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Volumn 44, Issue 5, 2004, Pages 379-407

Structural, biological, and evolutionary relationships of plant food allergens sensitizing via the gastrointestinal tract

Author keywords

Cupins; Cysteine; Prolamins; Protease; Protein families; Structure

Indexed keywords

CUPINS; CYSTEINE; PROLAMINS; PROTEIN FAMILIES;

EID: 5444259323     PISSN: 10408398     EISSN: None     Source Type: Journal    
DOI: 10.1080/10408690490489224     Document Type: Article
Times cited : (190)

References (221)
  • 2
    • 0027354589 scopus 로고
    • Gene structure and expression of rice seed allergenic proteins belonging to the α-amylase/trypsin inhibitor family
    • Adachi, T., Izumi, H., Yamada, T., Tanaka, K., Takeuchi, S., Nakamura, R., and Matsuda, T. 1993. Gene structure and expression of rice seed allergenic proteins belonging to the α-amylase/trypsin inhibitor family. Plant Mol. Biol., 21:239-248.
    • (1993) Plant Mol. Biol. , vol.21 , pp. 239-248
    • Adachi, T.1    Izumi, H.2    Yamada, T.3    Tanaka, K.4    Takeuchi, S.5    Nakamura, R.6    Matsuda, T.7
  • 3
    • 0032797422 scopus 로고    scopus 로고
    • Role of carbohydrate moieties in IgE binding to allergenic components of Cupressus arizonica pollen extract
    • Afferni, C., Iacovacci, P., Barletta, B., Di Felice, G., Tinghino, R., Mari, A., and Pini, C. 1999. Role of carbohydrate moieties in IgE binding to allergenic components of Cupressus arizonica pollen extract. Clin. Exp. Allergy, 29:1087-1094.
    • (1999) Clin. Exp. Allergy , vol.29 , pp. 1087-1094
    • Afferni, C.1    Iacovacci, P.2    Barletta, B.3    Di Felice, G.4    Tinghino, R.5    Mari, A.6    Pini, C.7
  • 4
    • 0031694207 scopus 로고    scopus 로고
    • Clinical relevance of carbohydrate allergen epitopes
    • Alberse, R.C. 1998. Clinical relevance of carbohydrate allergen epitopes. Allergy, 53(45 Suppl):54-57.
    • (1998) Allergy , vol.53 , Issue.45 SUPPL. , pp. 54-57
    • Alberse, R.C.1
  • 5
    • 0033836431 scopus 로고    scopus 로고
    • Structural biology of allergens
    • Alberse, R.C. 2000. Structural biology of allergens. J. Allergy Clin. Immunol., 106:228-238.
    • (2000) J. Allergy Clin. Immunol. , vol.106 , pp. 228-238
    • Alberse, R.C.1
  • 6
    • 0029094762 scopus 로고
    • Classification of rice allergenic protein cDNAs belonging to the α-amylase/trypsin inhibitor gene family
    • Alvarez, A.M., Adachi, T., Nakase, M., Aoki, N., Nakamura, R., and Matsuda, T. 1995.Classification of rice allergenic protein cDNAs belonging to the α-amylase/trypsin inhibitor gene family. Biochim. et Biophys. Acta, 1251:201-204.
    • (1995) Biochim. et Biophys. Acta , vol.1251 , pp. 201-204
    • Alvarez, A.M.1    Adachi, T.2    Nakase, M.3    Aoki, N.4    Nakamura, R.5    Matsuda, T.6
  • 7
    • 0030330364 scopus 로고    scopus 로고
    • Allergic reactions to foods
    • Anderson, J.A. 1996. Allergic reactions to foods. Crit. Rev. Food Sci. Nutr., 36(Suppl):S19-38.
    • (1996) Crit. Rev. Food Sci. Nutr. , vol.36 , Issue.SUPPL.
    • Anderson, J.A.1
  • 8
    • 0024966809 scopus 로고
    • Nucleotide sequences of the two high-molecular-weight glutenin genes from the D-genome of a hexaploid bread wheat, Triticum aestivum L. cv Cheyenne
    • Anderson, O.D., Greene, F.C., Yip, R.E., Halford, N.G., Shewry, P.R., and Malpica-Romero, J.-M. 1989. Nucleotide sequences of the two high-molecular-weight glutenin genes from the D-genome of a hexaploid bread wheat, Triticum aestivum L. cv Cheyenne. Nucleic Acids Research, 17:461-462.
    • (1989) Nucleic Acids Research , vol.17 , pp. 461-462
    • Anderson, O.D.1    Greene, F.C.2    Yip, R.E.3    Halford, N.G.4    Shewry, P.R.5    Malpica-Romero, J.-M.6
  • 9
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • "The Arabidopsis genome initiative"
    • "The Arabidopsis genome initiative" 2000. Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature, 408:796-815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 12
    • 0019156319 scopus 로고
    • Structure of actinidin after refinement at 1.7 Å resolution
    • Baker, E.N. 1980. Structure of actinidin after refinement at 1.7 Å resolution. J. Mol. Biol., 141:441-484.
    • (1980) J. Mol. Biol. , vol.141 , pp. 441-484
    • Baker, E.N.1
  • 13
    • 0030073025 scopus 로고    scopus 로고
    • Identification of the glycosylation site of a major soybean allergen, Gly m Bd 30K
    • Bando, N., Tsuji, H., Yamanishi, R., Nio, N., and Ogawa, T. 1996. Identification of the glycosylation site of a major soybean allergen, Gly m Bd 30K. Biosci. Biotechnol. Biochem., 60:347-8.
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 347-348
    • Bando, N.1    Tsuji, H.2    Yamanishi, R.3    Nio, N.4    Ogawa, T.5
  • 14
    • 0001639807 scopus 로고
    • Molecular analysis of γ-gliadin gene families at the complex Gli-1 locus of bread wheat (T. aestivum L.)
    • Bartels, D., Altosaar, I., Harberd, N.P., Barker, R.E, and Thompson, R.D. 1986. Molecular analysis of γ-gliadin gene families at the complex Gli-1 locus of bread wheat (T. aestivum L.), Theor. Appl. Genet., 72:845-853.
    • (1986) Theor. Appl. Genet. , vol.72 , pp. 845-853
    • Bartels, D.1    Altosaar, I.2    Harberd, N.P.3    Barker, R.E.4    Thompson, R.D.5
  • 15
    • 85004788238 scopus 로고
    • Studies on the specificity of human IgE-antibodies to the plant proteases papain and bromelain
    • Baur, X. 1979. Studies on the specificity of human IgE-antibodies to the plant proteases papain and bromelain. Clin. Allergy, 9:451-457.
    • (1979) Clin. Allergy , vol.9 , pp. 451-457
    • Baur, X.1
  • 16
    • 0029809256 scopus 로고    scopus 로고
    • IgE cross-reactivity between birch pollen, mugwort pollen and celery is due to at least three distinct cross-reacting allergens: Immunoblot investigation of the birch-mugwort-celery syndrome
    • Bauer, L., Ebner, C., Hirschwehr, R., Wuthrich, B., Pichler, C., Fritsch, R., Scheiner, O., and Kraft, D. 1996. IgE cross-reactivity between birch pollen, mugwort pollen and celery is due to at least three distinct cross-reacting allergens: Immunoblot investigation of the birch-mugwort-celery syndrome. Clin. Exp. Allergy, 26:1161-1170.
    • (1996) Clin. Exp. Allergy , vol.26 , pp. 1161-1170
    • Bauer, L.1    Ebner, C.2    Hirschwehr, R.3    Wuthrich, B.4    Pichler, C.5    Fritsch, R.6    Scheiner, O.7    Kraft, D.8
  • 17
    • 0034501229 scopus 로고    scopus 로고
    • Soybean glycinin Gl acidic chain shares IgE epitopes with peanut allergen Ara h 3
    • Beardslee, T.A., Zeece, M.G., Sarath, G., and Markwell, J.P. 2000. Soybean glycinin Gl acidic chain shares IgE epitopes with peanut allergen Ara h 3. Int. Arch. Allergy Immunol., 123:299-307.
    • (2000) Int. Arch. Allergy Immunol. , vol.123 , pp. 299-307
    • Beardslee, T.A.1    Zeece, M.G.2    Sarath, G.3    Markwell, J.P.4
  • 19
    • 0001686333 scopus 로고
    • Throughout the brewing process barley lipid transfer protein 1 is transformed into a more foam-promoting form
    • Bech, L. M., Vaag, P., Heinemann, B., and Breddam, K. 1995. Throughout the brewing process barley lipid transfer protein 1 is transformed into a more foam-promoting form. In: Procc. Congr. Eur. Brew. Com. Lisbon, pp. 561-568.
    • (1995) Procc. Congr. Eur. Brew. Com. Lisbon , pp. 561-568
    • Bech, L.M.1    Vaag, P.2    Heinemann, B.3    Breddam, K.4
  • 20
    • 0028535314 scopus 로고
    • PCR cloning and expression analysis of cDNAs encoding cysteine proteinases from germinating seeds of Vicia sativa L
    • Becker, C., Fischer, J., Nong, V.H., and Müntz, K. 1994. PCR cloning and expression analysis of cDNAs encoding cysteine proteinases from germinating seeds of Vicia sativa L. Plant Mol. Biol., 26:1207-1212.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1207-1212
    • Becker, C.1    Fischer, J.2    Nong, V.H.3    Müntz, K.4
  • 21
    • 0032480808 scopus 로고
    • Structural determinants of the bifunctional corn Hageman factor inhibitor: X-ray crystal structure at 1.95 angstrom resolution
    • Behnke, C.A., Yee, V.C., Le Trong, I., Pedersen, L.C., Stenkamp, R.E., Kim, S.S., Reeck, G.R., and Teller, D.C. 1988. Structural determinants of the bifunctional corn Hageman factor inhibitor: X-ray crystal structure at 1.95 angstrom resolution. Biochem., 37:15277-15288.
    • (1988) Biochem. , vol.37 , pp. 15277-15288
    • Behnke, C.A.1    Yee, V.C.2    Le Trong, I.3    Pedersen, L.C.4    Stenkamp, R.E.5    Kim, S.S.6    Reeck, G.R.7    Teller, D.C.8
  • 23
    • 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., and Sampson, H.A. (2002). Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing: Seed storage proteins as common food allergens. J. Allergy Clin. Immunol., 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
  • 25
    • 0001909782 scopus 로고    scopus 로고
    • The structure and biosynthesis of legume seed storage proteins: A biological solution to the storage of nitrogen in seeds
    • Boulter, D. and Croy, R.R.D. 1997. The structure and biosynthesis of legume seed storage proteins: A biological solution to the storage of nitrogen in seeds. Adv. Bot. Res., 27:1-84
    • (1997) Adv. Bot. Res. , vol.27 , pp. 1-84
    • Boulter, D.1    Croy, R.R.D.2
  • 26
    • 0033928258 scopus 로고    scopus 로고
    • Molecular and biochemical classification of plant-derived food allergens
    • Breiteneder, H. and Ebner, C. 2000. Molecular and biochemical classification of plant-derived food allergens. J. Allergy Clin. Immunol., 106:27-36.
