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Volumn , Issue , 2005, Pages 649-674

Molecular design of soybean proteins for enhanced food quality

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EID: 84866723981     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (1)

References (76)
  • 1
    • 0026462509 scopus 로고
    • Plant food protein engineering
    • Kinsella, J.E., ed., San Diego, CA: Academic Press
    • Utsumi, S. Plant food protein engineering. In: Advances in Food and Nutrition Research, Kinsella, J.E., ed., San Diego, CA: Academic Press, 1992, Vol. 36, pp 89-208.
    • (1992) Advances in Food and Nutrition Research , vol.36 , pp. 89-208
    • Utsumi, S.1
  • 2
    • 0037714099 scopus 로고
    • Changes in plasma lipid levels in young healthy volunteers by adding an extruder-cooked soy protein to conventional meals
    • Kito, M., T. Moriyama, Y. Kimura, H. Kambara. Changes in plasma lipid levels in young healthy volunteers by adding an extruder-cooked soy protein to conventional meals. Biosci. Biotechnol. Biochem. 57:354-355, 1993.
    • (1993) Biosci. Biotechnol. Biochem , vol.57 , pp. 354-355
    • Kito, M.1    Moriyama, T.2    Kimura, Y.3    Kambara, H.4
  • 4
    • 0036966831 scopus 로고    scopus 로고
    • Effects of Bowman-Birk inhibitor on rat colon carcinogenesis
    • Kennedy, A.R., P.C. Billings, X.S. Wan, P.M. Newberne. Effects of Bowman-Birk inhibitor on rat colon carcinogenesis. Nutr. Cancer 43:174-186, 2002.
    • (2002) Nutr. Cancer , vol.43 , pp. 174-186
    • Kennedy, A.R.1    Billings, P.C.2    Wan, X.S.3    Newberne, P.M.4
  • 5
    • 0036468843 scopus 로고    scopus 로고
    • Effects of the Bowman-Birk inhibitor on growth, invasion, and clonogenic survival of human prostate epithelial cells and prostate cancer cells
    • Kennedy, A.R., X.S. Wan. Effects of the Bowman-Birk inhibitor on growth, invasion, and clonogenic survival of human prostate epithelial cells and prostate cancer cells. Prostate 50:125-133, 2002.
    • (2002) Prostate , vol.50 , pp. 125-133
    • Kennedy, A.R.1    Wan, X.S.2
  • 7
    • 0035680564 scopus 로고    scopus 로고
    • Development of Bowman-Birk inhibitor for chemoprevention of oral head and neck cancer
    • Meyskens, F.L. Development of Bowman-Birk inhibitor for chemoprevention of oral head and neck cancer. Ann. N.Y. Acad. Sci. 952:116-123, 2001.
    • (2001) Ann. N.Y. Acad. Sci , vol.952 , pp. 116-123
    • Meyskens, F.L.1
  • 8
    • 0032964107 scopus 로고    scopus 로고
    • A soybean cDNA encoding a chromatin-binding peptide inhibits mitosis of mammalian cells
    • Galvez, A.F., B.O. de Lumen. A soybean cDNA encoding a chromatin-binding peptide inhibits mitosis of mammalian cells. Nat. Biotechnol. 17:495-500, 1999.
    • (1999) Nat. Biotechnol , vol.17 , pp. 495-500
    • Galvez, A.F.1    de Lumen, B.O.2
  • 9
    • 0033279943 scopus 로고    scopus 로고
    • Molecular strategies to improve the nutritional quality of legume proteins
    • de Lumen, B.O., A.F. Galvez, M.J. Revilleza, D.C. Krenz. Molecular strategies to improve the nutritional quality of legume proteins. Adv. Exp. Med. Biol. 464:117-126, 1999.
