메뉴 건너뛰기




Volumn 111, Issue , 2014, Pages 165-183

Preventive and therapeutic potential of peptides from cereals against cancer

Author keywords

Anticancer; Bioactive peptides; Cereals; Maize

Indexed keywords

AMARANTH; ANTINEOPLASTIC AGENT; PEPTIDE; ENZYME; LUNASIN PROTEIN, BARLEY; VEGETABLE PROTEIN;

EID: 84910044710     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2014.03.044     Document Type: Review
Times cited : (95)

References (107)
  • 1
    • 35448966215 scopus 로고    scopus 로고
    • Whole grain phytochemicals and health
    • Liu R.H. Whole grain phytochemicals and health. J Cereal Sci 2007, 46:207-219.
    • (2007) J Cereal Sci , vol.46 , pp. 207-219
    • Liu, R.H.1
  • 4
    • 84910045992 scopus 로고    scopus 로고
    • Bioavailability and safety of food peptides
    • CRC Press, N.S. Hettiarachchy, K. Sato, M.R. Marshall, A. Kannan (Eds.)
    • de Mejia E., Martinez-Villaluenga C., Fernandez D., Urado D., Sato K. Bioavailability and safety of food peptides. Food proteins pept 2012, 297-330. CRC Press. N.S. Hettiarachchy, K. Sato, M.R. Marshall, A. Kannan (Eds.).
    • (2012) Food proteins pept , pp. 297-330
    • de Mejia, E.1    Martinez-Villaluenga, C.2    Fernandez, D.3    Urado, D.4    Sato, K.5
  • 5
    • 77957604071 scopus 로고    scopus 로고
    • The role of nutraceutical proteins and peptides in apoptosis, angiogenesis, and metastasis of cancer cells
    • De Mejia E.G., Dia V.P. The role of nutraceutical proteins and peptides in apoptosis, angiogenesis, and metastasis of cancer cells. Cancer Metastasis Rev 2010, 29:511-528.
    • (2010) Cancer Metastasis Rev , vol.29 , pp. 511-528
    • De Mejia, E.G.1    Dia, V.P.2
  • 6
    • 45849147682 scopus 로고    scopus 로고
    • Bioactive peptides and proteins from foods: indication for health effects
    • Möller N.P., Scholz-Ahrens K.E., Roos N., Schrezenmeir J. Bioactive peptides and proteins from foods: indication for health effects. Eur J Nutr 2008, 47:171-182.
    • (2008) Eur J Nutr , vol.47 , pp. 171-182
    • Möller, N.P.1    Scholz-Ahrens, K.E.2    Roos, N.3    Schrezenmeir, J.4
  • 7
    • 84889675077 scopus 로고    scopus 로고
    • Potential of bioactive proteins and peptides for prevention and treatment of mass non-communicable diseases
    • Belović M., Mastilović J. Potential of bioactive proteins and peptides for prevention and treatment of mass non-communicable diseases. Food Feed Res 2011, 38:51-61.
    • (2011) Food Feed Res , vol.38 , pp. 51-61
    • Belović, M.1    Mastilović, J.2
  • 8
    • 84879151240 scopus 로고    scopus 로고
    • Identification of bioactive peptides from cereal storage proteins and their potential role in prevention of chronic diseases
    • Cavazos A., Gonzalez de Mejia E. Identification of bioactive peptides from cereal storage proteins and their potential role in prevention of chronic diseases. Compr Rev Food Sci Food Saf 2013, 12:364-380.
    • (2013) Compr Rev Food Sci Food Saf , vol.12 , pp. 364-380
    • Cavazos, A.1    Gonzalez de Mejia, E.2
  • 9
    • 84868252159 scopus 로고    scopus 로고
    • Apoptosis in human hepatoma HepG2 cells induced by corn peptides and its anti-tumor efficacy in H22 tumor bearing mice
    • Li J.-T., Zhang J.-L., He H., Ma Z.-L., Nie Z.-K., Wang Z.-Z., et al. Apoptosis in human hepatoma HepG2 cells induced by corn peptides and its anti-tumor efficacy in H22 tumor bearing mice. Food Chem Toxicol 2013, 5:297-305.
    • (2013) Food Chem Toxicol , vol.5 , pp. 297-305
    • Li, J.-T.1    Zhang, J.-L.2    He, H.3    Ma, Z.-L.4    Nie, Z.-K.5    Wang, Z.-Z.6
  • 10
    • 70350057568 scopus 로고    scopus 로고
    • Apoptosis in cancer: key molecular signaling pathways and therapy targets
    • Burz C., Berindan-Neagoe I., Balacescu O., Irimie A. Apoptosis in cancer: key molecular signaling pathways and therapy targets. Acta Oncol 2009, 48:811-821.
    • (2009) Acta Oncol , vol.48 , pp. 811-821
    • Burz, C.1    Berindan-Neagoe, I.2    Balacescu, O.3    Irimie, A.4
  • 11
    • 52749085743 scopus 로고    scopus 로고
    • Targeted manipulation of apoptosis in cancer treatment
    • Call J.a, Eckhardt S.G., Camidge D.R. Targeted manipulation of apoptosis in cancer treatment. Lancet Oncol 2008, 9:1002-1011.
    • (2008) Lancet Oncol , vol.9 , pp. 1002-1011
    • Call, J.A.1    Eckhardt, S.G.2    Camidge, D.R.3
  • 12
  • 13
  • 14
    • 84880747672 scopus 로고    scopus 로고
    • Mechanism of action of conventional and targeted anticancer therapies: reinstating immunosurveillance
    • Zitvogel L., Galluzzi L., Smyth M.J., Kroemer G. Mechanism of action of conventional and targeted anticancer therapies: reinstating immunosurveillance. Immunity 2013, 39:74-88.