    • (2000) J. Allergy Clin. Immunol. , vol.106 , pp. 27-36
    • Breiteneder, H.1    Ebner, C.2
  • 31
    • 0023891803 scopus 로고
    • Allergenicity of major component proteins of soybean determined by enzyme-linked immunosorbent assay (ELISA) and immunoblotting in children with atopic dermatitis and positive soy challenge
    • Burks, A.W., Brooks, J.R., and Sampson, H.A. 1988. Allergenicity of major component proteins of soybean determined by enzyme-linked immunosorbent assay (ELISA) and immunoblotting in children with atopic dermatitis and positive soy challenge. J. Allergy Clin. Immunol., 81:1135-1142.
    • (1988) J. Allergy Clin. Immunol. , vol.81 , pp. 1135-1142
    • Burks, A.W.1    Brooks, J.R.2    Sampson, H.A.3
  • 32
    • 0027049679 scopus 로고
    • Identification and characterization of a second major peanut allergen, Ara h III, with use of the sera of patients with atopic dermatitis and positive peanut challenge
    • Burks, A.W., Williams, L.W., Connaughton, C., Cockrell, G., O'Brien, T.J., and Helm, R.M. 1992b. Identification and characterization of a second major peanut allergen, Ara h III, with use of the sera of patients with atopic dermatitis and positive peanut challenge. J. Allergy Clin. Immunol., 90:962-969.
    • (1992) J. Allergy Clin. Immunol. , vol.90 , pp. 962-969
    • Burks, A.W.1    Williams, L.W.2    Connaughton, C.3    Cockrell, G.4    O'Brien, T.J.5    Helm, R.M.6
  • 33
    • 0026045826 scopus 로고
    • Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges
    • Burks, A.W., Williams, L.W., Helm, R.M., Connaughton, C., Cockrell, G., and O'Brien, T. 1991. Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges. J. Allergy Clin. Immunol., 88:172-179.
    • (1991) J. Allergy Clin. Immunol. , vol.88 , pp. 172-179
    • Burks, A.W.1    Williams, L.W.2    Helm, R.M.3    Connaughton, C.4    Cockrell, G.5    O'Brien, T.6
  • 34
    • 0027049679 scopus 로고
    • Identification and characterization of a second major peanut allergen, Ara h II, with use of the sera of patients with atopic dermatitis and positive peanut challenge
    • Burks, A.W., Williams, L.W., Connaughton, C., Cockrell, G., O'Brien, T.J., and Helm, R.M. 1992a. Identification and characterization of a second major peanut allergen, Ara h II, with use of the sera of patients with atopic dermatitis and positive peanut challenge. J. Allergy Clin. Immunol., 90:962-969.
    • (1992) J. Allergy Clin. Immunol. , vol.90 , pp. 962-969
    • Burks, A.W.1    Williams, L.W.2    Connaughton, C.3    Cockrell, G.4    O'Brien, T.J.5    Helm, R.M.6
  • 35
    • 0002710166 scopus 로고    scopus 로고
    • A multigene family of trypsin/α-amylase inhibitors from cereals
    • Eds., Shewry, P.R., and Casey, R., Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Carbonero, P. and García-Olmedo, F. 1999. A multigene family of trypsin/α-amylase inhibitors from cereals In: Seed Proteins. pp. 617-633. Eds., Shewry, P.R., and Casey, R., Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1999) Seed Proteins , pp. 617-633
    • Carbonero, P.1    García-Olmedo, F.2
  • 37
    • 0033199578 scopus 로고    scopus 로고
    • The crystal structure of a wheat nonspecific lipid transfer protein (ns-LTP1) complexed with two molecules of phospholipid at 2.1 angstrom resolution
    • Charvolin, D., Douliez, J.-P, Marion, D., Cohen-Addad, C., and Pebay-Peyroula, E. 1999. The crystal structure of a wheat nonspecific lipid transfer protein (ns-LTP1) complexed with two molecules of phospholipid at 2.1 angstrom resolution. Eur. J. Biochem., 264:562-568.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 562-568
    • Charvolin, D.1    Douliez, J.-P.2    Marion, D.3    Cohen-Addad, C.4    Pebay-Peyroula, E.5
  • 39
    • 0033401394 scopus 로고    scopus 로고
    • Allergenicity of maillard reaction products from peanut proteins
    • Chung, S.-Y. and Champagne, E.T. 1999. Allergenicity of maillard reaction products from peanut proteins. J. Agric. Food Chem., 47:5227-5231.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 5227-5231
    • Chung, S.-Y.1    Champagne, E.T.2
  • 40
    • 0001586896 scopus 로고
    • Localization of sequences in wheat endosperm protein genes which confer tissue-specific expression in tobacco
    • Colot, V., Robert, L.S., Kavanagh, T.A., Bevan, M.W., and Thompson, R.D. 1987. Localization of sequences in wheat endosperm protein genes which confer tissue-specific expression in tobacco. EMBO J., 6:3559-3564.
    • (1987) EMBO J. , vol.6 , pp. 3559-3564
    • Colot, V.1    Robert, L.S.2    Kavanagh, T.A.3    Bevan, M.W.4    Thompson, R.D.5
  • 41
    • 0031571267 scopus 로고    scopus 로고
    • Allergenic properties of ovomucoid in man
    • Cooke, S.K. and Sampson, H.A. 1997. Allergenic properties of ovomucoid in man. J. Immunol., 159:2026-2032.
    • (1997) J. Immunol. , vol.159 , pp. 2026-2032
    • Cooke, S.K.1    Sampson, H.A.2
  • 42
    • 0029902382 scopus 로고    scopus 로고
    • Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
    • Coulombe, R., Grochulski, P., Sivaraman, J., Menard, R., Mort, J.S., and Cygler, M. 1996. Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J., 15:5492-5503.
    • (1996) EMBO J. , vol.15 , pp. 5492-5503
    • Coulombe, R.1    Grochulski, P.2    Sivaraman, J.3    Menard, R.4    Mort, J.S.5    Cygler, M.6
  • 43
    • 0028989022 scopus 로고
    • Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium umfolding of bovine β-lactoglobulin
    • Creamer, L.K. 1995. Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium umfolding of bovine β-lactoglobulin. Biochem., 34:7170-7176.
    • (1995) Biochem. , vol.34 , pp. 7170-7176
    • Creamer, L.K.1
  • 44
    • 0020993171 scopus 로고
    • cDNA clones for Brassica napus seed storage proteins: Evidence from nucleotide sequence analysis that both submits of napin are cleaved from a precursor polypepetide
    • Crouch, M.T., Tenbarge, K.M., Simon, A.E., and Ferl, R. 1983. cDNA clones for Brassica napus seed storage proteins: Evidence from nucleotide sequence analysis that both submits of napin are cleaved from a precursor polypepetide. J. Mol. Appl. Genet., 2:273-283.
    • (1983) J. Mol. Appl. Genet. , vol.2 , pp. 273-283
    • Crouch, M.T.1    Tenbarge, K.M.2    Simon, A.E.3    Ferl, R.4
  • 46
    • 0000037420 scopus 로고
    • Purification and characterization of zein-degrading proteases from endosperm of germinating maize seeds
    • de Barros, E.G. and Larkins, B.A. 1990. Purification and characterization of zein-degrading proteases from endosperm of germinating maize seeds. Plant Physiol., 94:297-303.
    • (1990) Plant Physiol. , vol.94 , pp. 297-303
    • De Barros, E.G.1    Larkins, B.A.2
  • 47
    • 49349130487 scopus 로고
    • Legumin and vicilin, storage proteins of legume seeds
    • Derbyshire, E., Wright, D.J., and Boulter, D. 1976. Legumin and vicilin, storage proteins of legume seeds. Phytochem., 15:3-24.
    • (1976) Phytochem. , vol.15 , pp. 3-24
    • Derbyshire, E.1    Wright, D.J.2    Boulter, D.3
  • 48
    • 2642661481 scopus 로고    scopus 로고
    • Asthma caused by Ficus benjamina latex: Evidence of cross-reactivity with fig fruit and papain
    • Diez-Gomez, M.L., Quirce, S., Aragoneses. E., and Cuevas, M. 1998. Asthma caused by Ficus benjamina latex: Evidence of cross-reactivity with fig fruit and papain. Ann. Allergy Asthma Immunol., 80:24-30.
    • (1998) Ann. Allergy Asthma Immunol. , vol.80 , pp. 24-30
    • Diez-Gomez, M.L.1    Quirce, S.2    Aragoneses, E.3    Cuevas, M.4
  • 49
    • 0001698926 scopus 로고
    • Allergenicity of food proteins interacted with oxisized lipids in soybean-sensitivie individuals
    • Doke, S., Nakamura, R., and Toril, S. 1989. Allergenicity of food proteins interacted with oxisized lipids in soybean-sensitivie individuals. Agric. Biol. Chem., 53:1231-1235.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 1231-1235
    • Doke, S.1    Nakamura, R.2    Toril, S.3
  • 50
    • 0033853295 scopus 로고    scopus 로고
    • Structure, biological and technological function of lipid transfer proteins and indolines, the major lipid binding proteins from cereal kernels
    • Douliez, J.-P., Michon, T., Elmorjani, K., and Marion, D. 2000. Structure, biological and technological function of lipid transfer proteins and indolines, the major lipid binding proteins from cereal kernels. J. Cereal. Sci., 32:1-20.
    • (2000) J. Cereal. Sci. , vol.32 , pp. 1-20
    • Douliez, J.-P.1    Michon, T.2    Elmorjani, K.3    Marion, D.4
  • 51
    • 0030087809 scopus 로고    scopus 로고
    • Isolation and analysis of cDNAs encoding tomato cysteine proteases expressed during leaf senescence
    • Drake, R., John, I., Farrell, A., Cooper, W., Schuch, W., and Grierson, D. 1996. Isolation and analysis of cDNAs encoding tomato cysteine proteases expressed during leaf senescence. Plant Mol. Biol., 30:755-767.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 755-767
    • Drake, R.1    John, I.2    Farrell, A.3    Cooper, W.4    Schuch, W.5    Grierson, D.6
  • 52
    • 0031948520 scopus 로고    scopus 로고
    • Cupins: A new superfamily of functionally diverse proteins that include germins and plant storage proteins
    • Dunwell, J.M. 1998. Cupins: A new superfamily of functionally diverse proteins that include germins and plant storage proteins, Biotechnol. Genet. Eng. Rev., 15:1-32.
