메뉴 건너뛰기




Volumn 8, Issue 2, 2009, Pages 114-127

Antifungal and antiparasitic activities of lactoferrin

Author keywords

Antifungal; Antimicrobial peptides; Antiparasitic; Iron; Lactoferrin; Mycosis; Natural immunity; Parasitic diseases

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMPHOTERICIN B; ANTIFUNGAL AGENT; FLUCONAZOLE; KALIOCIN 1; LACTOFERRICIN; LACTOFERRICIN B; LACTOFERRICIN[17-31]; LACTOFERRICIN[20-25]; LACTOFERRIN; LACTOFERRIN AMPIN[265-284]; LACTOFERRIN PEP; LACTOFERRIN[1-11]; LACTOFERRIN[21-31]; PEPSIN HYDROLYSATE; PEPTIDE 2; UNCLASSIFIED DRUG;

EID: 67651120180     PISSN: 18715214     EISSN: None     Source Type: Journal    
DOI: 10.2174/187152109787846105     Document Type: Article
Times cited : (23)

References (127)
  • 2
    • 8244256698 scopus 로고    scopus 로고
    • Reiter, B.; Oram J.D.: Group N Streptococcal phage lysin. J. Gen. Microbiol., 1963, 32, 29-32.
    • Reiter, B.; Oram J.D.: Group N Streptococcal phage lysin. J. Gen. Microbiol., 1963, 32, 29-32.
  • 3
    • 0013968292 scopus 로고
    • Immunohistochemical localization and bacteriostatic properties of an iron-binding protein from bronchial mucus
    • Masson, P. L., Heremans, J. F., Prignot, J. J., Wauters, G. Immunohistochemical localization and bacteriostatic properties of an iron-binding protein from bronchial mucus. Thorax, 1966, 21, 538-44
    • (1966) Thorax , vol.21 , pp. 538-544
    • Masson, P.L.1    Heremans, J.F.2    Prignot, J.J.3    Wauters, G.4
  • 4
    • 28344457682 scopus 로고    scopus 로고
    • Lactoferrin: An important host defence against microbial and viral attack
    • Valenti, P.; Antonini, G. Lactoferrin: an important host defence against microbial and viral attack. Cell Mol. Life Sci., 2005, 62, 2576-87.
    • (2005) Cell Mol. Life Sci , vol.62 , pp. 2576-2587
    • Valenti, P.1    Antonini, G.2
  • 5
    • 58149113170 scopus 로고    scopus 로고
    • Jenssen, H.; Hancock, R.E.W. Antimicrobial properties of lactoferrin Biochimie, 2008 [Epub ahead of print] (Doi: doi:10.1016/ j.biochi.2008.05.015)
    • Jenssen, H.; Hancock, R.E.W. Antimicrobial properties of lactoferrin Biochimie, 2008 [Epub ahead of print] (Doi: doi:10.1016/ j.biochi.2008.05.015)
  • 6
    • 0742269683 scopus 로고    scopus 로고
    • Comparison of the epidemiology, drug resistance mechanisms, and virulence of Candida dubliniensis and Candida albicans
    • Sullivan, D.J.; Moran, G.P.; Pinjon, E.; Al-Mosaid, A.; Stokes, C.; Vaughan, C.; Coleman, D.C. Comparison of the epidemiology, drug resistance mechanisms, and virulence of Candida dubliniensis and Candida albicans. FEMS Yeast Res., 2004, 4, 369-76.
    • (2004) FEMS Yeast Res , vol.4 , pp. 369-376
    • Sullivan, D.J.1    Moran, G.P.2    Pinjon, E.3    Al-Mosaid, A.4    Stokes, C.5    Vaughan, C.6    Coleman, D.C.7
  • 7
    • 0027441959 scopus 로고
    • Effects of itraconazole on cytochrome P-450-dependent sterol 14 α-demethylation and reduction of 3-ketosteroids in Cryptococcus neoformans
    • Van den Bossche, H.; Marichal, P.; Le Jeune, L.; Coene, M.C.; Gorrens, J.; Cools, W. Effects of itraconazole on cytochrome P-450-dependent sterol 14 α-demethylation and reduction of 3-ketosteroids in Cryptococcus neoformans. Antimicrob. Agents Chemother., 1993, 37, 2101-5.
    • (1993) Antimicrob. Agents Chemother , vol.37 , pp. 2101-2105
    • Van den Bossche, H.1    Marichal, P.2    Le Jeune, L.3    Coene, M.C.4    Gorrens, J.5    Cools, W.6
  • 9
    • 30344443097 scopus 로고    scopus 로고
    • Antimicrobial peptides enhance the Candidacidal activity of antifungal drugs by promoting the efflux of ATP from Candida cells
    • Tanida, T.; Okamoto, T.; Ueta, E.; Yamamoto, T.; Osaki, T. Antimicrobial peptides enhance the Candidacidal activity of antifungal drugs by promoting the efflux of ATP from Candida cells. J. Antimicrob. Chemother., 2006, 57, 94-103.
    • (2006) J. Antimicrob. Chemother , vol.57 , pp. 94-103
    • Tanida, T.1    Okamoto, T.2    Ueta, E.3    Yamamoto, T.4    Osaki, T.5
  • 10
    • 0033278237 scopus 로고    scopus 로고
    • Natural defenses against Candida colonization breakdown in the oral cavities of the elderly
    • Lockhart, S. R.; Joly, S.; Vargas, K.; Swails-Wenger, J.; Enger, L.; Soll, D. R. Natural defenses against Candida colonization breakdown in the oral cavities of the elderly. J. Dent. Res., 1999, 78, 857-68.
    • (1999) J. Dent. Res , vol.78 , pp. 857-868
    • Lockhart, S.R.1    Joly, S.2    Vargas, K.3    Swails-Wenger, J.4    Enger, L.5    Soll, D.R.6
  • 11
    • 0025314139 scopus 로고
    • Oral and esophageal Candida albicans infection in hyposalivatory rats
    • Meitner, S. W.; Bowen, W. H.; Haidaris C. G. Oral and esophageal Candida albicans infection in hyposalivatory rats. Infect. Immun., 1990, 58, 2228-36.
    • (1990) Infect. Immun , vol.58 , pp. 2228-2236
    • Meitner, S.W.1    Bowen, W.H.2    Haidaris, C.G.3
  • 12
    • 0005580502 scopus 로고
    • Candidiosis of the oropharynx
    • Bailliere Tindale, London, United Kingdom
    • Odds, F. C. Candidiosis of the oropharynx, In Candida and candidosis: a review and bibliography. Bailliere Tindale, London, United Kingdom, 1988; pp. 117-23.
    • (1988) Candida and candidosis: A review and bibliography , pp. 117-123
    • Odds, F.C.1
  • 13
    • 0027204928 scopus 로고
    • Effect of sialoadenectomy on the carriage of Candida albicans in the mouths of rats
    • Jorge, A. O.; Totti, M. A.; de Almeida O. P.; Scully C. Effect of sialoadenectomy on the carriage of Candida albicans in the mouths of rats. J. Oral Pathol. Med., 1993, 22, 138-40.
