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Volumn 90, Issue 3, 2012, Pages 233-244

Lactoferrin, a bird's eye view

Author keywords

Anticancer; Antimicrobial; Endotoxin; Immuno modulator; Iron binding protein; Transcription factor

Indexed keywords

ANTICANCER; ANTIMICROBIAL; ENDOTOXIN; IMMUNO-MODULATOR; IRON-BINDING PROTEIN;

EID: 84861361791     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/o2012-016     Document Type: Article
Times cited : (216)

References (122)
  • 1
    • 84859387081 scopus 로고    scopus 로고
    • Neutrophil function: From mechanisms to disease
    • 10.1146/annurev-immunol-020711-074942 22224774
    • Amulic B. Cazalet C. Hayes G.L. Metzler K.D. Zychlinsky A. 2012. Neutrophil function: from mechanisms to disease. Annu. Rev. Immunol. 30 (1): 459-489. 10.1146/annurev-immunol-020711-074942 22224774
    • (2012) Annu. Rev. Immunol. , vol.30 , Issue.1 , pp. 459-489
    • Amulic, B.1    Cazalet, C.2    Hayes, G.L.3    Metzler, K.D.4    Zychlinsky, A.5
  • 3
    • 12744263109 scopus 로고    scopus 로고
    • Enhancement of endotoxin neutralization by coupling of a C12-alkyl chain to a lactoferricin-derived peptide
    • 10.1042/BJ20041270 15344905
    • Andrä J. Lohner K. Blondelle S.E. Jerala R. Moriyon I. Koch M.H.J. et al. 2005. Enhancement of endotoxin neutralization by coupling of a C12-alkyl chain to a lactoferricin-derived peptide. Biochem. J. 385 (1): 135 - 143. 10.1042/BJ20041270 15344905
    • (2005) Biochem. J. , vol.385 , Issue.1 , pp. 135-143
    • Andr, J.1    Lohner, K.2    Blondelle, S.E.3    Jerala, R.4    Moriyon, I.5    Koch, M.H.J.6
  • 5
    • 0017389761 scopus 로고
    • A bactericidal effect for human lactoferrin
    • 10.1126/science.327545 327545
    • Arnold R.R. Cole M.F. McGhee J.R. 1977. A bactericidal effect for human lactoferrin. Science, 197 (4300): 263-265. 10.1126/science.327545 327545
    • (1977) Science , vol.197 , Issue.4300 , pp. 263-265
    • Arnold, R.R.1    Cole, M.F.2    McGhee, J.R.3
  • 6
    • 34248587437 scopus 로고    scopus 로고
    • The effects of lactoferrin on myelopoiesis: Can we resolve the controversy?
    • 17410054
    • Artym J. Zimecki M. 2007. The effects of lactoferrin on myelopoiesis: can we resolve the controversy? Postepy Hig. Med. Dosw. (Online), 61: 129-150. 17410054
    • (2007) Postepy Hig. Med. Dosw. (Online) , vol.61 , pp. 129-150
    • Artym, J.1    Zimecki, M.2
  • 7
    • 79955991518 scopus 로고    scopus 로고
    • Bovine lactoferrin structures promoting corneal epithelial wound healing in vitro
    • 10.1167/iovs.10-6352 21282581
    • Ashby B. Garrett Q. Willcox M. 2011. Bovine lactoferrin structures promoting corneal epithelial wound healing in vitro. Invest. Ophthalmol. Vis. Sci. 52 (5): 2719-2726. 10.1167/iovs.10-6352 21282581
    • (2011) Invest. Ophthalmol. Vis. Sci. , vol.52 , Issue.5 , pp. 2719-2726
    • Ashby, B.1    Garrett, Q.2    Willcox, M.3
  • 8
    • 0023793522 scopus 로고
    • Molecular structure of serum transferrin at 3.3-A resolution
    • 10.1021/bi00415a061 3179277
    • Bailey S. Evans R.W. Garratt R.C. Gorinsky B. Hasnain S. Horsburgh C. et al. 1988. Molecular structure of serum transferrin at 3.3-A resolution. Biochemistry, 27 (15): 5804-5812. 10.1021/bi00415a061 3179277
