메뉴 건너뛰기




Volumn 27, Issue 4, 2011, Pages 357-388

The preventive potential of milk and colostrum proteins and protein fragments

Author keywords

Biological activity; Colostrum; Disease; Milk; Peptides; Preventive potential; Proteins

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS;

EID: 79960372598     PISSN: 87559129     EISSN: 15256103     Source Type: Journal    
DOI: 10.1080/87559129.2011.563396     Document Type: Article
Times cited : (40)

References (279)
  • 1
    • 0344306321 scopus 로고    scopus 로고
    • Bovine colostrums: A review of clinical uses
    • Kelly, G.S. Bovine colostrums: a review of clinical uses. Alternative Medicine Review 2003, 8, 378-394.
    • (2003) Alternative Medicine Review , vol.8 , pp. 378-394
    • Kelly, G.S.1
  • 5
    • 50649103014 scopus 로고    scopus 로고
    • Comparison of digestibility and quality of intact proteins with their respective hydrolysates
    • Potier, M.; Tomé, D. Comparison of digestibility and quality of intact proteins with their respective hydrolysates. Journal of AOAC International 2008, 91, 1002-1005.
    • (2008) Journal of AOAC International , vol.91 , pp. 1002-1005
    • Potier, M.1    Tomé, D.2
  • 7
    • 52149091407 scopus 로고    scopus 로고
    • Approach to milk protein allergy in infants
    • Brill, H. Approach to milk protein allergy in infants. Canadian Family Physician 2008, 54, 1258-1264.
    • (2008) Canadian Family Physician , vol.54 , pp. 1258-1264
    • Brill, H.1
  • 9
    • 0032877184 scopus 로고    scopus 로고
    • Therapeutic peptides revisited
    • Latham, P.W. Therapeutic peptides revisited. Nature Biotechnology 1999, 17, 755-758.
    • (1999) Nature Biotechnology , vol.17 , pp. 755-758
    • Latham, P.W.1
  • 12
    • 84984458687 scopus 로고
    • Bioactive peptides derived from milk proteins. Structural, physiological and analytical aspects
    • Schlimme, E.; Meisel, H. Bioactive peptides derived from milk proteins. Structural, physiological and analytical aspects. Nahrung 1995, 39, 1-20.
    • (1995) Nahrung , vol.39 , pp. 1-20
    • Schlimme, E.1    Meisel, H.2
  • 14
    • 33645880763 scopus 로고    scopus 로고
    • The cryptome: A subset of the proteome, comprising cryptic peptides with distinct bioactivities
    • Autelitano, D.J.; Rajic, A.; Smith, A.I.; Berndt, M.C.; Ilag, L.L.; Vadas, M. The cryptome: a subset of the proteome, comprising cryptic peptides with distinct bioactivities. Drug Discovery Today 2006, 11, 306-314.
    • (2006) Drug Discovery Today , vol.11 , pp. 306-314
    • Autelitano, D.J.1    Rajic, A.2    Smith, A.I.3    Berndt, M.C.4    Ilag, L.L.5    Vadas, M.6
  • 15
    • 36148988384 scopus 로고    scopus 로고
    • Cryptides: Buried secrets in proteins
    • Pimenta, D.C.; Lebrun, I. Cryptides: buried secrets in proteins. Peptides 2007, 28, 2403-2410.
    • (2007) Peptides , vol.28 , pp. 2403-2410
    • Pimenta, D.C.1    Lebrun, I.2
  • 17
    • 0033828099 scopus 로고    scopus 로고
    • Bioactive peptides in dairy products: Synthesis and interaction with proteolytic enzymes
    • Smacchi, E.; Gobbetti, M. Bioactive peptides in dairy products: synthesis and interaction with proteolytic enzymes. Food Microbiology 2000, 17, 129-141.
    • (2000) Food Microbiology , vol.17 , pp. 129-141
    • Smacchi, E.1    Gobbetti, M.2
  • 18
    • 0038058742 scopus 로고    scopus 로고
    • Bioactive proteins and peptides from food sources. Application of bioprocesses used in isolation and recovery
    • Kitts, D.D.; Weiler, K. Bioactive proteins and peptides from food sources. Application of bioprocesses used in isolation and recovery. Current Pharmaceutical Design 2003, 9, 1309-1323.
    • (2003) Current Pharmaceutical Design , vol.9 , pp. 1309-1323
    • Kitts, D.D.1    Weiler, K.2
  • 19
    • 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. Current Pharmaceutical Design 2003, 9, 1297-1308.
    • (2003) Current Pharmaceutical Design , vol.9 , pp. 1297-1308
    • Korhonen, H.1    Pihlanto, A.2
  • 21
    • 33747503962 scopus 로고    scopus 로고
    • Bioactive peptides: Production and functionality
    • Korhonen, H.; Pihlanto, A. Bioactive peptides: production and functionality. International Dairy Journal 2006, 16, 945-960.
    • (2006) International Dairy Journal , vol.16 , pp. 945-960
    • Korhonen, H.1    Pihlanto, A.2
  • 22
    • 0742296736 scopus 로고    scopus 로고
    • Milk proteins hydrolysates and bioactive peptides
    • In, 3rd ed.; Ed: Fox, P.F.; McSweeney, P.L.H.; Kluwer Academic/Plenum Publishers:, New York
    • FitzGerald, R.J.; Meisel, H. Milk proteins hydrolysates and bioactive peptides. In Advanced Dairy Chemistry. Proteins, 3rd ed.; Ed: Fox, P.F.; McSweeney, P.L.H.; Kluwer Academic/Plenum Publishers:, New York, 2003; 675-698.
    • (2003) Advanced Dairy Chemistry. Proteins , pp. 675-698
    • FitzGerald, R.J.1    Meisel, H.2
  • 23
    • 34247134078 scopus 로고    scopus 로고
    • Technological options for the production of health-promoting proteins and peptides derived from milk and colostrums
    • Korhonen, H.; Pihlanto, A. Technological options for the production of health-promoting proteins and peptides derived from milk and colostrums. Current Pharmaceutical Design 2007, 13, 829-843.
    • (2007) Current Pharmaceutical Design , vol.13 , pp. 829-843
    • Korhonen, H.1    Pihlanto, A.2
  • 24
    • 33747508611 scopus 로고    scopus 로고
    • Milk-derived bioactive peptides: Formation and prospects for health promotion
    • In, Ed: Shortt, C.: O'Brien, J.; CRC Press: Boca Raton, FL
    • Korhonen, H.; Pihlanto-Leppälä, A. Milk-derived bioactive peptides: formation and prospects for health promotion. In Handbook of Functional Dairy Products. Functional Foods and Nutraceuticals; Ed: Shortt, C.: O'Brien, J.; CRC Press: Boca Raton, FL, 2004; 109-124.
    • (2004) Handbook of Functional Dairy Products. Functional Foods and Nutraceuticals , pp. 109-124
    • Korhonen, H.1    Pihlanto-Leppälä, A.2
  • 25
    • 16444386368 scopus 로고    scopus 로고
    • Multifunctional peptides encrypted in milk proteins
    • Meisel, H. Multifunctional peptides encrypted in milk proteins. BioFactors 2004, 21, 55-61.
    • (2004) BioFactors , vol.21 , pp. 55-61
    • Meisel, H.1
  • 26
    • 34247122823 scopus 로고    scopus 로고
    • Casein phosphopeptides in oral health-chemistry and clinical applications
    • Cross, K.J.; Huq, N.L.; Reynolds, E.C. Casein phosphopeptides in oral health-chemistry and clinical applications. Current Pharmaceutical Design 2007, 13, 793-800.
    • (2007) Current Pharmaceutical Design , vol.13 , pp. 793-800
    • Cross, K.J.1    Huq, N.L.2    Reynolds, E.C.3
  • 27
    • 34247148223 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibitory peptides derived from food proteins: Biochemistry, bioactivity and production
    • Murray, B.A.; FitzGerald, R.J. Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production. Current Pharmaceutical Design 2007, 13, 773-791.
    • (2007) Current Pharmaceutical Design , vol.13 , pp. 773-791
    • Murray, B.A.1    FitzGerald, R.J.2
  • 28
    • 34247176776 scopus 로고    scopus 로고
    • A role for milk proteins and their peptides in cancer prevention
    • Parodi, P.W. A role for milk proteins and their peptides in cancer prevention. Current Pharmaceutical Design 2007, 13, 813-828.
    • (2007) Current Pharmaceutical Design , vol.13 , pp. 813-828
    • Parodi, P.W.1
  • 29
    • 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. Current Opinion in Biotechnology 2007, 18, 163-169.
    • (2007) Current Opinion in Biotechnology , vol.18 , pp. 163-169
    • Hartmann, R.1    Meisel, H.2
  • 30
    • 33947363724 scopus 로고    scopus 로고
    • Milk-derived proteins and peptides of potential therapeutic and nutritive value
    • Zimecki. M.; Kruzel, M.L. Milk-derived proteins and peptides of potential therapeutic and nutritive value. Journal of Experimental Therapeutics and Oncology 2007, 6, 89-106.
    • (2007) Journal of Experimental Therapeutics and Oncology , vol.6 , pp. 89-106
    • Zimecki, M.1    Kruzel, M.L.2
  • 32
    • 58149132303 scopus 로고    scopus 로고
    • Biofunctional properties of bioactive peptides of milk origin
    • Haque, E.; Chand, R.; Kapila, S. Biofunctional properties of bioactive peptides of milk origin. Food Reviews International 2009, 25, 28-43.
    • (2009) Food Reviews International , vol.25 , pp. 28-43
    • Haque, E.1    Chand, R.2    Kapila, S.3
  • 35
    • 0009855250 scopus 로고    scopus 로고
    • Milk protein-derived bioactive peptides-novel opportunities for health promotion
    • Korhonen, H.; Pihlanto-Leppälä, A. Milk protein-derived bioactive peptides-novel opportunities for health promotion. Bulletin of the IDF 2001, 363, 17-26.
    • (2001) Bulletin of the IDF , vol.363 , pp. 17-26
    • Korhonen, H.1    Pihlanto-Leppälä, A.2
  • 36
    • 85145125271 scopus 로고    scopus 로고
    • Biologically active peptides released in fermented milk: Role and functions
    • In, Functional Foods and Nutraceutical Series; Ed: Farnworth, T.; CRC Press: Boca Raton, FL
    • Matar, C.; LeBlanc, J.G.; Martin, L.; Perdigón, G. Biologically active peptides released in fermented milk: role and functions. In Handbook of Fermented Functional Foods. Functional Foods and Nutraceutical Series; Ed: Farnworth, T.; CRC Press: Boca Raton, FL, 2003; 177-201.
    • (2003) Handbook of Fermented Functional Foods , pp. 177-201
    • Matar, C.1    LeBlanc, J.G.2    Martin, L.3    Perdigón, G.4
  • 37
    • 38949186542 scopus 로고    scopus 로고
    • Occurrence of the angiotensinconverting enzyme-inhibiting tripeptides Val-Pro-Pro and Ile-Pro-Pro in different cheese varieties of Swiss origin
    • Bütikofer, U.; Meyer, J.; Sieber, R.; Wlather, B.; Wechsler, D. Occurrence of the angiotensinconverting enzyme-inhibiting tripeptides Val-Pro-Pro and Ile-Pro-Pro in different cheese varieties of Swiss origin. Journal of Dairy Science 2008, 91, 29-38.