    • (1999) Adv. Exp. Med. Biol , vol.464 , pp. 117-126
    • de Lumen, B.O.1    Galvez, A.F.2    Revilleza, M.J.3    Krenz, D.C.4
  • 10
    • 0035887086 scopus 로고    scopus 로고
    • Chemopreventive property of a soybean peptide (lunasin) that binds to deacetylated histones and inhibits acetylation
    • Galvez A.F., N. Chen, J. Macasieb, B.O. de Lumen. Chemopreventive property of a soybean peptide (lunasin) that binds to deacetylated histones and inhibits acetylation. Cancer Res. 61:7473-7478, 2001.
    • (2001) Cancer Res , vol.61 , pp. 7473-7478
    • Galvez, A.F.1    Chen, N.2    Macasieb, J.3    de Lumen, B.O.4
  • 11
    • 0030981283 scopus 로고    scopus 로고
    • Molecular design of soybean glycinins with enhanced food qualities and development of crops producing such glycinins
    • Damodaran, S., ed., New York: Plenum Press
    • Utsumi, S., T. Katsube, T. Ishige, F. Takaiwa. Molecular design of soybean glycinins with enhanced food qualities and development of crops producing such glycinins. In: Food Proteins and Lipids, Damodaran, S., ed., New York: Plenum Press, 1997, pp 1-15.
    • (1997) Food Proteins and Lipids , pp. 1-15
    • Utsumi, S.1    Katsube, T.2    Ishige, T.3    Takaiwa, F.4
  • 12
    • 0003654206 scopus 로고    scopus 로고
    • Food protein engineering of soybean proteins and the development of soy-rice
    • Shewry, P.R., J.A. Napier, P. Davis, eds., London: Portland Press
    • Katsube, T., N. Maruyama, F. Takaiwa, S. Utsumi. Food protein engineering of soybean proteins and the development of soy-rice. In: Engineering Crop Plants for Industrial End Uses, Shewry, P.R., J.A. Napier, P. Davis, eds., London: Portland Press, 1998, pp 65-76.
    • (1998) Engineering Crop Plants for Industrial End Uses , pp. 65-76
    • Katsube, T.1    Maruyama, N.2    Takaiwa, F.3    Utsumi, S.4
  • 13
    • 49349130487 scopus 로고
    • Legumin and vicilin, storage proteins of legume seeds
    • Derbyshire, E., D.J. Wright, D. Boulter. Legumin and vicilin, storage proteins of legume seeds. Phytochemistry 15:3-24, 1976.
    • (1976) Phytochemistry , vol.15 , pp. 3-24
    • Derbyshire, E.1    Wright, D.J.2    Boulter, D.3
  • 14
    • 0000172656 scopus 로고
    • The seed globulins: Part II
    • Hudson, B.J.F., ed., London: Elsevier
    • Wright, D.J. The seed globulins: part II. In: Developments in Food Proteins: 5, Hudson, B.J.F., ed., London: Elsevier, 1987, pp 81-157.
    • (1987) Developments in Food Proteins: 5 , pp. 81-157
    • Wright, D.J.1
  • 15
    • 0032404009 scopus 로고    scopus 로고
    • The roles of the N-linked glycans and extension regions of soybean B-conglycinin in folding, assembly and structural features
    • Maruyama, N., T. Katsube, Y. Wada, M.H. Oh, A.P. Barba de la Rosa, E. Okuda, S. Nakagawa, S. Utsumi. The roles of the N-linked glycans and extension regions of soybean B-conglycinin in folding, assembly and structural features. Eur. J. Biochem. 258:854-862, 1998.
    • (1998) Eur. J. Biochem , vol.258 , pp. 854-862
    • Maruyama, N.1    Katsube, T.2    Wada, Y.3    Oh, M.H.4    Barba de la Rosa, A.P.5    Okuda, E.6    Nakagawa, S.7    Utsumi, S.8
  • 16
    • 85052678887 scopus 로고    scopus 로고
    • Structure-function relationships of soy proteins
    • Damodaran, S., A. Paraf, eds., New York: Marcel Dekker
    • Utsumi, S., Y. Matsumura, T. Mori. Structure-function relationships of soy proteins. In: Food Proteins and Their Applications, Damodaran, S., A. Paraf, eds., New York: Marcel Dekker, 1997, pp 257-291.