    • (1988) Biochemistry , vol.27 , Issue.15 , pp. 5804-5812
    • Bailey, S.1    Evans, R.W.2    Garratt, R.C.3    Gorinsky, B.4    Hasnain, S.5    Horsburgh, C.6
  • 9
    • 3342963515 scopus 로고    scopus 로고
    • Lactoferrin and iron: Structural and dynamic aspects of binding and release
    • 10.1023/B:BIOM.0000027694.40260.70 15222467
    • Baker H.M. Baker E.N. 2004. Lactoferrin and iron: structural and dynamic aspects of binding and release. Biometals, 17 (3): 209-216. 10.1023/B:BIOM. 0000027694.40260.70 15222467
    • (2004) Biometals , vol.17 , Issue.3 , pp. 209-216
    • Baker, H.M.1    Baker, E.N.2
  • 10
    • 84861356856 scopus 로고    scopus 로고
    • A structural perspective on lactoferrin function
    • This issue. 10.1139/o11-071 22292559
    • Baker H.M. Baker E.N. 2012. A structural perspective on lactoferrin function. Biochem. Cell Biol.,. This issue. 10.1139/o11-071 22292559
    • (2012) Biochem. Cell Biol.
    • Baker, H.M.1    Baker, E.N.2
  • 11
    • 77953253806 scopus 로고    scopus 로고
    • The lactoferrin receptor complex in Gram negative bacteria
    • 10.1007/s10534-010-9299-z 20155302
    • Beddek A.J. Schryvers A.B. 2010. The lactoferrin receptor complex in Gram negative bacteria. Biometals, 23 (3): 377-386. 10.1007/s10534-010-9299-z 20155302
    • (2010) Biometals , vol.23 , Issue.3 , pp. 377-386
    • Beddek, A.J.1    Schryvers, A.B.2
  • 12
    • 0026716132 scopus 로고
    • Identification of the bactericidal domain of lactoferrin
    • 10.1016/0167-4838(92)90346-F 1599934
    • Bellamy W. Takase M. Yamauchi K. Wakabayashi H. Kawase K. Tomita M. 1992. Identification of the bactericidal domain of lactoferrin. Biochim. Biophys. Acta, 1121 (1-2): 130-136. 10.1016/0167-4838(92)90346-F 1599934
    • (1992) Biochim. Biophys. Acta , vol.1121 , Issue.12 , pp. 130-136
    • Bellamy, W.1    Takase, M.2    Yamauchi, K.3    Wakabayashi, H.4    Kawase, K.5    Tomita, M.6
  • 13
    • 78649905095 scopus 로고    scopus 로고
    • The status of diagnostic markers for inflammatory bowel disease
    • 10.1007/s11894-010-0145-9 20890737
    • Beniwal P. Harrell L. 2010. The status of diagnostic markers for inflammatory bowel disease. Curr. Gastroenterol. Rep. 12 (6): 479-484. 10.1007/s11894-010-0145-9 20890737
    • (2010) Curr. Gastroenterol. Rep. , vol.12 , Issue.6 , pp. 479-484
    • Beniwal, P.1    Harrell, L.2
  • 14
    • 3342878515 scopus 로고    scopus 로고
    • The antiviral activity of the milk protein lactoferrin against the human immunodeficiency virus type 1
    • 10.1023/B:BIOM.0000027707.82911.be 15222480
    • Berkhout B. Floris R. Recio I. Visser S. 2004. The antiviral activity of the milk protein lactoferrin against the human immunodeficiency virus type 1. Biometals, 17 (3): 291-294. 10.1023/B:BIOM.0000027707.82911.be 15222480
    • (2004) Biometals , vol.17 , Issue.3 , pp. 291-294
    • Berkhout, B.1    Floris, R.2    Recio, I.3    Visser, S.4
  • 15
    • 80052256989 scopus 로고    scopus 로고
    • Antiviral properties of lactoferrin- A natural immunity molecule
    • 10.3390/molecules16086992 21847071
    • Berlutti F. Pantanella F. Natalizi T. Frioni A. Paesano R. Polimeni A. Valenti P. 2011. Antiviral properties of lactoferrin- A natural immunity molecule. Molecules, 16 (8): 6992-7018. 10.3390/molecules16086992 21847071