    • (2008) Journal of Dairy Science , vol.91 , pp. 29-38
    • Bütikofer, U.1    Meyer, J.2    Sieber, R.3    Wlather, B.4    Wechsler, D.5
  • 38
    • 0037307257 scopus 로고    scopus 로고
    • A fermented milk high in bioactive peptides has a blood pressure-lowering effect in hypertensive subjects
    • Seppo, L.; Jauhiainen, T.; Poussa, T.; Korpela, R. A fermented milk high in bioactive peptides has a blood pressure-lowering effect in hypertensive subjects. American Journal of Clinical Nutrition 2003, 77, 326-330.
    • (2003) American Journal of Clinical Nutrition , vol.77 , pp. 326-330
    • Seppo, L.1    Jauhiainen, T.2    Poussa, T.3    Korpela, R.4
  • 39
    • 0002260166 scopus 로고    scopus 로고
    • Protein digestion and assimilation
    • In, Ed: Yamada, T.; Lippincott, Williams & Wilkins: Philadelphia
    • Ganalpathy, V.; Leibach, F.H. Protein digestion and assimilation. In Textbook of Gastroenterology; Ed: Yamada, T.; Lippincott, Williams & Wilkins: Philadelphia, 1999; 456-467.
    • (1999) Textbook of Gastroenterology , pp. 456-467
    • Ganalpathy, V.1    Leibach, F.H.2
  • 42
    • 33646664658 scopus 로고    scopus 로고
    • Transport systems for opioid peptides in mammalian tissues
    • Ganapathy, V.; Miyauchi, S. Transport systems for opioid peptides in mammalian tissues. The AAPS Journal 2005, 7, 852-885.
    • (2005) The AAPS Journal , vol.7 , pp. 852-885
    • Ganapathy, V.1    Miyauchi, S.2
  • 43
    • 0032853619 scopus 로고    scopus 로고
    • Intestinal peptide transport systems and oral drug availability
    • Yang, C.Y.; Dantzig, A.H.; Pidgeon, C. Intestinal peptide transport systems and oral drug availability. Pharmaceutical Research 1999, 16, 1331-1343.
    • (1999) Pharmaceutical Research , vol.16 , pp. 1331-1343
    • Yang, C.Y.1    Dantzig, A.H.2    Pidgeon, C.3
  • 44
    • 16244418685 scopus 로고    scopus 로고
    • Current strategies used to enhance the paracellular transport of therapeutic polypeptides across the intestinal epithelium
    • Salamat-Miller, N.; Johnston, T.P. Current strategies used to enhance the paracellular transport of therapeutic polypeptides across the intestinal epithelium. International Journal of Pharmaceutics 2005, 294, 201-216.
    • (2005) International Journal of Pharmaceutics , vol.294 , pp. 201-216
    • Salamat-Miller, N.1    Johnston, T.P.2
  • 45
    • 0030853188 scopus 로고    scopus 로고
    • The effect of β-turn structure on the passive diffusion of peptides across Caco-2 cells monolayers
    • Knip, G.T.; Vander Velde, D.G.; Siahaan, T.J.; Borchardt, R.T. The effect of β-turn structure on the passive diffusion of peptides across Caco-2 cells monolayers. Pharmaceutical Research 1997, 14, 1332-1341.
    • (1997) Pharmaceutical Research , vol.14 , pp. 1332-1341
    • Knip, G.T.1    Vander Velde, D.G.2    Siahaan, T.J.3    Borchardt, R.T.4
  • 46
    • 0033007311 scopus 로고    scopus 로고
    • Effect of chain length on adsorption of biologically active peptides from the gastrointestinal tract
    • Roberts, P.R.; Burney, J.D.; Black, K.W.; Zaloga, G.P. Effect of chain length on adsorption of biologically active peptides from the gastrointestinal tract. Digestion 1999, 60, 332-337.
    • (1999) Digestion , vol.60 , pp. 332-337
    • Roberts, P.R.1    Burney, J.D.2    Black, K.W.3    Zaloga, G.P.4
  • 49
    • 70349998626 scopus 로고    scopus 로고
    • Therapeutic application of peptides and proteins: Parenteral forever?
    • Antosova, Z.; Mackova, M.; Kral, V.; Macek, T. Therapeutic application of peptides and proteins: parenteral forever? Trends in Biotechnology 2009, 27, 628-635.
    • (2009) Trends in Biotechnology , vol.27 , pp. 628-635
    • Antosova, Z.1    Mackova, M.2    Kral, V.3    Macek, T.4
  • 51
    • 70349153142 scopus 로고    scopus 로고
    • Effect of peptides derived from food proteins on blood pressure: A metaanalysis of randomized controlled trials
    • Pripp, A.H. Effect of peptides derived from food proteins on blood pressure: a metaanalysis of randomized controlled trials. Food and Nutrition Research 2008, 52.
    • (2008) Food and Nutrition Research , vol.52
    • Pripp, A.H.1
  • 55
    • 40449115854 scopus 로고    scopus 로고
    • Peptidomics: The integrated approach of MS, hyphenated techniques and bioinformatics for neuropeptide analysis
    • Boonen, K.; Landuyt, B.; Baggerman, G.; Husson, S.J.; Huybrechts, J.; Schoofs, L. Peptidomics: the integrated approach of MS, hyphenated techniques and bioinformatics for neuropeptide analysis. Journal of Separation Science 2008, 31, 427-445.
    • (2008) Journal of Separation Science , vol.31 , pp. 427-445
    • Boonen, K.1    Landuyt, B.2    Baggerman, G.3    Husson, S.J.4    Huybrechts, J.5    Schoofs, L.6
  • 58
    • 75849153303 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt) in 2010
    • The UniProt Consortium
    • The UniProt Consortium. The Universal Protein Resource (UniProt) in 2010. Nucleic Acids Research 2010, 38, D142-D148.
    • (2010) Nucleic Acids Research , vol.38 , pp. 142-148
  • 61
    • 33846036096 scopus 로고    scopus 로고
    • The worldwide Protein Data Bank (wwPDB): Ensuring a single, uniform archive of PDB data
    • Berman, H.; Henrick, K.; Nakamura, H.; Markley, J.L. The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data. Nucleic Acids Research 2007, 35, D301-D303.
    • (2007) Nucleic Acids Research , vol.35 , pp. 301-303
    • Berman, H.1    Henrick, K.2    Nakamura, H.3    Markley, J.L.4
  • 63
    • 33646068775 scopus 로고    scopus 로고
    • Information management for the study of allergies
    • Brusic, V. Information management for the study of allergies. Inflammation & Allergy-Drug Targets 2006, 5, 35-42.
    • (2006) Inflammation & Allergy-Drug Targets , vol.5 , pp. 35-42
    • Brusic, V.1
  • 64
    • 67650257527 scopus 로고    scopus 로고
    • Allergen databases and allergen semantics
    • Gendel, S.M. Allergen databases and allergen semantics. Regulatory Toxicology and Pharmacology 2009, 54(3 Suppl.), S7-S10.
    • (2009) Regulatory Toxicology and Pharmacology , vol.54 , Issue.3 SUPPL. , pp. 7-10
    • Gendel, S.M.1
  • 66
    • 67649484376 scopus 로고    scopus 로고
    • Immunoinformatics: Current trends and future directions
    • Tong, J.C.; Ren, E.C. Immunoinformatics: current trends and future directions. Drug Discovery Today 2009, 14, 684-689.
    • (2009) Drug Discovery Today , vol.14 , pp. 684-689
    • Tong, J.C.1    Ren, E.C.2
  • 67
    • 85122909243 scopus 로고    scopus 로고
    • Database of protein and bioactive peptide sequences
    • In, Ed: Minc, Y.; Shahidi, F.; CRC: Boca Raton, FL
    • Dziuba, J.; Iwaniak, A. Database of protein and bioactive peptide sequences. In Nutraceutical Proteins and Peptides in Health and Disease; Ed: Minc, Y.; Shahidi, F.; CRC: Boca Raton, FL, 2006; 543-563.
    • (2006) Nutraceutical Proteins and Peptides in Health and Disease , pp. 543-563
    • Dziuba, J.1    Iwaniak, A.2
  • 69
    • 34548658287 scopus 로고    scopus 로고
    • PepBank-a database of peptides based on sequence text mining and public peptide data sources
    • Art. No. 280
    • Shtatland, T.; Guettler, D.; Kossodo, M.; Pivovarov, M.; Weissleder, R. PepBank-a database of peptides based on sequence text mining and public peptide data sources. BMC Bioinformatics 2007, 8, Art. No. 280.
    • (2007) BMC Bioinformatics , vol.8
    • Shtatland, T.1    Guettler, D.2    Kossodo, M.3    Pivovarov, M.4    Weissleder, R.5
  • 70
    • 70449719005 scopus 로고    scopus 로고
    • Enhancing navigation in biomedical databases by community voting and database-driven text classification
    • Art. No. 317
    • Duchrow, T.; Shtatland, T.; Guettler, D.; Pivovarov, M.; Kramer, S.; Weissleder, R. Enhancing navigation in biomedical databases by community voting and database-driven text classification. BMC Bioinformatics 2009, 10, Art. No. 317.
    • (2009) BMC Bioinformatics , vol.10
    • Duchrow, T.1    Shtatland, T.2    Guettler, D.3    Pivovarov, M.4    Kramer, S.5    Weissleder, R.6
  • 71
    • 20444421255 scopus 로고    scopus 로고
    • Structural properties of proteolytic accessible bioactive fragments of selected animal proteins
    • Dziuba, J.; Niklewicz M.; Iwaniak, A.; Darewicz M.; Minkiewicz, P. Structural properties of proteolytic accessible bioactive fragments of selected animal proteins. Polimery 2005, 50, 424-428.
    • (2005) Polimery , vol.50 , pp. 424-428
    • Dziuba, J.1    Niklewicz, M.2    Iwaniak, A.3    Darewicz, M.4    Minkiewicz, P.5
  • 72
    • 41149094954 scopus 로고    scopus 로고
    • Food proteins as precursors of bioactive peptides-division into families
    • Dziuba, M.; Darewicz, M. Food proteins as precursors of bioactive peptides-division into families. Food Science and Technology International 2007, 13, 393-404.
    • (2007) Food Science and Technology International , vol.13 , pp. 393-404
    • Dziuba, M.1    Darewicz, M.2
  • 74
    • 67651155986 scopus 로고    scopus 로고
    • Bovine κ-casein variants result in different angiotensin I converting enzyme (ACE) inhibitory peptides
    • Weimann, C.; Meisel, H.; Erhardt, G. Bovine κ-casein variants result in different angiotensin I converting enzyme (ACE) inhibitory peptides. Journal of Dairy Science 2009, 92, 1885-1888.