    • (1997) Food Proteins and Their Applications , pp. 257-291
    • Utsumi, S.1    Matsumura, Y.2    Mori, T.3
  • 18
    • 33947094131 scopus 로고
    • Major proteins of soybean seeds: Subunit structure of B-conglycinin
    • Thanh, V.H., K. Shibasaki. Major proteins of soybean seeds: subunit structure of B-conglycinin. J. Agric. Food Chem. 26:692-695, 1978.
    • (1978) J. Agric. Food Chem , vol.26 , pp. 692-695
    • Thanh, V.H.1    Shibasaki, K.2
  • 19
    • 0000366854 scopus 로고
    • Heterogeneity of soybean glycinin
    • Utsumi, S., H. Inaba, T. Mori. Heterogeneity of soybean glycinin. Phytochemistry 20:585-589, 1981.
    • (1981) Phytochemistry , vol.20 , pp. 585-589
    • Utsumi, S.1    Inaba, H.2    Mori, T.3
  • 20
    • 0027951481 scopus 로고
    • An induced mutant line lacking the A subunit of B-conglycinin in soybean [Glycine max (L.) Merril]
    • Takahashi, K., H. Banba, A. Kikuchi, M. Ito, S. Nakamura. An induced mutant line lacking the A subunit of B-conglycinin in soybean [Glycine max (L.) Merril]. Breed. Sci. 44:65-66, 1994.
    • (1994) Breed. Sci , vol.44 , pp. 65-66
    • Takahashi, K.1    Banba, H.2    Kikuchi, A.3    Ito, M.4    Nakamura, S.5
  • 21
    • 0029914085 scopus 로고    scopus 로고
    • Inheritance of the A-subunit deficiency of B-conglycinin in soybean [Glycine max (L.) Merril] line induced by y-ray irradiation
    • Takahashi, K., Y. Mizuno, S. Yumoto, K. Kitamura, S. Nakamura. Inheritance of the A-subunit deficiency of B-conglycinin in soybean [Glycine max (L.) Merril] line induced by y-ray irradiation. Breed. Sci. 46:251-255, 1996.
    • (1996) Breed. Sci , vol.46 , pp. 251-255
    • Takahashi, K.1    Mizuno, Y.2    Yumoto, S.3    Kitamura, K.4    Nakamura, S.5
  • 22
    • 0007618001 scopus 로고    scopus 로고
    • Inheritance of glycinin subunits and characterization of glycinin molecules lacking the subunits in soybean [Glycine max (L.) Merril]
    • Yagasaki, K., N. Kaizuma, K. Kitamura. Inheritance of glycinin subunits and characterization of glycinin molecules lacking the subunits in soybean [Glycine max (L.) Merril]. Breed. Sci. 46:11-15, 1996.
    • (1996) Breed. Sci , vol.46 , pp. 11-15
    • Yagasaki, K.1    Kaizuma, N.2    Kitamura, K.3
  • 23
    • 0000800863 scopus 로고    scopus 로고
    • Biochemical characterization of soybean protein consisting of different subunits of glycinin
    • Yagasaki, K., T. Takagi, M. Sasaki, K. Kitamura. Biochemical characterization of soybean protein consisting of different subunits of glycinin. J. Agric. Food Chem. 45:656-660, 1997.
    • (1997) J. Agric. Food Chem , vol.45 , pp. 656-660
    • Yagasaki, K.1    Takagi, T.2    Sasaki, M.3    Kitamura, K.4
  • 24
    • 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., T. Izard, M. Beuchat, R.J. Blagrobe, P.M. Colman. 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.