    • (2011) Molecules , vol.16 , Issue.8 , pp. 6992-7018
    • Berlutti, F.1    Pantanella, F.2    Natalizi, T.3    Frioni, A.4    Paesano, R.5    Polimeni, A.6    Valenti, P.7
  • 16
    • 0036449471 scopus 로고    scopus 로고
    • LPS in microbial pathogenesis: Promise and fulfilment
    • 12537691
    • Beutler B. 2002. LPS in microbial pathogenesis: promise and fulfilment. J. Endotoxin Res. 8 (5): 329-335. 12537691
    • (2002) J. Endotoxin Res. , vol.8 , Issue.5 , pp. 329-335
    • Beutler, B.1
  • 17
    • 51149097174 scopus 로고    scopus 로고
    • The forward genetic dissection of afferent innate immunity
    • 10.1007/978-3-540-75203-5-1 18727485
    • Beutler B. Moresco E.M. 2008. The forward genetic dissection of afferent innate immunity. Curr. Top. Microbiol. Immunol. 321: 3-26. 10.1007/978-3-540- 75203-5-1 18727485
    • (2008) Curr. Top. Microbiol. Immunol. , vol.321 , pp. 3-26
    • Beutler, B.1    Moresco, E.M.2
  • 18
    • 68949212053 scopus 로고    scopus 로고
    • Milk ribonuclease-enriched lactoferrin induces positive effects on bone turnover markers in postmenopausal women
    • 10.1007/s00198-009-0839-8 19172341
    • Bharadwaj S. Naidu A.G. Betageri G.V. Prasadarao N.V. Naidu A.S. 2009. Milk ribonuclease-enriched lactoferrin induces positive effects on bone turnover markers in postmenopausal women. Osteoporos. Int. 20 (9): 1603-1611. 10.1007/s00198-009-0839-8 19172341
    • (2009) Osteoporos. Int. , vol.20 , Issue.9 , pp. 1603-1611
    • Bharadwaj, S.1    Naidu, A.G.2    Betageri, G.V.3    Prasadarao, N.V.4    Naidu, A.S.5
  • 19
    • 78651272183 scopus 로고    scopus 로고
    • Inflammatory responses improve with milk ribonuclease-enriched lactoferrin supplementation in postmenopausal women
    • 10.1007/s00011-010-0211-7 20473630
    • Bharadwaj S. Naidu T.A. Betageri G.V. Prasadarao N.V. Naidu A.S. 2010. Inflammatory responses improve with milk ribonuclease-enriched lactoferrin supplementation in postmenopausal women. Inflamm. Res. 59 (11): 971-978. 10.1007/s00011-010-0211-7 20473630
    • (2010) Inflamm. Res. , vol.59 , Issue.11 , pp. 971-978
    • Bharadwaj, S.1    Naidu, T.A.2    Betageri, G.V.3    Prasadarao, N.V.4    Naidu, A.S.5
  • 20
    • 66849091817 scopus 로고    scopus 로고
    • Oral bovine lactoferrin improves bone status of ovariectomized mice
    • 10.1152/ajpendo.90938.2008 19336659
    • Blais A. Malet A. Mikogami T. Martin-Rouas C. Tome D. 2009. Oral bovine lactoferrin improves bone status of ovariectomized mice. Am. J. Physiol. Endocrinol. Metab. 296 (6): E1281-E1288. 10.1152/ajpendo.90938.2008 19336659
    • (2009) Am. J. Physiol. Endocrinol. Metab. , vol.296 , Issue.6
    • Blais, A.1    Malet, A.2    Mikogami, T.3    Martin-Rouas, C.4    Tome, D.5
  • 21
    • 84861371938 scopus 로고    scopus 로고
    • Chimerization of lactoferricin and lactoferrampin peptides strongly potentiates the killing activity against Candida albicans
    • This issue. 10.1139/o11-085 22364313
    • Bolscher J. Nazmi K. van Marle J. van 't Hof W. Veerman E. 2012. Chimerization of lactoferricin and lactoferrampin peptides strongly potentiates the killing activity against Candida albicans. Biochem. Cell Biol. This issue. 10.1139/o11-085 22364313
    • (2012) Biochem. Cell Biol.