    • (2009) Journal of Dairy Science , vol.92 , pp. 1885-1888
    • Weimann, C.1    Meisel, H.2    Erhardt, G.3
  • 76
    • 79958065278 scopus 로고    scopus 로고
    • Update of the list of allergenic proteins from milk, based on local amino acid sequence identity with known epitopes from bovine milk proteins-a short report
    • Minkiewicz, P.; Dziuba, J.; Gładkowska, I. Update of the list of allergenic proteins from milk, based on local amino acid sequence identity with known epitopes from bovine milk proteins-a short report. Polish Journal of Food and Nutrition Sciences 2011, 61, 153-158.
    • (2011) Polish Journal of Food and Nutrition Sciences , vol.61 , pp. 153-158
    • Minkiewicz, P.1    Dziuba, J.2    Gładkowska, I.3
  • 78
    • 58149185126 scopus 로고    scopus 로고
    • BRENDA, AMENDA and FRENDA the enzyme information system: New content and tools in 2009
    • Chang, A.; Scheer, M.; Grote, A.; Schomburg, I.; Schomburg, D. BRENDA, AMENDA and FRENDA the enzyme information system: new content and tools in 2009. Nucleic Acids Research 2009, 37, D588-D592.
    • (2009) Nucleic Acids Research , vol.37 , pp. 588-592
    • Chang, A.1    Scheer, M.2    Grote, A.3    Schomburg, I.4    Schomburg, D.5
  • 80
    • 58149179971 scopus 로고    scopus 로고
    • ExplorEnz: The primary source of the IUBMB enzyme list
    • McDonald, A.G.; Boyce, S.; Tipton K. F. ExplorEnz: the primary source of the IUBMB enzyme list. Nucleic Acids Research 2009, 37, D593-D597.
    • (2009) Nucleic Acids Research , vol.37 , pp. 593-597
    • McDonald, A.G.1    Boyce, S.2    Tipton, K.F.3
  • 81
    • 79951810546 scopus 로고    scopus 로고
    • A large and accurate collection of peptidase cleavages in the MEROPS database
    • Art. No. bap015
    • Rawlings, N.D. A large and accurate collection of peptidase cleavages in the MEROPS database. Database 2009, 1, Art. No. bap015.
    • (2009) Database , vol.1
    • Rawlings, N.D.1
  • 85
    • 34248152120 scopus 로고    scopus 로고
    • Mass spectrometry data analysis in the proteomics era
    • Forner, F.; Foster, L.J.; Toppo, S. Mass spectrometry data analysis in the proteomics era. Current Bioinformatics 2007, 2, 63-93.
    • (2007) Current Bioinformatics , vol.2 , pp. 63-93
    • Forner, F.1    Foster, L.J.2    Toppo, S.3
  • 86
    • 40649126964 scopus 로고    scopus 로고
    • Informatics for peptide retention properties in proteomic LC-MS
    • Shinoda, K.; Sugimoto, M.; Tomita, M.; Ishihama, Y. Informatics for peptide retention properties in proteomic LC-MS. Proteomics 2008, 8, 787-798.
    • (2008) Proteomics , vol.8 , pp. 787-798
    • Shinoda, K.1    Sugimoto, M.2    Tomita, M.3    Ishihama, Y.4
  • 87
    • 61349150487 scopus 로고    scopus 로고
    • Predictions of peptides' retention times in reversed-phase liquid chromatography as a new supportive tool to improve protein identification in proteomics
    • Ba{ogonek}czek, T.; Kaliszan, R. Predictions of peptides' retention times in reversed-phase liquid chromatography as a new supportive tool to improve protein identification in proteomics. Proteomics 2009, 9, 835-847.
    • (2009) Proteomics , vol.9 , pp. 835-847
    • Baczek, T.1    Kaliszan, R.2
  • 88
    • 48749121266 scopus 로고    scopus 로고
    • Antihypertensive effect of an angiotensin converting enzyme inhibitory peptide from enzyme modified cheese
    • Tonouchi, H.; Suzuki, M.; Uchida, M.; Oda, M. Antihypertensive effect of an angiotensin converting enzyme inhibitory peptide from enzyme modified cheese. Journal of Dairy Research 2008, 75, 284-290.
    • (2008) Journal of Dairy Research , vol.75 , pp. 284-290
    • Tonouchi, H.1    Suzuki, M.2    Uchida, M.3    Oda, M.4
  • 90
    • 0012128060 scopus 로고    scopus 로고
    • Database of biologically active peptide sequences
    • Dziuba, J.; Minkiewicz, P.; Nałe{ogonek}cz, D.; Iwaniak, A. Database of biologically active peptide sequences. Nahrung 1999, 43, 190-195.
    • (1999) Nahrung , vol.43 , pp. 190-195
    • Dziuba, J.1    Minkiewicz, P.2    Nałecz, D.3    Iwaniak, A.4
  • 91
    • 2342569607 scopus 로고    scopus 로고
    • A quantitative in silico analysis calculates the angiotensin I converting enzyme (ACE) inhibitory activity in pea and whey protein digests
    • Vermeirssen, V.; van den Bent, A.; Van Camp, J.; van Amerongen, A.; Verstraete, W. A quantitative in silico analysis calculates the angiotensin I converting enzyme (ACE) inhibitory activity in pea and whey protein digests. Biochimie 2004, 86, 231-239.
    • (2004) Biochimie , vol.86 , pp. 231-239
    • Vermeirssen, V.1    van den Bent, A.2    van Camp, J.3    van Amerongen, A.4    Verstraete, W.5
  • 92
    • 60749085370 scopus 로고    scopus 로고
    • Critical evaluation of the use of bioinformatics as a theoretical tool to find high-potential sources of ACE inhibitory peptides
    • Vercruysse, L.; Smagghe, G.; van der Bent, A.; van Amerongen, A.; Ongenaert, M.; van Camp, J. Critical evaluation of the use of bioinformatics as a theoretical tool to find high-potential sources of ACE inhibitory peptides. Peptides 2009, 30, 575-582.
    • (2009) Peptides , vol.30 , pp. 575-582
    • Vercruysse, L.1    Smagghe, G.2    van der Bent, A.3    van Amerongen, A.4    Ongenaert, M.5    van Camp, J.6
  • 94
    • 50949122245 scopus 로고    scopus 로고
    • Bridging protein local structures and protein functions
    • Liu, Z.P.; Wu, L.-Y.; Wang, Y.; Zhang, X.-S.; Chen, L. Bridging protein local structures and protein functions. Amino Acids 2008, 35, 627-650.
    • (2008) Amino Acids , vol.35 , pp. 627-650
    • Liu, Z.P.1    Wu, L.-Y.2    Wang, Y.3    Zhang, X.-S.4    Chen, L.5
  • 95
    • 33747823564 scopus 로고    scopus 로고
    • MEME: Discovering and analyzing DNA and protein sequence motifs
    • Bailey, T.L.; Williams, N.; Misleh, C.; Li, W.W. MEME: discovering and analyzing DNA and protein sequence motifs. Nucleic Acids Research 2006, 34, 369-373.
    • (2006) Nucleic Acids Research , vol.34 , pp. 369-373
    • Bailey, T.L.1    Williams, N.2    Misleh, C.3    Li, W.W.4
  • 96
    • 44949239504 scopus 로고    scopus 로고
    • Discovering sequence motifs with arbitrary insertions and deletions
    • Art. No. e1000071
    • Frith, M.C.; Saunders, N.F.W.; Kobe, B.; Bailey, T.L. Discovering sequence motifs with arbitrary insertions and deletions. PLoS Computational Biology 2008, 4, Art. No. e1000071.
    • (2008) PLoS Computational Biology , vol.4
    • Frith, M.C.1    Saunders, N.F.W.2    Kobe, B.3    Bailey, T.L.4
  • 98
    • 34547163510 scopus 로고    scopus 로고
    • Computational characterisation and identification of peptides for in silico detection of potentially celiac-toxic proteins
    • Darewicz, M.; Dziuba, J.; Minkiewicz P. Computational characterisation and identification of peptides for in silico detection of potentially celiac-toxic proteins. Food Science and Technology International 2007, 13, 125-133.
    • (2007) Food Science and Technology International , vol.13 , pp. 125-133
    • Darewicz, M.1    Dziuba, J.2    Minkiewicz, P.3
  • 99
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time of flight mass spectrometry and BLAST homology searching
    • Shevchenko, A.; Sunyaev, S.; Loboda, A.; Shevchenko, A.; Bork, P., Ens, W.; Standing, K.G. Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time of flight mass spectrometry and BLAST homology searching. Analytical Chemistry 2001, 73, 1917-1926.
    • (2001) Analytical Chemistry , vol.73 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Shevchenko, A.4    Bork, P.5    Ens, W.6    Standing, K.G.7
  • 102
    • 67349201369 scopus 로고    scopus 로고
    • Bovine milk intolerance in celiac disease is related to IgA reactivity to α-and β-caseins
    • Cabrera-Chávez, F.; Calderón de la Barca, A.M. Bovine milk intolerance in celiac disease is related to IgA reactivity to α-and β-caseins. Nutrition 2009, 25, 715-716.
    • (2009) Nutrition , vol.25 , pp. 715-716
    • Cabrera-Chávez, F.1    Calderón de la Barca, A.M.2
  • 104
    • 0033990061 scopus 로고    scopus 로고
    • Flexible sequence similarity searching with the FASTA3 program package
    • Pearson, W.R. Flexible sequence similarity searching with the FASTA3 program package. Methods in Molecular Biology 2000, 132, 185-219.
    • (2000) Methods in Molecular Biology , vol.132 , pp. 185-219
    • Pearson, W.R.1
  • 105
    • 27444437848 scopus 로고    scopus 로고
    • Quantitative structure activity relationship modelling of peptides and proteins as a tool in food science
    • Pripp, A.H.; Isakson, T.; Stepaniak, L.; Sørhaug, T.; Ardö, Y.; Quantitative structure activity relationship modelling of peptides and proteins as a tool in food science. Trends in Food Science and Technology 2005, 16, 484-494.
    • (2005) Trends in Food Science and Technology , vol.16 , pp. 484-494
    • Pripp, A.H.1    Isakson, T.2    Stepaniak, L.3    Sørhaug, T.4    Ardö, Y.5
  • 106
    • 47349088078 scopus 로고    scopus 로고
    • Recent advances in QSAR and their applications in predicting the activities of chemical molecules, peptides and proteins for drug design
    • Du, Q.-S.; Huang, R.-B.; Chou, K.-C. Recent advances in QSAR and their applications in predicting the activities of chemical molecules, peptides and proteins for drug design. Current Protein and Peptide Science 2008, 9, 248-259.
    • (2008) Current Protein and Peptide Science , vol.9 , pp. 248-259
    • Du, Q.-S.1    Huang, R.-B.2    Chou, K.-C.3
  • 109
    • 10444265979 scopus 로고    scopus 로고
    • Quantitative structure activity relationship (QSAR) of ACE-inhibitory peptides derived from milk proteins
    • Pripp, A.H.; Isaksson, T.; Stepaniak, L.; Sørhaug, T. Quantitative structure activity relationship (QSAR) of ACE-inhibitory peptides derived from milk proteins. European Food Research and Technology 2004, 219, 579-583.
    • (2004) European Food Research and Technology , vol.219 , pp. 579-583
    • Pripp, A.H.1    Isaksson, T.2    Stepaniak, L.3    Sørhaug, T.4
  • 110
    • 31044454896 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship of prolyl oligopeptidase inhibitory peptides derived from β-casein using simple amino acid descriptors
    • Pripp, A.H. Quantitative structure-activity relationship of prolyl oligopeptidase inhibitory peptides derived from β-casein using simple amino acid descriptors. Journal of Agricultural and Food Chemistry 2006, 54, 224-228.