    • (1994) J. Mol. Biol , vol.238 , pp. 748-776
    • Lawrence, M.C.1    Izard, T.2    Beuchat, M.3    Blagrobe, R.J.4    Colman, P.M.5
  • 28
    • 0000172656 scopus 로고
    • The seed globulins: Part II
    • London: Elsevier
    • Wright, D.J. The seed globulins: part II. In: Developments in Food Proteins: 6. London: Elsevier, 1987, pp 119-178.
    • (1987) Developments in Food Proteins: 6 , pp. 119-178
    • Wright, D.J.1
  • 31
    • 0031948520 scopus 로고    scopus 로고
    • Cupins: A new superfamily of functionally diverse proteins that include ger-mins and plant seed storage proteins
    • Dunwell, J.M. Cupins: a new superfamily of functionally diverse proteins that include ger-mins and plant seed storage proteins. Biotechnol. Genet. Eng. Rev. 15:1-32, 1998.
    • (1998) Biotechnol. Genet. Eng. Rev , vol.15 , pp. 1-32
    • Dunwell, J.M.1
  • 32
    • 0031888149 scopus 로고    scopus 로고
    • Microbial relatives of seed storage proteins: Conservation of motifs in a functionally diverse superfamily of enzymes
    • Dunwell, J.M., P.J. Gane. Microbial relatives of seed storage proteins: conservation of motifs in a functionally diverse superfamily of enzymes. J. Mol. Evol. 46:147-154, 1998.
    • (1998) J. Mol. Evol , vol.46 , pp. 147-154
    • Dunwell, J.M.1    Gane, P.J.2
  • 34
    • 0037129976 scopus 로고    scopus 로고
    • Structure of oxalate decarboxylase from Bacillus subtilis at 1.75 Å resolution
    • Anand, R., P.C. Dorrestein, C. Kinsland, T.P. Begley, S.E. Ealick. Structure of oxalate decarboxylase from Bacillus subtilis at 1.75 Å resolution. Biochemistry 41:7659-7669, 2002.
    • (2002) Biochemistry , vol.41 , pp. 7659-7669
    • Anand, R.1    Dorrestein, P.C.2    Kinsland, C.3    Begley, T.P.4    Ealick, S.E.5
  • 36
    • 0037070503 scopus 로고    scopus 로고
    • Structure-function relationships of soybean proteins revealed by using recombinant systems
    • Utsumi, S., N. Maruyama, R. Satoh, M. Adachi. Structure-function relationships of soybean proteins revealed by using recombinant systems. Enzyme Microb. Tech. 30:284-288, 2002.
    • (2002) Enzyme Microb. Tech , vol.30 , pp. 284-288
    • Utsumi, S.1    Maruyama, N.2    Satoh, R.3    Adachi, M.4
  • 39
    • 3543097257 scopus 로고    scopus 로고
    • Structure of the core region of the soybean B-conglycinin A\ subunit
    • Maruyama, Y., N. Maruyama, B. Mikami, S. Utsumi. Structure of the core region of the soybean B-conglycinin A\ subunit. Acta Cryst. D60:289-297, 2004.
    • (2004) Acta Cryst , vol.D60 , pp. 289-297
    • Maruyama, Y.1    Maruyama, N.2    Mikami, B.3    Utsumi, S.4
  • 40
    • 0026777217 scopus 로고
    • Contribution of the hydrophobic effect to globular protein stability
    • Pace, C.N. Contribution of the hydrophobic effect to globular protein stability. J. Mol. Biol. 226:29-35, 1992.
    • (1992) J. Mol. Biol , vol.226 , pp. 29-35
    • Pace, C.N.1
  • 41
  • 42
    • 0030748521 scopus 로고    scopus 로고
    • The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifexpyrophilus at 1.9 Å resolution: Structural basis for thermostability
    • Lim, J.H., Y.G. Yu, Y.S. Han, S. Cho, B.Y. Ahn, S.H. Kim, Y. Cho. The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifexpyrophilus at 1.9 Å resolution: structural basis for thermostability. J. Mol. Biol. 270:259-274, 1997.
