Publications
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“Effects of VEGF/VEGFR/K-ras signaling pathways on miRNA21 levels in hepatocellular carcinoma tissues in rats”, vol. 14, pp. 671-679, 2015.
, “Effects of lovastatin on hepatic expression of the low-density lipoprotein receptor in nephrotic rats”, vol. 13, pp. 938-944, 2014.
, “A novel polymorphism of the lactoferrin gene and its association with milk composition and body traits in dairy goats”, vol. 9, pp. 2199-2206, 2010.
, Brandl N, Zemann A, Kaupe I, Marlovits S, et al. (2010). Signal transduction and metabolism in chondrocytes is modulated by lactoferrin. Osteoarthritis Cartilage 18: 117-125.
http://dx.doi.org/10.1016/j.joca.2009.08.012
PMid:19747587
Bullen JJ (1972). Iron-binding proteins in milk and resistance to Escherichia coli infection in infants. Proc. R. Soc. Med. 65: 1086.
PMid:4568537 PMCid:1644425
Cohen MS, Britigan BE, French M and Bean K (1987). Preliminary observations on lactoferrin secretion in human vaginal mucus: variation during the menstrual cycle, evidence of hormonal regulation, and implications for infection with Neisseria gonorrhoeae. Am. J. Obstet. Gynecol. 157: 1122-1125.
PMid:3120589
Cornish J (2004). Lactoferrin promotes bone growth. Biometals 17: 331-335.
http://dx.doi.org/10.1023/B:BIOM.0000027713.18694.91
PMid:15222486
Cornish J, Grey AB, Naot D and Palmano KP (2005). Lactoferrin and bone: an overview of recent progress. Aust. J. Dairy Technol. 60: 53-57.
Gutteridge JM, Paterson SK, Segal AW and Halliwell B (1981). Inhibition of lipid peroxidation by the iron-binding protein lactoferrin. Biochem. J. 199: 259-261.
PMid:7337708 PMCid:1163360
Jenssen H and Hancock RE (2009). Antimicrobial properties of lactoferrin. Biochimie 91: 19-29.
http://dx.doi.org/10.1016/j.biochi.2008.05.015
PMid:18573312
Jeremy B (1995). Lactoferrin: a multifunctional immunoregulatory protein? Immunol. Today 16: 417-419.
http://dx.doi.org/10.1016/0167-5699(95)80016-6
Kim SJ, Sohn BH, Jeong S, Pak KW, et al. (1999). High-level expression of human lactoferrin in milk of transgenic mice using genomic lactoferrin sequence. J. Biochem. 126: 320-325.
http://dx.doi.org/10.1093/oxfordjournals.jbchem.a022452
PMid:10423524
Kinsella JE and Whitehead DM (1989). Proteins in whey: chemical, physical, and functional properties. Adv. Food Nutr. Res. 33: 343-438.
http://dx.doi.org/10.1016/S1043-4526(08)60130-8
Lan XY, Pan CY, Chen H and Zhang CL (2007). An AluI PCR-RFLP detecting a silent allele at the goat POU1F1 locus and its association with production traits. Small Ruminant Res. 73: 8-12.
http://dx.doi.org/10.1016/j.smallrumres.2006.10.009
Leon-Sicairos N, Canizalez-Roman A, de la Garza M, Reyes-Lopez M, et al. (2009). Bactericidal effect of lactoferrin and lactoferrin chimera against halophilic Vibrio parahaemolyticus. Biochimie 91: 133-140.
http://dx.doi.org/10.1016/j.biochi.2008.06.009
PMid:18625283
Li GH, Zhang Y, Sun DX and Li N (2004). Study on the polymorphism of bovine lactoferrin gene and its relationship with mastitis. Anim. Biotechnol. 15: 67-76.
http://dx.doi.org/10.1081/ABIO-120037899
PMid:15248601
Liu LH, Gladwell W and Teng CT (2002). Detection of exon polymorphisms in the human lactoferrin gene. Biochem. Cell Biol. 80: 17-22.
http://dx.doi.org/10.1139/o01-207
PMid:11908638
Livney YD (2010). Milk proteins as vehicles for bioactives. Curr. Opin. Colloid Interface Sci. 15: 73-83.
http://dx.doi.org/10.1016/j.cocis.2009.11.002
Masson PL, Heremans JF and Dive CH (1966). An iron-binding protein common to many external secretions. Clin. Chim. Acta 14: 735-739.
http://dx.doi.org/10.1016/0009-8981(66)90004-0
Mohamed JA, DuPont HL, Jiang ZD, Belkind-Gerson J, et al. (2007). A novel single-nucleotide polymorphism in the lactoferrin gene is associated with susceptibility to diarrhea in North American travelers to Mexico. Clin. Infect. Dis. 44: 945-952.
http://dx.doi.org/10.1086/512199
PMid:17342646
Nei M and Roychoudhury AK (1974). Sampling variances of heterozygosity and genetic distance. Genetics 76: 379-390.
PMid:4822472 PMCid:1213072
Nei M and Li WH (1979). Mathematical model for studying genetic variation in terms of restriction endonucleases. Proc. Natl. Acad. Sci. U. S. A. 76: 5269-5273.
http://dx.doi.org/10.1073/pnas.76.10.5269
PMid:291943 PMCid:413122
Nichols BL, McKee KS, Henry JF and Putman M (1987). Human lactoferrin stimulates thymidine incorporation into DNA of rat crypt cells. Pediatr. Res. 21: 563-567.
http://dx.doi.org/10.1203/00006450-198706000-00011
PMid:3496579
Park I, Schaeffer E, Sidoli A, Baralle FE, et al. (1985). Organization of the human transferrin gene: direct evidence that it originated by gene duplication. Proc. Natl. Acad. Sci. U. S. A. 82: 3149-3153.
http://dx.doi.org/10.1073/pnas.82.10.3149
PMid:3858812 PMCid:397732
Teng CT, Pentecost BT, Marshall A, Solomon A, et al. (1987). Assignment of the lactotransferrin gene to human chromosome 3 and to mouse chromosome 9. Somat. Cell Mol. Genet. 13: 689-693.
http://dx.doi.org/10.1007/BF01534490
PMid:3478818
Teng CT, Pentecost BT, Chen YH, Newbold RR, et al. (1989). Lactotransferrin gene expression in the mouse uterus and mammary gland. Endocrinology 124: 992-999.
http://dx.doi.org/10.1210/endo-124-2-992
PMid:2463910
Williams J (1982). The evolution of transferrin. Trends Biochem. Sci. 7: 394-397.
http://dx.doi.org/10.1016/0968-0004(82)90183-9
Yamauchi K, Tomita M, Giehl TJ and Ellison RT III (1993). Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun. 61: 719-728.
PMid:8423097 PMCid:302785
Yamauchi K, Wakabayashi H, Shin K and Takase M (2006). Bovine lactoferrin: benefits and mechanism of action against infections. Biochem. Cell Biol. 84: 291-296.
http://dx.doi.org/10.1139/o06-054
PMid:16936799