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , pp. 224-228
    • Pripp, A.H.1
  • 111
    • 27844480599 scopus 로고    scopus 로고
    • Initial proteolysis of milk proteins and its effect on formation of ACEinhibitory peptides during gastrointestinal proteolysis: A bioinformatic approach
    • Pripp, A.H. Initial proteolysis of milk proteins and its effect on formation of ACEinhibitory peptides during gastrointestinal proteolysis: a bioinformatic approach. European Food Research and Technology 2005, 221, 712-716.
    • (2005) European Food Research and Technology , vol.221 , pp. 712-716
    • Pripp, A.H.1
  • 112
    • 33846199139 scopus 로고    scopus 로고
    • Modelling relationship between angiotensin-(I)-converting enzyme inhibition and the bitter taste of peptides
    • Pripp, A.H.; Ardö, Y. Modelling relationship between angiotensin-(I)-converting enzyme inhibition and the bitter taste of peptides. Food Chemistry 2007, 102, 880-888.
    • (2007) Food Chemistry , vol.102 , pp. 880-888
    • Pripp, A.H.1    Ardö, Y.2
  • 113
    • 34250643512 scopus 로고    scopus 로고
    • Docking and virtual screening of ACE inhibitory dipeptides
    • Pripp, A.H. Docking and virtual screening of ACE inhibitory dipeptides. European Food Research and Technology 2007, 225, 589-592.
    • (2007) European Food Research and Technology , vol.225 , pp. 589-592
    • Pripp, A.H.1
  • 114
    • 67649622659 scopus 로고    scopus 로고
    • The High Throughput Sequence Annotation Service (HT-SAS)-the shortcut from sequence to true Medline words
    • Art. No. 148
    • Kaczanowski, S.; Siedlecki, P.; Zielenkiewicz, P. The High Throughput Sequence Annotation Service (HT-SAS)-the shortcut from sequence to true Medline words. BMC Bioinformatics 2009, 10, Art. No. 148.
    • (2009) BMC Bioinformatics , vol.10
    • Kaczanowski, S.1    Siedlecki, P.2    Zielenkiewicz, P.3
  • 115
    • 63549134041 scopus 로고    scopus 로고
    • Allergen atlas: A comprehensive knowledge center and analysis resource for allergen information
    • Tong, J.C.; Lim, S.J.; Muh, H.C.; Chew, F.T.; Tammi, M.T. Allergen atlas: a comprehensive knowledge center and analysis resource for allergen information. Bioinformatics 2009, 25, 979-980.
    • (2009) Bioinformatics , vol.25 , pp. 979-980
    • Tong, J.C.1    Lim, S.J.2    Muh, H.C.3    Chew, F.T.4    Tammi, M.T.5
  • 116
    • 33644504193 scopus 로고    scopus 로고
    • Development of Allergen Database for Food Safety (ADFS): An integrated database to search allergens and predict allergenicity
    • Nakamura, R.; Teshima, R.; Talagi, K.; Sawada, J.-I. Development of Allergen Database for Food Safety (ADFS): an integrated database to search allergens and predict allergenicity. Bulletin of the National Institute for Health Science 2005, 123, 32-36.
    • (2005) Bulletin of the National Institute for Health Science , vol.123 , pp. 32-36
    • Nakamura, R.1    Teshima, R.2    Talagi, K.3    Sawada, J.-I.4
  • 117
    • 34248380799 scopus 로고    scopus 로고
    • Bioinformatics applied to allergy: Allergen databases, from collecting sequence information to data integration. The Allergome platform as a model
    • Mari, A.; Scala, E.; Palazzo, P.; Ridolfi, S.; Zennaro, D.; Carabella, G. Bioinformatics applied to allergy: Allergen databases, from collecting sequence information to data integration. The Allergome platform as a model. Cellular Immunology 2006, 244, 97-100.
    • (2006) Cellular Immunology , vol.244 , pp. 97-100
    • Mari, A.1    Scala, E.2    Palazzo, P.3    Ridolfi, S.4    Zennaro, D.5    Carabella, G.6
  • 119
    • 13244265577 scopus 로고    scopus 로고
    • Allermatch™, a webtool for the prediction of potential allergenicity according to current FAO/WHO Codex Alimentarius guidelines
    • Art. No. 133
    • Fiers, W.E.J.; Kleter, G.A.; Nijland, H.; Peijnenburg, A.A.C.M.; Nap, J.P.; van Ham, R.C.H.J. Allermatch™, a webtool for the prediction of potential allergenicity according to current FAO/WHO Codex Alimentarius guidelines. BMC Bioinformatics 2004, 5, Art. No. 133.
    • (2004) BMC Bioinformatics , vol.5
    • Fiers, W.E.J.1    Kleter, G.A.2    Nijland, H.3    Peijnenburg, A.A.C.M.4    Nap, J.P.5    van Ham, R.C.H.J.6
  • 123
  • 125
    • 0037216795 scopus 로고    scopus 로고
    • Computer-aided characteristics of proteins as potential precursors of bioactive peptides
    • Dziuba, J.; Iwaniak, A.; Minkiewicz, P. Computer-aided characteristics of proteins as potential precursors of bioactive peptides. Polimery 2003, 48, 50-53.
    • (2003) Polimery , vol.48 , pp. 50-53
    • Dziuba, J.1    Iwaniak, A.2    Minkiewicz, P.3
  • 131
    • 0037195251 scopus 로고    scopus 로고
    • Just the beginning: Novel functions for angiotensin-converting enzymes
    • Eriksson, U.; Danilczyk, U.; Penninger, J.M. Just the beginning: novel functions for angiotensin-converting enzymes. Current Biology 2002, 12, R745-R752.
    • (2002) Current Biology , vol.12 , pp. 745-752
    • Eriksson, U.1    Danilczyk, U.2    Penninger, J.M.3
  • 134
    • 34248591348 scopus 로고    scopus 로고
    • Pharmacological, immunological and gene targeting of the rennin-angiotensin system for treatment of cardiovascular disease
    • Igic, R.; Behnia, R. Pharmacological, immunological and gene targeting of the rennin-angiotensin system for treatment of cardiovascular disease. Current Pharmaceutical Design 2007, 13, 1199-1214.
    • (2007) Current Pharmaceutical Design , vol.13 , pp. 1199-1214
    • Igic, R.1    Behnia, R.2
  • 135
    • 34248345563 scopus 로고    scopus 로고
    • The renin angiotensin system in the regulation of angiogenesis
    • Heffelfinger, S.C. The renin angiotensin system in the regulation of angiogenesis. Current Pharmaceutical Design 2007, 13, 1215-1229.
    • (2007) Current Pharmaceutical Design , vol.13 , pp. 1215-1229
    • Heffelfinger, S.C.1
  • 136
    • 34248388973 scopus 로고    scopus 로고
    • The two fACEs of the tissue rennin-angiotensin systems: Implication in cardiovascular diseases
    • Lazartigues, E.; Feng, Y.; Lavoie, J.L. The two fACEs of the tissue rennin-angiotensin systems: implication in cardiovascular diseases. Current Pharmaceutical Design 2007, 13, 1231-1245.
    • (2007) Current Pharmaceutical Design , vol.13 , pp. 1231-1245
    • Lazartigues, E.1    Feng, Y.2    Lavoie, J.L.3
  • 137
    • 62549157381 scopus 로고    scopus 로고
    • The intracellular renin-angiotensin system in the heart
    • Kumar, R.; Singh, V.P.; Baker, K.M. The intracellular renin-angiotensin system in the heart. Current Hypertension Reports 2009, 11, 104-110.
    • (2009) Current Hypertension Reports , vol.11 , pp. 104-110
    • Kumar, R.1    Singh, V.P.2    Baker, K.M.3
  • 139
    • 0030749136 scopus 로고    scopus 로고
    • Biochemical properties of regulatory peptides derived from milk proteins
    • Meisel, H. Biochemical properties of regulatory peptides derived from milk proteins. Biopolymers 1997, 43, 119-128.
    • (1997) Biopolymers , vol.43 , pp. 119-128
    • Meisel, H.1
  • 140
    • 0002554452 scopus 로고
    • Inhibitors of angiotensin-converting-enzyme derived from bovine casein (casokinins)
    • In, Brantl, V.; Teschemacher, H., Eds.; VCH: Weinheim, Germany
    • Meisel, H.; Schlimme, E. Inhibitors of angiotensin-converting-enzyme derived from bovine casein (casokinins). In β-Casomorphins and Related Peptides: Recent Developments; Brantl, V.; Teschemacher, H., Eds.; VCH: Weinheim, Germany, 1994; 27-33.
    • (1994) β-Casomorphins and Related Peptides: Recent Developments , pp. 27-33
    • Meisel, H.1    Schlimme, E.2
  • 141
    • 48749121266 scopus 로고    scopus 로고
    • Antihypertensive effect of an angiotensin converting enzyme inhibitory peptide from enzyme modified cheese
    • Tonouchi, H.; Suzuki, M.; Uchida, M.; Oda, M. Antihypertensive effect of an angiotensin converting enzyme inhibitory peptide from enzyme modified cheese. Journal of Dairy Research 2008, 75, 284-290.
    • (2008) Journal of Dairy Research , vol.75 , pp. 284-290
    • Tonouchi, H.1    Suzuki, M.2    Uchida, M.3    Oda, M.4
  • 142
    • 0036380805 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme-inhibitory peptides in Manchego cheeses manufactured with different starter cultures
    • Gómez-Ruiz, J.A.; Ramos, M.; Recio, I. Angiotensin-converting enzyme-inhibitory peptides in Manchego cheeses manufactured with different starter cultures. International Dairy Journal 2002, 12, 697-706.
    • (2002) International Dairy Journal , vol.12 , pp. 697-706
    • Gómez-Ruiz, J.A.1    Ramos, M.2    Recio, I.3
  • 143
    • 0030202780 scopus 로고    scopus 로고
    • Identification of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus Cp790
    • Maeno, M.; Yamamoto, N.; Takano, T. Identification of an antihypertensive peptide from casein hydrolysate produced by a proteinase from Lactobacillus helveticus Cp790. Journal of Dairy Science 1996, 79, 1316-1321.
    • (1996) Journal of Dairy Science , vol.79 , pp. 1316-1321
    • Maeno, M.1    Yamamoto, N.2    Takano, T.3
  • 144
    • 0029286291 scopus 로고
    • Purification and characterization of angiotensin-I-converting enzyme inhibitors from sour milk
    • Nakamura, Y.; Yamamoto, N.; Sakai, K.; Okubo, A.; Yamazaki, S.; Takano, T. Purification and characterization of angiotensin-I-converting enzyme inhibitors from sour milk. Journal of Dairy Science 1995, 78, 777-783.