    • (2013) Immunity , vol.39 , pp. 74-88
    • Zitvogel, L.1    Galluzzi, L.2    Smyth, M.J.3    Kroemer, G.4
  • 15
    • 84868020147 scopus 로고    scopus 로고
    • Peptides as therapeutics with enhanced bioactivity
    • Goodwin D., Simerska P., Toth I. Peptides as therapeutics with enhanced bioactivity. Curr Med Chem 2012, 19:4451-4461.
    • (2012) Curr Med Chem , vol.19 , pp. 4451-4461
    • Goodwin, D.1    Simerska, P.2    Toth, I.3
  • 18
    • 40849151851 scopus 로고    scopus 로고
    • Targeting tumors with peptides from natural sources
    • Bhutia S.K., Maiti T.K. Targeting tumors with peptides from natural sources. Trends Biotechnol 2008, 26:210-217.
    • (2008) Trends Biotechnol , vol.26 , pp. 210-217
    • Bhutia, S.K.1    Maiti, T.K.2
  • 19
    • 84871050291 scopus 로고    scopus 로고
    • On the selectivity and efficacy of defense peptides with respect to cancer cells
    • Harris F., Dennison S., Singh J., Phoenix D.A. On the selectivity and efficacy of defense peptides with respect to cancer cells. Med Res Rev 2011, 33:190-234.
    • (2011) Med Res Rev , vol.33 , pp. 190-234
    • Harris, F.1    Dennison, S.2    Singh, J.3    Phoenix, D.A.4
  • 20
    • 77956688199 scopus 로고    scopus 로고
    • Antioxidative peptides from food proteins: a review
    • Sarmadi B.H., Ismail A. Antioxidative peptides from food proteins: a review. Peptides 2010, 31:1949-1956.
    • (2010) Peptides , vol.31 , pp. 1949-1956
    • Sarmadi, B.H.1    Ismail, A.2
  • 22
    • 0042235025 scopus 로고    scopus 로고
    • The anticarcinogenic potential of soybean lectin and lunasin
    • De Mejia E.G., Bradford T., Hasler C. The anticarcinogenic potential of soybean lectin and lunasin. Nutr Rev 2003, 61:239-246.
    • (2003) Nutr Rev , vol.61 , pp. 239-246
    • De Mejia, E.G.1    Bradford, T.2    Hasler, C.3
  • 23
    • 84910096125 scopus 로고    scopus 로고
    • Chemistry and Biological Properties of Soybean Peptides and Proteins.
    • In: Cadwallader KR, Chang SKC, editors. Chem. texture, flavor soy, 236th ACS National Meeting in Philadelphia, PA, August 17-21, 2008.: Washington, DC: American Chemical Society; [New York]: Distributed by Oxford University Press, c2010;
    • González de Mejia E, Dia VP. Chemistry and Biological Properties of Soybean Peptides and Proteins. In: Cadwallader KR, Chang SKC, editors. Chem. texture, flavor soy, 236th ACS National Meeting in Philadelphia, PA, August 17-21, 2008.: Washington, DC: American Chemical Society; [New York]: Distributed by Oxford University Press, c2010; 2010, p. 131-51.
    • (2010) , pp. 131-151
    • González de, M.E.1    Dia, V.P.2
  • 24
    • 61349187630 scopus 로고    scopus 로고
    • Lunasin and Bowman-Birk protease inhibitor (BBI) in US commercial soy foods
    • Hernández-Ledesma B., Hsieh C.-C., de Lumen B.O. Lunasin and Bowman-Birk protease inhibitor (BBI) in US commercial soy foods. Food Chem 2009, 115:574-580.
    • (2009) Food Chem , vol.115 , pp. 574-580
    • Hernández-Ledesma, B.1    Hsieh, C.-C.2    de Lumen, B.O.3
  • 25
    • 0015501044 scopus 로고
    • Isolation and properties of complexes of the Bowman-Birk soybean inhibitor with isolation and properties of complexes soybean inhibitor with trypsin and chymotrypsin *
    • Seidl D.S., Liener I.E. Isolation and properties of complexes of the Bowman-Birk soybean inhibitor with isolation and properties of complexes soybean inhibitor with trypsin and chymotrypsin *. J Biol Chem 1972, 247:3533-3538.
    • (1972) J Biol Chem , vol.247 , pp. 3533-3538
    • Seidl, D.S.1    Liener, I.E.2
  • 26
    • 0023645219 scopus 로고
    • Amino acid sequence of a soybean (glycine max) seed polypeptide having a poly (l-aspartic acid) structure
    • Odani S., Koide T., Ono T. Amino acid sequence of a soybean (glycine max) seed polypeptide having a poly (l-aspartic acid) structure. J Biol Chem 1987, 262:10502-10505.
    • (1987) J Biol Chem , vol.262 , pp. 10502-10505
    • Odani, S.1    Koide, T.2    Ono, T.3
  • 27
    • 38049048144 scopus 로고    scopus 로고
    • In vitro digestibility of the cancer-preventive soy peptides lunasin and BBI
    • Park J.H., Jeong H.J., De Lumen B.O. In vitro digestibility of the cancer-preventive soy peptides lunasin and BBI. J Agric Food Chem 2007, 55:10703-10706.
    • (2007) J Agric Food Chem , vol.55 , pp. 10703-10706
    • Park, J.H.1    Jeong, H.J.2    De Lumen, B.O.3
  • 28
    • 84857467921 scopus 로고    scopus 로고
    • Recombinant production of the therapeutic peptide lunasin
    • Kyle S., James K.a R., McPherson M.J. Recombinant production of the therapeutic peptide lunasin. Microb Cell Fact 2012, 11:28.
    • (2012) Microb Cell Fact , vol.11 , pp. 28
    • Kyle, S.1    James, K.A.R.2    McPherson, M.J.3
  • 29
    • 77955849431 scopus 로고    scopus 로고
    • Recombinant expression of bioactive peptide lunasin in Escherichia coli
    • Liu C.-F., Pan T.-M. Recombinant expression of bioactive peptide lunasin in Escherichia coli. Appl Microbiol Biotechnol 2010, 88:177-186.