    • Bolscher, J.1    Nazmi, K.2    Van Marle, J.3    Van 'T Hof, W.4    Veerman, E.5
  • 22
    • 34447561633 scopus 로고    scopus 로고
    • Neutrophil granules: A library of innate immunity proteins
    • 10.1016/j.it.2007.06.002 17627888
    • Borregaard N. Sorensen O.E. Theilgaard-Monch K. 2007. Neutrophil granules: a library of innate immunity proteins. Trends Immunol. 28 (8): 340-345. 10.1016/j.it.2007.06.002 17627888
    • (2007) Trends Immunol. , vol.28 , Issue.8 , pp. 340-345
    • Borregaard, N.1    Sorensen, O.E.2    Theilgaard-Monch, K.3
  • 23
    • 34447525439 scopus 로고    scopus 로고
    • Beneficial suicide: Why neutrophils die to make NETs
    • 10.1038/nrmicro1710 17632569
    • Brinkmann V. Zychlinsky A. 2007. Beneficial suicide: why neutrophils die to make NETs. Nat. Rev. Microbiol. 5 (8): 577-582. 10.1038/nrmicro1710 17632569
    • (2007) Nat. Rev. Microbiol. , vol.5 , Issue.8 , pp. 577-582
    • Brinkmann, V.1    Zychlinsky, A.2
  • 24
    • 80052724738 scopus 로고    scopus 로고
    • Discovery and development of a synthetic peptide derived from lactoferrin for clinical use
    • 10.1016/j.peptides.2011.07.017 21827807
    • Brouwer C.P. Rahman M. Welling M.M. 2011. Discovery and development of a synthetic peptide derived from lactoferrin for clinical use. Peptides, 32 (9): 1953-1963. 10.1016/j.peptides.2011.07.017 21827807
    • (2011) Peptides , vol.32 , Issue.9 , pp. 1953-1963
    • Brouwer, C.P.1    Rahman, M.2    Welling, M.M.3
  • 25
    • 0033018848 scopus 로고    scopus 로고
    • Increased levels of lactoferrin in synovial fluid but not in serum from patients with rheumatoid arthritis
    • 10.1007/s005990050059 10356661
    • Caccavo D. Sebastiani G.D. Di Monaco C. Guido F. Galeazzi M. Ferri G.M. et al. 1999. Increased levels of lactoferrin in synovial fluid but not in serum from patients with rheumatoid arthritis. Int. J. Clin. Lab. Res. 29 (1): 30-35. 10.1007/s005990050059 10356661
    • (1999) Int. J. Clin. Lab. Res. , vol.29 , Issue.1 , pp. 30-35
    • Caccavo, D.1    Sebastiani, G.D.2    Di Monaco, C.3    Guido, F.4    Galeazzi, M.5    Ferri, G.M.6
  • 26
    • 84857999363 scopus 로고    scopus 로고
    • The structural basis of transferrin sequestration by transferrin-binding protein B
    • 10.1038/nsmb.2251 22343719
    • Calmettes C. Alcantara J. Yu R.H. Schryvers A.B. Moraes T.F. 2012. The structural basis of transferrin sequestration by transferrin-binding protein B. Nat. Struct. Mol. Biol. 19 (3): 358-360. 10.1038/nsmb.2251 22343719