    • (1995) Journal of Dairy Science , vol.78 , pp. 777-783
    • Nakamura, Y.1    Yamamoto, N.2    Sakai, K.3    Okubo, A.4    Yamazaki, S.5    Takano, T.6
  • 145
    • 57149088481 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides in skim milk fermented with Lactobacillus helveticus 130B4 from camel milk in Inner Mongolia, China
    • Shuangquan.; Tsuda, H.; Miyamoto, T. Angiotensin I-converting enzyme inhibitory peptides in skim milk fermented with Lactobacillus helveticus 130B4 from camel milk in Inner Mongolia, China. Journal of the Science of Food and Agriculture 2008, 88, 2688-2692.
    • (2008) Journal of the Science of Food and Agriculture , vol.88 , pp. 2688-2692
    • Shuangquan1    Tsuda, H.2    Miyamoto, T.3
  • 148
    • 0033161658 scopus 로고    scopus 로고
    • Purification and characterization of an antihypertensive peptides from a yogurt-like product fermented by Lactobacillus helvetius CPN4
    • Yamamoto, N.; Maeno, M.; Takano, T. Purification and characterization of an antihypertensive peptides from a yogurt-like product fermented by Lactobacillus helvetius CPN4. Journal of Dairy Science 1999, 82, 1388-1393.
    • (1999) Journal of Dairy Science , vol.82 , pp. 1388-1393
    • Yamamoto, N.1    Maeno, M.2    Takano, T.3
  • 150
    • 33846024711 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme inhibitory activity of milk protein hydrolysates: Effect of substrate, enzyme and time of hydrolysis
    • Otte, J.; Shalaby, S.M.; Zakora, M.; Pripp, A.H.; EL-Shabrawy, S.A. Angiotensin-converting enzyme inhibitory activity of milk protein hydrolysates: effect of substrate, enzyme and time of hydrolysis. International Dairy Journal 2007, 17, 488-503.
    • (2007) International Dairy Journal , vol.17 , pp. 488-503
    • Otte, J.1    Shalaby, S.M.2    Zakora, M.3    Pripp, A.H.4    El-Shabrawy, S.A.5
  • 151
    • 47749104885 scopus 로고    scopus 로고
    • ACE-inhibitory and antihypertensive properties of a bovine casein hydrolysate
    • Miguel, M.; Contreras, M.M.; Recio, I.; Aleixandre, A. ACE-inhibitory and antihypertensive properties of a bovine casein hydrolysate. Food Chemistry 2009, 112, 211-214.
    • (2009) Food Chemistry , vol.112 , pp. 211-214
    • Miguel, M.1    Contreras, M.M.2    Recio, I.3    Aleixandre, A.4
  • 158
    • 58349118271 scopus 로고    scopus 로고
    • Casein peptides with inhibitory activity on lipid oxidation in beef homogenates and mechanically deboned poultry meat
    • Rossini, K.; Noreña, C.P.Z.; Cladera-Olivera, F.; Brandelli, A. Casein peptides with inhibitory activity on lipid oxidation in beef homogenates and mechanically deboned poultry meat. LWT-Food Science and Technology 2009, 42, 862-867.
    • (2009) LWT-Food Science and Technology , vol.42 , pp. 862-867
    • Rossini, K.1    Noreña, C.P.Z.2    Cladera-Olivera, F.3    Brandelli, A.4
  • 159
    • 0027966985 scopus 로고
    • Metabolic effects of opiates and opioid peptides
    • Molina, P.E.; Abumrad, N.N. Metabolic effects of opiates and opioid peptides. Advances in Neuroimmunology 1994, 4, 105-116.
    • (1994) Advances in Neuroimmunology , vol.4 , pp. 105-116
    • Molina, P.E.1    Abumrad, N.N.2
  • 160
    • 22544468502 scopus 로고    scopus 로고
    • Biochemical properties of peptides encrypted in bovine milk proteins
    • Meisel, H. Biochemical properties of peptides encrypted in bovine milk proteins. Current Medicinal Chemistry 2005, 12, 1905-1919.
    • (2005) Current Medicinal Chemistry , vol.12 , pp. 1905-1919
    • Meisel, H.1
  • 161
    • 0030925770 scopus 로고    scopus 로고
    • Inhibition of bovine trypsin by the phosphorylated N-terminal part (1-105) of β-casein
    • Bouhallab, S.; Sapin, B.; Mollé, D.; Henry, G.; Léonil, J. Inhibition of bovine trypsin by the phosphorylated N-terminal part (1-105) of β-casein. Journal of Peptide Research 1997, 49, 23-27.
    • (1997) Journal of Peptide Research , vol.49 , pp. 23-27
    • Bouhallab, S.1    Sapin, B.2    Mollé, D.3    Henry, G.4    Léonil, J.5
  • 162
    • 0041428158 scopus 로고    scopus 로고
    • Relation of beta-casomorphin to apnea in sudden infant death syndrome
    • Sun, Z.; Zhang, Z.; Wang, X.; Cade, R.; Elmer, Z.; Fregly, M. Relation of beta-casomorphin to apnea in sudden infant death syndrome. Peptides 2003, 24, 937-943.
    • (2003) Peptides , vol.24 , pp. 937-943
    • Sun, Z.1    Zhang, Z.2    Wang, X.3    Cade, R.4    Elmer, Z.5    Fregly, M.6
  • 163
    • 0026873867 scopus 로고
    • Inhibition of prolyl endopeptidase by synthetic β-casein peptides and their derivatives with C-terminal prolinol or prolinal
    • Asano, M.; Nio, N.; Ariyoshi, Y. Inhibition of prolyl endopeptidase by synthetic β-casein peptides and their derivatives with C-terminal prolinol or prolinal. Bioscience, Biotechnology and Biochemistry 1992, 56, 976-977.
    • (1992) Bioscience, Biotechnology and Biochemistry , vol.56 , pp. 976-977
    • Asano, M.1    Nio, N.2    Ariyoshi, Y.3
  • 164
    • 41949135032 scopus 로고    scopus 로고
    • Structure, function and biological relevance of prolyl endopeptidase
    • Polgár, L.; Szeltner, Z. Structure, function and biological relevance of prolyl endopeptidase. Current Protein and Peptide Science 2008, 9, 96-107.
    • (2008) Current Protein and Peptide Science , vol.9 , pp. 96-107
    • Polgár, L.1    Szeltner, Z.2
  • 165
    • 48249130118 scopus 로고    scopus 로고
    • Prolyl-specific peptidases and their inhibitors in biological processes
    • Juillerat-Jeanneret, L. Prolyl-specific peptidases and their inhibitors in biological processes. Current Chemical Biology 2008, 2, 97-109.
    • (2008) Current Chemical Biology , vol.2 , pp. 97-109
    • Juillerat-Jeanneret, L.1
  • 166
    • 17644386230 scopus 로고    scopus 로고
    • Psysicochemical characterization of casein phosphopeptide-amorphous calcium phosphate nanocomplexes
    • Cross, K.J.; Huq, N.L.; Palamara, J.E.; Perich, J.W.; Reynolds, E.C. Psysicochemical characterization of casein phosphopeptide-amorphous calcium phosphate nanocomplexes. Journal of Biological Chemistry 2005, 280, 15362-15369.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 15362-15369
    • Cross, K.J.1    Huq, N.L.2    Palamara, J.E.3    Perich, J.W.4    Reynolds, E.C.5
  • 167
    • 0029636155 scopus 로고
    • Characterization of tryptic casein phosphopeptides prepared under industrially relevant conditions
    • Adamson, N.J.; Reynolds, E.C. Characterization of tryptic casein phosphopeptides prepared under industrially relevant conditions. Biotechnology and Bioengineering 1995, 45, 196-204.
    • (1995) Biotechnology and Bioengineering , vol.45 , pp. 196-204
    • Adamson, N.J.1    Reynolds, E.C.2
  • 168
    • 0000847065 scopus 로고    scopus 로고
    • Absorption digestive du fer lie an caseinophosphopeptide 1-25 de la β-caseine
    • Perés, J.M.; Bouhallab, S.; Bureau, F.; Maubois, J.L.; Arhan, P.; Bougle, D. Absorption digestive du fer lie an caseinophosphopeptide 1-25 de la β-caseine. Lait 1997, 77, 433-440.
    • (1997) Lait , vol.77 , pp. 433-440
    • Perés, J.M.1    Bouhallab, S.2    Bureau, F.3    Maubois, J.L.4    Arhan, P.5    Bougle, D.6
  • 169
    • 0036512079 scopus 로고    scopus 로고
    • A clinical trial of the anticaries efficacy of casein derivatives complexed with calcium phosphate in patients with salivary gland dysfunction
    • Hay, K.D.; Thomson, W.M. A clinical trial of the anticaries efficacy of casein derivatives complexed with calcium phosphate in patients with salivary gland dysfunction. Oral Surgery, Oral Medicine, Oral Pathology, Oral Radiology and Endodontology 2002, 93, 271-275.
    • (2002) Oral Surgery, Oral Medicine, Oral Pathology, Oral Radiology and Endodontology , vol.93 , pp. 271-275
    • Hay, K.D.1    Thomson, W.M.2
  • 170
    • 0038735306 scopus 로고    scopus 로고
    • Antimicrobial peptides from food proteins
    • Pellegrini, A. Antimicrobial peptides from food proteins. Current Pharmaceutical Design 2003, 9, 1225-1238.
    • (2003) Current Pharmaceutical Design , vol.9 , pp. 1225-1238
    • Pellegrini, A.1
  • 171
    • 0030041615 scopus 로고    scopus 로고
    • Antibacterial and immunostimulating casein-derived substances from milk, casecidin, isracidin peptides
    • Lahov, E.; Regelson, A. Antibacterial and immunostimulating casein-derived substances from milk, casecidin, isracidin peptides. Food and Chemical Toxicology 1996, 34, 131-145.
    • (1996) Food and Chemical Toxicology , vol.34 , pp. 131-145
    • Lahov, E.1    Regelson, A.2
  • 174
    • 0141816841 scopus 로고    scopus 로고
    • Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolysed caseins of milk from six species
    • Minervini, F.; Algaron, F.; Rizello, G.C.; Fox, P.F.; Monnet, V.; Gobbetti, M. Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolysed caseins of milk from six species. Applied and Environmental Microbiology 2003, 69, 5297-5305.
    • (2003) Applied and Environmental Microbiology , vol.69 , pp. 5297-5305
    • Minervini, F.1    Algaron, F.2    Rizello, G.C.3    Fox, P.F.4    Monnet, V.5    Gobbetti, M.6
  • 175
    • 58249117728 scopus 로고    scopus 로고
    • Antimicrobial activity of two peptides casecidin 15 and 17, found naturally in bovine colostrum
    • Birkemo, G.A.; O'Sullivan, O.; Ross, R.P.; Hill, C. Antimicrobial activity of two peptides casecidin 15 and 17, found naturally in bovine colostrum. Journal of AppliedMicrobiolology 2009, 106, 233-240.
    • (2009) Journal of AppliedMicrobiolology , vol.106 , pp. 233-240
    • Birkemo, G.A.1    O'Sullivan, O.2    Ross, R.P.3    Hill, C.4
  • 177
    • 60849088259 scopus 로고    scopus 로고
    • Evaluation of an antimicrobial ingredient prepared from a Lactobacillus acidophilus casein fermentate against Enterobacter sakazakii
    • Hayes, M.; Barrett, E.; Ross, R.P.; Fitzgerald, G.F.; Hill, C.; Stanton, C. Evaluation of an antimicrobial ingredient prepared from a Lactobacillus acidophilus casein fermentate against Enterobacter sakazakii. Journal of Food Protection 2009, 72, 340-346.