    • (2010) Appl Microbiol Biotechnol , vol.88 , pp. 177-186
    • Liu, C.-F.1    Pan, T.-M.2
  • 30
    • 84877130395 scopus 로고    scopus 로고
    • Lunasin in cereal seeds: what is the origin?
    • Mitchell R., Lovegrove A., Shewry P. Lunasin in cereal seeds: what is the origin?. J Cereal Sci 2013, 57:267-269.
    • (2013) J Cereal Sci , vol.57 , pp. 267-269
    • Mitchell, R.1    Lovegrove, A.2    Shewry, P.3
  • 31
    • 78650679342 scopus 로고    scopus 로고
    • Apoptosis of human breast cancer cells induced by hemagglutinin from Phaseolus vulgaris cv. Legumi secchi
    • Lam S.K., Ng T.B. Apoptosis of human breast cancer cells induced by hemagglutinin from Phaseolus vulgaris cv. Legumi secchi. Food Chem 2011, 126:595-602.
    • (2011) Food Chem , vol.126 , pp. 595-602
    • Lam, S.K.1    Ng, T.B.2
  • 32
    • 26244452026 scopus 로고    scopus 로고
    • Tannins, trypsin inhibitors and lectin cytotoxicity in tepary (Phaseolus acutifolius) and common (Phaseolus vulgaris) beans
    • De Mejia E.G., Del Carmen Valadez-Vega M., Reynoso-Camacho R., Loarca-Pina G. Tannins, trypsin inhibitors and lectin cytotoxicity in tepary (Phaseolus acutifolius) and common (Phaseolus vulgaris) beans. Plant Foods Hum Nutr 2005, 60:137-145.
    • (2005) Plant Foods Hum Nutr , vol.60 , pp. 137-145
    • De Mejia, E.G.1    Del Carmen, V.V.M.2    Reynoso-Camacho, R.3    Loarca-Pina, G.4
  • 33
    • 58549103081 scopus 로고    scopus 로고
    • Isolation and biochemical characterization of a novel leguminous defense peptide with antifungal and antiproliferative potency
    • Wang S., Rao P., Ye X. Isolation and biochemical characterization of a novel leguminous defense peptide with antifungal and antiproliferative potency. Appl Microbiol Biotechnol 2009, 82:79-86.
    • (2009) Appl Microbiol Biotechnol , vol.82 , pp. 79-86
    • Wang, S.1    Rao, P.2    Ye, X.3
  • 34
    • 33846588323 scopus 로고    scopus 로고
    • Isolation and characterization of an antifungal peptide with antiproliferative activity from seeds of Phaseolus vulgaris cv. "Spotted Bean"
    • Wang H.X., Ng T.B. Isolation and characterization of an antifungal peptide with antiproliferative activity from seeds of Phaseolus vulgaris cv. "Spotted Bean". Appl Microbiol Biotechnol 2007, 74:125-130.
    • (2007) Appl Microbiol Biotechnol , vol.74 , pp. 125-130
    • Wang, H.X.1    Ng, T.B.2
  • 35
    • 2942565729 scopus 로고    scopus 로고
    • Nutritional aspects of cereals
    • McKevith B. Nutritional aspects of cereals. Nutr Bull 2004, 29:111-142.
    • (2004) Nutr Bull , vol.29 , pp. 111-142
    • McKevith, B.1
  • 36
    • 77953441545 scopus 로고    scopus 로고
    • Colon and breast anti-cancer effects of peptide hydrolysates derived from rice bran
    • Kannan A., Hettiarachchy N., Narayan S. Colon and breast anti-cancer effects of peptide hydrolysates derived from rice bran. Open Bioact Compd J 2009, 2:17-20.
    • (2009) Open Bioact Compd J , vol.2 , pp. 17-20
    • Kannan, A.1    Hettiarachchy, N.2    Narayan, S.3
  • 37
    • 84904433867 scopus 로고    scopus 로고
    • The comparison of prolamins extracted from different varieties of wheat, barley, rye and triticale species: amino acid composition, electrophoresis and immunodetection
    • Mickowska B., Socha P., Urminská D., Cieślik E. The comparison of prolamins extracted from different varieties of wheat, barley, rye and triticale species: amino acid composition, electrophoresis and immunodetection. J Microbiol Biotechnol Food Sci 2012, 1:742-752.
    • (2012) J Microbiol Biotechnol Food Sci , vol.1 , pp. 742-752
    • Mickowska, B.1    Socha, P.2    Urminská, D.3    Cieślik, E.4
  • 38
    • 79960845541 scopus 로고    scopus 로고
    • Effects of enzymatic hydrolysis on molecular structure and antioxidant activity of barley hordein
    • Bamdad F., Wu J., Chen L. Effects of enzymatic hydrolysis on molecular structure and antioxidant activity of barley hordein. J Cereal Sci 2011, 54:20-28.
    • (2011) J Cereal Sci , vol.54 , pp. 20-28
    • Bamdad, F.1    Wu, J.2    Chen, L.3
  • 39
    • 67349160258 scopus 로고    scopus 로고
    • Antioxidative properties of partially purified barley hordein, rice bran protein fractions and their hydrolysates
    • Chanput W., Theerakulkait C., Nakai S. Antioxidative properties of partially purified barley hordein, rice bran protein fractions and their hydrolysates. J Cereal Sci 2009, 49:422-428.
    • (2009) J Cereal Sci , vol.49 , pp. 422-428
    • Chanput, W.1    Theerakulkait, C.2    Nakai, S.3
  • 40
    • 0037048768 scopus 로고    scopus 로고
    • Barley lunasin suppresses ras-induced colony formation and inhibits core histone acetylation in mammalian cells
    • Jeong H.J., Lam Y., de Lumen B.O. Barley lunasin suppresses ras-induced colony formation and inhibits core histone acetylation in mammalian cells. J Agric Food Chem 2002, 50:5903-5908.