    • (1993) J. Oral Pathol. Med , vol.22 , pp. 138-140
    • Jorge, A.O.1    Totti, M.A.2    de Almeida, O.P.3    Scully, C.4
  • 14
    • 0028487096 scopus 로고
    • Animal models of oral candidiasis. A review
    • Allen, C. M. Animal models of oral candidiasis. A review. Oral Surg. Oral Med. Oral Pathol., 1994, 78, 216-21.
    • (1994) Oral Surg. Oral Med. Oral Pathol , vol.78 , pp. 216-221
    • Allen, C.M.1
  • 16
    • 0023888810 scopus 로고    scopus 로고
    • Oppenheim, F. G.; T. Xu, F. M.; McMillian, S. M.; Levitz, R. D.; Diamond, G. D.; Offner, Troxler R. F. Histatins, a novel family of histidinerich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. J. Biol. Chem., 1988, 263, 7472-77.
    • Oppenheim, F. G.; T. Xu, F. M.; McMillian, S. M.; Levitz, R. D.; Diamond, G. D.; Offner, Troxler R. F. Histatins, a novel family of histidinerich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. J. Biol. Chem., 1988, 263, 7472-77.
  • 17
    • 0021263092 scopus 로고
    • Fungistatic and fungicidal activity of human parotid salivary histidinerich polypeptides on Candida albicans
    • Pollock, J. J.; Denepitiya, L.; Mackay, B. J.; Iacona, V. J. Fungistatic and fungicidal activity of human parotid salivary histidinerich polypeptides on Candida albicans. Infect. Immun., 1984, 44, 702-7.
    • (1984) Infect. Immun , vol.44 , pp. 702-707
    • Pollock, J.J.1    Denepitiya, L.2    Mackay, B.J.3    Iacona, V.J.4
  • 19
    • 0142228796 scopus 로고    scopus 로고
    • Decreased excretion of antimicrobial proteins and peptides in saliva of patients with oral candidiasis
    • Tanida, T.; Okamoto, T.; Okamoto, A.; Wang, H.; Hamada, T.; Ueta, E.; Osaki, T. J. Decreased excretion of antimicrobial proteins and peptides in saliva of patients with oral candidiasis. Oral Pathol. Med., 2003, 32, 586-94.
    • (2003) Oral Pathol. Med , vol.32 , pp. 586-594
    • Tanida, T.1    Okamoto, T.2    Okamoto, A.3    Wang, H.4    Hamada, T.5    Ueta, E.6    Osaki, T.J.7
  • 22
    • 33645111877 scopus 로고    scopus 로고
    • Natural resistance, iron and infection: A challenge for clinical medicine
    • Bullen, J. J.; Rogers, H. J.; Spalding, P. B.; Ward, C. G. Natural resistance, iron and infection: a challenge for clinical medicine. J. Med. Microbiol., 2006, 55, 251-8.
    • (2006) J. Med. Microbiol , vol.55 , pp. 251-258
    • Bullen, J.J.1    Rogers, H.J.2    Spalding, P.B.3    Ward, C.G.4
  • 23
    • 0034640466 scopus 로고    scopus 로고
    • A high-affinity iron permease essential for Candida albicans virulence
    • Ramanan, N.; Wang, T. A high-affinity iron permease essential for Candida albicans virulence. Science, 2000, 288, 1062-4.
    • (2000) Science , vol.288 , pp. 1062-1064
    • Ramanan, N.1    Wang, T.2
  • 24
    • 0020381256 scopus 로고
    • A mechanism of susceptibility to mucormycosis in diabetic ketoacidosis: Transferrin and iron availability
    • Artis, W. M.; Fountain, J. A.; Delcher, H. K.; Jones, H. E. A mechanism of susceptibility to mucormycosis in diabetic ketoacidosis: transferrin and iron availability. Diabetes, 1982, 31, 1109-14.
    • (1982) Diabetes , vol.31 , pp. 1109-1114
    • Artis, W.M.1    Fountain, J.A.2    Delcher, H.K.3    Jones, H.E.4
  • 25
    • 0018936054 scopus 로고
    • Transferrin dependent growth inhibition of yeast-phase Histoplasma capsulatum by human serum and lymph
    • Sutcliffe, M. C.; Savage, A. M.; Alford, R. H. Transferrin dependent growth inhibition of yeast-phase Histoplasma capsulatum by human serum and lymph. J. Infect. Dis., 1980, 142, 209-19.
    • (1980) J. Infect. Dis , vol.142 , pp. 209-219
    • Sutcliffe, M.C.1    Savage, A.M.2    Alford, R.H.3
  • 26
    • 33846988264 scopus 로고    scopus 로고
    • Whey-derived free fatty acids suppress the germination of Candida albicans in vitro
    • Clément, M.; Tremblay, J.; Lange, M.; Thibodeau, J.; Belhumeur, P. Whey-derived free fatty acids suppress the germination of Candida albicans in vitro. FEMS Yeast Res., 2007, 7, 276-85.
    • (2007) FEMS Yeast Res , vol.7 , pp. 276-285
    • Clément, M.1    Tremblay, J.2    Lange, M.3    Thibodeau, J.4    Belhumeur, P.5
  • 27
    • 0034253475 scopus 로고    scopus 로고
    • Lactoferrin is responsible for the fungistatic effect of human milk
    • Andersson, Y.; Lindquist, S.; Lagerqvist, C.; Hernell, O. Lactoferrin is responsible for the fungistatic effect of human milk. Early Hum. Dev., 2000, 59, 95-105
    • (2000) Early Hum. Dev , vol.59 , pp. 95-105
    • Andersson, Y.1    Lindquist, S.2    Lagerqvist, C.3    Hernell, O.4
  • 28
    • 0015225776 scopus 로고
    • Lactoferrin in milk from different species
    • Masson, P.L.; Heremans, J.F. Lactoferrin in milk from different species. Comp. Biochem. Physiol., 1971, 39B, 119-29.
    • (1971) Comp. Biochem. Physiol , vol.39 B , pp. 119-129
    • Masson, P.L.1    Heremans, J.F.2
  • 29
    • 0019553882 scopus 로고
    • Developmental changes in the composition of beagle dog milk
    • Lonnerdal, B.; Keen, C.L.; Hurley, L.S.; Fisher, G.L. Developmental changes in the composition of beagle dog milk. Am. J. Vet. Res., 1981, 42, 662-6.
    • (1981) Am. J. Vet. Res , vol.42 , pp. 662-666
    • Lonnerdal, B.1    Keen, C.L.2    Hurley, L.S.3    Fisher, G.L.4
  • 30
    • 0016800028 scopus 로고
    • Transferrin, iron and dermatophytes. 1. Serum dermatophyte inhibitory component definitively identified as unsaturated transferrin
    • King, R. D.; Kahn, H. A.; Foye, J. C.; Greenberg, J. H.; Jones, H. E. Transferrin, iron and dermatophytes. 1. Serum dermatophyte inhibitory component definitively identified as unsaturated transferrin. J. Lab. Clin. Med., 1975, 86, 204-12.