    • (2009) Journal of Food Protection , vol.72 , pp. 340-346
    • Hayes, M.1    Barrett, E.2    Ross, R.P.3    Fitzgerald, G.F.4    Hill, C.5    Stanton, C.6
  • 178
    • 0037100364 scopus 로고    scopus 로고
    • Production of granulocyte colony-stimulating factor in the nonspecific acute phase response enhances host resistance to bacterial infection
    • Noursadeghi, M.; Bickerstaff, M.C.; Herbert, J.; Moyes, D.; Cohen, J.; Pepys, M.B. Production of granulocyte colony-stimulating factor in the nonspecific acute phase response enhances host resistance to bacterial infection. Journal of Immunology 2002, 169, 913-919.
    • (2002) Journal of Immunology , vol.169 , pp. 913-919
    • Noursadeghi, M.1    Bickerstaff, M.C.2    Herbert, J.3    Moyes, D.4    Cohen, J.5    Pepys, M.B.6
  • 179
    • 33746916083 scopus 로고    scopus 로고
    • Novel therapies based on cationic antimicrobial peptides
    • Pereira, H.A. Novel therapies based on cationic antimicrobial peptides. Current Pharmaceutical Biotechnology 2006, 7, 229-234.
    • (2006) Current Pharmaceutical Biotechnology , vol.7 , pp. 229-234
    • Pereira, H.A.1
  • 180
    • 0024329210 scopus 로고
    • Biologically active casein peptides implicated in immunomodulation
    • Migliore-Samour, D.; Floc'h, F.; Jollès, P. Biologically active casein peptides implicated in immunomodulation. Journal of Dairy Research 1989, 56, 357-362.
    • (1989) Journal of Dairy Research , vol.56 , pp. 357-362
    • Migliore-Samour, D.1    Floc'h, F.2    Jollès, P.3
  • 181
    • 0040531807 scopus 로고    scopus 로고
    • Immunostimulatory action of a commercially available casein phosphopeptide preparation, CPP-III in cell cultures
    • Hata, I.; Ueda, J.; Otani, H. Immunostimulatory action of a commercially available casein phosphopeptide preparation, CPP-III in cell cultures. Milchwissenschaft 1999, 54, 3-7.
    • (1999) Milchwissenschaft , vol.54 , pp. 3-7
    • Hata, I.1    Ueda, J.2    Otani, H.3
  • 182
    • 0021677121 scopus 로고
    • Immunostimulating hexapeptide from human casein: Amino acid sequence, synthesis and biological properties
    • Parker, F.; Migliore-Samour, D.; Floc'h, F. Immunostimulating hexapeptide from human casein: amino acid sequence, synthesis and biological properties. European Journal of Biochemistry 1984, 145, 677-682.
    • (1984) European Journal of Biochemistry , vol.145 , pp. 677-682
    • Parker, F.1    Migliore-Samour, D.2    Floc'h, F.3
  • 184
    • 0032801518 scopus 로고    scopus 로고
    • Metabolic fate of nociceptin/orphanin FQ in the rat spinal cord and biological activity of its release fragment
    • Suder, P.; Kotlińska, J.; Smoluch, M.T.; Sällberg, M.; Silberring, J. Metabolic fate of nociceptin/orphanin FQ in the rat spinal cord and biological activity of its release fragment. Peptides 1999, 20, 239-247.
    • (1999) Peptides , vol.20 , pp. 239-247
    • Suder, P.1    Kotlińska, J.2    Smoluch, M.T.3    Sällberg, M.4    Silberring, J.5
  • 185
    • 0041851095 scopus 로고    scopus 로고
    • Stimulatory effect of a dietary casein phosphopeptide preparation on the mucosal IgA response of mice to orally ingested lipopolysaccharide from Salmonella typhinurium
    • Otani, H.; Nakano, K.; Kawahara, T. Stimulatory effect of a dietary casein phosphopeptide preparation on the mucosal IgA response of mice to orally ingested lipopolysaccharide from Salmonella typhinurium. Bioscience Biotechnology and Biochemistry 2003, 67, 729-735.
    • (2003) Bioscience Biotechnology and Biochemistry , vol.67 , pp. 729-735
    • Otani, H.1    Nakano, K.2    Kawahara, T.3
  • 186
    • 0028849897 scopus 로고
    • Dietary protection against diabetes in NOD mice: Lack of a major change in the immune system
    • Hermitte, L.; Atlan-Gepner, C.; Payan, M.J.; Mehelleb, M.; Vialettes, B. Dietary protection against diabetes in NOD mice: lack of a major change in the immune system. Diabete Metabolism 1995, 21, 261-268.
    • (1995) Diabete Metabolism , vol.21 , pp. 261-268
    • Hermitte, L.1    Atlan-Gepner, C.2    Payan, M.J.3    Mehelleb, M.4    Vialettes, B.5
  • 188
    • 0031055268 scopus 로고    scopus 로고
    • Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine β-lactoglobulin
    • Mullally, M.M.; Meisel, H.; FitzGerald, R.J. Identification of a novel angiotensin-I-converting enzyme inhibitory peptide corresponding to a tryptic fragment of bovine β-lactoglobulin. FEBS Letters 1997, 402, 99-101.
    • (1997) FEBS Letters , vol.402 , pp. 99-101
    • Mullally, M.M.1    Meisel, H.2    FitzGerald, R.J.3
  • 189
    • 0034494479 scopus 로고    scopus 로고
    • Effects of milk-derived bioactives: An overview
    • Shah, N. Effects of milk-derived bioactives: an overview. British Journal of Nutrition 2000, 84(Suppl. 1), S3-S10.
    • (2000) British Journal of Nutrition , vol.84 , Issue.SUPPL. 1 , pp. 3-10
    • Shah, N.1
  • 191
    • 3242782703 scopus 로고    scopus 로고
    • Structural analysis of a new anti-hypertensive peptide (beta-lactosin B) isolated from a commercial whey product
    • Murakami, M.; Tonouchi, H.; Takahashi, R.; Kitazawa, H.; Kawai, Y.; Negishi, H.; Saito, T. Structural analysis of a new anti-hypertensive peptide (beta-lactosin B) isolated from a commercial whey product. Journal of Dairy Science 2004, 87, 1967-1974.
    • (2004) Journal of Dairy Science , vol.87 , pp. 1967-1974
    • Murakami, M.1    Tonouchi, H.2    Takahashi, R.3    Kitazawa, H.4    Kawai, Y.5    Negishi, H.6    Saito, T.7
  • 192
    • 1542681459 scopus 로고    scopus 로고
    • rRNA probe used to quantify the effects of glycomacropeptide and alpha-lactalbumin supplementation on the predominant groups of intestinal bacteria of infant rhesus monkeys challenged with enteropathogenic Escherichia coli
    • Bruck, W.M.; Kelleher, S.L.; Gibson, G.G.; Nielsen, K.E.; Chatterton, D.E.; Lönnerdal, B. rRNA probe used to quantify the effects of glycomacropeptide and alpha-lactalbumin supplementation on the predominant groups of intestinal bacteria of infant rhesus monkeys challenged with enteropathogenic Escherichia coli. Journal of Pediatriatrics, Gastroenterology and Nutrition 2003, 37, 273-280.
    • (2003) Journal of Pediatriatrics, Gastroenterology and Nutrition , vol.37 , pp. 273-280
    • Bruck, W.M.1    Kelleher, S.L.2    Gibson, G.G.3    Nielsen, K.E.4    Chatterton, D.E.5    Lönnerdal, B.6
  • 193
    • 1542405871 scopus 로고    scopus 로고
    • Human alpha-lactalbumin made lethal to tumor cells (HAMLET) kills human glioblastoma cells in brain xenografts by an apoptosis-like mechanism and prolongs survival
    • Fischer, W.; Gustafsson, L.; Mossberg, A.K.; Gronli, J.; Mork, S.; Bjerkvig, S.; Svanborg, C. Human alpha-lactalbumin made lethal to tumor cells (HAMLET) kills human glioblastoma cells in brain xenografts by an apoptosis-like mechanism and prolongs survival. Cancer Research 2004, 64, 2105-2112.
    • (2004) Cancer Research , vol.64 , pp. 2105-2112
    • Fischer, W.1    Gustafsson, L.2    Mossberg, A.K.3    Gronli, J.4    Mork, S.5    Bjerkvig, S.6    Svanborg, C.7
  • 194
    • 13244274907 scopus 로고    scopus 로고
    • Stability of HAMLET-A kinetically trapped α-lactalbumin oleic acid complex
    • Fast, J.; Mossberg, A.K.; Svanborg, C.; Linse, S. Stability of HAMLET-A kinetically trapped α-lactalbumin oleic acid complex. Protein Science 2005, 14, 329-340.
    • (2005) Protein Science , vol.14 , pp. 329-340
    • Fast, J.1    Mossberg, A.K.2    Svanborg, C.3    Linse, S.4
  • 199
    • 0034633086 scopus 로고    scopus 로고
    • Bioactive peptides derived from bovine whey proteins: Opioid and ACEinhibitory peptides
    • Pihlanto-Leppälä, A. Bioactive peptides derived from bovine whey proteins: opioid and ACEinhibitory peptides. Trends in Food Science and Technology 2001, 11, 347-356.
    • (2001) Trends in Food Science and Technology , vol.11 , pp. 347-356
    • Pihlanto-Leppälä, A.1
  • 200
    • 0034085615 scopus 로고    scopus 로고
    • The bovine protein alphalactalbumin increases the plasma ratio of tryptophan to the other large neutral amino acids, and in vulnerable subjects raises brain serotonin activity, reduces cortisol concentration, and improves mood under stress
    • Markus, C.R.; Olivier, B.; Panhuysen, G.E.; Van Der Gugten, J.; Alles, M.S.; Tuiten, A.; Westenberg, H.G.; Fekkes, D.; Koppeschaar, H.F.; de Haan, E.E. The bovine protein alphalactalbumin increases the plasma ratio of tryptophan to the other large neutral amino acids, and in vulnerable subjects raises brain serotonin activity, reduces cortisol concentration, and improves mood under stress. American Journal of Clinical Nutrition 2000, 71, 1536-1544.
    • (2000) American Journal of Clinical Nutrition , vol.71 , pp. 1536-1544
    • Markus, C.R.1    Olivier, B.2    Panhuysen, G.E.3    van der Gugten, J.4    Alles, M.S.5    Tuiten, A.6    Westenberg, H.G.7    Fekkes, D.8    Koppeschaar, H.F.9    de Haan, E.E.10
  • 201
    • 0347626245 scopus 로고    scopus 로고
    • Alpha-lactalbuminenriched diets enhance serotonin release and induce anxiolytic and rewarding effects in the rat
    • Orosco, M.; Rouch, C.; Beslot, F.; Feurte, S.; Regnault, A.; Dauge, V. Alpha-lactalbuminenriched diets enhance serotonin release and induce anxiolytic and rewarding effects in the rat. Behavior and Brain Research 2004, 48, 1-10.