    • (2002) J Agric Food Chem , vol.50 , pp. 5903-5908
    • Jeong, H.J.1    Lam, Y.2    de Lumen, B.O.3
  • 41
    • 78249282622 scopus 로고    scopus 로고
    • Lunasin is prevalent in barley and is bioavailable and bioactive in in vivo and in vitro studies
    • Jeong H., Jeong J. Lunasin is prevalent in barley and is bioavailable and bioactive in in vivo and in vitro studies. Nutr Cancer 2010, 62:1113-1119.
    • (2010) Nutr Cancer , vol.62 , pp. 1113-1119
    • Jeong, H.1    Jeong, J.2
  • 42
    • 84890508448 scopus 로고    scopus 로고
    • Lunasin in wheat: a chemical and molecular study on its presence or absence
    • Dinelli G., Bregola V., Bosi S., Fiori J., Gotti R., Simonetti E., et al. Lunasin in wheat: a chemical and molecular study on its presence or absence. Food Chem 2014, 151:520-525.
    • (2014) Food Chem , vol.151 , pp. 520-525
    • Dinelli, G.1    Bregola, V.2    Bosi, S.3    Fiori, J.4    Gotti, R.5    Simonetti, E.6
  • 43
    • 84873995617 scopus 로고    scopus 로고
    • Maize proteomics: an insight into the biology of an important cereal crop
    • Pechanova O., Takáč T., Samaj J., Pechan T. Maize proteomics: an insight into the biology of an important cereal crop. Proteomics 2013, 13:637-662.
    • (2013) Proteomics , vol.13 , pp. 637-662
    • Pechanova, O.1    Takáč, T.2    Samaj, J.3    Pechan, T.4
  • 44
    • 46049118997 scopus 로고    scopus 로고
    • Influence of drying temperature on the solubility, the purity of isolates and the electrophoretic patterns of corn proteins
    • Malumba P., Vanderghem C., Deroanne C., Béra F. Influence of drying temperature on the solubility, the purity of isolates and the electrophoretic patterns of corn proteins. Food Chem 2008, 111:564-572.
    • (2008) Food Chem , vol.111 , pp. 564-572
    • Malumba, P.1    Vanderghem, C.2    Deroanne, C.3    Béra, F.4
  • 45
    • 80054969593 scopus 로고    scopus 로고
    • Histochemical analysis and protein content of maize landraces (Zea mays L.)
    • Uarrota V., Schmidt E. Histochemical analysis and protein content of maize landraces (Zea mays L.). J Agron 2011, 10:92-98.
    • (2011) J Agron , vol.10 , pp. 92-98
    • Uarrota, V.1    Schmidt, E.2
  • 46
    • 46049116527 scopus 로고    scopus 로고
    • In vitro antioxidant activity of protein hydrolysates prepared from corn gluten meal
    • Li X., Han L., Chen L. In vitro antioxidant activity of protein hydrolysates prepared from corn gluten meal. J Sci Food Agric 2008, 1666:1660-1666.
    • (2008) J Sci Food Agric , vol.1666 , pp. 1660-1666
    • Li, X.1    Han, L.2    Chen, L.3
  • 47
    • 43649091361 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme-inhibitory peptides from commercial wet- and dry-milled corn germ
    • Parris N., Moreau R.a, Johnston D.B., Dickey L.C., Aluko R.E. Angiotensin I converting enzyme-inhibitory peptides from commercial wet- and dry-milled corn germ. J Agric Food Chem 2008, 56:2620-2623.
    • (2008) J Agric Food Chem , vol.56 , pp. 2620-2623
    • Parris, N.1    Moreau, R.A.2    Johnston, D.B.3    Dickey, L.C.4    Aluko, R.E.5
  • 48
    • 34948841863 scopus 로고    scopus 로고
    • Peptide with angiotensin I-converting enzyme inhibitory activity from hydrolyzed corn gluten meal
    • Yang Y., Tao G., Liu P., Liu J. Peptide with angiotensin I-converting enzyme inhibitory activity from hydrolyzed corn gluten meal. J Agric Food Chem 2007, 55:7891-7895.
    • (2007) J Agric Food Chem , vol.55 , pp. 7891-7895
    • Yang, Y.1    Tao, G.2    Liu, P.3    Liu, J.4
  • 50
    • 0030914153 scopus 로고    scopus 로고
    • Inhibitory effect of peptide prepared from corn gluten meal on 7, 12-dimethylbenz anthracene-induced mammary tumor progression in rats
    • Yamaguchi M., Takeuchi M., Ebihara K. Inhibitory effect of peptide prepared from corn gluten meal on 7, 12-dimethylbenz anthracene-induced mammary tumor progression in rats. Nutr Res 1997, 17:1121-1130.
    • (1997) Nutr Res , vol.17 , pp. 1121-1130
    • Yamaguchi, M.1    Takeuchi, M.2    Ebihara, K.3
  • 52
    • 49449093779 scopus 로고    scopus 로고
    • Is the in vitro antioxidant potential of whole-grain cereals and cereal products well reflected in vivo?
    • Fardet A., Rock E., Rémésy C. Is the in vitro antioxidant potential of whole-grain cereals and cereal products well reflected in vivo?. J Cereal Sci 2008, 48:258-276.
    • (2008) J Cereal Sci , vol.48 , pp. 258-276
    • Fardet, A.1    Rock, E.2    Rémésy, C.3
  • 53
    • 77649340408 scopus 로고    scopus 로고
    • Prolamin, a rice protein, augments anti-leukaemia immune response
    • Chen Y., Chen Y., Wu C., Yu C., Liao H. Prolamin, a rice protein, augments anti-leukaemia immune response. J Cereal Sci 2010, 51:189-197.