    • (1997) J. Mol. Biol , vol.270 , pp. 259-274
    • Lim, J.H.1    Yu, Y.G.2    Han, Y.S.3    Cho, S.4    Ahn, B.Y.5    Kim, S.H.6    Cho, Y.7
  • 43
    • 0035448574 scopus 로고    scopus 로고
    • Ion pairs and the thermotolerance of proteins from hyperthermophiles: A "traffic rule" for hot roads
    • Karshikoff, A., R. Ladenstein. Ion pairs and the thermotolerance of proteins from hyperthermophiles: a "traffic rule" for hot roads. Trends Biochem. Sci. 26:550-556, 2001.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 550-556
    • Karshikoff, A.1    Ladenstein, R.2
  • 44
    • 0029115963 scopus 로고
    • The optimization of protein-solvent interactions: Thermostability and the role of hydrophobic and electrostatic interactions
    • Spassov, V.Z., A.D. Karshikoff, R. Ladensten. The optimization of protein-solvent interactions: thermostability and the role of hydrophobic and electrostatic interactions. Protein Sci. 4:1516-1527, 1995.
    • (1995) Protein Sci , vol.4 , pp. 1516-1527
    • Spassov, V.Z.1    Karshikoff, A.D.2    Ladensten, R.3
  • 45
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
    • Matthews, B.W., H. Nicholson, W.J. Becktel. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc. Natl. Acad. Sci. USA 84:6663-6667, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 46
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Gerhard, V., W. Stefanie, A. Patrick. Protein thermal stability, hydrogen bonds, and ion pairs. J. Mol. Biol. 269:631-643, 1997.
    • (1997) J. Mol. Biol , vol.269 , pp. 631-643
    • Gerhard, V.1    Stefanie, W.2    Patrick, A.3
  • 48
    • 0005695733 scopus 로고    scopus 로고
    • Molecular strategies to enhance the nutritional quality of legume protein: An update
    • de Lumen, B.O., H. Uchimiya. Molecular strategies to enhance the nutritional quality of legume protein: an update. AgBiotech. News Info. 9:53N-58N, 1997.
    • (1997) AgBiotech. News Info , vol.9 , pp. 53N-58N
    • de Lumen, B.O.1    Uchimiya, H.2
  • 49
    • 0024986425 scopus 로고
    • Improvement of nutritional value and functional properties of soybean glycinin by protein engineering
    • Kim, C.S., S. Kamiya, T. Sato, S. Utsumi, M. Kito. Improvement of nutritional value and functional properties of soybean glycinin by protein engineering. Protein Eng. 3:725-731, 1990.
    • (1990) Protein Eng , vol.3 , pp. 725-731
    • Kim, C.S.1    Kamiya, S.2    Sato, T.3    Utsumi, S.4    Kito, M.5
  • 50
    • 0027145384 scopus 로고
    • Synthesis, processing and accumulation of modified glycinins of soybean in the seeds, leaves and stems of transgenic tobacco
    • Utsumi, S., S. Kitagawa, T. Katsube, I.J. Kang, A.B. Gidamis, F. Takaiwa, M. Kito. Synthesis, processing and accumulation of modified glycinins of soybean in the seeds, leaves and stems of transgenic tobacco. Plant Sci. 92:191-202, 1993.
    • (1993) Plant Sci , vol.92 , pp. 191-202
    • Utsumi, S.1    Kitagawa, S.2    Katsube, T.3    Kang, I.J.4    Gidamis, A.B.5    Takaiwa, F.6    Kito, M.7
  • 51
    • 0028888555 scopus 로고
    • High level accumulation of soybean glycinin in vacuole-derived protein bodies in the endosperm tissue of transgenic tobacco seed
    • Takaiwa, F., T. Katsube, S. Kitagawa, T. Hisaga, M. Kito, S. Utsumi. High level accumulation of soybean glycinin in vacuole-derived protein bodies in the endosperm tissue of transgenic tobacco seed. Plant Sci. 111:39-19, 1995.