    • (2004) Behavior and Brain Research , vol.48 , pp. 1-10
    • Orosco, M.1    Rouch, C.2    Beslot, F.3    Feurte, S.4    Regnault, A.5    Dauge, V.6
  • 202
    • 0035964785 scopus 로고    scopus 로고
    • Inhibition of human immunodeficiency virus type 1 reverse transcriptase, protease and integrase by bovine milk proteins
    • Ng, T.B.; Lam, T.L.; Au, T.K.; Ye, X.Y.; Wan, C.C. Inhibition of human immunodeficiency virus type 1 reverse transcriptase, protease and integrase by bovine milk proteins. Life Sciences 2001, 69, 2217-2223.
    • (2001) Life Sciences , vol.69 , pp. 2217-2223
    • Ng, T.B.1    Lam, T.L.2    Au, T.K.3    Ye, X.Y.4    Wan, C.C.5
  • 205
    • 58149125767 scopus 로고    scopus 로고
    • A structural framework for understanding the multifunctional character of lactoferrin
    • Baker, E.N.; Baker, H.M. A structural framework for understanding the multifunctional character of lactoferrin. Biochimie 2009, 91, 3-10.
    • (2009) Biochimie , vol.91 , pp. 3-10
    • Baker, E.N.1    Baker, H.M.2
  • 206
    • 58149131710 scopus 로고    scopus 로고
    • Role of lactoferrin in the tear film
    • Flanagan, J.L.; Willcox, M.D.P. Role of lactoferrin in the tear film. Biochimie 2009, 91, 35-43.
    • (2009) Biochimie , vol.91 , pp. 35-43
    • Flanagan, J.L.1    Willcox, M.D.P.2
  • 207
    • 58149113170 scopus 로고    scopus 로고
    • Antimicrobial properties of lactoferrin
    • Jenssen, H.; Hancock, R.E.W. Antimicrobial properties of lactoferrin. Biochimie 2009, 91, 19-29.
    • (2009) Biochimie , vol.91 , pp. 19-29
    • Jenssen, H.1    Hancock, R.E.W.2
  • 208
    • 58149121478 scopus 로고    scopus 로고
    • Effect of lactoferrin on enteric pathogens
    • Ochoa, T.J.; Cleary, T.G. Effect of lactoferrin on enteric pathogens. Biochimie 2009, 91, 30-34.
    • (2009) Biochimie , vol.91 , pp. 30-34
    • Ochoa, T.J.1    Cleary, T.G.2
  • 209
    • 58149105930 scopus 로고    scopus 로고
    • The influence of lactoferrin, orally administered, on systemic iron homeostasis in pregnant women suffering of iron deficiency and iron deficiency anaemia
    • Paesano, R.; Pietropaoli, M.; Gessani, S.; Valenti, P. The influence of lactoferrin, orally administered, on systemic iron homeostasis in pregnant women suffering of iron deficiency and iron deficiency anaemia. Biochimie 2009, 91, 44-51.
    • (2009) Biochimie , vol.91 , pp. 44-51
    • Paesano, R.1    Pietropaoli, M.2    Gessani, S.3    Valenti, P.4
  • 210
    • 58149140244 scopus 로고    scopus 로고
    • Immunomodulatory effects of lactoferrin on antigen presenting cells
    • Puddu, P.; Valenti, P.; Gessani, S. Immunomodulatory effects of lactoferrin on antigen presenting cells. Biochimie 2009, 91, 11-18.
    • (2009) Biochimie , vol.91 , pp. 11-18
    • Puddu, P.1    Valenti, P.2    Gessani, S.3
  • 213
    • 0032924742 scopus 로고    scopus 로고
    • Construction and synthesis of lactoferricin derivatives with enhanced antibacterial activity
    • Rekdal, Ø.; Andersen, J.; Vorland, L.H.; Svendsen, J.S. Construction and synthesis of lactoferricin derivatives with enhanced antibacterial activity. Journal of Peptide Science 1999, 5, 32-45.
    • (1999) Journal of Peptide Science , vol.5 , pp. 32-45
    • Rekdal, O.1    Andersen, J.2    Vorland, L.H.3    Svendsen, J.S.4
  • 218
    • 58149127828 scopus 로고    scopus 로고
    • Bactericidal activity of LFchimera is stronger and less sensitive to ionic strength than its constituent lactoferricin and lactoferrampin peptides
    • Bolscher, J.G.M.; Adão, R.; Nazmi, K.; van den Keybus, P.A.M.; van't Hof, W.; Nieuw Amerongen, A.V.; Bastos, M.; Veerman, E.C.I. Bactericidal activity of LFchimera is stronger and less sensitive to ionic strength than its constituent lactoferricin and lactoferrampin peptides. Biochimie 2009, 91, 123-132.
    • (2009) Biochimie , vol.91 , pp. 123-132
    • Bolscher, J.G.M.1    Adão, R.2    Nazmi, K.3    van den Keybus, P.A.M.4    van't Hof, W.5    Nieuw Amerongen, A.V.6    Bastos, M.7    Veerman, E.C.I.8
  • 220
    • 58149105937 scopus 로고    scopus 로고
    • Novel lactoferrampin antimicrobial peptides derived from human lactoferrin
    • Haney, E.F., Nazmi, K.; Lau, F.; Bolscher, J.G.M.; Vogel, H.J. Novel lactoferrampin antimicrobial peptides derived from human lactoferrin. Biochimie 2009, 91, 141-154.
    • (2009) Biochimie , vol.91 , pp. 141-154
    • Haney, E.F.1    Nazmi, K.2    Lau, F.3    Bolscher, J.G.M.4    Vogel, H.J.5
  • 222
    • 0026095436 scopus 로고
    • Killing of gram-negative bacteria by lactoferrin and lysozyme
    • Ellison, R.T.; Giehl, T.J. Killing of gram-negative bacteria by lactoferrin and lysozyme. Journal of Clinical Investigation 1991, 88, 1088-1091.
    • (1991) Journal of Clinical Investigation , vol.88 , pp. 1088-1091
    • Ellison, R.T.1    Giehl, T.J.2
  • 223
    • 0036562847 scopus 로고    scopus 로고
    • Effect of lactoferrin in combination with penicilin on the morphology and physiology of Staphylococcus aureus isolated from bovine mastitis
    • Diarra, M.S.; Petitclerc, D.; Lacasse, P. Effect of lactoferrin in combination with penicilin on the morphology and physiology of Staphylococcus aureus isolated from bovine mastitis. Journal of Dairy Science 2002, 85, 1141-1149.
    • (2002) Journal of Dairy Science , vol.85 , pp. 1141-1149
    • Diarra, M.S.1    Petitclerc, D.2    Lacasse, P.3
  • 225
    • 58149140247 scopus 로고    scopus 로고
    • Bovine lactoferrin and lactoferricin interfere with intracellular trafficking of Herpes simplex virus-1
    • Marr, A.K.; Jenssen, H.; Roshan Moriri, M.; Hancock, R.E.W.; Panté, N. Bovine lactoferrin and lactoferricin interfere with intracellular trafficking of Herpes simplex virus-1. Biochimie 2009, 91, 160-164.
    • (2009) Biochimie , vol.91 , pp. 160-164
    • Marr, A.K.1    Jenssen, H.2    Roshan Moriri, M.3    Hancock, R.E.W.4    Panté, N.5
  • 226
    • 58549104530 scopus 로고    scopus 로고
    • Inhibition of HBV infection by bovine lactoferrin and iron-, zinc-saturated lactoferrin
    • Li, S.; Zhou, H.; Huang, G.; Liu, N. Inhibition of HBV infection by bovine lactoferrin and iron-, zinc-saturated lactoferrin. Medical Microbiology and Immunology 2009, 198, 19-25.
    • (2009) Medical Microbiology and Immunology , vol.198 , pp. 19-25
    • Li, S.1    Zhou, H.2    Huang, G.3    Liu, N.4
  • 231
    • 53349090565 scopus 로고    scopus 로고
    • A lactoferrin-derived peptide with cationic residues concentrated in a region of its helical structure induces necrotic cell death in a leukemic cell line (HL-60)
    • Onishi, J.; Roy, M.K.; Juneja, L.R.; Watanabe, Y.; Tamai, Y. A lactoferrin-derived peptide with cationic residues concentrated in a region of its helical structure induces necrotic cell death in a leukemic cell line (HL-60). Journal of Peptide Science 2008, 14, 1032-1038.
    • (2008) Journal of Peptide Science , vol.14 , pp. 1032-1038
    • Onishi, J.1    Roy, M.K.2    Juneja, L.R.3    Watanabe, Y.4    Tamai, Y.5
  • 234
    • 58149115086 scopus 로고    scopus 로고
    • Proteomic approach to the identification of novel delta-lactoferrin target genes: Characterization of DcpS, an mRNA scavenger decapping enzyme
    • Mariller, C.; Hardivillé, S.; Hoedt, E.; Benaïssa, M.; Mazurier, J.; Pierce, A. Proteomic approach to the identification of novel delta-lactoferrin target genes: characterization of DcpS, an mRNA scavenger decapping enzyme. Biochimie 2009, 91, 109-122.
    • (2009) Biochimie , vol.91 , pp. 109-122
    • Mariller, C.1    Hardivillé, S.2    Hoedt, E.3    Benaïssa, M.4    Mazurier, J.5    Pierce, A.6
  • 235
    • 58149134848 scopus 로고    scopus 로고
    • Requirement of the JNKassociated Bcl-2 pathway for human lactoferrin-induced apoptosis in the Jurkat leukemia T cell line
    • Lee, S.-H.; Park, S.W.; Pyo, C.-W.; Yoo, N.-K.; Kim, J.; Choi, S.-Y. Requirement of the JNKassociated Bcl-2 pathway for human lactoferrin-induced apoptosis in the Jurkat leukemia T cell line. Biochimie 2009, 91, 102-108.
    • (2009) Biochimie , vol.91 , pp. 102-108
    • Lee, S.-H.1    Park, S.W.2    Pyo, C.-W.3    Yoo, N.-K.4    Kim, J.5    Choi, S.-Y.6
  • 236
    • 0023787471 scopus 로고
    • KRDS-a tetrapeptide derived from lactoferrin inhibits binding of monoclonal antibodies against glycoprotein IIb-IIIa on ADP stimulated platelets and megakaryocytes
    • Raha, S.; Dosquet, C.; Abgrall, J.F.; Jollès, P.; Fiat, A.-M.; Caen, J.P. KRDS-a tetrapeptide derived from lactoferrin inhibits binding of monoclonal antibodies against glycoprotein IIb-IIIa on ADP stimulated platelets and megakaryocytes. Blood 1988, 72, 172-178.
    • (1988) Blood , vol.72 , pp. 172-178
    • Raha, S.1    Dosquet, C.2    Abgrall, J.F.3    Jollès, P.4    Fiat, A.-M.5    Caen, J.P.6
  • 238
    • 0346252379 scopus 로고    scopus 로고
    • Recombinant human lactoferrin ingestion attenuates indomethacin-induced enteropathy in vivo in healthy volunteers
    • Troost, F.J.; Saris, W.H.M.; Brummer, R.-J.M. Recombinant human lactoferrin ingestion attenuates indomethacin-induced enteropathy in vivo in healthy volunteers. European Journal of Clinical Nutrition 2003, 57, 1579-1585.