    • (2010) J Cereal Sci , vol.51 , pp. 189-197
    • Chen, Y.1    Chen, Y.2    Wu, C.3    Yu, C.4    Liao, H.5
  • 54
    • 33745747265 scopus 로고    scopus 로고
    • In vitro actions on human cancer cells and the liquid chromatography-mass spectrometry/mass spectrometry fingerprint of phytochemicals in rice protein isolate
    • Yu S., Fang N., Li Q., Zhang J., Luo H., Ronis M., et al. In vitro actions on human cancer cells and the liquid chromatography-mass spectrometry/mass spectrometry fingerprint of phytochemicals in rice protein isolate. J Agric Food Chem 2006, 54:4482-4492.
    • (2006) J Agric Food Chem , vol.54 , pp. 4482-4492
    • Yu, S.1    Fang, N.2    Li, Q.3    Zhang, J.4    Luo, H.5    Ronis, M.6
  • 55
    • 58849131577 scopus 로고    scopus 로고
    • Human colon and liver cancer cell proliferation inhibition by peptide hydrolysates derived from heat-stabilized defatted rice bran
    • Kannan A., Hettiarachchy N., Johnson M.G., Nannapaneni R. Human colon and liver cancer cell proliferation inhibition by peptide hydrolysates derived from heat-stabilized defatted rice bran. J Agric Food Chem 2008, 56:11643-11647.
    • (2008) J Agric Food Chem , vol.56 , pp. 11643-11647
    • Kannan, A.1    Hettiarachchy, N.2    Johnson, M.G.3    Nannapaneni, R.4
  • 56
    • 77955659706 scopus 로고    scopus 로고
    • Human cancer cell proliferation inhibition by a pentapeptide isolated and characterized from rice bran
    • Kannan A., Hettiarachchy N.S., Lay J.O., Liyanage R. Human cancer cell proliferation inhibition by a pentapeptide isolated and characterized from rice bran. Peptides 2010, 31:1629-1634.
    • (2010) Peptides , vol.31 , pp. 1629-1634
    • Kannan, A.1    Hettiarachchy, N.S.2    Lay, J.O.3    Liyanage, R.4
  • 58
    • 70449635964 scopus 로고    scopus 로고
    • The cancer preventive seed peptide lunasin from rye is bioavailable and bioactive
    • Jeong H.J., Lee J.R., Jeong J.B., Park J.H., Cheong Y., de Lumen B.O. The cancer preventive seed peptide lunasin from rye is bioavailable and bioactive. Nutr Cancer 2009, 61:680-686.
    • (2009) Nutr Cancer , vol.61 , pp. 680-686
    • Jeong, H.J.1    Lee, J.R.2    Jeong, J.B.3    Park, J.H.4    Cheong, Y.5    de Lumen, B.O.6
  • 61
    • 67349268149 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme-inhibitory peptide fractions from albumin 1 and globulin as obtained of amaranth grain
    • Tovar-Pérez E.G., Guerrero-Legarreta I., Farrés-González A., Soriano-Santos J. Angiotensin I-converting enzyme-inhibitory peptide fractions from albumin 1 and globulin as obtained of amaranth grain. Food Chem 2009, 116:437-444.
    • (2009) Food Chem , vol.116 , pp. 437-444
    • Tovar-Pérez, E.G.1    Guerrero-Legarreta, I.2    Farrés-González, A.3    Soriano-Santos, J.4
  • 62
    • 78751580546 scopus 로고    scopus 로고
    • Amaranth seed protein hydrolysates have in vivo and in vitro antihypertensive activity
    • Fritz M., Vecchi B., Rinaldi G., Añón M.C. Amaranth seed protein hydrolysates have in vivo and in vitro antihypertensive activity. Food Chem 2011, 126:878-884.
    • (2011) Food Chem , vol.126 , pp. 878-884
    • Fritz, M.1    Vecchi, B.2    Rinaldi, G.3    Añón, M.C.4
  • 63
    • 0034625508 scopus 로고    scopus 로고
    • Separation and detection techniques for peptides and proteins in stability research and bioanalysis
    • Underberg W.J., Hoitink M.a, Reubsaet J.L., Waterval J.C. Separation and detection techniques for peptides and proteins in stability research and bioanalysis. J Chromatogr B Biomed Sci Appl 2000, 742:401-409.
    • (2000) J Chromatogr B Biomed Sci Appl , vol.742 , pp. 401-409
    • Underberg, W.J.1    Hoitink, M.A.2    Reubsaet, J.L.3    Waterval, J.C.4
  • 65
    • 84856032752 scopus 로고    scopus 로고
    • Food protein-derived bioactive peptides: production, processing, and potential health benefits
    • Udenigwe C.C., Aluko R.E. Food protein-derived bioactive peptides: production, processing, and potential health benefits. J Food Sci 2012, 77:R11-R24.
    • (2012) J Food Sci , vol.77 , pp. R11-R24
    • Udenigwe, C.C.1    Aluko, R.E.2
  • 66
    • 0036745679 scopus 로고    scopus 로고
    • Methods for fractionation, separation and profiling of proteins and peptides
    • Issaq H., Conrads T.P., Janini G., Veenstra T.D. Methods for fractionation, separation and profiling of proteins and peptides. Electrophoresis 2002, 23:3048-3061.
    • (2002) Electrophoresis , vol.23 , pp. 3048-3061
    • Issaq, H.1    Conrads, T.P.2    Janini, G.3    Veenstra, T.D.4
  • 67
    • 34147123803 scopus 로고    scopus 로고
    • Food-derived peptides with biological activity: from research to food applications
    • Hartmann R., Meisel H. Food-derived peptides with biological activity: from research to food applications. Curr Opin Biotechnol 2007, 18:163-169.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 163-169
    • Hartmann, R.1    Meisel, H.2
  • 68
    • 35448968595 scopus 로고    scopus 로고
    • Antimicrobial and human cancer cell cytotoxic effect of synthetic angiotensin-converting enzyme (ACE) inhibitory peptides
    • Jang A., Jo C., Kang K.-S., Lee M. Antimicrobial and human cancer cell cytotoxic effect of synthetic angiotensin-converting enzyme (ACE) inhibitory peptides. Food Chem 2008, 107:327-336.