    • (1975) J. Lab. Clin. Med , vol.86 , pp. 204-212
    • King, R.D.1    Kahn, H.A.2    Foye, J.C.3    Greenberg, J.H.4    Jones, H.E.5
  • 32
    • 1342344975 scopus 로고    scopus 로고
    • Survival of Aspergillus fumigatus in serum involves removal of iron from transferrin: The role of siderophores
    • Hissen, A.H.T.; Chow, J. M. T.; Pinto, L. J.; Moore M. M. Survival of Aspergillus fumigatus in serum involves removal of iron from transferrin: the role of siderophores. Infect. Immun., 2004, 72, 1402-8.
    • (2004) Infect. Immun , vol.72 , pp. 1402-1408
    • Hissen, A.H.T.1    Chow, J.M.T.2    Pinto, L.J.3    Moore, M.M.4
  • 33
    • 0022574292 scopus 로고
    • Interaction between lactoferrin and ovotransferrin and Candida cells
    • Valenti, P.; Visca, P.; Antonini, G.; Orsi, N. Interaction between lactoferrin and ovotransferrin and Candida cells. FEMS Microbiol. Lett., 1986, 33, 271-5.
    • (1986) FEMS Microbiol. Lett , vol.33 , pp. 271-275
    • Valenti, P.1    Visca, P.2    Antonini, G.3    Orsi, N.4
  • 34
    • 0016658221 scopus 로고
    • Inhibition of Escherichia coli by bovine colostrum and post-colostral milk. II. The bacteriostatic effect of lactoferrin on a serum susceptible and serum resistant strain of E. coli
    • Reiter, B.; Brock, J.H.; Steel E.D. Inhibition of Escherichia coli by bovine colostrum and post-colostral milk. II. The bacteriostatic effect of lactoferrin on a serum susceptible and serum resistant strain of E. coli. Immunology, 1975, 28, 83-95.
    • (1975) Immunology , vol.28 , pp. 83-95
    • Reiter, B.1    Brock, J.H.2    Steel, E.D.3
  • 36
    • 18344408431 scopus 로고    scopus 로고
    • Modulation of In vitro fungicidal activity of human lactoferrin against Candida albicans by extracellular cation concentration and target cell metabolic activity
    • Viejo-Díaz, M.; Andrès, M. T. S.; Fierro J. F. Modulation of In vitro fungicidal activity of human lactoferrin against Candida albicans by extracellular cation concentration and target cell metabolic activity. Antimicrob. Agents Chemother., 2004, 48, 1242-8.
    • (2004) Antimicrob. Agents Chemother , vol.48 , pp. 1242-1248
    • Viejo-Díaz, M.1    Andrès, M.T.S.2    Fierro, J.F.3
  • 38
    • 0027232811 scopus 로고    scopus 로고
    • Bellamy, W; Wakabayashi, H.; Takase, M.; Kawase, K.; Shimamura, S.; Tomita, M. Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin. Med. Microbiol. Immunol., 1993, 182, 97-105.
    • Bellamy, W; Wakabayashi, H.; Takase, M.; Kawase, K.; Shimamura, S.; Tomita, M. Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin. Med. Microbiol. Immunol., 1993, 182, 97-105.
  • 41
    • 0035083899 scopus 로고    scopus 로고
    • A novel bovine lactoferrin peptide, FKCRRWQWRM, suppresses Candida cell growth and activates neutrophils
    • Ueta, E.; Tanida, T.; Osaki, T. A novel bovine lactoferrin peptide, FKCRRWQWRM, suppresses Candida cell growth and activates neutrophils. J. Pept. Res., 2001, 57, 240-9.
    • (2001) J. Pept. Res , vol.57 , pp. 240-249
    • Ueta, E.1    Tanida, T.2    Osaki, T.3
  • 42
    • 0031807119 scopus 로고    scopus 로고
    • Inhibition of hyphal growth of azole resistant strains of Candida albicans by triazole antifungal agents in the presence of lactoferrin-related compounds
    • Wakabayashi, H.; Abe, S.; Teraguchi, S.; Hayasawa, H.; Yamaguchi, H. Inhibition of hyphal growth of azole resistant strains of Candida albicans by triazole antifungal agents in the presence of lactoferrin-related compounds. Antimicrob. Agents Chemoteher., 1998, 42, 1587-91.
    • (1998) Antimicrob. Agents Chemoteher , vol.42 , pp. 1587-1591
    • Wakabayashi, H.1    Abe, S.2    Teraguchi, S.3    Hayasawa, H.4    Yamaguchi, H.5
  • 44
    • 0031888968 scopus 로고    scopus 로고
    • The effect of the new triazole, voriconazole (UK-109,496), on the interactions of Candida albicans and Candida krusei with endothelial cells
    • Fratti, R.A.; Belanger, P.H.; Sanati, H.; Ghannoum, M.A. The effect of the new triazole, voriconazole (UK-109,496), on the interactions of Candida albicans and Candida krusei with endothelial cells. J. Chemother., 1998, 10, 7-16.
    • (1998) J. Chemother , vol.10 , pp. 7-16
    • Fratti, R.A.1    Belanger, P.H.2    Sanati, H.3    Ghannoum, M.A.4
  • 45
    • 0028297361 scopus 로고
    • Adherence of Candida albicans germ tubes to murine tissues in an ex vivo assay
    • López-Ribot, J. L.; Vespa, M.N,; Chaffin, W.L. Adherence of Candida albicans germ tubes to murine tissues in an ex vivo assay. Can. J. Microbiol., 1994, 40, 77-81.
    • (1994) Can. J. Microbiol , vol.40 , pp. 77-81
    • López-Ribot, J.L.1    Vespa, M.N.2    Chaffin, W.L.3
  • 46
    • 0028050465 scopus 로고
    • Pathogenesis of Candida infections
    • Odds, F.C. Pathogenesis of Candida infections. J. Am. Acad. Dermatol., 1994, 31, S2-5.
    • (1994) J. Am. Acad. Dermatol , vol.31
    • Odds, F.C.1
  • 47
    • 33750795816 scopus 로고    scopus 로고
    • Activity and mode of action against fungal phytopathogens of bovine lactoferricin-derived peptides
    • Munoz, A.; Marcos, J.F. Activity and mode of action against fungal phytopathogens of bovine lactoferricin-derived peptides. J. Appl. Microbiol., 2006, 101, 1199-207.
    • (2006) J. Appl. Microbiol , vol.101 , pp. 1199-1207
    • Munoz, A.1    Marcos, J.F.2
  • 48
    • 0141918811 scopus 로고    scopus 로고
    • Lactoferrin: A multifunctional protein with antimicrobial properties
    • Farnaud, S.; Evans R. W. Lactoferrin: a multifunctional protein with antimicrobial properties. Mol. Immunol., 2003, 40, 395-405.