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , Issue.3 , pp. 358-360
    • Calmettes, C.1    Alcantara, J.2    Yu, R.H.3    Schryvers, A.B.4    Moraes, T.F.5
  • 27
    • 1342264310 scopus 로고    scopus 로고
    • Structure of the human transferrin receptor-transferrin complex
    • 10.1016/S0092-8674(04)00130-8 14980223
    • Cheng Y. Zak O. Aisen P. Harrison S.C. Walz T. 2004. Structure of the human transferrin receptor-transferrin complex. Cell, 116 (4): 565-576. 10.1016/S0092-8674(04)00130-8 14980223
    • (2004) Cell , vol.116 , Issue.4 , pp. 565-576
    • Cheng, Y.1    Zak, O.2    Aisen, P.3    Harrison, S.C.4    Walz, T.5
  • 28
    • 78651370006 scopus 로고    scopus 로고
    • Siderophore uptake in bacteria and the battle for iron with the host; A bird's eye view
    • 10.1007/s10534-010-9361-x 20596754
    • Chu B.C. Garcia-Herrero A. Johanson T.H. Krewulak K.D. Lau C.K. Peacock R.S. et al. 2010. Siderophore uptake in bacteria and the battle for iron with the host; a bird's eye view. Biometals, 23 (4): 601-611. 10.1007/s10534-010- 9361-x 20596754
    • (2010) Biometals , vol.23 , Issue.4 , pp. 601-611
    • Chu, B.C.1    Garcia-Herrero, A.2    Johanson, T.H.3    Krewulak, K.D.4    Lau, C.K.5    Peacock, R.S.6
  • 29
    • 34147188469 scopus 로고    scopus 로고
    • Platelet TLR4 activates neutrophil extracellular traps to ensnare bacteria in septic blood
    • 10.1038/nm1565 17384648
    • Clark S.R. Ma A.C. Tavener S.A. McDonald B. Goodarzi Z. Kelly M.M. et al. 2007. Platelet TLR4 activates neutrophil extracellular traps to ensnare bacteria in septic blood. Nat. Med. 13 (4): 463-469. 10.1038/nm1565 17384648
    • (2007) Nat. Med. , vol.13 , Issue.4 , pp. 463-469
    • Clark, S.R.1    Ma, A.C.2    Tavener, S.A.3    McDonald, B.4    Goodarzi, Z.5    Kelly, M.M.6
  • 30
    • 4344694236 scopus 로고    scopus 로고
    • Lactoferrin is a potent regulator of bone cell activity and increases bone formation in vivo
    • 10.1210/en.2003-1307 15166119
    • Cornish J. Callon K.E. Naot D. Palmano K.P. Banovic T. Bava U. et al. 2004. Lactoferrin is a potent regulator of bone cell activity and increases bone formation in vivo. Endocrinology, 145 (9): 4366-4374. 10.1210/en.2003-1307 15166119
    • (2004) Endocrinology , vol.145 , Issue.9 , pp. 4366-4374
    • Cornish, J.1    Callon, K.E.2    Naot, D.3    Palmano, K.P.4    Banovic, T.5    Bava, U.6
  • 32
    • 84856913526 scopus 로고    scopus 로고
    • Mucosal healing in inflammatory bowel disease- A true paradigm of success?