    • (1995) Plant Sci , vol.111 , pp. 19-39
    • Takaiwa, F.1    Katsube, T.2    Kitagawa, S.3    Hisaga, T.4    Kito, M.5    Utsumi, S.6
  • 52
    • 0028140751 scopus 로고
    • Expression and accumulation of normal and modified soybean glycinins in potato tubers
    • Utsumi, S., S. Kitagawa, T. Katsube, T. Higasa, M. Kito, F. Takaiwa, T. Ishige. Expression and accumulation of normal and modified soybean glycinins in potato tubers. Plant Sci. 102:181-188, 1994.
    • (1994) Plant Sci , vol.102 , pp. 181-188
    • Utsumi, S.1    Kitagawa, S.2    Katsube, T.3    Higasa, T.4    Kito, M.5    Takaiwa, F.6    Ishige, T.7
  • 55
    • 0019484689 scopus 로고
    • Differences in subunit composition of glycinin among soybean cultivars
    • Mori, T., S. Utsumi, H. Inaba, K. Kitamura, K. Harada. Differences in subunit composition of glycinin among soybean cultivars. J. Agric. Food. Chem. 29:20-23, 1981.
    • (1981) J. Agric. Food. Chem , vol.29 , pp. 20-23
    • Mori, T.1    Utsumi, S.2    Inaba, H.3    Kitamura, K.4    Harada, K.5
  • 57
    • 0009789698 scopus 로고
    • Formation of pseudoglycinins and their gel hardness
    • Mori, T., T. Nakamura, S. Utsumi. Formation of pseudoglycinins and their gel hardness. J. Agric. Food Chem. 30:828-831, 1982.
    • (1982) J. Agric. Food Chem , vol.30 , pp. 828-831
    • Mori, T.1    Nakamura, T.2    Utsumi, S.3
  • 58
    • 0037768175 scopus 로고
    • Formation of pseudoglycinins from intermediary subunits of glycinin and their gel properties and network structure
    • Nakamura, T., S. Utsumi, T. Mori. Formation of pseudoglycinins from intermediary subunits of glycinin and their gel properties and network structure. Agric. Biol. Chem. 49:2733-2740, 1985.
    • (1985) Agric. Biol. Chem , vol.49 , pp. 2733-2740
    • Nakamura, T.1    Utsumi, S.2    Mori, T.3
  • 59
    • 0006278588 scopus 로고
    • Effect of deletion of disulfide bonds by protein engineering on the conformation and functional properties of soybean proglycinin
    • Utsumi, S., A.B. Gidamis, J. Kanamori, I.J. Kang, M. Kito. Effect of deletion of disulfide bonds by protein engineering on the conformation and functional properties of soybean proglycinin. J. Agric. Food Chem. 41:687-691, 1993.
    • (1993) J. Agric. Food Chem , vol.41 , pp. 687-691
    • Utsumi, S.1    Gidamis, A.B.2    Kanamori, J.3    Kang, I.J.4    Kito, M.5
  • 60
    • 0042303912 scopus 로고    scopus 로고
    • Crystal structures and structural stabilities of the disulfide bond-deficient soybean proglycinin mutants C12G and C88S
    • Adachi, M., E. Okuda, Y. Kaneda, A. Hashimoto, A.D. Shutov, C. Becker, K. M ntz, S. Utsumi. Crystal structures and structural stabilities of the disulfide bond-deficient soybean proglycinin mutants C12G and C88S. J. Agric. Food Chem., 51:4633-1639, 2003.
    • (2003) J. Agric. Food Chem , vol.51 , pp. 1639-4633
    • Adachi, M.1    Okuda, E.2    Kaneda, Y.3    Hashimoto, A.4    Shutov, A.D.5    Becker, C.6    Mntz, K.7    Utsumi, S.8
  • 61
    • 0029442621 scopus 로고
    • Potentiation of the antihypertensive activity of orally administered ovokinin, a vasorelaxing peptide derived from ovalbumin, by emulsification in egg phosphatidylcholine
    • Fujita, H., R. Sasaki, M. Yoshikawa. Potentiation of the antihypertensive activity of orally administered ovokinin, a vasorelaxing peptide derived from ovalbumin, by emulsification in egg phosphatidylcholine. Biosci. Biotechnol. Biochem. 59:2344-2345, 1995.