    • (1998) Biotechnol. Genet. Eng. Rev. , vol.15 , pp. 1-32
    • Dunwell, J.M.1
  • 53
    • 0031888149 scopus 로고    scopus 로고
    • Microbial relatives of seed storage proteins: Conservation of motifs in a functionally diverse superfamily of enzymes
    • Dunwell, J.M. and Gane, PJ. 1998. Microbial relatives of seed storage proteins: Conservation of motifs in a functionally diverse superfamily of enzymes. J. Mol. Evol., 46:147-154.
    • (1998) J. Mol. Evol. , vol.46 , pp. 147-154
    • Dunwell, J.M.1    Gane, P.J.2
  • 54
    • 0030590851 scopus 로고    scopus 로고
    • DNA cloning, sequence analysis and allergological characterization of Par j 2.0101, a new major allergen of the Parietaria judaica pollen
    • Duro, G., Colombo, P., Costa, M.A., Izzo, V., Porcasi, R., Di Fiore, R., Locorotondo, G., Mirisola, M.G., Cocchiara, R., and Geraci, D. 1996. cDNA cloning, sequence analysis and allergological characterization of Par j 2.0101, a new major allergen of the Parietaria judaica pollen. FEBS Letts., 399:295-295.
    • (1996) FEBS Letts. , vol.399 , pp. 295-295
    • Duro, G.1    Colombo, P.2    Costa, M.A.3    Izzo, V.4    Porcasi, R.5    Di Fiore, R.6    Locorotondo, G.7    Mirisola, M.G.8    Cocchiara, R.9    Geraci, D.10
  • 55
    • 0030569330 scopus 로고    scopus 로고
    • Disulphide structure of a sunflower seed albumin: Conserved and variant disulphide bonds in the cereal prolamin superfamily
    • Egorov, T.A., Odintsova, T.I., Musolyamov, A.Kh., Fido, R., Tatham, A.S., and Shewry, P.R. 1996. Disulphide structure of a sunflower seed albumin: Conserved and variant disulphide bonds in the cereal prolamin superfamily. FEBS Letts., 396:285-288.
    • (1996) FEBS Letts. , vol.396 , pp. 285-288
    • Egorov, T.A.1    Odintsova, T.I.2    Musolyamov, A.K.3    Fido, R.4    Tatham, A.S.5    Shewry, P.R.6
  • 56
    • 0029853742 scopus 로고    scopus 로고
    • Identification of unique peanut and soy allergens in sera adsorbed with cross-reacting antibodies
    • Eigenmann, P.A., Burks, A.W., Bannon, G.A., and Sampson, H.A. 1996. Identification of unique peanut and soy allergens in sera adsorbed with cross-reacting antibodies. J. Allergy Clin. Immunol., 98:969-978.
    • (1996) J. Allergy Clin. Immunol. , vol.98 , pp. 969-978
    • Eigenmann, P.A.1    Burks, A.W.2    Bannon, G.A.3    Sampson, H.A.4
  • 60
    • 0033624194 scopus 로고    scopus 로고
    • The families of papain- and legumain-like cysteine proteinases from embryonic axes and cotyledons of Vicia seeds: Developmental patterns, intracelular localization and functions in globulin proteolysis
    • Fischer, J., Becker, C., Hillmer, S., Horstmann, C., Neubohn, B., Schlereth, A., Senyuk, V., Shutov, A. and Müntz, K. 2000. The families of papain- and legumain-like cysteine proteinases from embryonic axes and cotyledons of Vicia seeds: Developmental patterns, intracelular localization and functions in globulin proteolysis. Plant Mol. Biol., 43:83-101.
    • (2000) Plant Mol. Biol. , vol.43 , pp. 83-101
    • Fischer, J.1    Becker, C.2    Hillmer, S.3    Horstmann, C.4    Neubohn, B.5    Schlereth, A.6    Senyuk, V.7    Shutov, A.8    Müntz, K.9
  • 61
    • 0024083829 scopus 로고
    • Papain anaphylaxis: A case report
    • Freye, H.B. 1988. Papain anaphylaxis: A case report. Allergy Proc., 9:571-574.
    • (1988) Allergy Proc. , vol.9 , pp. 571-574
    • Freye, H.B.1
  • 62
    • 0028322135 scopus 로고
    • Kiwi fruit allergy - A new birch pollen-associated food allergy
    • Gall, H., Kalveram, K.J., Forck, G., and Sterry, W. 1994, Kiwi fruit allergy - A new birch pollen-associated food allergy. J. Allergy Clin. Immunol., 94, 70-76.
    • (1994) J. Allergy Clin. Immunol. , vol.94 , pp. 70-76
    • Gall, H.1    Kalveram, K.J.2    Forck, G.3    Sterry, W.4
  • 63
    • 0031979636 scopus 로고    scopus 로고
    • Modeling based on the structure of vicilins predicts a histidine cluster in the active site of oxalate oxidase
    • Gane, P.J., Dunwell, J.M., and Warwicker, J. 1998. Modeling based on the structure of vicilins predicts a histidine cluster in the active site of oxalate oxidase. J. Mol. Evol., 46:488-493.
    • (1998) J. Mol. Evol. , vol.46 , pp. 488-493
    • Gane, P.J.1    Dunwell, J.M.2    Warwicker, J.3
  • 66
    • 0030833172 scopus 로고    scopus 로고
    • A novel thermostable inhibitor of trypsin and subtilisin from the seeds of Brassica nigra: Amino acid sequence, inhibitory and spectroscopic properties and thermostability
    • Genov, N., Goshev, I., Nikolova, D., Georgieva, D.N., Filippi, B., and Svendsen, I. 1997. A novel thermostable inhibitor of trypsin and subtilisin from the seeds of Brassica nigra: Amino acid sequence, inhibitory and spectroscopic properties and thermostability. Biochim. Biophys. Acta, 134:157-164.
    • (1997) Biochim. Biophys. Acta , vol.134 , pp. 157-164
    • Genov, N.1    Goshev, I.2    Nikolova, D.3    Georgieva, D.N.4    Filippi, B.5    Svendsen, I.6
  • 67
    • 0344928902 scopus 로고
    • Hypersensibilitié aux virus, température et protéines solubles chez le Nicotiana Xanthi-n c. Apparition de nouvelles macromolécules lors de la répression de la synthése virale
    • Gianinazzi, S., Martin, C., and Vallée, J.C. 1969. Hypersensibilitié aux virus, température et protéines solubles chez le Nicotiana Xanthi-n c. Apparition de nouvelles macromolécules lors de la répression de la synthése virale. Compte rendu de l'Académie des Sciences de Paris D, 268:800-802.
    • (1969) Compte Rendu de L'Académie des Sciences de Paris D , vol.268 , pp. 800-802
    • Gianinazzi, S.1    Martin, C.2    Vallée, J.C.3
  • 68
    • 0027973368 scopus 로고
    • Three-dimensional structure in solution of a wheat lipid-transfer protein from multidimensional 1H-NMR data. A new folding for lipid carriers
    • Gincel, E., Simorre, J.P., Caille, A., Marion, D., Ptak, M., and Vovelle, F. 1994. Three-dimensional structure in solution of a wheat lipid-transfer protein from multidimensional 1H-NMR data. A new folding for lipid carriers. Eur. J. Biochem., 226:413-422.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 413-422
    • Gincel, E.1    Simorre, J.P.2    Caille, A.3    Marion, D.4    Ptak, M.5    Vovelle, F.6
  • 69
    • 0031105881 scopus 로고    scopus 로고
    • A cysteine endopeptidase isolated from castor bean endosperm microbodies processes the glyoxysomal malate dehydrongenase precursor protein
    • Gietl C., Wimmer, B., Adamec, J., and Kalousek, F. 1997. A cysteine endopeptidase isolated from castor bean endosperm microbodies processes the glyoxysomal malate dehydrongenase precursor protein. Plant Physiol., 113:863-871.
    • (1997) Plant Physiol. , vol.113 , pp. 863-871
    • Gietl, C.1    Wimmer, B.2    Adamec, J.3    Kalousek, F.4
  • 70
    • 0032080910 scopus 로고
    • Comparison of solution and crystal structures of maize nonspecific lipid transfer protein: A model for a potential in vivo lipid carrier protein
    • Gomar, J., Sodano, P., Sy, D., Shin, D.H., Lee, J.Y., Sub, S.W., Marion, D., Vovelle, F., and Ptak, M. 1988. Comparison of solution and crystal structures of maize nonspecific lipid transfer protein: A model for a potential in vivo lipid carrier protein. Proteins-Struct. Fund. Genet., 31:160-171.
    • (1988) Proteins-struct. Fund. Genet. , vol.31 , pp. 160-171
    • Gomar, J.1    Sodano, P.2    Sy, D.3    Shin, D.H.4    Lee, J.Y.5    Sub, S.W.6    Marion, D.7    Vovelle, F.8    Ptak, M.9
  • 71
    • 0030005766 scopus 로고    scopus 로고
    • Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds
    • Gomar, J., Petit, M.C., Sodano, P., Sy, D., Marion, D., Kader, J.C., Vovelle, F., and Ptak, M. 1996. Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds. Protein Sci., 5:565-577.
    • (1996) Protein Sci. , vol.5 , pp. 565-577
    • Gomar, J.1    Petit, M.C.2    Sodano, P.3    Sy, D.4    Marion, D.5    Kader, J.C.6    Vovelle, F.7    Ptak, M.8
  • 73
  • 74
    • 0033167935 scopus 로고    scopus 로고
    • Grass group I allergens (beta-expansins) are novel, papain-related proteinases
    • Grobe, K., Becker, W.M., Schlaak, M., and Petersen, A. 1999. Grass group I allergens (beta-expansins) are novel, papain-related proteinases. Eur. J. Biochem., 263:33-40.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 33-40
    • Grobe, K.1    Becker, W.M.2    Schlaak, M.3    Petersen, A.4
  • 75
    • 0030587773 scopus 로고    scopus 로고
    • The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft
    • Groves, M.R., Taylor, M.A., Scott, M., Cummings, N.J., Pickersgill, R.W., and Jenkins, J.A. 1996. The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft. Structure, 4:1193-1203.