    • (2008) Food Chem , vol.107 , pp. 327-336
    • Jang, A.1    Jo, C.2    Kang, K.-S.3    Lee, M.4
  • 69
    • 0038397146 scopus 로고    scopus 로고
    • Food-derived bioactive peptides-opportunities for designing future foods
    • Korhonen H., Pihlanto a Food-derived bioactive peptides-opportunities for designing future foods. Curr Pharm Des 2003, 9:1297-1308.
    • (2003) Curr Pharm Des , vol.9 , pp. 1297-1308
    • Korhonen, H.1    Pihlanto, A.2
  • 70
    • 71449111669 scopus 로고    scopus 로고
    • Effect of protein hydrolysates from germinated soybean on cancerous cells of the human cervix: an in vitro study
    • Mora-Escobedo R., Robles-Ramírez M.D.C., Ramón-Gallegos E., Reza-Alemán R. Effect of protein hydrolysates from germinated soybean on cancerous cells of the human cervix: an in vitro study. Plant Foods Hum Nutr 2009, 64:271-278.
    • (2009) Plant Foods Hum Nutr , vol.64 , pp. 271-278
    • Mora-Escobedo, R.1    Robles-Ramírez, M.D.C.2    Ramón-Gallegos, E.3    Reza-Alemán, R.4
  • 71
    • 84883554130 scopus 로고    scopus 로고
    • Optimisation of antioxidant peptide preparation from corn gluten meal
    • Zhuang H., Tang N., Dong S.-T., Sun B., Liu J.-B. Optimisation of antioxidant peptide preparation from corn gluten meal. J Sci Food Agric 2013, 93:3264-3270.
    • (2013) J Sci Food Agric , vol.93 , pp. 3264-3270
    • Zhuang, H.1    Tang, N.2    Dong, S.-T.3    Sun, B.4    Liu, J.-B.5
  • 72
    • 33744947035 scopus 로고    scopus 로고
    • Selective separation of peptides contained in a rapeseed (Brassica campestris L.) protein hydrolysate using UF/NF membranes
    • Tessier B., Harscoat-Schiavo C., Marc I. Selective separation of peptides contained in a rapeseed (Brassica campestris L.) protein hydrolysate using UF/NF membranes. J Agric Food Chem 2006, 54:3578-3584.
    • (2006) J Agric Food Chem , vol.54 , pp. 3578-3584
    • Tessier, B.1    Harscoat-Schiavo, C.2    Marc, I.3
  • 73
    • 84865710230 scopus 로고    scopus 로고
    • Concentration and selective fractionation of an antihypertensive peptide from an alfalfa white proteins hydrolysate by mixed ion-exchange centrifugal partition chromatography
    • Boudesocque L., Kapel R., Paris C., Dhulster P., Marc I., Renault J.-H. Concentration and selective fractionation of an antihypertensive peptide from an alfalfa white proteins hydrolysate by mixed ion-exchange centrifugal partition chromatography. J Chromatogr B Analyt Technol Biomed Life Sci 2012, 905:23-30.
    • (2012) J Chromatogr B Analyt Technol Biomed Life Sci , vol.905 , pp. 23-30
    • Boudesocque, L.1    Kapel, R.2    Paris, C.3    Dhulster, P.4    Marc, I.5    Renault, J.-H.6
  • 74
    • 84860624979 scopus 로고    scopus 로고
    • A peptide fraction from germinated soybean protein down-regulates PTTG1 and TOP2A mRNA expression, inducing apoptosis in cervical cancer cells
    • Robles-Ramírez M.D.C., Ramón-Gallegos E., Mora-Escobedo R., Torres-Torres N. A peptide fraction from germinated soybean protein down-regulates PTTG1 and TOP2A mRNA expression, inducing apoptosis in cervical cancer cells. J Exp Ther Oncol 2012, 9:255-263.
    • (2012) J Exp Ther Oncol , vol.9 , pp. 255-263
    • Robles-Ramírez, M.D.C.1    Ramón-Gallegos, E.2    Mora-Escobedo, R.3    Torres-Torres, N.4
  • 75
    • 84865779303 scopus 로고    scopus 로고
    • Production and functional characterisation of antioxidative hydrolysates from corn protein via enzymatic hydrolysis and ultrafiltration
    • Zhou K., Sun S., Canning C. Production and functional characterisation of antioxidative hydrolysates from corn protein via enzymatic hydrolysis and ultrafiltration. Food Chem 2012, 135:1192-1197.
    • (2012) Food Chem , vol.135 , pp. 1192-1197
    • Zhou, K.1    Sun, S.2    Canning, C.3
  • 77
    • 55749100643 scopus 로고    scopus 로고
    • Peptide enrichment and protein fractionation using selective electrophoresis
    • Ly L., Wasinger V.C. Peptide enrichment and protein fractionation using selective electrophoresis. Proteomics 2008, 8:4197-4208.
    • (2008) Proteomics , vol.8 , pp. 4197-4208
    • Ly, L.1    Wasinger, V.C.2
  • 78
    • 0034855204 scopus 로고    scopus 로고
    • Prefractionation of protein samples for proteome analysis using reversed-phase high-performance liquid chromatography
    • Badock V., Steinhusen U., Bommert K., Otto a Prefractionation of protein samples for proteome analysis using reversed-phase high-performance liquid chromatography. Electrophoresis 2001, 22:2856-2864.
    • (2001) Electrophoresis , vol.22 , pp. 2856-2864
    • Badock, V.1    Steinhusen, U.2    Bommert, K.3    Otto, A.4
  • 79
    • 84863008002 scopus 로고    scopus 로고
    • Divergent-flow isoelectric focusing for separation and preparative analysis of peptides
    • Duša F., Křenková J., Moravcová D., Kahle V., Slais K. Divergent-flow isoelectric focusing for separation and preparative analysis of peptides. Electrophoresis 2012, 33:1687-1694.
