Wang, Q.4    Qin, G.5    Tian, S.6
  • 74
    • 84866638697 scopus 로고    scopus 로고
    • Analysis of high allergenicity airborne pollen dispersion: common ragweed study case in Lithuania
    • Šauliene I., Veriankaite L. Analysis of high allergenicity airborne pollen dispersion: common ragweed study case in Lithuania. Ann Agric Environ Med 2012, 19:415-419.
    • (2012) Ann Agric Environ Med , vol.19 , pp. 415-419
    • Šauliene, I.1    Veriankaite, L.2
  • 76
    • 34547802296 scopus 로고    scopus 로고
    • A proteomic study to identify soya allergens-the human response to transgenic versus non-transgenic soya samples
    • Batista R., Martins I., Jeno P., Ricardo C.P., Oliveira M.M. 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.
    • (2007) Int Arch Allergy Immunol , vol.144 , pp. 29-38
    • Batista, R.1    Martins, I.2    Jeno, P.3    Ricardo, C.P.4    Oliveira, M.M.5
  • 77
    • 77953154379 scopus 로고    scopus 로고
    • Changes in protein expression profiles between a low phytic acid rice (Oryza sativa L. ssp. japonica) line and its parental line: a proteomic and bioinformatic approach
    • Emami K., Morris N.J., Cockell S.J., Golebiowska G., Shu Q.Y., Gatehouse A.M. Changes in protein expression profiles between a low phytic acid rice (Oryza sativa L. ssp. japonica) line and its parental line: a proteomic and bioinformatic approach. J Agric Food Chem 2010, 58:6912-6922.
    • (2010) J Agric Food Chem , vol.58 , pp. 6912-6922
    • Emami, K.1    Morris, N.J.2    Cockell, S.J.3    Golebiowska, G.4    Shu, Q.Y.5    Gatehouse, A.M.6
  • 78
    • 77956131272 scopus 로고    scopus 로고
    • Immunoproteomic and two-dimensional difference gel electrophoresis analysis of Arabidopsis dehydration response element-binding protein 1A (DREB1A)-transgenic potato
    • Nakamura R., Satoh R., Nakamura R., Shimazaki T., Kasuga M., Yamaguchi-Shinozaki K., et al. Immunoproteomic and two-dimensional difference gel electrophoresis analysis of Arabidopsis dehydration response element-binding protein 1A (DREB1A)-transgenic potato. Biol Pharm Bull 2010, 33(8):1418-1425.
    • (2010) Biol Pharm Bull , vol.33 , Issue.8 , pp. 1418-1425
    • Nakamura, R.1    Satoh, R.2    Nakamura, R.3    Shimazaki, T.4    Kasuga, M.5    Yamaguchi-Shinozaki, K.6
  • 79
    • 84858748677 scopus 로고    scopus 로고
    • Characterization of maize allergens - MON810 vs. its non-transgenic counterpart
    • Fonseca C., Planchon S., Renaut J., Oliveira M.M., Batista R. Characterization of maize allergens - MON810 vs. its non-transgenic counterpart. J Proteomics 2012, 75:2027-2037.
    • (2012) J Proteomics , vol.75 , pp. 2027-2037
    • Fonseca, C.1    Planchon, S.2    Renaut, J.3    Oliveira, M.M.4    Batista, R.5
  • 80
    • 78349312925 scopus 로고    scopus 로고
    • Evolution of seed allergen quantification-from antibodies to mass spectrometry
    • Stevenson S.E., Houston N.L., Thelen J.J. Evolution of seed allergen quantification-from antibodies to mass spectrometry. Regul Toxicol Pharmacol 2010, 58:S36-S41.
    • (2010) Regul Toxicol Pharmacol , vol.58
    • Stevenson, S.E.1    Houston, N.L.2    Thelen, J.J.3
  • 81
    • 63649131272 scopus 로고    scopus 로고
    • Validation of gel-free, label-free quantitative proteomics approaches: applications for seed allergen profiling
    • Stevenson S.E., Chu Y., Ozias-Akins P., Thelen J.J. Validation of gel-free, label-free quantitative proteomics approaches: applications for seed allergen profiling. J Proteomics 2009, 72:555-566.
    • (2009) J Proteomics , vol.72 , pp. 555-566
    • Stevenson, S.E.1    Chu, Y.2    Ozias-Akins, P.3    Thelen, J.J.4
  • 82
    • 70349975885 scopus 로고    scopus 로고
    • A comparative proteomics approach to detect unintended effects in transgenic Arabidopsis
    • Ren Y., Lv J., Wang H., Li L., Peng Y., Qu L.J. A comparative proteomics approach to detect unintended effects in transgenic Arabidopsis. J Genet Genomics 2009, 36:629-639.