    • 22347830
    • Dave M. Loftus E.V. Jr. 2012. Mucosal healing in inflammatory bowel disease- A true paradigm of success? Gastroenterol. Hepatol. (N.Y.), 8 (1): 29-38. 22347830
    • (2012) Gastroenterol. Hepatol. (N.Y.) , vol.8 , Issue.1 , pp. 29-38
    • Dave, M.1    Loftus Jr., E.V.2
  • 33
    • 0023905150 scopus 로고
    • Specific binding of lactoferrin to brush-border membrane: Ontogeny and effect of glycan chain
    • 2833117
    • Davidson L.A. Lonnerdal B. 1988. Specific binding of lactoferrin to brush-border membrane: ontogeny and effect of glycan chain. Am. J. Physiol. 254 (4): G580-G585. 2833117
    • (1988) Am. J. Physiol. , vol.254 , Issue.4
    • Davidson, L.A.1    Lonnerdal, B.2
  • 34
    • 45549085804 scopus 로고    scopus 로고
    • Lactoferrin acts as an alarmin to promote the recruitment and activation of APCs and antigen-specific immune responses
    • 18453607
    • de la Rosa G. Yang D. Tewary P. Varadhachary A. Oppenheim J.J. 2008. Lactoferrin acts as an alarmin to promote the recruitment and activation of APCs and antigen-specific immune responses. J. Immunol. 180 (10): 6868-6876. 18453607
    • (2008) J. Immunol. , vol.180 , Issue.10 , pp. 6868-6876
    • De La Rosa, G.1    Yang, D.2    Tewary, P.3    Varadhachary, A.4    Oppenheim, J.J.5
  • 35
    • 23944483437 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Tools for intracellular delivery of therapeutics
    • 10.1007/s00018-005-5109-0 15968462
    • Deshayes S. Morris M.C. Divita G. Heitz F. 2005. Cell-penetrating peptides: tools for intracellular delivery of therapeutics. Cell. Mol. Life Sci. 62 (16): 1839-1849. 10.1007/s00018-005-5109-0 15968462
    • (2005) Cell. Mol. Life Sci. , vol.62 , Issue.16 , pp. 1839-1849
    • Deshayes, S.1    Morris, M.C.2    Divita, G.3    Heitz, F.4
  • 36
    • 79958111407 scopus 로고    scopus 로고
    • A randomized, double-blind, placebo-controlled, phase II study of oral talactoferrin in combination with carboplatin and paclitaxel in previously untreated locally advanced or metastatic non-small cell lung cancer
    • 10.1097/JTO.0b013e3182156250 21532506
    • Digumarti R. Wang Y. Raman G. Doval D.C. Advani S.H. Julka P.K. et al. 2011. A randomized, double-blind, placebo-controlled, phase II study of oral talactoferrin in combination with carboplatin and paclitaxel in previously untreated locally advanced or metastatic non-small cell lung cancer. J. Thorac. Oncol. 6 (6): 1098-1103. 10.1097/JTO.0b013e3182156250 21532506
    • (2011) J. Thorac. Oncol. , vol.6 , Issue.6 , pp. 1098-1103
    • Digumarti, R.1    Wang, Y.2    Raman, G.3    Doval, D.C.4    Advani, S.H.5    Julka, P.K.6
  • 37
    • 9644287934 scopus 로고    scopus 로고
    • The synthetic N-terminal peptide of human lactoferrin, hLF(1-11), is highly effective against experimental infection caused by multidrug-resistant Acinetobacter baumannii
    • 10.1128/AAC.48.12.4919-4921.2004 15561882
    • Dijkshoorn L. Brouwer C.P. Bogaards S.J. Nemec A. van den Broek P.J. Nibbering P.H. 2004. The synthetic N-terminal peptide of human lactoferrin, hLF(1-11), is highly effective against experimental infection caused by multidrug-resistant Acinetobacter baumannii. Antimicrob. Agents Chemother. 48 (12): 4919-4921. 10.1128/AAC.48.12.4919-4921.2004 15561882