    • (2012) Electrophoresis , vol.33 , pp. 1687-1694
    • Duša, F.1    Křenková, J.2    Moravcová, D.3    Kahle, V.4    Slais, K.5
  • 80
    • 20744440660 scopus 로고    scopus 로고
    • On-line concentration of peptides and proteins with the hyphenation of polymer monolithic immobilized metal affinity chromatography and capillary electrophoresis
    • Zhang L., Zhang L., Zhang W., Zhang Y. On-line concentration of peptides and proteins with the hyphenation of polymer monolithic immobilized metal affinity chromatography and capillary electrophoresis. Electrophoresis 2005, 26:2172-2178.
    • (2005) Electrophoresis , vol.26 , pp. 2172-2178
    • Zhang, L.1    Zhang, L.2    Zhang, W.3    Zhang, Y.4
  • 81
    • 84874622504 scopus 로고    scopus 로고
    • Single-shot using capillary zone electrophoresis-electrospray ionization-tandem mass spectrometry with production of more than 1 250 Escherichia coli peptide identifications in a 50min separation
    • Zhu G., Sun L., Yan X., Dovichi N.J. Single-shot using capillary zone electrophoresis-electrospray ionization-tandem mass spectrometry with production of more than 1 250 Escherichia coli peptide identifications in a 50min separation. Anal Chem 2013, 85:2569-2573.
    • (2013) Anal Chem , vol.85 , pp. 2569-2573
    • Zhu, G.1    Sun, L.2    Yan, X.3    Dovichi, N.J.4
  • 82
    • 84867795781 scopus 로고    scopus 로고
    • On-line CE/ESI/MS interfacing: recent developments and applications in proteomics
    • Krenkova J., Foret F. On-line CE/ESI/MS interfacing: recent developments and applications in proteomics. Proteomics 2012, 12:2978-2990.
    • (2012) Proteomics , vol.12 , pp. 2978-2990
    • Krenkova, J.1    Foret, F.2
  • 84
    • 78650430661 scopus 로고    scopus 로고
    • Quantification of α-polylysine: a comparison of four UV/vis spectrophotometric methods
    • Grotzky A., Manaka Y., Fornera S., Willeke M., Walde P. Quantification of α-polylysine: a comparison of four UV/vis spectrophotometric methods. Anal Methods 2010, 2:1448-1455.
    • (2010) Anal Methods , vol.2 , pp. 1448-1455
    • Grotzky, A.1    Manaka, Y.2    Fornera, S.3    Willeke, M.4    Walde, P.5
  • 86
    • 0000369624 scopus 로고
    • A method for the determination of amino acid sequence in peptides
    • Edman P. A method for the determination of amino acid sequence in peptides. Arch Biochem 1949, 22.
    • (1949) Arch Biochem , vol.22
    • Edman, P.1
  • 87
    • 0014064044 scopus 로고
    • A protein sequenator
    • Edman P., Begg G. A protein sequenator. Eur J Biochem 1967, 1:80-91.
    • (1967) Eur J Biochem , vol.1 , pp. 80-91
    • Edman, P.1    Begg, G.2
  • 88
    • 0017346884 scopus 로고
    • Rapid analysis of amino acid phenylthiohydantoins by high-performance liquid chromatography
    • Zimmerman C.L., Appella E., Pisano J.J. Rapid analysis of amino acid phenylthiohydantoins by high-performance liquid chromatography. Anal Biochem 1977, 77:569-573.
    • (1977) Anal Biochem , vol.77 , pp. 569-573
    • Zimmerman, C.L.1    Appella, E.2    Pisano, J.J.3
  • 89
    • 0035836750 scopus 로고    scopus 로고
    • Attomole level protein sequencing by Edman degradation coupled with accelerator mass spectrometry
    • Miyashita M., Presley J.M., Buchholz B.A., Lam K.S., Lee Y.M., Vogel J.S., et al. Attomole level protein sequencing by Edman degradation coupled with accelerator mass spectrometry. Proc Natl Acad Sci U S A 2001, 98:4403-4408.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 4403-4408
    • Miyashita, M.1    Presley, J.M.2    Buchholz, B.A.3    Lam, K.S.4    Lee, Y.M.5    Vogel, J.S.6
  • 90
    • 50649104560 scopus 로고    scopus 로고
    • Application of mass spectrometry to the characterization and quantification of food-derived bioactive peptides
    • Contreras M del M., López-Expósito I., Hernández-Ledesma B., Ramos M., Recio I. Application of mass spectrometry to the characterization and quantification of food-derived bioactive peptides. J AOAC Int 2008, 91:981-994.
    • (2008) J AOAC Int , vol.91 , pp. 981-994
    • Contreras M del, M.1    López-Expósito, I.2    Hernández-Ledesma, B.3    Ramos, M.4    Recio, I.5
  • 91
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn J.B., Mann M., Meng C.K., Wong S.F., Whitehouse C.M. Electrospray ionization for mass spectrometry of large biomolecules. Science 1989, 246:64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 92
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas M., Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal Chem 1988, 60:2299-2301.
    • (1988) Anal Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 93
    • 84857872572 scopus 로고    scopus 로고
    • Separation and identification of isomeric glycopeptides by high field asymmetric waveform ion mobility spectrometry
    • Creese A.J., Cooper H.J. Separation and identification of isomeric glycopeptides by high field asymmetric waveform ion mobility spectrometry. Anal Chem 2012, 84:2597-2601.