    • (2003) Mol. Immunol , vol.40 , pp. 395-405
    • Farnaud, S.1    Evans, R.W.2
  • 49
    • 21444435350 scopus 로고    scopus 로고
    • Different anticandida activities of two human lactoferrin-derived peptides, Lfpep and kaliocin-1
    • Viejo-Dìaz, M.; Andrès M. T. S.; Fierro. J. F. Different anticandida activities of two human lactoferrin-derived peptides, Lfpep and kaliocin-1. Antimicrob. Agents Chemother., 2005, 49, 2583-88.
    • (2005) Antimicrob. Agents Chemother , vol.49 , pp. 2583-2588
    • Viejo-Dìaz, M.1    Andrès, M.T.S.2    Fierro, J.F.3
  • 51
    • 0036090558 scopus 로고    scopus 로고
    • Internal thiols and reactive oxygen species in candidacidal activity exerted by an N-terminal peptide of human lactoferrin
    • Lupetti, A.; Paulusma-Annema, A.; Senesi, S.; Campa, M.; Van Dissel, J.T.; Nibbering, P.H. Internal thiols and reactive oxygen species in candidacidal activity exerted by an N-terminal peptide of human lactoferrin. Antimicrob. Agents. Chemother., 2002, 46, 1634-9.
    • (2002) Antimicrob. Agents. Chemother , vol.46 , pp. 1634-1639
    • Lupetti, A.1    Paulusma-Annema, A.2    Senesi, S.3    Campa, M.4    Van Dissel, J.T.5    Nibbering, P.H.6
  • 52
    • 4644292546 scopus 로고    scopus 로고
    • Release of calcium from intracellular stores and subsequent uptake by mitochondria are essential for the candidacidal activity of an N-terminal peptide of human lactoferrin
    • Lupetti, A.; Brouwer, C.P.; Dogterom-Ballering, H.E.; Senesi, S.; Campa, M.; Van Dissel, J.T.; Nibbering, P.H. Release of calcium from intracellular stores and subsequent uptake by mitochondria are essential for the candidacidal activity of an N-terminal peptide of human lactoferrin. J. Antimicrob. Chemother., 2004, 54, 603-8.
    • (2004) J. Antimicrob. Chemother , vol.54 , pp. 603-608
    • Lupetti, A.1    Brouwer, C.P.2    Dogterom-Ballering, H.E.3    Senesi, S.4    Campa, M.5    Van Dissel, J.T.6    Nibbering, P.H.7
  • 54
    • 67651131921 scopus 로고    scopus 로고
    • Haney, E. F.; Nazmi, K.; Lau F.; Bolscher, J.G.M.; Vogel H. Biochimie, 2008 Epub ahead of print (DOI: doi:10.1016/j.biochi.2008.04.013)
    • Haney, E. F.; Nazmi, K.; Lau F.; Bolscher, J.G.M.; Vogel H. Biochimie, 2008 Epub ahead of print (DOI: doi:10.1016/j.biochi.2008.04.013)
  • 55
    • 33744454723 scopus 로고    scopus 로고
    • Synthetic Porcine Lactoferricin with a 20-Residue Peptide Exhibits Antimicrobial Activity against Escherichia coli, Staphylococcus aureus, and Candida albicans
    • Chen, H.L.; Yen, C.C.; Lu, C.Y.; Yu, C.H.; Chen, C.M. Synthetic Porcine Lactoferricin with a 20-Residue Peptide Exhibits Antimicrobial Activity against Escherichia coli, Staphylococcus aureus, and Candida albicans. J. Agric. Food Chem., 2006, 54, 3277-82.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 3277-3282
    • Chen, H.L.1    Yen, C.C.2    Lu, C.Y.3    Yu, C.H.4    Chen, C.M.5
  • 56
    • 0030457861 scopus 로고    scopus 로고
    • Cooperative anti-Candida effects of lactoferrin or its peptides in combination with azole antifungal agents
    • Wakabayashi, H.; Abe, S.; Okutomi, T.; Tansho, S.; Kawase, K.; Yamaguchi, H. Cooperative anti-Candida effects of lactoferrin or its peptides in combination with azole antifungal agents. Microbiol. Immunol., 1996, 40, 821-5.
    • (1996) Microbiol. Immunol , vol.40 , pp. 821-825
    • Wakabayashi, H.1    Abe, S.2    Okutomi, T.3    Tansho, S.4    Kawase, K.5    Yamaguchi, H.6
  • 57
    • 0032707616 scopus 로고    scopus 로고
    • Synergistic fungistatic effects of lactoferrin in combination with antifungal drugs against Clinical Candida Isolates
    • Kuipers, M. E.; De Vries, H. G.; Eikelboom, M. C.; Meijer, D. K. F.; Swart, P. J. Synergistic fungistatic effects of lactoferrin in combination with antifungal drugs against Clinical Candida Isolates. Antimicrob. Agents Chemother., 1999, 43, 2635-41.
    • (1999) Antimicrob. Agents Chemother , vol.43 , pp. 2635-2641
    • Kuipers, M.E.1    De Vries, H.G.2    Eikelboom, M.C.3    Meijer, D.K.F.4    Swart, P.J.5
  • 58
    • 7244230000 scopus 로고    scopus 로고
    • Activated lactoferrin and fluconazole synergism against Candida albicans and Candida glabrata vaginal isolates
    • Naidu, A.S.; Fowler, R.S.; Martinez, C.; Chen, J.; Tulpinski, J. Activated lactoferrin and fluconazole synergism against Candida albicans and Candida glabrata vaginal isolates. J. Reprod. Med., 2004, 49, 800-7.
    • (2004) J. Reprod. Med , vol.49 , pp. 800-807
    • Naidu, A.S.1    Fowler, R.S.2    Martinez, C.3    Chen, J.4    Tulpinski, J.5
  • 59
    • 0031665031 scopus 로고    scopus 로고
    • Enhanced anti-Candida activity of neutrophils and azole antifungal agents in the presence of lactoferrin-related compounds
    • Wakabayashi, H.; Okutomi, T.; Abe, S.; Hayasawa, H.; Tomita, M.; Yamaguchi, H. Enhanced anti-Candida activity of neutrophils and azole antifungal agents in the presence of lactoferrin-related compounds. Adv. Exp. Med. Biol., 1998, 443, 229-37.
    • (1998) Adv. Exp. Med. Biol , vol.443 , pp. 229-237
    • Wakabayashi, H.1    Okutomi, T.2    Abe, S.3    Hayasawa, H.4    Tomita, M.5    Yamaguchi, H.6
  • 62
    • 0033485687 scopus 로고    scopus 로고
    • Modulation of neutrophil functions in host defense against disseminated Candida albicans infection in mice
    • Kullberg, B. J.; Netea, M. G.; Vonk, A. G.; van der Meer, J. W. Modulation of neutrophil functions in host defense against disseminated Candida albicans infection in mice. FEMS Immunol. Med. Microbiol., 1999, 26, 299-307.