    • (1996) Structure , vol.4 , pp. 1193-1203
    • Groves, M.R.1    Taylor, M.A.2    Scott, M.3    Cummings, N.J.4    Pickersgill, R.W.5    Jenkins, J.A.6
  • 83
    • 0025241366 scopus 로고
    • Identification of soybean allergens by immunoblotting with sera from soy-allergic adults
    • Herian, A.M., Taylor, S.L., and Bush, R.K. 1990. Identification of soybean allergens by immunoblotting with sera from soy-allergic adults. Int. Arch. Allergy Appl. Immunol., 92:193-198.
    • (1990) Int. Arch. Allergy Appl. Immunol. , vol.92 , pp. 193-198
    • Herian, A.M.1    Taylor, S.L.2    Bush, R.K.3
  • 84
    • 0028818335 scopus 로고
    • A major house dust mite allergen disrupts the immunoglobulin E network by selectively cleaving CD23: Innate protection by antiproteases
    • Hewitt, C.R., Brown, A.P., Hart, B.J., and Pritchard, D.I. 1995. A major house dust mite allergen disrupts the immunoglobulin E network by selectively cleaving CD23: Innate protection by antiproteases. J. Exp. Med., 182:1537-1544.
    • (1995) J. Exp. Med. , vol.182 , pp. 1537-1544
    • Hewitt, C.R.1    Brown, A.P.2    Hart, B.J.3    Pritchard, D.I.4
  • 87
    • 0033909638 scopus 로고    scopus 로고
    • Plant allergens and pathogenesis-related proteins
    • Hoffmann-Sommergruber, K. 2000. Plant allergens and pathogenesis-related proteins. Int. Arch. Allergy Immunol., 122:155-166.
    • (2000) Int. Arch. Allergy Immunol. , vol.122 , pp. 155-166
    • Hoffmann-Sommergruber, K.1
  • 88
    • 0036724414 scopus 로고    scopus 로고
    • The rise of atopy and links to infection
    • Hopkin, J.M. (2002). The rise of atopy and links to infection. Allergy, 57(Suppl 72):5-9.
    • (2002) Allergy , vol.57 , Issue.SUPPL. 72 , pp. 5-9
    • Hopkin, J.M.1
  • 89
    • 0034929179 scopus 로고    scopus 로고
    • Isolation and characterization of wheat ω-gliadin genes
    • Hsia, C.C. and Anderson, O.D. 2001. Isolation and characterization of wheat ω-gliadin genes. Theor. Appl. Genet., 103:37-44.
    • (2001) Theor. Appl. Genet. , vol.103 , pp. 37-44
    • Hsia, C.C.1    Anderson, O.D.2
  • 90
    • 0032517293 scopus 로고    scopus 로고
    • Analysis of thermal stability of soy globulins using monoclonal antibodies
    • Huang, L., Mills, E.N.C., and Morgan, M.R.A. 1998. Analysis of thermal stability of soy globulins using monoclonal antibodies. Biochim. Biophys. Acta, 1388:215-226.
    • (1998) Biochim. Biophys. Acta , vol.1388 , pp. 215-226
    • Huang, L.1    Mills, E.N.C.2    Morgan, M.R.A.3
  • 91
    • 0025375416 scopus 로고
    • The Ricinus communis 2S albumin precursor: A single preprotein may be processed into two different heterodimeric storage proteins
    • Irwin, S.D., Keen, J.N., Findlay, J.B.C., and Lord, J.M. 1990. The Ricinus communis 2S albumin precursor: A single preprotein may be processed into two different heterodimeric storage proteins. Mol. Gen. Genet., 222:400-408.
    • (1990) Mol. Gen. Genet. , vol.222 , pp. 400-408
    • Irwin, S.D.1    Keen, J.N.2    Findlay, J.B.C.3    Lord, J.M.4
  • 92
    • 0018566969 scopus 로고
    • Complete structure of the carbohydrate moiety of stem bromelain. An application of the almond glycopeptidase for structural studies of glycopeptides
    • Ishihara, H., Takahashi, N., Oguri, S., and Tejima, S. (1979). Complete structure of the carbohydrate moiety of stem bromelain. An application of the almond glycopeptidase for structural studies of glycopeptides. J. Biol. Chem, 254:10715-10719.
    • (1979) J. Biol. Chem , vol.254 , pp. 10715-10719
    • Ishihara, H.1    Takahashi, N.2    Oguri, S.3    Tejima, S.4
  • 93
    • 0026586668 scopus 로고
    • Nucleotide sequence of a cDNA clone encoding a major allergenic a protein in rice seeds. Homology of the deduced amino acid sequence with members of α-amylase/trypsin inhibitor family
    • Izumi, H., Adachi, T., Fujii, N., Matsuda, T., Nakamura, R., Tanaka, K., Urisu, A., and Kurosawa, Y. 1992. Nucleotide sequence of a cDNA clone encoding a major allergenic a protein in rice seeds. Homology of the deduced amino acid sequence with members of α-amylase/trypsin inhibitor family. FEBS Letts., 301:213-216.
    • (1992) FEBS Letts. , vol.301 , pp. 213-216
    • Izumi, H.1    Adachi, T.2    Fujii, N.3    Matsuda, T.4    Nakamura, R.5    Tanaka, K.6    Urisu, A.7    Kurosawa, Y.8
  • 94
    • 0029347066 scopus 로고    scopus 로고
    • Association of a 33-kD cysteine proteinase found in corn callus with the inhibition of fall armyworm larval growth
    • Jiang, B.-H., Siregar, U., Willeford, K.O., Luthe, D.S., and Williams, W.P. 1996. Association of a 33-kD cysteine proteinase found in corn callus with the inhibition of fall armyworm larval growth. Plant Physiol., 108:1631-1640.
    • (1996) Plant Physiol. , vol.108 , pp. 1631-1640
    • Jiang, B.-H.1    Siregar, U.2    Willeford, K.O.3    Luthe, D.S.4    Williams, W.P.5
  • 96
    • 0029310609 scopus 로고
    • Ethylene-regulated expression of a carnation cysteine proteinase during flower petal senescence
    • Jones, M.L., Larsen, P.B., and Woodson, W.R. 1995. Ethylene-regulated expression of a carnation cysteine proteinase during flower petal senescence. Plant Mol. Biol., 28:505-512.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 505-512
    • Jones, M.L.1    Larsen, P.B.2    Woodson, W.R.3
  • 97
    • 0041151794 scopus 로고
    • Formation of digestion intermediate of glycinin
    • Kamata Y. and Shibasaki, K. 1978. Formation of digestion intermediate of glycinin. Agric. Biol. Chem., 42:2323-2329.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 2323-2329
    • Kamata, Y.1    Shibasaki, K.2
  • 98
    • 0025113503 scopus 로고
    • Molecular cloning of a protein associated with soybean seed oil bodies that is similar to thiol proteases of the papain family
    • Kalinski, A., Weisemann, J.M., Matthews, B.F., and Herman, E.M. 1990. Molecular cloning of a protein associated with soybean seed oil bodies that is similar to thiol proteases of the papain family. J. Biol. Chem., 265:13843-13848.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13843-13848
    • Kalinski, A.1    Weisemann, J.M.2    Matthews, B.F.3    Herman, E.M.4
  • 102
    • 0033981221 scopus 로고    scopus 로고
    • The polyprotein lipid binding proteins of nematodes
    • Kennedy, M.W. 2000. The polyprotein lipid binding proteins of nematodes. Biochim. Biophys. Acta, 1476:149-164.
    • (2000) Biochim. Biophys. Acta , vol.1476 , pp. 149-164
    • Kennedy, M.W.1
  • 104
  • 105
    • 0027552820 scopus 로고
    • The three-dimensional structure of canavalin from jack bean (Canavalia ensiformis)
    • Ko, T.P., Ng, J.D., and McPherson, A. 1993. The three-dimensional structure of canavalin from jack bean (Canavalia ensiformis). Plant Physiol., 101:729-744.
    • (1993) Plant Physiol. , vol.101 , pp. 729-744
    • Ko, T.P.1    Ng, J.D.2    McPherson, A.3
  • 106
    • 0034096545 scopus 로고    scopus 로고
    • The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 A resolution
    • Ko, T.P., Day, J., and McPherson, A. 2000. The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 A resolution, Acta Crystallogr. D Biol. Crystallogr., 56:411-420.
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 411-420
    • Ko, T.P.1    Day, J.2    McPherson, A.3
  • 107
    • 0026029034 scopus 로고
    • Amino acid and cDNA sequences of a methionine-rich 2S protein from sunflower seed (Helianthus amuus L.)
    • Kortt, A.A., Caldwell, J.B., Lilley, G.G., and Higgins, T.J.V. 1991. Amino acid and cDNA sequences of a methionine-rich 2S protein from sunflower seed (Helianthus amuus L.). Eur. J. Bioch., 195:329-334.
    • (1991) Eur. J. Bioch. , vol.195 , pp. 329-334
    • Kortt, A.A.1    Caldwell, J.B.2    Lilley, G.G.3    Higgins, T.J.V.4
  • 108
    • 0022419276 scopus 로고
    • Molecular evolution of the seed storage proteins of barley, rye and wheat
    • Kreis, M., Forde, E.G., Rahman, S., Miflin, B.J., and Shewry, P.R. 1985. Molecular evolution of the seed storage proteins of barley, rye and wheat. J. Mol. Biol., 183:499-502.
    • (1985) J. Mol. Biol. , vol.183 , pp. 499-502
    • Kreis, M.1    Forde, E.G.2    Rahman, S.3    Miflin, B.J.4    Shewry, P.R.5
  • 109
    • 0034235923 scopus 로고    scopus 로고
    • Oxalate oxidases and differentiating surface structure in wheat: Germins
    • Lane, B.C. 2000. Oxalate oxidases and differentiating surface structure in wheat: Germins. Biochem. J., 349:309-321.
    • (2000) Biochem. J. , vol.349 , pp. 309-321
    • Lane, B.C.1
  • 112
    • 0028361114 scopus 로고
    • Structure of phaseolin at 2.2 Å resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins
    • Lawrence, M.C., Izard, T., Beuchat, M., Blagrove, R.J., and Colman, P.M. 1994. Structure of phaseolin at 2.2 Å resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. J. Mol. Biol., 238:748-776.
    • (1994) J. Mol. Biol. , vol.238 , pp. 748-776
    • Lawrence, M.C.1    Izard, T.2    Beuchat, M.3    Blagrove, R.J.4    Colman, P.M.5
  • 113
    • 0032548996 scopus 로고
    • Rice non-specific lipid transfer protein: The 1.6 angstrom crystal structure in the unliganded state reveals a small hydrophobic cavity
    • Lee, J.Y., Min, K., Cha, H., Shin, D.H., Hwang, K.Y., and Sun, S.W. 1988. Rice non-specific lipid transfer protein: The 1.6 angstrom crystal structure in the unliganded state reveals a small hydrophobic cavity. J. Mol. Biol., 276:437-448.