    • (2009) J Genet Genomics , vol.36 , pp. 629-639
    • Ren, Y.1    Lv, J.2    Wang, H.3    Li, L.4    Peng, Y.5    Qu, L.J.6
  • 83
    • 84860636295 scopus 로고    scopus 로고
    • Proteomics insight into the biological safety of transgenic modification of rice as compared with conventional genetic breeding and spontaneous genotypic variation
    • Gong C.Y., Li Q., Yu H.T., Wang Z., Wang T. Proteomics insight into the biological safety of transgenic modification of rice as compared with conventional genetic breeding and spontaneous genotypic variation. Proteome Res 2012, 11(5):3019-3029.
    • (2012) Proteome Res , vol.11 , Issue.5 , pp. 3019-3029
    • Gong, C.Y.1    Li, Q.2    Yu, H.T.3    Wang, Z.4    Wang, T.5
  • 84
    • 67650240664 scopus 로고    scopus 로고
    • Proteomics tools and resources for investigating protein allergens in oilseeds
    • Thelen J.J. Proteomics tools and resources for investigating protein allergens in oilseeds. Regul Toxicol Pharmacol 2009, 54:S41-S45.
    • (2009) Regul Toxicol Pharmacol , vol.54
    • Thelen, J.J.1
  • 85
    • 78349313419 scopus 로고    scopus 로고
    • Natural variability in abundance of prevalent soybean proteins
    • Natarajan S.S. Natural variability in abundance of prevalent soybean proteins. Regul Toxicol Pharmacol 2010, 58:S26-S29.
    • (2010) Regul Toxicol Pharmacol , vol.58
    • Natarajan, S.S.1
  • 86
    • 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
  • 87
    • 0036968792 scopus 로고    scopus 로고
    • Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing: seed storage proteins as common food allergens
    • Beyer K., Bardina L., Grishina G., Sampson H.A. Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing: seed storage proteins as common food allergens. J Allergy Clin Immunol 2002, 110:154-159.
    • (2002) J Allergy Clin Immunol , vol.110 , pp. 154-159
    • Beyer, K.1    Bardina, L.2    Grishina, G.3    Sampson, H.A.4
  • 88
    • 34447534358 scopus 로고    scopus 로고
    • Generation of allergen-enriched protein fractions of Hevea brasiliensis latex for in vitro and in vivo diagnosis
    • Wagner S., Bublin M., Hafner C., Kopp T., Allwardt D., Seifert U., et al. Generation of allergen-enriched protein fractions of Hevea brasiliensis latex for in vitro and in vivo diagnosis. Int Arch Allergy Immunol 2007, 143:246-254.
    • (2007) Int Arch Allergy Immunol , vol.143 , pp. 246-254
    • Wagner, S.1    Bublin, M.2    Hafner, C.3    Kopp, T.4    Allwardt, D.5    Seifert, U.6
  • 89
    • 33645118960 scopus 로고    scopus 로고
    • Design of tomato fruits with reduced allergenicity by dsRNAi-mediated inhibition of ns-LTP (Lyc e 3) expression
    • Le L.Q., Lorenz Y., Scheurer S., Fötisch K., Enrique E., Bartra J., et al. Design of tomato fruits with reduced allergenicity by dsRNAi-mediated inhibition of ns-LTP (Lyc e 3) expression. Plant Biotechnol J 2006, 4:231-242.
    • (2006) Plant Biotechnol J , vol.4 , pp. 231-242
    • Le, L.Q.1    Lorenz, Y.2    Scheurer, S.3    Fötisch, K.4    Enrique, E.5    Bartra, J.6
  • 90
    • 65249170075 scopus 로고    scopus 로고
    • Evidence for novel tomato seed allergens: IgE-reactive legumin and vicilin proteins identified by multidimensional protein fractionation-mass spectrometry and in silico epitope modeling
    • Bässler O.Y., Weiss J., Wienkoop S., Lehmann K., Scheler C., Dölle S., et al. Evidence for novel tomato seed allergens: IgE-reactive legumin and vicilin proteins identified by multidimensional protein fractionation-mass spectrometry and in silico epitope modeling. J Proteome Res 2009, 8:1111-1122.
    • (2009) J Proteome Res , vol.8 , pp. 1111-1122
    • Bässler, O.Y.1    Weiss, J.2    Wienkoop, S.3    Lehmann, K.4    Scheler, C.5    Dölle, S.6


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