    • (1995) Biosci. Biotechnol. Biochem , vol.59 , pp. 2344-2345
    • Fujita, H.1    Sasaki, R.2    Yoshikawa, M.3
  • 62
    • 0030030101 scopus 로고    scopus 로고
    • Studies on the ileum-contracting mechanism and identification as a complement C3a receptor agonist of oryzatensin, a bioactive peptide derived from rice albumin
    • Takahashi, M., S. Moriguchi, M. Ikeno, S. Kono, K. Ohata, H. Usui, K. Kurahashi, R. Sasaki, M. Yoshikawa. Studies on the ileum-contracting mechanism and identification as a complement C3a receptor agonist of oryzatensin, a bioactive peptide derived from rice albumin. Peptides 17:5-12, 1996.
    • (1996) Peptides , vol.17 , pp. 5-12
    • Takahashi, M.1    Moriguchi, S.2    Ikeno, M.3    Kono, S.4    Ohata, K.5    Usui, H.6    Kurahashi, K.7    Sasaki, R.8    Yoshikawa, M.9
  • 63
    • 0029095148 scopus 로고
    • Isolation and characterization of ovokinin, a bradykinin B1 agonist peptide derived from ovalbumin
    • Fujita, H., H. Usui, K. Kurahashi, M. Yoshikawa. Isolation and characterization of ovokinin, a bradykinin B1 agonist peptide derived from ovalbumin. Peptides 16:785-790, 1995.
    • (1995) Peptides , vol.16 , pp. 785-790
    • Fujita, H.1    Usui, H.2    Kurahashi, K.3    Yoshikawa, M.4
  • 64
    • 0032760778 scopus 로고    scopus 로고
    • LKPNM: A prodrug type ACE-inhibitory peptide derived from fish protein
    • Fujita, H., M. Yoshikawa. LKPNM: a prodrug type ACE-inhibitory peptide derived from fish protein. Immunopharmacology 44:123-127, 1999.
    • (1999) Immunopharmacology , vol.44 , pp. 123-127
    • Fujita, H.1    Yoshikawa, M.2
  • 65
    • 0031917223 scopus 로고    scopus 로고
    • Decreased serum total cholesterol concentration is associated with high intake of soy products in Japanese men and women
    • Nagata, C., N. Takatsuka, Y. Kurisu, H. Shimizu. Decreased serum total cholesterol concentration is associated with high intake of soy products in Japanese men and women. J. Nutr. 128:209-213, 1998.
    • (1998) J. Nutr , vol.128 , pp. 209-213
    • Nagata, C.1    Takatsuka, N.2    Kurisu, Y.3    Shimizu, H.4
  • 66
    • 3643098896 scopus 로고    scopus 로고
    • Cholesterol-lowering effect of soy protein in normocholesterolemic and hypercholesterolemic men
    • Wong, W.W., E.O. Smith, J.E. Stuff, D.L. Hachey, W.C. Heird, H.J. Pownell. Cholesterol-lowering effect of soy protein in normocholesterolemic and hypercholesterolemic men. Am. J. Clin. Nutr. 68:1385S-1389S, 1998.
    • (1998) Am. J. Clin. Nutr , vol.68 , pp. 1385S-1389S
    • Wong, W.W.1    Smith, E.O.2    Stuff, J.E.3    Hachey, D.L.4    Heird, W.C.5    Pownell, H.J.6
  • 68
    • 0025118262 scopus 로고
    • Cholesterol-lowering activity of various undigested fractions of soybean protein in rats
    • Sugano, M., S. Goto, Y. Yamada, K. Yoshida, Y. Hashimoto, T. Matsuo, M. Kimoto. Cholesterol-lowering activity of various undigested fractions of soybean protein in rats. J. Nutr. 120:977-985, 1990.