    • (1988) J. Mol. Biol. , vol.276 , pp. 437-448
    • Lee, J.Y.1    Min, K.2    Cha, H.3    Shin, D.H.4    Hwang, K.Y.5    Sun, S.W.6
  • 114
    • 0031975276 scopus 로고    scopus 로고
    • Allergens in pepper and paprika. Immunologic investigation of the celery-birch-mugwort-spice syndrome
    • Leitner, A., Jensen-Jarolim, E., Grimm, R., Wuthrich, B., Ebner H., Scheiner, O., Kraft, D., and Ebner, C. 1998. Allergens in pepper and paprika. Immunologic investigation of the celery-birch-mugwort-spice syndrome. Allergy, 53:36-41.
    • (1998) Allergy , vol.53 , pp. 36-41
    • Leitner, A.1    Jensen-Jarolim, E.2    Grimm, R.3    Wuthrich, B.4    Ebner, H.5    Scheiner, O.6    Kraft, D.7    Ebner, C.8
  • 115
    • 0035910388 scopus 로고    scopus 로고
    • Surprisingly high stability of lipid transfer protein, LTP1, towards denaturant, heat and proteases
    • Lindorff-Larsen, K., and Winther, J.R. 2001. Surprisingly high stability of lipid transfer protein, LTP1, towards denaturant, heat and proteases. FEBS Letts., 488:145-148.
    • (2001) FEBS Letts. , vol.488 , pp. 145-148
    • Lindorff-Larsen, K.1    Winther, J.R.2
  • 116
    • 0001478561 scopus 로고
    • Amino acid sequence of conglutin δ, a sulfurrich seed protein of Lupinus angustifolius L. Sequence homology with the C-III α-amylase inhibitor from wheat
    • Lilley, G.G. and Inglis, A.S. 1986. Amino acid sequence of conglutin δ, a sulfurrich seed protein of Lupinus angustifolius L. Sequence homology with the C-III α-amylase inhibitor from wheat. FEBS Letts., 195:235-241.
    • (1986) FEBS Letts. , vol.195 , pp. 235-241
    • Lilley, G.G.1    Inglis, A.S.2
  • 117
    • 0027530456 scopus 로고
    • Purification, complete amino acid sequence and structural characterization of the heat-stable sweet protein, mabinlin II
    • Liu, X., Maeda, S., Hu, Z., Aiuchi, T., Nakaya, K., and Kurihara, Y. 1993. Purification, complete amino acid sequence and structural characterization of the heat-stable sweet protein, mabinlin II. Eur. J. Biochem., 211:281-287.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 281-287
    • Liu, X.1    Maeda, S.2    Hu, Z.3    Aiuchi, T.4    Nakaya, K.5    Kurihara, Y.6
  • 121
    • 0029125701 scopus 로고
    • Protease activation during apoptosis: Death by a thousand cuts?
    • Martin, S.J. and Green, D.R. 1995. Protease activation during apoptosis: Death by a thousand cuts? Cell, 82:349-352.
    • (1995) Cell , vol.82 , pp. 349-352
    • Martin, S.J.1    Green, D.R.2
  • 123
    • 0023692298 scopus 로고
    • Primary structure of the major allergen of yellow mustard (Sinapis alba L.) seed, Sin a I
    • Menendez-Arias, L., Moneo, I., Dominguez, J., and Rodriguez, R. 1988. Primary structure of the major allergen of yellow mustard (Sinapis alba L.) seed, Sin a I. Eur. J. Biochem., 177:159-166.
    • (1988) Eur. J. Biochem. , vol.177 , pp. 159-166
    • Menendez-Arias, L.1    Moneo, I.2    Dominguez, J.3    Rodriguez, R.4
  • 124
    • 0030152393 scopus 로고    scopus 로고
    • A major cysteine proteinase, EPB, in germinating barley seeds: Structure of two intronless genes and regulation of expression
    • Mikkonen, A., Porali, I., Cercos, M., and Ho, T.-H.D. 1996. A major cysteine proteinase, EPB, in germinating barley seeds: Structure of two intronless genes and regulation of expression. Plant Mol. Biol., 31:239-254.
    • (1996) Plant Mol. Biol. , vol.31 , pp. 239-254
    • Mikkonen, A.1    Porali, I.2    Cercos, M.3    Ho, T.-H.D.4
  • 125
  • 126
    • 0030751220 scopus 로고    scopus 로고
    • Characterization of allergens in kiwi fruit and detection of cross-reactivities with allergens of birch pollen and related fruits
    • Möller, M., Pascke, A., Vieluf, D., Kayma, M., Vieths, S., and Steinhart, H. 1997. Characterization of allergens in kiwi fruit and detection of cross-reactivities with allergens of birch pollen and related fruits. Food Agric. Immunol., 9:107-121.
    • (1997) Food Agric. Immunol. , vol.9 , pp. 107-121
    • Möller, M.1    Pascke, A.2    Vieluf, D.3    Kayma, M.4    Vieths, S.5    Steinhart, H.6
  • 129
    • 0033563080 scopus 로고    scopus 로고
    • Sequence-divergent units of the ABA-1 polyprotein array of the nematode Ascaris sum have similar fatty-acid- And retinol-binding properties but different binding-site environments
    • Moore, J., McDermott, L., Price, N.C., Kelly, S.M., Cooper, A., and Kennedy, M.W. 1999. Sequence-divergent units of the ABA-1 polyprotein array of the nematode Ascaris sum have similar fatty-acid- and retinol-binding properties but different binding-site environments. Biochem. J., 340:337-343.
    • (1999) Biochem. J. , vol.340 , pp. 337-343
    • Moore, J.1    McDermott, L.2    Price, N.C.3    Kelly, S.M.4    Cooper, A.5    Kennedy, M.W.6
  • 130
    • 0018890096 scopus 로고
    • Kunitz soybean trypsin inhibitor; A specific allergen in food anaphylaxis
    • Moroz, L.A. and Yang, W.H. 1980. Kunitz soybean trypsin inhibitor; a specific allergen in food anaphylaxis. N. Engl. J. Med., 302:1126-1128.
    • (1980) N. Engl. J. Med. , vol.302 , pp. 1126-1128
    • Moroz, L.A.1    Yang, W.H.2
  • 131
    • 0003754307 scopus 로고
    • Synthesis, processing and targeting of legume seed proteins
    • Eds., Shewry, PR. and Stobart, K., Oxford University Press, Oxford
    • Müntz, K., Jung, R., and Saalbach, G. 1993. Synthesis, processing and targeting of legume seed proteins. In: Seed Storage Compounds: Biosynthesis, Interactions, and Manipulations, pp. 128-146. Eds., Shewry, PR. and Stobart, K., Oxford University Press, Oxford.
    • (1993) Seed Storage Compounds: Biosynthesis, Interactions, and Manipulations , pp. 128-146
    • Müntz, K.1    Jung, R.2    Saalbach, G.3
  • 132
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A. G., Brenner, S. E., Hubbard, T., and Chothia, C. 1995. SCOP: A structural classification of proteins database for the investigation of sequences and structures J. Mol. Biol., 247:536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 133
    • 0030221939 scopus 로고    scopus 로고
    • Rice allergenic protein and molecular-genetic approach for hypoallergenic rice
    • Nakamura, R., and Matsuda,.T. 1996. Rice allergenic protein and molecular-genetic approach for hypoallergenic rice. Biosci. Biotech. Biochem., 60:1215-1221.
    • (1996) Biosci. Biotech. Biochem. , vol.60 , pp. 1215-1221
    • Nakamura, R.1    Matsuda, T.2
  • 136
    • 0036338765 scopus 로고    scopus 로고
    • Varietal difference in actinidin concentration and protease activity in the kiwi fruit juice
    • Nishiyama, I. and Oota, T. 2002. Varietal difference in actinidin concentration and protease activity in the kiwi fruit juice. J. Jap. Soc. Food Sci. Technol., 49:401-408.
    • (2002) J. Jap. Soc. Food Sci. Technol. , vol.49 , pp. 401-408
    • Nishiyama, I.1    Oota, T.2
  • 137
    • 0027496855 scopus 로고
    • Disulfide bridge structure of the heat-stable sweet protein mabinlin II
    • Nirasawa, S., Liu, C., Nishino, T., and Kurihara, Y. 1993. Disulfide bridge structure of the heat-stable sweet protein mabinlin II, Biochim. Biophys. Acta., 1202:277-280.
    • (1993) Biochim. Biophys. Acta. , vol.1202 , pp. 277-280
    • Nirasawa, S.1    Liu, C.2    Nishino, T.3    Kurihara, Y.4
  • 139
    • 0030815231 scopus 로고    scopus 로고
    • Tertiary and quaternary structures of 0.19 alpha-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 angstrom resolution
    • Oda, Y., Matsunaga, T., Fukuyama, K., Miyazaki, T., and Morimoto, T. 1997. Tertiary and quaternary structures of 0.19 alpha-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 angstrom resolution. Biochemistry, 36:13503-13511.
    • (1997) Biochemistry , vol.36 , pp. 13503-13511
    • Oda, Y.1    Matsunaga, T.2    Fukuyama, K.3    Miyazaki, T.4    Morimoto, T.5
  • 140
    • 0027620748 scopus 로고
    • Identification of the soyabean allergenic proteins, Gly m Bd 30K, with the soybean seed 34kDa oil-body-associated protein
    • Ogawa, T., Tsuji, H., Bando, N., Kitamura, K., Zhu, Y.-L., Hirano, H., and Nishikawa, K. 1993. Identification of the soyabean allergenic proteins, Gly m Bd 30K, with the soybean seed 34kDa oil-body-associated protein. Biosci. Biotech. Biochem., 57:1030-1033.
    • (1993) Biosci. Biotech. Biochem. , vol.57 , pp. 1030-1033
    • Ogawa, T.1    Tsuji, H.2    Bando, N.3    Kitamura, K.4    Zhu, Y.-L.5    Hirano, H.6    Nishikawa, K.7
  • 142
    • 5444274973 scopus 로고    scopus 로고
    • Identification of IgE-binding epitopes of the Brazil nut 2S albumin allergen
    • Oommen, A., Kelly, J., Benson, A., and Hefle, S. 2000. Identification of IgE-binding epitopes of the Brazil nut 2S albumin allergen. J. Allergy Clin. Immunol., 105:402.