    • (2012) Anal Chem , vol.84 , pp. 2597-2601
    • Creese, A.J.1    Cooper, H.J.2
  • 95
    • 33845960314 scopus 로고    scopus 로고
    • How to discriminate between leucine and isoleucine by low energy ESI-TRAP MSn
    • Armirotti A., Millo E., Damonte G. How to discriminate between leucine and isoleucine by low energy ESI-TRAP MSn. J Am Soc Mass Spectrom 2007, 18:57-63.
    • (2007) J Am Soc Mass Spectrom , vol.18 , pp. 57-63
    • Armirotti, A.1    Millo, E.2    Damonte, G.3
  • 96
    • 79251496133 scopus 로고    scopus 로고
    • Post-translational modifications in secreted peptide hormones in plants
    • Matsubayashi Y. Post-translational modifications in secreted peptide hormones in plants. Plant Cell Physiol 2011, 52:5-13.
    • (2011) Plant Cell Physiol , vol.52 , pp. 5-13
    • Matsubayashi, Y.1
  • 98
    • 67649563273 scopus 로고    scopus 로고
    • Quantification of post-translationally modified peptides of bovine α-crystallin using tandem mass tags and electron transfer dissociation
    • Viner R.I., Zhang T., Second T., Zabrouskov V. Quantification of post-translationally modified peptides of bovine α-crystallin using tandem mass tags and electron transfer dissociation. J Proteomics 2009, 72:874-885.
    • (2009) J Proteomics , vol.72 , pp. 874-885
    • Viner, R.I.1    Zhang, T.2    Second, T.3    Zabrouskov, V.4
  • 99
    • 84868123896 scopus 로고    scopus 로고
    • Use of CID/ETD mass spectrometry to analyze glycopeptides
    • [Unit-12.1111]
    • Mechref Y. Use of CID/ETD mass spectrometry to analyze glycopeptides. Curr Protoc Protein Sci 2012, 0 12. [Unit-12.1111].
    • (2012) Curr Protoc Protein Sci
    • Mechref, Y.1
  • 100
    • 77953911347 scopus 로고    scopus 로고
    • Mass spectrometric identification of oxidative modifications of tryptophan residues in proteins: chemical artifact or post-translational modification?
    • Perdivara I., Deterding L.J., Przybylski M., Tomer K.B. Mass spectrometric identification of oxidative modifications of tryptophan residues in proteins: chemical artifact or post-translational modification?. J Am Soc Mass Spectrom 2010, 21:1114-1117.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 1114-1117
    • Perdivara, I.1    Deterding, L.J.2    Przybylski, M.3    Tomer, K.B.4
  • 101
    • 84866373857 scopus 로고    scopus 로고
    • MMass as a software tool for the annotation of cyclic peptide tandem mass spectra
    • Niedermeyer T.H.J., Strohalm M. mMass as a software tool for the annotation of cyclic peptide tandem mass spectra. PLoS One 2012, 7:e44913.
    • (2012) PLoS One , vol.7 , pp. e44913
    • Niedermeyer, T.H.J.1    Strohalm, M.2
  • 102
    • 13844319908 scopus 로고    scopus 로고
    • PepNovo: de novo peptide sequencing via probabilistic network modeling
    • Frank A., Pevzner P. PepNovo: de novo peptide sequencing via probabilistic network modeling. Anal Chem 2005, 77:964-973.
    • (2005) Anal Chem , vol.77 , pp. 964-973
    • Frank, A.1    Pevzner, P.2
  • 103
    • 84881019650 scopus 로고    scopus 로고
    • UniNovo: a universal tool for de novo peptide sequencing
    • Jeong K., Kim S., Pevzner P.a UniNovo: a universal tool for de novo peptide sequencing. Bioinformatics 2013, 29:1953-1962.
    • (2013) Bioinformatics , vol.29 , pp. 1953-1962
    • Jeong, K.1    Kim, S.2    Pevzner, P.A.3
  • 104
    • 84893299991 scopus 로고    scopus 로고
    • MASSyPup - an "Out of the Box" solution for the analysis of mass spectrometry data
    • Winkler R. MASSyPup - an "Out of the Box" solution for the analysis of mass spectrometry data. J Mass Spectrom 2014, 49:37-42.
    • (2014) J Mass Spectrom , vol.49 , pp. 37-42
    • Winkler, R.1
  • 105
    • 80055022984 scopus 로고    scopus 로고
    • X-ray crystallographic structure of the cyclic di-amino acid peptide: N,N'-Diacetyl-cyclo(Gly-Gly)
    • Mendham A.P., Spencer J., Chowdhry B.Z., Dines T.J., Mujahid M., Palmer R.a, et al. X-ray crystallographic structure of the cyclic di-amino acid peptide: N,N'-Diacetyl-cyclo(Gly-Gly). J Chem Crystallogr 2011, 41:1323-1327.
    • (2011) J Chem Crystallogr , vol.41 , pp. 1323-1327
    • Mendham, A.P.1    Spencer, J.2    Chowdhry, B.Z.3    Dines, T.J.4    Mujahid, M.5    Palmer, R.A.6
  • 106
    • 84885489624 scopus 로고    scopus 로고
    • NMR of peptides
    • Wiley-VCH Verlag GmbH & Co. KGaA, I. Bertini, K.S. McGreevy, G. Parigi (Eds.)
    • Beck J.G., Frank A.O., Kessler H. NMR of peptides. NMR biomol 2012, 328-344. Wiley-VCH Verlag GmbH & Co. KGaA. I. Bertini, K.S. McGreevy, G. Parigi (Eds.).
    • (2012) NMR biomol , pp. 328-344
    • Beck, J.G.1    Frank, A.O.2    Kessler, H.3
  • 107
    • 0031154435 scopus 로고    scopus 로고
    • NMR spectroscopy of peptides and proteins. Practical considerations
    • Hinds M.G., Norton R.S. NMR spectroscopy of peptides and proteins. Practical considerations. Mol Biotechnol 1997, 7:315-331.
    • (1997) Mol Biotechnol , vol.7 , pp. 315-331
    • Hinds, M.G.1    Norton, R.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.