    • (1999) FEMS Immunol. Med. Microbiol , vol.26 , pp. 299-307
    • Kullberg, B.J.1    Netea, M.G.2    Vonk, A.G.3    van der Meer, J.W.4
  • 63
    • 0035001420 scopus 로고    scopus 로고
    • Lactoferrin peptide increases the survival of Candida albicans-inoculated mice by upregulating neutrophil and macrophage functions, especially in combination with amphotericin B and granulocyte-macrophage colony-stimulating factor
    • Tanida, T.; Rao, F.; Hamada, T.; Ueta, E. Osaki, T. Lactoferrin peptide increases the survival of Candida albicans-inoculated mice by upregulating neutrophil and macrophage functions, especially in combination with amphotericin B and granulocyte-macrophage colony-stimulating factor. Infect. Immun., 2001, 69, 3883-90.
    • (2001) Infect. Immun , vol.69 , pp. 3883-3890
    • Tanida, T.1    Rao, F.2    Hamada, T.3    Ueta, E.4    Osaki, T.5
  • 66
    • 0036801043 scopus 로고    scopus 로고
    • Effect of lactoferrin feeding on the host antifungal response in guinea-pigs infected or immunised with Trichophyton mentagrophytes
    • Wakabayashi, H.; Takakura, N.; Yamauchi, K.; Teraguchi, S.; Uchida, K.; Yamaguchi, H.; Tamura, Y. Effect of lactoferrin feeding on the host antifungal response in guinea-pigs infected or immunised with Trichophyton mentagrophytes. J. Med. Microbiol., 2002, 51, 844-50.
    • (2002) J. Med. Microbiol , vol.51 , pp. 844-850
    • Wakabayashi, H.1    Takakura, N.2    Yamauchi, K.3    Teraguchi, S.4    Uchida, K.5    Yamaguchi, H.6    Tamura, Y.7
  • 67
    • 0037241403 scopus 로고    scopus 로고
    • Lactoferrin feeding augments peritoneal macrophage activities in mice intraperitoneally injected with inactivated Candida albicans
    • Wakabayashi, H.; Takakura, N.; Teraguchi, S.; Tamura, Y. Lactoferrin feeding augments peritoneal macrophage activities in mice intraperitoneally injected with inactivated Candida albicans. Microbiol. Immunol., 2003, 47, 37-43.
    • (2003) Microbiol. Immunol , vol.47 , pp. 37-43
    • Wakabayashi, H.1    Takakura, N.2    Teraguchi, S.3    Tamura, Y.4
  • 68
    • 33748418332 scopus 로고    scopus 로고
    • Regulation of physiological and pathological Th1 and Th2 responses by lactoferrin
    • Fischer, R.; Debbabi, H.; Dubarry, M.; Boyaka P.; Tomè, D. Regulation of physiological and pathological Th1 and Th2 responses by lactoferrin. Biochem. Cell. Biol., 2006, 84, 303-22.
    • (2006) Biochem. Cell. Biol , vol.84 , pp. 303-322
    • Fischer, R.1    Debbabi, H.2    Dubarry, M.3    Boyaka, P.4    Tomè, D.5
  • 70
    • 3342947834 scopus 로고    scopus 로고
    • Protection against infections by oral lactoferrin: Evaluation in animal models
    • Teraguchi, S.; Wakabayashi, H.; Kuwata, H.; Yamauchi, K.; Tamura, Y. Protection against infections by oral lactoferrin: Evaluation in animal models. BioMetals, 2004, 17, 231-4.
    • (2004) BioMetals , vol.17 , pp. 231-234
    • Teraguchi, S.1    Wakabayashi, H.2    Kuwata, H.3    Yamauchi, K.4    Tamura, Y.5
  • 71
    • 9144240592 scopus 로고    scopus 로고
    • Regulation of fungal infection by a combination of amphotericin b and peptide 2, a lactoferrin peptide that activates neutrophils clinical and diagnostic laboratory
    • Okamoto, T.; Tanida, T.; Wei, B.; Ueta, E.; Yamamoto, T.; Osaki T. Regulation of fungal infection by a combination of amphotericin b and peptide 2, a lactoferrin peptide that activates neutrophils clinical and diagnostic laboratory. Immunology, 2004, 11, 1111-9.
    • (2004) Immunology , vol.11 , pp. 1111-1119
    • Okamoto, T.1    Tanida, T.2    Wei, B.3    Ueta, E.4    Yamamoto, T.5    Osaki, T.6
  • 72
    • 67651127686 scopus 로고    scopus 로고
    • Yamauchi, K.; Hiruma, M.; Yamazaki, N. In: Clinical evaluation of orally administered bovine lactoferrin for treatment of tinea pedis. Shimazaki K, Tsuda H, Tomita M, Kuwata T, Perraudin J-P Eds. Lactoferrin: Structure, Function and Applications. Elsevier: Amsterdam, 2000; pp. 377-81,
    • Yamauchi, K.; Hiruma, M.; Yamazaki, N. In: Clinical evaluation of orally administered bovine lactoferrin for treatment of tinea pedis. Shimazaki K, Tsuda H, Tomita M, Kuwata T, Perraudin J-P Eds. Lactoferrin: Structure, Function and Applications. Elsevier: Amsterdam, 2000; pp. 377-81,
  • 74
    • 67651129325 scopus 로고    scopus 로고
    • Abe, S, Okutomi, T, Tansho, S, Ishibashi, H, Wakabayashi, H, Teraguchi, S, Hayasawa, H, Yamaguchi, H. Shimazaki, K, Tsuda, H, Tomita, M, Kuwata, T, Perraudin, J. P. Eds, Elsevier Science B.V, Amsterdam, The Netherlands
    • Abe, S.; Okutomi, T.; Tansho, S.; Ishibashi, H.; Wakabayashi, H.; Teraguchi, S.; Hayasawa, H.; Yamaguchi, H. Shimazaki, K.; Tsuda, H.; Tomita, M.; Kuwata, T.; Perraudin, J. P. Eds., In: Proceedings of the 4th International Conference on Lactoferrin: structure, function and applications. Elsevier Science B.V., Amsterdam, The Netherlands, 2000.
    • (2000) Proceedings of the 4th International Conference on Lactoferrin: Structure, function and applications
  • 75
    • 0033757611 scopus 로고    scopus 로고
    • Complete response of severe, refractory oral candidiasis to mouthwash containing lactoferrin and lysozyme
    • Masci, J. R. Complete response of severe, refractory oral candidiasis to mouthwash containing lactoferrin and lysozyme. AIDS, 2000, 14, 2403-4.
    • (2000) AIDS , vol.14 , pp. 2403-2404
    • Masci, J.R.1
  • 78
    • 0021257520 scopus 로고
    • Role of iron in intracellular growth of Trypanosoma cruzi
    • Loo, V.G.; Lalonde, R.G. Role of iron in intracellular growth of Trypanosoma cruzi. Infect. Immun., 1984, 45, 726-30.