    • (2000) J. Allergy Clin. Immunol. , vol.105 , pp. 402
    • Oommen, A.1    Kelly, J.2    Benson, A.3    Hefle, S.4
  • 156
    • 0029884666 scopus 로고    scopus 로고
    • Skin testing with recombinant allergens rBet v 1 and birch profilin, rBet v 2: Diagnostic value for birch pollen and associated allergies
    • Pauli, G., Oster, J.P., Deviller, P., Heiss, S., Bessot, J.C., Susani, M., Ferreira, F., Kraft, D., and Valenta, R. 1996. Skin testing with recombinant allergens rBet v 1 and birch profilin, rBet v 2: Diagnostic value for birch pollen and associated allergies. J. Allergy Clin. Immunol., 97:1100-1109.
    • (1996) J. Allergy Clin. Immunol. , vol.97 , pp. 1100-1109
    • Pauli, G.1    Oster, J.P.2    Deviller, P.3    Heiss, S.4    Bessot, J.C.5    Susani, M.6    Ferreira, F.7    Kraft, D.8    Valenta, R.9
  • 157
    • 0033868878 scopus 로고    scopus 로고
    • A unique 22-kD cysteine proteinase accumulates in response to larval feeding in maize genotypes resistant to fall armyworm and other lepidoptera
    • Pechan, T., Ye, L., Chang, Y.-M., Mitra, A., Lin, L., Davis, F.M., Williams, W.P., and Luthe, D.S. 2000. A unique 22-kD cysteine proteinase accumulates in response to larval feeding in maize genotypes resistant to fall armyworm and other lepidoptera. The Plant Cell, 12:1031-1040.
    • (2000) The Plant Cell , vol.12 , pp. 1031-1040
    • Pechan, T.1    Ye, L.2    Chang, Y.-M.3    Mitra, A.4    Lin, L.5    Davis, F.M.6    Williams, W.P.7    Luthe, D.S.8
  • 158
    • 0034667892 scopus 로고    scopus 로고
    • Selective neoglycosylation increases the structural stability of vicilin, the 7S storage protein of pea seeds
    • Pedrosa, C., De Felice, F.G., Trisciuzzi, C., and Ferreira, S.T. 2000. Selective neoglycosylation increases the structural stability of vicilin, the 7S storage protein of pea seeds. Arch. Biochem. Biophys., 15:203-210.
    • (2000) Arch. Biochem. Biophys. , vol.15 , pp. 203-210
    • Pedrosa, C.1    De Felice, F.G.2    Trisciuzzi, C.3    Ferreira, S.T.4
  • 159
    • 0001289346 scopus 로고
    • The effect of thermal and proteolytic processing on glycinin, the 11S globulin of soy (Glycine max) - A study utilising monoclonal and polyclonal antibodies
    • Plumb, G.W., Mills, E.N.C., Tatton, M.J., D'Ursel, C.C.M., Lambert, N., and Morgan, M.R.A. 1994. The effect of thermal and proteolytic processing on glycinin, the 11S globulin of soy (Glycine max) - a study utilising monoclonal and polyclonal antibodies. J. Agric. Food Chem., 42:705-710.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 705-710
    • Plumb, G.W.1    Mills, E.N.C.2    Tatton, M.J.3    D'Ursel, C.C.M.4    Lambert, N.5    Morgan, M.R.A.6
  • 161
    • 0027539294 scopus 로고
    • Purification and sequencing of radish seed calmodlin antagonists phosphorylated by calcium-dependent protein kinase
    • Polya, G.M., Chandra, S., and Condron, R. 1993. Purification and sequencing of radish seed calmodlin antagonists phosphorylated by calcium-dependent protein kinase. Plant Physiol., 101:545-551.
    • (1993) Plant Physiol. , vol.101 , pp. 545-551
    • Polya, G.M.1    Chandra, S.2    Condron, R.3
  • 162
    • 0033082341 scopus 로고    scopus 로고
    • Solution structure of a lipid transfer protein extracted from rice seeds - Comparison with homologous proteins
    • Poznanski, J., Sodano, P., Suh, S.W., Lee, J.Y., Ptak, M., and Vovelle, F. 1999. Solution structure of a lipid transfer protein extracted from rice seeds - Comparison with homologous proteins. Euro. J. Biochem., 259:692-708.
    • (1999) Euro. J. Biochem. , vol.259 , pp. 692-708
    • Poznanski, J.1    Sodano, P.2    Suh, S.W.3    Lee, J.Y.4    Ptak, M.5    Vovelle, F.6
  • 164
    • 0027479821 scopus 로고
    • Evolutionary families of peptidases
    • Rawlings, N.D. and Barrett, A.J. 1993. Evolutionary families of peptidases. Biochem. J., 290:205-218.
    • (1993) Biochem. J. , vol.290 , pp. 205-218
    • Rawlings, N.D.1    Barrett, A.J.2
  • 165
    • 0001144526 scopus 로고
    • Seed storage proteins: The enzyme inhibitors
    • Richardson, M. 1991. Seed storage proteins: The enzyme inhibitors. Methods in Plant Biochemistry, 5:259-305.
    • (1991) Methods in Plant Biochemistry , vol.5 , pp. 259-305
    • Richardson, M.1
  • 166
    • 0029658209 scopus 로고    scopus 로고
    • H-1 NMR assignment and global fold of napin BnIb, a representative 2S albumin seed protein
    • Rico, M., Bruix, M., Gonzalez, C., Monsalve, R.I., and Rodriguez, R. 1996. H-1 NMR assignment and global fold of napin BnIb, a representative 2S albumin seed protein. Biochem., 35:5672-5682.
    • (1996) Biochem. , vol.35 , pp. 5672-5682
    • Rico, M.1    Bruix, M.2    Gonzalez, C.3    Monsalve, R.I.4    Rodriguez, R.5
  • 167
    • 0034857869 scopus 로고    scopus 로고
    • Detection and stability of the major almond allergen in foods
    • Roux, K.H., Teuber, S.S., Robotham, J.M., and Sathe, S.K. 2001. Detection and stability of the major almond allergen in foods. J. Agric. Food Chem., 49:2131-2136.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 2131-2136
    • Roux, K.H.1    Teuber, S.S.2    Robotham, J.M.3    Sathe, S.K.4
  • 168
    • 0035262426 scopus 로고    scopus 로고
    • Pollution and allergic airways disease
    • Salvi, S. 2001. Pollution and allergic airways disease. Curr. Opin. Allergy Clin. Immunol., 1:35-41.
    • (2001) Curr. Opin. Allergy Clin. Immunol. , vol.1 , pp. 35-41
    • Salvi, S.1
  • 169
    • 0030174782 scopus 로고    scopus 로고
    • Specific binding of allergenic soybean protein Gly m Bd 30K with alpha'-and alpha-subunits of conglycinin in soy milk
    • Samoto, M., Miyazaki, C., Akasaka, T., Mori, H., and Kawamura, Y. 1996. Specific binding of allergenic soybean protein Gly m Bd 30K with alpha'-and alpha-subunits of conglycinin in soy milk. Biosci. Biotech. Biochem., 60:1006-1010.
    • (1996) Biosci. Biotech. Biochem. , vol.60 , pp. 1006-1010
    • Samoto, M.1    Miyazaki, C.2    Akasaka, T.3    Mori, H.4    Kawamura, Y.5
  • 172
    • 0035038558 scopus 로고    scopus 로고
    • Recombinant allergens Pru av 1 and Pru av 4 and a newly identified lipid transfer protein in the in vitro diagnosis of cherry allergy
    • Scheurer, S., Pastorello, E.A., Wangorsch, A., Kastner, M., Haustein, D., and Vieths, S. 2001. Recombinant allergens Pru av 1 and Pru av 4 and a newly identified lipid transfer protein in the in vitro diagnosis of cherry allergy. J. Allergy Clin. Immunol., 107:724-731.
    • (2001) J. Allergy Clin. Immunol. , vol.107 , pp. 724-731
    • Scheurer, S.1    Pastorello, E.A.2    Wangorsch, A.3    Kastner, M.4    Haustein, D.5    Vieths, S.6
  • 173
    • 0028871972 scopus 로고
    • Der p I, a major allergen of the house dust mite, proteolytically cleaves the low-affinity receptor for human IgE (CD23)
    • Schulz, O., Laing, P., Sewell, H.F., and Shakib, F. 1995. Der p I, a major allergen of the house dust mite, proteolytically cleaves the low-affinity receptor for human IgE (CD23). Eur. J. Immunol., 25:3191-3194.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 3191-3194
    • Schulz, O.1    Laing, P.2    Sewell, H.F.3    Shakib, F.4
  • 174
    • 0034991489 scopus 로고    scopus 로고
    • Identification of four novel potato (Solanum tubero-sum) allergens belonging to the family of soybean tryosin inhibitors
    • Seppala, U., Majamaa, H., Turjanmaa, K., Helin, J., Reunala, T., Kalkkinen, N., and Palosuo, T. 2001. Identification of four novel potato (Solanum tubero-sum) allergens belonging to the family of soybean tryosin inhibitors. Allergy, 56:619-626.
    • (2001) Allergy , vol.56 , pp. 619-626
    • Seppala, U.1    Majamaa, H.2    Turjanmaa, K.3    Helin, J.4    Reunala, T.5    Kalkkinen, N.6    Palosuo, T.7
  • 175
    • 0000078132 scopus 로고    scopus 로고
    • Enzyme inhibitors of seeds: Types and properties
    • Eds., Shewry, P.R., and Casey, R., Kluwer Academic Publishers: Dordrecht, The Netherlands
    • Shewry, P.R. 1999. Enzyme inhibitors of seeds: types and properties. In: Seed Proteins. pp. 587-615. Eds., Shewry, P.R., and Casey, R., Kluwer Academic Publishers: Dordrecht, The Netherlands.
    • (1999) Seed Proteins , pp. 587-615
    • Shewry, P.R.1
  • 176
    • 0025357314 scopus 로고
    • The prolamin storage proteins of cereal seeds: Structure and evolution
    • Shewry, P.R. and Tatham, A.S. 1990. The prolamin storage proteins of cereal seeds: Structure and evolution. Biochem. J., 267:1-12.
    • (1990) Biochem. J. , vol.267 , pp. 1-12
    • Shewry, P.R.1    Tatham, A.S.2
  • 177
    • 0004290554 scopus 로고    scopus 로고
    • Kluwer Academic Publishers: Dordrecht, The Netherlands
    • Shewry, P.R. and Casey, R. Eds. 1999. Seed Proteins. Kluwer Academic Publishers: Dordrecht, The Netherlands.
    • (1999) Seed Proteins
    • Shewry, P.R.1    Casey, R.2
  • 178
    • 77956761508 scopus 로고    scopus 로고
    • Plant proteins that confer resistance to pests and pathogens
    • Ed., Callow, J., Academic Press
    • Shewry, P.R. and Lucas, J.A. 1997. Plant proteins that confer resistance to pests and pathogens. In: Advances in Botanical Research. Vol. 26, pp. 135-192. Ed., Callow, J., Academic Press.