    • (2004) Antimicrob. Agents Chemother. , vol.48 , Issue.12 , pp. 4919-4921
    • Dijkshoorn, L.1    Brouwer, C.P.2    Bogaards, S.J.3    Nemec, A.4    Van Den Broek, P.J.5    Nibbering, P.H.6
  • 38
    • 73649137166 scopus 로고    scopus 로고
    • A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency
    • 10.1074/jbc.M109.036426 19858187
    • Duchardt F. Ruttekolk I.R. Verdurmen W.P. Lortat-Jacob H. Burck J. Hufnagel H. et al. 2009. A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency. J. Biol. Chem. 284 (52): 36099-36108. 10.1074/jbc.M109.036426 19858187
    • (2009) J. Biol. Chem. , vol.284 , Issue.52 , pp. 36099-36108
    • Duchardt, F.1    Ruttekolk, I.R.2    Verdurmen, W.P.3    Lortat-Jacob, H.4    Burck, J.5    Hufnagel, H.6
  • 39
    • 0035915493 scopus 로고    scopus 로고
    • The binding of lactoferrin to glycosaminoglycans on enterocyte-like HT29-18-C1 cells is mediated through basic residues located in the N-terminus
    • 10.1016/S0304-4165(01)00222-7 11786226
    • El Yazidi-Belkoura I. Legrand D. Nuijens J. Slomianny M.C. van Berkel P. Spik G. 2001. The binding of lactoferrin to glycosaminoglycans on enterocyte-like HT29-18-C1 cells is mediated through basic residues located in the N-terminus. Biochim. Biophys. Acta, 1568 (3): 197-204. 10.1016/S0304- 4165(01)00222-7 11786226
    • (2001) Biochim. Biophys. Acta , vol.1568 , Issue.3 , pp. 197-204
    • El Yazidi-Belkoura, I.1    Legrand, D.2    Nuijens, J.3    Slomianny, M.C.4    Van Berkel, P.5    Spik, G.6
  • 40
    • 0029620277 scopus 로고
    • Lactoferrin-lipopolysaccharide interaction: Involvement of the 28-34 loop region of human lactoferrin in the high-affinity binding to Escherichia coli 055B5 lipopolysaccharide
    • 8554529
    • Elass-Rochard E. Roseanu A. Legrand D. Trif M. Salmon V. Motas C. et al. 1995. Lactoferrin-lipopolysaccharide interaction: involvement of the 28-34 loop region of human lactoferrin in the high-affinity binding to Escherichia coli 055B5 lipopolysaccharide. Biochem. J. 312 (3): 839-845. 8554529
    • (1995) Biochem. J. , vol.312 , Issue.3 , pp. 839-845
    • Elass-Rochard, E.1    Roseanu, A.2    Legrand, D.3    Trif, M.4    Salmon, V.5    Motas, C.6
  • 41
    • 33745441169 scopus 로고    scopus 로고
    • The antimicrobial peptide, lactoferricin B, is cytotoxic to neuroblastoma cells in vitro and inhibits xenograft growth in vivo
    • 10.1002/ijc.21886 16572423
    • Eliassen L.T. Berge G. Leknessund A. Wikman M. Lindin I. Lokke C. et al. 2006. The antimicrobial peptide, lactoferricin B, is cytotoxic to neuroblastoma cells in vitro and inhibits xenograft growth in vivo. Int. J. Cancer, 119 (3): 493-500. 10.1002/ijc.21886 16572423
    • (2006) Int. J. Cancer , vol.119 , Issue.3 , pp. 493-500
    • Eliassen, L.T.1    Berge, G.2    Leknessund, A.3    Wikman, M.4    Lindin, I.5    Lokke, C.6
  • 42
    • 51049104078 scopus 로고    scopus 로고
    • Talactoferrin stimulates wound healing with modulation of inflammation
    • 10.1016/j.jss.2007.12.754 18619616
    • Engelmayer J. Blezinger P. Varadhachary A. 2008. Talactoferrin stimulates wound healing with modulation of inflammation. J. Surg. Res. 149 (2): 278-286. 10.1016/j.jss.2007.12.754 18619616
    • (2008) J. Surg. Res. , vol.149 , Issue.2 , pp. 278-286