    • (2003) European Journal of Clinical Nutrition , vol.57 , pp. 1579-1585
    • Troost, F.J.1    Saris, W.H.M.2    Brummer, R.-J.M.3
  • 239
    • 0942279593 scopus 로고    scopus 로고
    • The mode of oral bovine lactoferrin administration influences mucosal and systemic immune responces in mice
    • Sfeir, R.M.; Dubarry, M.; Boyaka, P.N.; Rautureau, M.; Tomé, D. The mode of oral bovine lactoferrin administration influences mucosal and systemic immune responces in mice. Journal of Nutrition 2004, 134, 403-439.
    • (2004) Journal of Nutrition , vol.134 , pp. 403-439
    • Sfeir, R.M.1    Dubarry, M.2    Boyaka, P.N.3    Rautureau, M.4    Tomé, D.5
  • 240
    • 3342997837 scopus 로고    scopus 로고
    • Development of an enteric-coated lactoferrin tablet and its application
    • Shimizu, H. Development of an enteric-coated lactoferrin tablet and its application, Biometals 2004, 17, 343-347.
    • (2004) Biometals , vol.17 , pp. 343-347
    • Shimizu, H.1
  • 241
    • 0141450720 scopus 로고    scopus 로고
    • Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria
    • Masschalck, B.; Michiels, C.W. Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria. Critical Reviews in Microbiology 2003, 29, 191-214.
    • (2003) Critical Reviews in Microbiology , vol.29 , pp. 191-214
    • Masschalck, B.1    Michiels, C.W.2
  • 244
    • 0031774839 scopus 로고    scopus 로고
    • A novel anti-inflammatory activity of lysozyme: Modulation of serum complement activation
    • Ogundele, M.O. A novel anti-inflammatory activity of lysozyme: modulation of serum complement activation. Mediators of Inflammation 1998, 7, 363-365.
    • (1998) Mediators of Inflammation , vol.7 , pp. 363-365
    • Ogundele, M.O.1
  • 245
    • 0019461944 scopus 로고
    • Is Fleming's lysozyme an analgesic agent? An experimental reappraisal of clinical data
    • Bianchi, C. Is Fleming's lysozyme an analgesic agent? An experimental reappraisal of clinical data. European Journal of Pharmacology 1981, 71, 211-221.
    • (1981) European Journal of Pharmacology , vol.71 , pp. 211-221
    • Bianchi, C.1
  • 246
    • 0035964823 scopus 로고    scopus 로고
    • Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function
    • Ibrahim, H.R.; Matsuzaki, T.; Aoki, T. Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function. FEBS Letters 2001, 506, 27-32.
    • (2001) FEBS Letters , vol.506 , pp. 27-32
    • Ibrahim, H.R.1    Matsuzaki, T.2    Aoki, T.3
  • 247
    • 0036179432 scopus 로고    scopus 로고
    • Susceptibility of Heliobacter pylori and its urease activity to the peroxidase-hydrogen peroxide-thiocyanate antimicrobial system
    • Shin, K.; Yamauchi, K.; Teraguchi, S.; Hayasawa, H.; Imoto, I. Susceptibility of Heliobacter pylori and its urease activity to the peroxidase-hydrogen peroxide-thiocyanate antimicrobial system. Journal of Medical Microbiolology 2002, 51, 231-237.
    • (2002) Journal of Medical Microbiolology , vol.51 , pp. 231-237
    • Shin, K.1    Yamauchi, K.2    Teraguchi, S.3    Hayasawa, H.4    Imoto, I.5
  • 248
    • 0023636831 scopus 로고
    • A note on the effect of the lactoperoxidase systems on salmonellas in vitro and in vivo
    • Wray, C.; McLaren, I. A note on the effect of the lactoperoxidase systems on salmonellas in vitro and in vivo. Journal of Applied Bacteriology 1987, 62, 115-118.
    • (1987) Journal of Applied Bacteriology , vol.62 , pp. 115-118
    • Wray, C.1    McLaren, I.2
  • 249
    • 0034490329 scopus 로고    scopus 로고
    • In vivo antimicrobial and antiviral activity of components in bovine milk and colostrum involved in non-specific defence
    • van Hooijdonk, A.C.; Kussendrager, K.D.; Steijns, J.M. In vivo antimicrobial and antiviral activity of components in bovine milk and colostrum involved in non-specific defence. British Journal of Nutrition 2000, 84, S127-S134.
    • (2000) British Journal of Nutrition , vol.84 , pp. 27-134
    • van Hooijdonk, A.C.1    Kussendrager, K.D.2    Steijns, J.M.3
  • 250
    • 38949121728 scopus 로고    scopus 로고
    • Antimicrobial activity of nisin, reuterin and the lactoperoxidase system on Listeria monocytogenes and Stapylococcus aureus in cuajada, a semisolid dairy product manufactured in Spain
    • Arqués, J.L.; Rodríguez, E.; Nuñez, M.; Medina, M. Antimicrobial activity of nisin, reuterin and the lactoperoxidase system on Listeria monocytogenes and Stapylococcus aureus in cuajada, a semisolid dairy product manufactured in Spain. Journal of Dairy Science 2008, 91, 70-75.
    • (2008) Journal of Dairy Science , vol.91 , pp. 70-75
    • Arqués, J.L.1    Rodríguez, E.2    Nuñez, M.3    Medina, M.4
  • 251
    • 62549093512 scopus 로고    scopus 로고
    • Antimicrobial activity of lactoperoxidase system incorporated into cross-linked alginate films
    • Yener, F.Y.G.; Korel, F.; Yemeniciǒglu, A. Antimicrobial activity of lactoperoxidase system incorporated into cross-linked alginate films. Journal of Food Science 2009, 74, M73-M79.
    • (2009) Journal of Food Science , vol.74 , pp. 73-79
    • Yener, F.Y.G.1    Korel, F.2    Yemeniciǒglu, A.3
  • 252
    • 47649111355 scopus 로고    scopus 로고
    • Inhibitory effect of lactoperoxidase on the the secretion of proinflammatory cytokine interlukin-8 in human intestinal epithelial Caco-2 cells
    • Matsushita, A., Son, D.O.; Satsu, H.; Takano, Y.; Kawakami, H.; Totsuka, M. Inhibitory effect of lactoperoxidase on the the secretion of proinflammatory cytokine interlukin-8 in human intestinal epithelial Caco-2 cells. International Dairy Journal 2008, 18, 932-938.
    • (2008) International Dairy Journal , vol.18 , pp. 932-938
    • Matsushita, A.1    Son, D.O.2    Satsu, H.3    Takano, Y.4    Kawakami, H.5    Totsuka, M.6
  • 255
    • 0023757139 scopus 로고
    • Specific and nonspecific inhibition of adhesion of oral actinomyces and streptococci to erythrocytes and polystyreneby caseinoglycopeptide derivatives
    • Neeser, J.R.; Chambaz, A.; Del Vedovo, S.; Prigent, M.J.; Guggenheim, B. Specific and nonspecific inhibition of adhesion of oral actinomyces and streptococci to erythrocytes and polystyreneby caseinoglycopeptide derivatives. Infection and Immunity 1988, 56, 3201-3208.
    • (1988) Infection and Immunity , vol.56 , pp. 3201-3208
    • Neeser, J.R.1    Chambaz, A.2    Del Vedovo, S.3    Prigent, M.J.4    Guggenheim, B.5
  • 257
    • 0030288545 scopus 로고    scopus 로고
    • Influence of glycosylation on micelle-stabilizing ability and biological properties of C-terminal fragments of cow's κ-casein
    • Dziuba, J.; Minkiewicz, P. Influence of glycosylation on micelle-stabilizing ability and biological properties of C-terminal fragments of cow's κ-casein. International Dairy Journal 1996, 6, 1017-1044.
    • (1996) International Dairy Journal , vol.6 , pp. 1017-1044
    • Dziuba, J.1    Minkiewicz, P.2
  • 262
    • 85007963864 scopus 로고
    • Bifidus growth promoting effect of N-acetylneuraminic acid-containing substances
    • Idota, T.; Kawakami, H.; Nakajima, I. Bifidus growth promoting effect of N-acetylneuraminic acid-containing substances. Bioscience Biotechnology Biochemistry 1994, 58, 1720-1722.
    • (1994) Bioscience Biotechnology Biochemistry , vol.58 , pp. 1720-1722
    • Idota, T.1    Kawakami, H.2    Nakajima, I.3
  • 264
    • 0023709851 scopus 로고
    • Heterogeneity and physiological activity of bovine κ-casein proteolysis products
    • Stan, E.Y.; Ekimovskii, A.P.; Aleinik, S.I.; Zhuravlev, B.V. Heterogeneity and physiological activity of bovine κ-casein proteolysis products. Voprosy Pitanija 1988, 1, 39-43.
    • (1988) Voprosy Pitanija , vol.1 , pp. 39-43
    • Stan, E.Y.1    Ekimovskii, A.P.2    Aleinik, S.I.3    Zhuravlev, B.V.4
  • 265
    • 0038474028 scopus 로고    scopus 로고
    • Glycomacropeptide and α-lactalbumin supplementation of infant formula affects growth and nutritional status in infant rhesus monkeys
    • Kelleher, S.L.; Chatterton, D.; Nielsen, K.; Lönnerdal, B. Glycomacropeptide and α-lactalbumin supplementation of infant formula affects growth and nutritional status in infant rhesus monkeys. American Journal of Clinical Nutrition 2003, 77, 1261-1268.
    • (2003) American Journal of Clinical Nutrition , vol.77 , pp. 1261-1268
    • Kelleher, S.L.1    Chatterton, D.2    Nielsen, K.3    Lönnerdal, B.4
  • 267
    • 53049090835 scopus 로고    scopus 로고
    • Whey protein isolate and glycomacropeptide decrease weight gain and alter body composition in male Wistar rats
    • Royle, P.J.; McIntosh, G.H.; Clifton, P.M. Whey protein isolate and glycomacropeptide decrease weight gain and alter body composition in male Wistar rats. British Journal of Nutrition 2008, 100, 88-93.
    • (2008) British Journal of Nutrition , vol.100 , pp. 88-93
    • Royle, P.J.1    McIntosh, G.H.2    Clifton, P.M.3
  • 270
    • 0345549544 scopus 로고    scopus 로고
    • Antibacterials: Are the new entries enough to deal with the emerging resistance problems?
    • Barrett, C.T.; Barrett, J.F. Antibacterials: are the new entries enough to deal with the emerging resistance problems? Current Opinion in Biotechnology 2003, 14, 621-626.
    • (2003) Current Opinion in Biotechnology , vol.14 , pp. 621-626
    • Barrett, C.T.1    Barrett, J.F.2
  • 271
    • 0016325501 scopus 로고
    • Isolation and characterization of a proline-rich polypeptide from ovine colostrums
    • Janusz, M.; Lisowski, J.; Franek, F. Isolation and characterization of a proline-rich polypeptide from ovine colostrums. FEBS Letters 1974, 49, 276-279.
    • (1974) FEBS Letters , vol.49 , pp. 276-279
    • Janusz, M.1    Lisowski, J.2    Franek, F.3
  • 272


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.