    • (1997) Advances in Botanical Research , vol.26 , pp. 135-192
    • Shewry, P.R.1    Lucas, J.A.2
  • 179
    • 0002436454 scopus 로고    scopus 로고
    • The 2S albumin storage proteins
    • Eds., Shewry, P.R., and Casey, R., Kluwer Academic Publishers, Dordrecht
    • Shewry, P.R. and Pandya, M.J. 1999. The 2S albumin storage proteins. In: Seed Proteins pp. 563-586. Eds., Shewry, P.R., and Casey, R., Kluwer Academic Publishers, Dordrecht.
    • (1999) Seed Proteins , pp. 563-586
    • Shewry, P.R.1    Pandya, M.J.2
  • 180
    • 0002438570 scopus 로고    scopus 로고
    • The characterisation, structures and evolutionary relationships of prolamins
    • Eds., Shewry, P.R., and Casey, R., Kluwer Academic Publishers: Dordrecht
    • Shewry, P.R. and Tatham, A.S. 1999. The characterisation, structures and evolutionary relationships of prolamins In: Seed Proteins pp. 11-33. Eds., Shewry, P.R., and Casey, R., Kluwer Academic Publishers: Dordrecht.
    • (1999) Seed Proteins , pp. 11-33
    • Shewry, P.R.1    Tatham, A.S.2
  • 181
    • 0002140252 scopus 로고    scopus 로고
    • The prolamins of the triticeae
    • Eds., Shewry, P.R. and Casey, R., Kluwer Academic Publishers, Dordrecht
    • Shewry, P.R., Tatham, A.S., and Halford, N.G. 1999. The prolamins of the triticeae. In: Seed Proteins pp. 35-78. Eds., Shewry, P.R. and Casey, R., Kluwer Academic Publishers, Dordrecht.
    • (1999) Seed Proteins , pp. 35-78
    • Shewry, P.R.1    Tatham, A.S.2    Halford, N.G.3
  • 183
    • 0029643949 scopus 로고
    • High-resolution crystal-structure of the nonspecific lipid-transfer protein from maize seedlings
    • Shin, D.H., Lee, J.Y., Hwang, K.Y., Kim, K.K., and Suh, S.W. 1995. High-resolution crystal-structure of the nonspecific lipid-transfer protein from maize seedlings. Structure, 3:189-199.
    • (1995) Structure , vol.3 , pp. 189-199
    • Shin, D.H.1    Lee, J.Y.2    Hwang, K.Y.3    Kim, K.K.4    Suh, S.W.5
  • 184
    • 0032577580 scopus 로고    scopus 로고
    • Biochemical and structural analysis of the IgE binding sites on Ara h 1, an abundant and highly allergenic peanut protein
    • Shin, D.S., Compadre, C.M., Maleki, S.J., Kopper, R.A., Sampson, H., Huang, S.K, Burks, A.W., and Bannon, G.A. 1998. Biochemical and structural analysis of the IgE binding sites on Ara h 1, an abundant and highly allergenic peanut protein. J. Biol. Chem., 273:13753-13759.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13753-13759
    • Shin, D.S.1    Compadre, C.M.2    Maleki, S.J.3    Kopper, R.A.4    Sampson, H.5    Huang, S.K.6    Burks, A.W.7    Bannon, G.A.8
  • 185
    • 0033101490 scopus 로고    scopus 로고
    • The involvement of cysteine proteases and protease inhibitor genes in the regulation of programmed cell death in plants
    • Solomon, M., Belenghi, B., Delledonne, M., Menachem, E., and Levine, A. 1999. The involvement of cysteine proteases and protease inhibitor genes in the regulation of programmed cell death in plants. Plant Cell, 11:431-444.
    • (1999) Plant Cell , vol.11 , pp. 431-444
    • Solomon, M.1    Belenghi, B.2    Delledonne, M.3    Menachem, E.4    Levine, A.5
  • 187
    • 0029792616 scopus 로고    scopus 로고
    • The biochemistry of common aeroallergens
    • Stewart, G.A., and Thompson, P.J. 1996. The biochemistry of common aeroallergens. Clin. Exp. Allergy, 26:1020-1044.
    • (1996) Clin. Exp. Allergy , vol.26 , pp. 1020-1044
    • Stewart, G.A.1    Thompson, P.J.2
  • 189
    • 0029055108 scopus 로고
    • Determination of the three-dimensional structure of the bifunctional α-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy
    • Strobl, S., Mühlhahn, P., Bernstein, R., Wilscheck, R., Maskos, K., Wunderlich, M., Huber, R., Glockhuber, R., and Holak, T.A. 1995. Determination of the three-dimensional structure of the bifunctional α-amylase/trypsin inhibitor from ragi seeds by NMR spectroscopy. Biochemistry, 34:8281-8293.
    • (1995) Biochemistry , vol.34 , pp. 8281-8293
    • Strobl, S.1    Mühlhahn, P.2    Bernstein, R.3    Wilscheck, R.4    Maskos, K.5    Wunderlich, M.6    Huber, R.7    Glockhuber, R.8    Holak, T.A.9
  • 191
    • 0024893624 scopus 로고
    • Isolation and characterisation of a trypsiin inhibitor from the seeds of khorhabi (Brassica napus var Rapifem) belonging to the napin family of storage proteins
    • Svendsen, I., Nicolova, D., Goshev, I., and Genov, N. 1989. Isolation and characterisation of a trypsiin inhibitor from the seeds of khorhabi (Brassica napus var Rapifem) belonging to the napin family of storage proteins. Carlsberg Res. Commun., 54:231-239.
    • (1989) Carlsberg Res. Commun. , vol.54 , pp. 231-239
    • Svendsen, I.1    Nicolova, D.2    Goshev, I.3    Genov, N.4
  • 192
    • 0028298709 scopus 로고
    • Primary structure, spectroscopic and inhibitory properties of a two-chain trypsin inhibitor from the seeds of charlock (Sinapis arvensis L)., a member of the napin protein family
    • Svendsen, I., Nicolova, D., Goshev, I., and Genov, N. 1994. Primary structure, spectroscopic and inhibitory properties of a two-chain trypsin inhibitor from the seeds of charlock (Sinapis arvensis L)., a member of the napin protein family. Int. J. Peptide Protein Res,., 43:425-430.
    • (1994) Int. J. Peptide Protein Res. , vol.43 , pp. 425-430
    • Svendsen, I.1    Nicolova, D.2    Goshev, I.3    Genov, N.4
  • 193
    • 0034988593 scopus 로고    scopus 로고
    • Identification of allergen fractions of wheat flour responsible for anaphylactic reactions to wheat products in infants and young children
    • Takizawa, T., Arakawa, H., Tokuyama, K., and Morikawa, A. 2001. Identification of allergen fractions of wheat flour responsible for anaphylactic reactions to wheat products in infants and young children. Int. Arch. Allergy Immunol., 125:51-56.
    • (2001) Int. Arch. Allergy Immunol. , vol.125 , pp. 51-56
    • Takizawa, T.1    Arakawa, H.2    Tokuyama, K.3    Morikawa, A.4
  • 194
    • 0029877269 scopus 로고    scopus 로고
    • A major wheat allergen has a Gin-gin-gin-pro-pro motif identified as an IgE-binding epitope
    • Tanabe, S., Aral, S., Yanagihara, Y., Takahashi, K., and Watanabe, M. 1996. A major wheat allergen has a Gin-Gin-Gin-Pro-Pro motif identified as an IgE-binding epitope. Biochem. Biophys. Res Commun., 219:290-293.
    • (1996) Biochem. Biophys. Res Commun. , vol.219 , pp. 290-293
    • Tanabe, S.1    Aral, S.2    Yanagihara, Y.3    Takahashi, K.4    Watanabe, M.5
  • 195
    • 0033975390 scopus 로고    scopus 로고
    • Redox- And pH-dependent association of plastocyanin with lipid bilayers: Effects on protein conformation and thermal stability
    • Taneva, S.G., Donchev, A.A., Dimitrov, M.I., and Muga, A. 2000. Redox- and pH-dependent association of plastocyanin with lipid bilayers: Effects on protein conformation and thermal stability. Biochim. Biophys. Acta, 1463:429-438.
    • (2000) Biochim. Biophys. Acta , vol.1463 , pp. 429-438
    • Taneva, S.G.1    Donchev, A.A.2    Dimitrov, M.I.3    Muga, A.4
  • 196
    • 0033951882 scopus 로고    scopus 로고
    • The wide binding properties of a wheat nonspecific lipid transfer protein-Solution structure of a complex with prostaglandin B-2
    • Tassin-Moindrot, S., Caille, A., Douliez, J.-P., Marion, D., and Vovelle, F. 2000. The wide binding properties of a wheat nonspecific lipid transfer protein-Solution structure of a complex with prostaglandin B-2. Euro. J. Biochem., 267:1117-1124.
    • (2000) Euro. J. Biochem. , vol.267 , pp. 1117-1124
    • Tassin-Moindrot, S.1    Caille, A.2    Douliez, J.-P.3    Marion, D.4    Vovelle, F.5
  • 197
    • 0033504169 scopus 로고    scopus 로고
    • Identification, isolation, and characterization of Ole e 7, a new allergen of olive tree pollen
    • Tejera, M.L., Villalba, M., Batanero, E., and Rodriguez, R. 1999. Identification, isolation, and characterization of Ole e 7, a new allergen of olive tree pollen. J. Allergy Clin. Immunol. 104:797-802.
    • (1999) J. Allergy Clin. Immunol. , vol.104 , pp. 797-802
    • Tejera, M.L.1    Villalba, M.2    Batanero, E.3    Rodriguez, R.4
  • 198
    • 0027132885 scopus 로고
    • Synergistic enhancement of the antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and by barley trypsin inhibitors
    • Terras, F.R.G., Schoofs, H.M., Thevissen, K., Osbom, R.W., Vanderleyden, J., Cammuie, B.P.A., and Broekaert, W.F. 1993. Synergistic enhancement of the antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and by barley trypsin inhibitors. Plant Physiol., 103:1311-1319.
    • (1993) Plant Physiol. , vol.103 , pp. 1311-1319
    • Terras, F.R.G.1    Schoofs, H.M.2    Thevissen, K.3    Osbom, R.W.4    Vanderleyden, J.5    Cammuie, B.P.A.6    Broekaert, W.F.7
  • 200
    • 0031846740 scopus 로고    scopus 로고
    • Cloning and sequencing of a gene enconding a 2S albumin seed storage protein precursor from English walnut (Jugions regia), a major food allergen
    • Teuber, S.S., Dandekar, A.M., Peterson, W.R., and Sellers, C.L. 1998. Cloning and sequencing of a gene enconding a 2S albumin seed storage protein precursor from English walnut (Jugions regia), a major food allergen. J. Allergy Clin. Immunol., 101:807-814.