    • (1990) J. Nutr , vol.120 , pp. 977-985
    • Sugano, M.1    Goto, S.2    Yamada, Y.3    Yoshida, K.4    Hashimoto, Y.5    Matsuo, T.6    Kimoto, M.7
  • 69
    • 85004389273 scopus 로고
    • Bile acid-binding protein from soybean seed: Isolation, partial characterization and insulin-stimulating activity
    • Makino, S., H. Nakashima, K. Minami, R. Moriyama, S. Takano. Bile acid-binding protein from soybean seed: isolation, partial characterization and insulin-stimulating activity. Agric. Biol. Chem. 52:803-809, 1988.
    • (1988) Agric. Biol. Chem , vol.52 , pp. 803-809
    • Makino, S.1    Nakashima, H.2    Minami, K.3    Moriyama, R.4    Takano, S.5
  • 70
    • 0036218439 scopus 로고    scopus 로고
    • Resistant protein: Its existence and function beneficial to health
    • Kato, N., K. Iwami. Resistant protein: its existence and function beneficial to health. J. Nutr. Sci. Vitaminol. (Tokyo) 48:1-5, 2002.
    • (2002) J. Nutr. Sci. Vitaminol. (Tokyo) , vol.48 , pp. 1-5
    • Kato, N.1    Iwami, K.2
  • 71
    • 1842853403 scopus 로고    scopus 로고
    • Identification of the bile acid-binding region in the soy glycinin A1aB1b subunit
    • Choi, S.K., M. Adachi, S. Utsumi. Identification of the bile acid-binding region in the soy glycinin A1aB1b subunit. Biosci. Biotechnol. Biochem. 66:2395-2401, 2002.
    • (2002) Biosci. Biotechnol. Biochem , vol.66 , pp. 2395-2401
    • Choi, S.K.1    Adachi, M.2    Utsumi, S.3
  • 72
    • 0037431027 scopus 로고    scopus 로고
    • Soymetide, an immunostimulating peptide derived from soybean B-conglycinin, is an fMLP agonist
    • Tsuruki, T., K. Kishi, M. Takahashi, M. Tanaka, T. Matsukawa, M. Yoshikawa. Soymetide, an immunostimulating peptide derived from soybean B-conglycinin, is an fMLP agonist. FEBS Lett. 540:206-210, 2003.
    • (2003) FEBS Lett , vol.540 , pp. 206-210
    • Tsuruki, T.1    Kishi, K.2    Takahashi, M.3    Tanaka, M.4    Matsukawa, T.5    Yoshikawa, M.6
  • 74
    • 0001456433 scopus 로고    scopus 로고
    • A novel methionine-rich protein from soybean cotyledon: Cloning and characterization of cDNA (Accession No. AF005030) (PGR97-103)
    • Galvez, A.F., M.J.R. Revilleza, B.O. de Lumen. A novel methionine-rich protein from soybean cotyledon: cloning and characterization of cDNA (Accession No. AF005030) (PGR97-103). Plant Physiol. 114:1567, 1997.
    • (1997) Plant Physiol , vol.114 , pp. 1567
    • Galvez, A.F.1    Revilleza, M.J.R.2    de Lumen, B.O.3
  • 76
    • 0037048768 scopus 로고    scopus 로고
    • Barley lunasin suppresses ras-induced colony formation and inhibits core histone acetylation in mammalian cells
    • Jeong, H.J., Y. Lam, B.O. de Lumen. Barley lunasin suppresses ras-induced colony formation and inhibits core histone acetylation in mammalian cells. J. Agric. Food Chem. 50(21):5903-5908, 2002.
    • (2002) J. Agric. Food Chem , vol.50 , Issue.21 , pp. 5903-5908
    • Jeong, H.J.1    Lam, Y.2    de Lumen, B.O.3


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