    • (1984) Infect. Immun , vol.45 , pp. 726-730
    • Loo, V.G.1    Lalonde, R.G.2
  • 79
    • 0028223427 scopus 로고
    • Expression of glycosylphosphatidylinositol-anchored Trypanosoma brucei transferrin-binding protein complex in insect cells
    • Chaudhri, M.; Steverding, D.; Kittelberger, S.; Tjia, S.; Overath, P. Expression of glycosylphosphatidylinositol-anchored Trypanosoma brucei transferrin-binding protein complex in insect cells. Proc. Natl Acad. Sci. USA, 1994, 91, 6443-47.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6443-6447
    • Chaudhri, M.1    Steverding, D.2    Kittelberger, S.3    Tjia, S.4    Overath, P.5
  • 80
    • 0028362270 scopus 로고
    • Reconstitution of a surface transferring binding complex in insect form Trypanosoma brucei
    • Ligtenberg, M.J.L.; Bitter, W.; Kieft, R.; Steverding, D.; Janssen, H.; Calafat, J.; Borst, P. Reconstitution of a surface transferring binding complex in insect form Trypanosoma brucei. EMBO J., 1994, 13, 2565-73.
    • (1994) EMBO J , vol.13 , pp. 2565-2573
    • Ligtenberg, M.J.L.1    Bitter, W.2    Kieft, R.3    Steverding, D.4    Janssen, H.5    Calafat, J.6    Borst, P.7
  • 82
    • 0032576751 scopus 로고    scopus 로고
    • The role of transferrinreceptor variation in the host range of Trypanosoma brucei
    • Bitter, W.; Gerrits, H.; Kieft, R.; Borst, P. The role of transferrinreceptor variation in the host range of Trypanosoma brucei. Nature, 1998, 391, 499-502.
    • (1998) Nature , vol.391 , pp. 499-502
    • Bitter, W.1    Gerrits, H.2    Kieft, R.3    Borst, P.4
  • 83
    • 26244464871 scopus 로고    scopus 로고
    • Trypanosomes change their transferrin receptor expression to allow effective uptake of host transferring
    • Van Luenen, H.G.A.M.; Kieft, R.; Mussmann, R.; Engstler, M.; Riet, B.; Borst, P. Trypanosomes change their transferrin receptor expression to allow effective uptake of host transferring. Mol. Microbiol., 2005, 58, 151-65.
    • (2005) Mol. Microbiol , vol.58 , pp. 151-165
    • Van Luenen, H.G.A.M.1    Kieft, R.2    Mussmann, R.3    Engstler, M.4    Riet, B.5    Borst, P.6
  • 84
    • 0028861990 scopus 로고
    • Transferrin-binding protein complex is the receptor for transferrin uptake in Trypanosoma brucei
    • Steverding, D.; Stierhof, Y.D.; Fuchs, H.; Tauber, R.; Overath, P. Transferrin-binding protein complex is the receptor for transferrin uptake in Trypanosoma brucei. J. Cell Biol., 1995, 131, 1173-82.
    • (1995) J. Cell Biol , vol.131 , pp. 1173-1182
    • Steverding, D.1    Stierhof, Y.D.2    Fuchs, H.3    Tauber, R.4    Overath, P.5
  • 85
    • 0036525476 scopus 로고    scopus 로고
    • Leishmania chagasi: Uptake of iron bound to lactoferrin or transferrin requires an iron reductase
    • Wilson, M.E.; Lewis, T.S.; Miller, M.A.; McCormick, M.L.; Britigan, B.E. Leishmania chagasi: uptake of iron bound to lactoferrin or transferrin requires an iron reductase. Exp. Parasitol., 2002, 100, 196-207.
    • (2002) Exp. Parasitol , vol.100 , pp. 196-207
    • Wilson, M.E.1    Lewis, T.S.2    Miller, M.A.3    McCormick, M.L.4    Britigan, B.E.5
  • 87
    • 0030868997 scopus 로고    scopus 로고
    • Kininogenase activity by the major cysteinyl proteinase (cruzipain) from Trypanosoma cruzi
    • Del Nery, E.; Juliano, M.A.; Lima, A.A.; Scharfstein, J.; Juliano, L. Kininogenase activity by the major cysteinyl proteinase (cruzipain) from Trypanosoma cruzi. J. Biol. Chem., 1997, 272, 25713-18.
    • (1997) J. Biol. Chem , vol.272 , pp. 25713-25718
    • Del Nery, E.1    Juliano, M.A.2    Lima, A.A.3    Scharfstein, J.4    Juliano, L.5
  • 89
    • 0029045156 scopus 로고
    • The cysteine protease of Trypanosoma cruzi as a model for antiparasite drug design
    • McKerrow, J.H.; McGrath, M.E.; Engel, J.C. The cysteine protease of Trypanosoma cruzi as a model for antiparasite drug design. Parasitol. Today, 1995, 11, 279-82.
    • (1995) Parasitol. Today , vol.11 , pp. 279-282
    • McKerrow, J.H.1    McGrath, M.E.2    Engel, J.C.3
  • 90
    • 0032781317 scopus 로고    scopus 로고
    • Development of cysteine protease inhibitors as chemotherapy for parasitic diseases: Insights on safety, target validation, and mechanism of action
    • McKerrow, J.H. Development of cysteine protease inhibitors as chemotherapy for parasitic diseases: insights on safety, target validation, and mechanism of action. Int. J. Parasitol., 1999, 29, 833-37.
    • (1999) Int. J. Parasitol , vol.29 , pp. 833-837
    • McKerrow, J.H.1
  • 91
    • 0034278993 scopus 로고    scopus 로고
    • Cysteine proteinases of trypanosome parasites: Novel targets for chemotherapy
    • Caffrey, C.R.; Scory, S.; Steverding, D. Cysteine proteinases of trypanosome parasites: novel targets for chemotherapy. Curr. Drug. Targets, 2000, 1, 155-62.
    • (2000) Curr. Drug. Targets , vol.1 , pp. 155-162
    • Caffrey, C.R.1    Scory, S.2    Steverding, D.3
  • 92
    • 0036178381 scopus 로고    scopus 로고
    • Cysteine proteases of parasitic organisms
    • Sajid, M.; McKerrow, J.H. Cysteine proteases of parasitic organisms. Mol. Biochem. Parasitol., 2002, 120, 1-21.
    • (2002) Mol. Biochem. Parasitol , vol.120 , pp. 1-21
    • Sajid, M.1    McKerrow, J.H.2
  • 93
  • 95
    • 67651141031 scopus 로고    scopus 로고
    • Barrett, A.J.; Rawlings, N.D.; Woessner, J.F. In: Handbook of Proteolytic Enzymes; Academic Press: London and San Diego, 1998.
    • Barrett, A.J.; Rawlings, N.D.; Woessner, J.F. In: Handbook of Proteolytic Enzymes; Academic Press: London and San Diego, 1998.
  • 96
    • 9144235678 scopus 로고    scopus 로고
    • A cathepsin B-like protease is required for host protein degradation in Trypanosoma brucei
    • Mackey, Z.B.; O'Brien, T.C.; Greenbaum, D.C.; Blank, R.B.; McKerrow, J.H. A cathepsin B-like protease is required for host protein degradation in Trypanosoma brucei. J. Biol. Chem., 2004, 279, 48426-33.