    • (1998) J. Allergy Clin. Immunol. , vol.101 , pp. 807-814
    • Teuber, S.S.1    Dandekar, A.M.2    Peterson, W.R.3    Sellers, C.L.4
  • 201
    • 0032870631 scopus 로고    scopus 로고
    • Systemic allergic reaction to coconut (Cocos nucifera) in 2 subjects with hypersensitivity to tree nut and demonstration of cross-reactivity to legumin-like seed storage proteins: New coconut and walnut food allergens
    • Teuber, S.S., and Petersen, W.R. 1999. Systemic allergic reaction to coconut (Cocos nucifera) in 2 subjects with hypersensitivity to tree nut and demonstration of cross-reactivity to legumin-like seed storage proteins: New coconut and walnut food allergens. J. Allergy Clin. Immunol., 103:1180-1185.
    • (1999) J. Allergy Clin. Immunol. , vol.103 , pp. 1180-1185
    • Teuber, S.S.1    Petersen, W.R.2
  • 202
    • 0033406009 scopus 로고    scopus 로고
    • Identification and cloning of a complimentary DNA encoding a vicilin-like proprotein, Jug r 2, from English walnut kernel (Juglans regia), a major food allergen
    • Teuber, S., Jarvis, K.C., Dandekar, A.M., Peterson, W.R., and Ansari, A. 1999. Identification and cloning of a complimentary DNA encoding a vicilin-like proprotein, Jug r 2, from English walnut kernel (Juglans regia), a major food allergen. J. Allergy Clin. Immunol., 104:1111-1120.
    • (1999) J. Allergy Clin. Immunol. , vol.104 , pp. 1111-1120
    • Teuber, S.1    Jarvis, K.C.2    Dandekar, A.M.3    Peterson, W.R.4    Ansari, A.5
  • 203
    • 0001390643 scopus 로고
    • Major proteins of soybean seeds. Reversible and irreversible dissociation of β-congIycinin
    • Thanh, V.H. and Shibasaki, K. 1979. Major proteins of soybean seeds. Reversible and irreversible dissociation of β-congIycinin. J. Agric. Food Chem., 27:805-809.
    • (1979) J. Agric. Food Chem. , vol.27 , pp. 805-809
    • Thanh, V.H.1    Shibasaki, K.2
  • 205
    • 0026348398 scopus 로고
    • Organ-specific occurrence and expression of the isoforms of nonspecific lipid transfer protein in castor bean seedlings, and molecular-cloning of a full-length cDNA for a cotyledon-specific isoform
    • Tsuboi, S., Suga, T., Takishima, K., Mamiya, G., Matsui, K., Ozeki, Y., and Yamada, M. 1991. Organ-specific occurrence and expression of the isoforms of nonspecific lipid transfer protein in castor bean seedlings, and molecular-cloning of a full-length cDNA for a cotyledon-specific isoform. JBiochem., 110:823-831.
    • (1991) JBiochem. , vol.110 , pp. 823-831
    • Tsuboi, S.1    Suga, T.2    Takishima, K.3    Mamiya, G.4    Matsui, K.5    Ozeki, Y.6    Yamada, M.7
  • 206
    • 0033179482 scopus 로고    scopus 로고
    • The families of pathogenesis-related proteins, their activities and comparative analysis of PR-1 type proteins
    • van Loon, L.C. and van Strien, E.A. 1999. The families of pathogenesis-related proteins, their activities and comparative analysis of PR-1 type proteins. Physiol. Mol. Plant Pathol., 55:85-97.
    • (1999) Physiol. Mol. Plant Pathol. , vol.55 , pp. 85-97
    • Van Loon, L.C.1    Van Strien, E.A.2
  • 208
    • 0034031999 scopus 로고    scopus 로고
    • Antigliadin IgE-indicator of wheat allergy in atopic dermatitis
    • Varjonen, E., Vainio, E., and Kalimo, K. 2000. Antigliadin IgE-indicator of wheat allergy in atopic dermatitis. Allergy, 55:386-391.
    • (2000) Allergy , vol.55 , pp. 386-391
    • Varjonen, E.1    Vainio, E.2    Kalimo, K.3
  • 209
    • 0031045752 scopus 로고    scopus 로고
    • Life-threatening, recurrent anaphylaxis caused by allergy to gliadin and exercise
    • Varjonen, E., Vainio, E., and Kalimo, K. 1997. Life-threatening, recurrent anaphylaxis caused by allergy to gliadin and exercise. Clin, Exp. Allergy, 27:162-166.
    • (1997) Clin, Exp. Allergy , vol.27 , pp. 162-166
    • Varjonen, E.1    Vainio, E.2    Kalimo, K.3
  • 210
    • 0028860817 scopus 로고
    • Skin-prick test and RAST responses to cereals in children with atopic dermatitis. Characterization of IgE-binding components in wheat and oats by an immunoblotting method
    • Varjonen, E., Vainio, E., Kalimo, K., Juntunen-Backman, K., and Savolainen, J. 1995. Skin-prick test and RAST responses to cereals in children with atopic dermatitis. Characterization of IgE-binding components in wheat and oats by an immunoblotting method. Clin. Exp. Allergy, 25:1100-1107.
    • (1995) Clin. Exp. Allergy , vol.25 , pp. 1100-1107
    • Varjonen, E.1    Vainio, E.2    Kalimo, K.3    Juntunen-Backman, K.4    Savolainen, J.5
  • 212
    • 0032199537 scopus 로고    scopus 로고
    • Cow's milk allergens
    • Wal, J.-M. 1998. Cow's milk allergens. Allergy, 53:1013-1022.
    • (1998) Allergy , vol.53 , pp. 1013-1022
    • Wal, J.-M.1
  • 213
    • 0036971325 scopus 로고    scopus 로고
    • Ana o 1, a cashew (Anacardium occidental) allergen of the vicilin seed storage protein family
    • Wang, F., Robotham, J.M., Teuber, S.S., Tawde, P., Sathe, S.K., and Roux, K.H. 2002. Ana o 1, a cashew (Anacardium occidental) allergen of the vicilin seed storage protein family. J. Allergy Clin. Immunol., 110:160-166.
    • (2002) J. Allergy Clin. Immunol. , vol.110 , pp. 160-166
    • Wang, F.1    Robotham, J.M.2    Teuber, S.S.3    Tawde, P.4    Sathe, S.K.5    Roux, K.H.6
  • 214
    • 0033766314 scopus 로고    scopus 로고
    • Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities
    • Woo, E.J., Dunwell, J.M., Goodenough, P.W., Marvier, A.C., and Pickersgill, R.W. 2000. Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities. Nat. Struct. Biol., 7:1036-1040.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1036-1040
    • Woo, E.J.1    Dunwell, J.M.2    Goodenough, P.W.3    Marvier, A.C.4    Pickersgill, R.W.5
  • 215
    • 0000172656 scopus 로고
    • The seed globulins
    • Ed., Hudson, B.J.F. Elsevier Applied Science, London and New York
    • Wright, D.J. 1987. The seed globulins. In: Developments in Food Proteins. pp. 81-157. Ed., Hudson, B.J.F. Elsevier Applied Science, London and New York.
    • (1987) Developments in Food Proteins , pp. 81-157
    • Wright, D.J.1
  • 216
    • 0000172656 scopus 로고
    • The seed globulins - Part II
    • Ed., Hudson, B.J.F. Elsevier, London
    • Wright, D.J. 1988. The seed globulins - part II. In: Developments in Food Proteins. pp. 119-178. Ed., Hudson, B.J.F. Elsevier, London.
    • (1988) Developments in Food Proteins , pp. 119-178
    • Wright, D.J.1
  • 217
    • 0032873808 scopus 로고    scopus 로고
    • Analysis of the distribution of the major soybean seed allergen in a core collection of Glycine max accessions
    • Yaklich, R.W, Helm, R.M., Cockrell, G., and Herman, E.M. 1999. Analysis of the distribution of the major soybean seed allergen in a core collection of Glycine max accessions. Crop Sci., 39:1444-1447.
    • (1999) Crop Sci. , vol.39 , pp. 1444-1447
    • Yaklich, R.W.1    Helm, R.M.2    Cockrell, G.3    Herman, E.M.4
  • 218
    • 34247187913 scopus 로고
    • Molecular understanding of heat-induced phenomena of soybean protein
    • Yamauchi, P., Yamagishi, T., and Iwabuchi, S. 1991. Molecular understanding of heat-induced phenomena of soybean protein. Food Rev. Internat., 7:283-322.
    • (1991) Food Rev. Internat. , vol.7 , pp. 283-322
    • Yamauchi, P.1    Yamagishi, T.2    Iwabuchi, S.3
  • 219
    • 0002838981 scopus 로고
    • Occurrence of low molecular weight and high cysteine containing albumin storage proteins in oilseeds of disperse species
    • Youle, R.J. and Huang, A.H.C. 1981. Occurrence of low molecular weight and high cysteine containing albumin storage proteins in oilseeds of disperse species. Am. J. Botany, 68:44-48.
    • (1981) Am. J. Botany , vol.68 , pp. 44-48
    • Youle, R.J.1    Huang, A.H.C.2
  • 220
    • 0035104132 scopus 로고    scopus 로고
    • Disulfide bond effects on protein stability: Designed variants of Cucurbita maxima trypsin inhibitor-V
    • Zavodszky, M., Chen, C.W., Huang, J.K., Zolkiewski, M., Wen, L., Krishnamoorthi, R. 2001. Disulfide bond effects on protein stability: Designed variants of Cucurbita maxima trypsin inhibitor-V. Protein Sci., 10:149-160.
    • (2001) Protein Sci. , vol.10 , pp. 149-160
    • Zavodszky, M.1    Chen, C.W.2    Huang, J.K.3    Zolkiewski, M.4    Wen, L.5    Krishnamoorthi, R.6
  • 221
    • 0030870678 scopus 로고    scopus 로고
    • Multiple IgE-mediated sensitizations to enzymes after occupational exposure: Evaluation by skin prick test, RAST, and immunoblot
    • Zentner, A., Jeep, S., Wahl, R., Kunkel, G., and Kleine-Tebbe, J. 1997. Multiple IgE-mediated sensitizations to enzymes after occupational exposure: Evaluation by skin prick test, RAST, and immunoblot. Allergy, 52:928-934.
    • (1997) Allergy , vol.52 , pp. 928-934
    • Zentner, A.1    Jeep, S.2    Wahl, R.3    Kunkel, G.4    Kleine-Tebbe, J.5


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