    • (2004) J. Biol. Chem , vol.279 , pp. 48426-48433
    • Mackey, Z.B.1    O'Brien, T.C.2    Greenbaum, D.C.3    Blank, R.B.4    McKerrow, J.H.5
  • 98
    • 0024352727 scopus 로고
    • The prevalence and source of Toxoplasma infection in the environment
    • Jackson, M.H.; Hutchison, W.M. The prevalence and source of Toxoplasma infection in the environment. Adv. Parasitol., 1989, 28, 55-105.
    • (1989) Adv. Parasitol , vol.28 , pp. 55-105
    • Jackson, M.H.1    Hutchison, W.M.2
  • 99
    • 0002440986 scopus 로고
    • Kreier Ed, 2nd ed
    • Dubey, J.P. In: Parasitic protozoa; Kreier Ed., 2nd ed. 1993; Vol. 6, pp. 1-158.
    • (1993) Parasitic protozoa , vol.6 , pp. 1-158
    • Dubey, J.P.1
  • 100
    • 4243319734 scopus 로고
    • Ho-Yen, D.O, Joss, A.W.L. Eds, Oxford: Oxford University
    • Evans, R. In: Human toxoplasmosis; Ho-Yen, D.O.; Joss, A.W.L. Eds.; Oxford: Oxford University, 1992; pp. 26-55.
    • (1992) Human toxoplasmosis , pp. 26-55
    • Evans, R.1
  • 101
    • 0031958697 scopus 로고    scopus 로고
    • Structures of Toxoplasma gondii tachyzoites, bradyzoites, and sporozoites and biology and development of tissue cysts
    • Dubey, J.P.; Lindsay, D.S.; Speer, C.A. Structures of Toxoplasma gondii tachyzoites, bradyzoites, and sporozoites and biology and development of tissue cysts. Clin. Microbiol. Rev., 1998, 11, 267-99.
    • (1998) Clin. Microbiol. Rev , vol.11 , pp. 267-299
    • Dubey, J.P.1    Lindsay, D.S.2    Speer, C.A.3
  • 104
    • 18844460898 scopus 로고    scopus 로고
    • Toxoplasma gondii binds human lactoferrin but not transferrin
    • Dziadek, B.; Dzitko, K.; Dlugonska, H. Toxoplasma gondii binds human lactoferrin but not transferrin. Exp. Parasitol., 2005, 110, 165-7.
    • (2005) Exp. Parasitol , vol.110 , pp. 165-167
    • Dziadek, B.1    Dzitko, K.2    Dlugonska, H.3
  • 105
    • 34548568164 scopus 로고    scopus 로고
    • Identification of Toxoplasma gondii proteins binding human lactoferrin: A new aspect of rhoptry proteins function
    • Dziadek, B.; Dziadek, J.; Dlugonska, H. Identification of Toxoplasma gondii proteins binding human lactoferrin: a new aspect of rhoptry proteins function. Exp. Parasitol., 2007, 115, 277-82.
    • (2007) Exp. Parasitol , vol.115 , pp. 277-282
    • Dziadek, B.1    Dziadek, J.2    Dlugonska, H.3
  • 106
    • 0029684717 scopus 로고    scopus 로고
    • Growth inhibitory effects of bovine lactoferrin to Toxoplasma gondii parasites in murine somatic cells
    • Tanaka, T.; Omata, Y.; Saito, A.; Shimazaki, K.; Igarashi, I.; Suzuki, N. Growth inhibitory effects of bovine lactoferrin to Toxoplasma gondii parasites in murine somatic cells. J. Vet. Med. Sci., 1996, 58, 61-5.
    • (1996) J. Vet. Med. Sci , vol.58 , pp. 61-65
    • Tanaka, T.1    Omata, Y.2    Saito, A.3    Shimazaki, K.4    Igarashi, I.5    Suzuki, N.6
  • 107
    • 0030970179 scopus 로고    scopus 로고
    • Growth inhibitory effect of bovine lactoferrin on Toxoplasma gondii tachyzoites in murine macrophages: Role of radical oxygen and inorganic nitrogen oxide in Toxoplasma growth-inhibitory activity
    • Tanaka, T.; Omata, Y.; Narisawa, M.; Saito, A.; Shimazaki, K.; Igarashi, I.; Hirumi, H.; Suzuki, N. Growth inhibitory effect of bovine lactoferrin on Toxoplasma gondii tachyzoites in murine macrophages: role of radical oxygen and inorganic nitrogen oxide in Toxoplasma growth-inhibitory activity. Vet. Parasitol., 1997, 68, 27-33.
    • (1997) Vet. Parasitol , vol.68 , pp. 27-33
    • Tanaka, T.1    Omata, Y.2    Narisawa, M.3    Saito, A.4    Shimazaki, K.5    Igarashi, I.6    Hirumi, H.7    Suzuki, N.8
  • 108
    • 0032017952 scopus 로고    scopus 로고
    • Growth inhibitory effect of bovine lactoferrin to Toxoplasma gondii tachyzoites in murine macrophages: Tyrosine phosphorylation in murine macrophages induced by bovine lactoferrin
    • Tanaka, T.; Omata, Y.; Isamida, T.; Saito, A.; Shimazaki, K.; Yamauchi, K.; Suzuki, N. Growth inhibitory effect of bovine lactoferrin to Toxoplasma gondii tachyzoites in murine macrophages: tyrosine phosphorylation in murine macrophages induced by bovine lactoferrin. J. Vet. Med. Sci., 1998, 60, 369-71.
    • (1998) J. Vet. Med. Sci , vol.60 , pp. 369-371
    • Tanaka, T.1    Omata, Y.2    Isamida, T.3    Saito, A.4    Shimazaki, K.5    Yamauchi, K.6    Suzuki, N.7
  • 109
    • 34247586578 scopus 로고    scopus 로고
    • Toxoplasma gondii: Inhibition of the intracellular growth by human lactoferrin
    • Dzitko, K.; Dziadek, B.; Dziadek, J.; Długońska, H. Toxoplasma gondii: inhibition of the intracellular growth by human lactoferrin. Pol. J. Microbiol., 2007, 56, 25-32.
    • (2007) Pol. J. Microbiol , vol.56 , pp. 25-32
    • Dzitko, K.1    Dziadek, B.2    Dziadek, J.3    Długońska, H.4
  • 111
  • 113
    • 0023154279 scopus 로고
    • Plasmodium falciparum: Inhibition in vitro with lactoferrin, desferriferrithiocin, and desferricrocin
    • Fritsch, G.; Sawatzki, G.; Treumer, J.; Jung, A.; Spira, D.T. Plasmodium falciparum: inhibition in vitro with lactoferrin, desferriferrithiocin, and desferricrocin. Exp. Parasitol., 1987, 63, 1-9.
    • (1987) Exp. Parasitol , vol.63 , pp. 1-9
    • Fritsch, G.1    Sawatzki, G.2    Treumer, J.3    Jung, A.4    Spira, D.T.5
  • 114
    • 0029658307 scopus 로고    scopus 로고
    • Remnant lipoproteins inhibit malaria sporozoite invasion of hepatocytes
    • Sinnis, P.; Willnow, T.E.; Briones, M.R.; Herz, J.; Nussenzweig, V. Remnant lipoproteins inhibit malaria sporozoite invasion of hepatocytes. J. Exp. Med., 1996, 184, 945-54.
    • (1996) J. Exp. Med , vol.184 , pp. 945-954
    • Sinnis, P.1    Willnow, T.E.2    Briones, M.R.3    Herz, J.4    Nussenzweig, V.5
  • 115
    • 0029807992 scopus 로고    scopus 로고
    • Dual interaction of the malaria circumsporozoite protein with the low density lipoprotein receptor-related protein (LRP) and heparan sulfate proteoglycans
    • Shakibaei, M.; Frevert, U. Dual interaction of the malaria circumsporozoite protein with the low density lipoprotein receptor-related protein (LRP) and heparan sulfate proteoglycans. J. Exp. Med., 1996, 184, 1699-711.
    • (1996) J. Exp. Med , vol.184 , pp. 1699-1711
    • Shakibaei, M.1    Frevert, U.2
  • 116
    • 0032743533 scopus 로고    scopus 로고
    • A high capacity in vitro assay for measuring the cytoadherence of Plasmodium falciparum-infected erythrocytes
    • Prudhomme, J.G.; Sherman, I.W. A high capacity in vitro assay for measuring the cytoadherence of Plasmodium falciparum-infected erythrocytes. J. Immunol. Methods., 1999, 229, 169-76.
    • (1999) J. Immunol. Methods , vol.229 , pp. 169-176
    • Prudhomme, J.G.1    Sherman, I.W.2
  • 117
    • 0033168253 scopus 로고    scopus 로고
    • Inhibitory activity of human lactoferrin and its peptide on chondroitin sulfate A-, CD36-, and thrombospondin-mediated cytoadherence of plasmodium falciparum-infected erythrocytes
    • Eda, S.; Eda K.; Prudhomme, J.G.; Sherman, I.W. Inhibitory activity of human lactoferrin and its peptide on chondroitin sulfate A-, CD36-, and thrombospondin-mediated cytoadherence of plasmodium falciparum-infected erythrocytes. Blood, 1999, 94, 326-32.
    • (1999) Blood , vol.94 , pp. 326-332
    • Eda, S.1    Eda, K.2    Prudhomme, J.G.3    Sherman, I.W.4
  • 118
    • 0034055650 scopus 로고    scopus 로고
    • Inhibitory factors in breastmilk, maternal and infant sera against in vitro growth of Plasmodium falciparum malaria parasite
    • Kassim, O.O.; Ako-Anai, K.A.; Torimiro, S.E.; Hollowell, G.P.; Okoye, V.C.; Martin, S.K. Inhibitory factors in breastmilk, maternal and infant sera against in vitro growth of Plasmodium falciparum malaria parasite. J. Trop. Pediatr., 2000, 46, 2-6.
    • (2000) J. Trop. Pediatr , vol.46 , pp. 2-6
    • Kassim, O.O.1    Ako-Anai, K.A.2    Torimiro, S.E.3    Hollowell, G.P.4    Okoye, V.C.5    Martin, S.K.6
  • 119
    • 0020986293 scopus 로고
    • Killing of Giardia lamblia trophozoites by normal human milk
    • Gillin, F.D.; Reiner, D.S.; Wang, C.S. Killing of Giardia lamblia trophozoites by normal human milk. J. Cell Biochem., 1983, 23, 47-56.
    • (1983) J. Cell Biochem , vol.23 , pp. 47-56
    • Gillin, F.D.1    Reiner, D.S.2    Wang, C.S.3
  • 120
    • 0028828203 scopus 로고
    • Giardicidal activity of lactoferrin and N-terminal peptides
    • Turchany, J.M.; Aley, S.B.; Gillin, F.D. Giardicidal activity of lactoferrin and N-terminal peptides. Infect. Immun., 1995, 63, 4550-2.
    • (1995) Infect. Immun , vol.63 , pp. 4550-4552
    • Turchany, J.M.1    Aley, S.B.2    Gillin, F.D.3
  • 121
    • 0030614852 scopus 로고    scopus 로고
    • Ultrastructural effects of lactoferrin binding on Giardia lamblia trophozoites
    • Turchany, J.M.; McCaffery, J.M.; Aley, S.B.; Gillin, F.D. Ultrastructural effects of lactoferrin binding on Giardia lamblia trophozoites. J. Eukaryot. Microbiol., 1997, 44, 68-72.
    • (1997) J. Eukaryot. Microbiol , vol.44 , pp. 68-72
    • Turchany, J.M.1    McCaffery, J.M.2    Aley, S.B.3    Gillin, F.D.4
  • 122
    • 58149121478 scopus 로고    scopus 로고
    • Ochoa, T.J.; Cleary, T.G. Effect of lactoferrin on enteric pathogens. Biochimie 2008, [Epub ahead of print] (DOI: doi:10.1016/ j.biochi.2008.04.006)
    • Ochoa, T.J.; Cleary, T.G. Effect of lactoferrin on enteric pathogens. Biochimie 2008, [Epub ahead of print] (DOI: doi:10.1016/ j.biochi.2008.04.006)
  • 124
    • 0018896635 scopus 로고
    • The salutary effect of milk on amoebiasis and its reversal by iron
    • Murray, M.J.; Murray, A.; Murray, C.J. The salutary effect of milk on amoebiasis and its reversal by iron. Br. Med. J., 1980, 280, 1351-2.
    • (1980) Br. Med. J , vol.280 , pp. 1351-1352
    • Murray, M.J.1    Murray, A.2    Murray, C.J.3
  • 126
    • 33748424713 scopus 로고    scopus 로고
    • Microbicidal action of lactoferrin and lactoferricin and their synergistic effect with metronidazole in Entamoeba histolytica
    • León-Sicairos, N.; Reyes-López, M.; Ordaz-Pichardo, C.; de la Garza, M. Microbicidal action of lactoferrin and lactoferricin and their synergistic effect with metronidazole in Entamoeba histolytica. Biochem. Cell Biol., 2006, 84, 327-36.
    • (2006) Biochem. Cell Biol , vol.84 , pp. 327-336
    • León-Sicairos, N.1    Reyes-López, M.2    Ordaz-Pichardo, C.3    de la Garza, M.4
  • 127
    • 28344438950 scopus 로고    scopus 로고
    • Gifford, J. L.; Huntera H. N.; Vogel, H. J. Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties. Cell. Mol. Life Sci., 2005, 62, 2588-98.
    • Gifford, J. L.; Huntera H. N.; Vogel, H. J. Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties. Cell. Mol. Life Sci., 2005, 62, 2588-98.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.