    • Engelmayer, J.1    Blezinger, P.2    Varadhachary, A.3
  • 43
    • 84861355868 scopus 로고    scopus 로고
    • Hepcidin and iron homeostasis
    • press. 10.1016/j.bbamcr.2012.01.014 22306005
    • Ganz T. Nemeth E. 2012. Hepcidin and iron homeostasis. Biochim. Biophys. Acta,. In press. 10.1016/j.bbamcr.2012.01.014 22306005
    • (2012) Biochim. Biophys. Acta
    • Ganz, T.1    Nemeth, E.2
  • 44
  • 45
    • 80053105748 scopus 로고    scopus 로고
    • Lactoferrin and cancer in different cancer models
    • 10.2741/212 21622257
    • Gibbons J.A. Kanwar R.K. Kanwar J.R. 2011. Lactoferrin and cancer in different cancer models. Front. Biosci. (Schol. Ed.), 3 (1): 1080-1088. 10.2741/212 21622257
    • (2011) Front. Biosci. (Schol. Ed.) , vol.3 , Issue.1 , pp. 1080-1088
    • Gibbons, J.A.1    Kanwar, R.K.2    Kanwar, J.R.3
  • 46
    • 28344438950 scopus 로고    scopus 로고
    • Lactoferricin: A lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties
    • 10.1007/s00018-005-5373-z 16261252
    • Gifford J.L. Hunter H.N. Vogel H.J. 2005. Lactoferricin: a lactoferrin-derived peptide with antimicrobial, antiviral, antitumor and immunological properties. Cell. Mol. Life Sci. 62 (22): 2588-2598. 10.1007/s00018-005-5373-z 16261252
    • (2005) Cell. Mol. Life Sci. , vol.62 , Issue.22 , pp. 2588-2598
    • Gifford, J.L.1    Hunter, H.N.2    Vogel, H.J.3
  • 47
    • 84865554240 scopus 로고    scopus 로고
    • Elevated levels of salivary lactoferrin, a marker for chronic periodontitis?
    • press. 10.1111/j.1600-0765.2012.01479.x 22471324
    • Glimvall P. Wickström C. Jansson H. 2012. Elevated levels of salivary lactoferrin, a marker for chronic periodontitis? J. Periodontal Res. In press. 10.1111/j.1600-0765.2012.01479.x 22471324
    • (2012) J. Periodontal Res.
    • Glimvall, P.1    Wickström, C.2    Jansson, H.3
  • 48
    • 0001395327 scopus 로고
    • The isolation of a red protein from milk
    • 10.1021/ja01498a029
    • Groves M.L. 1960. The isolation of a red protein from milk. J. Am. Chem. Soc. 82 (13): 3345-3350. 10.1021/ja01498a029
    • (1960) J. Am. Chem. Soc. , vol.82 , Issue.13 , pp. 3345-3350
    • Groves, M.L.1
  • 49
    • 78649906171 scopus 로고    scopus 로고
    • Mucosal healing in inflammatory bowel disease: Where do we stand?
    • 10.1007/s11894-010-0146-8 20886319
    • Ha C. Kornbluth A. 2010. Mucosal healing in inflammatory bowel disease: where do we stand? Curr. Gastroenterol. Rep. 12 (6): 471-478. 10.1007/s11894-010-0146-8 20886319
    • (2010) Curr. Gastroenterol. Rep. , vol.12 , Issue.6 , pp. 471-478
    • Ha, C.1    Kornbluth, A.2
  • 50
    • 34948901365 scopus 로고    scopus 로고
    • Solution structures and model membrane interactions of lactoferrampin, an antimicrobial peptide derived from bovine lactoferrin
    • 10.1016/j.bbamem.2007.04.018 17560539
    • Haney E.F. Lau F. Vogel H.J. 2007. Solution structures and model membrane interactions of lactoferrampin, an antimicrobial peptide derived from bovine lactoferrin. Biochim. Biophys. Acta, 1768 (10): 2355-2364. 10.1016/j.bbamem. 2007.04.018 17560539
    • (2007) Biochim. Biophys. Acta , vol.1768 , Issue.10 , pp. 2355-2364
    • Haney, E.F.1    Lau, F.2    Vogel, H.J.3
  • 51
    • 58149105937 scopus 로고    scopus 로고
    • Novel lactoferrampin antimicrobial peptides derived from human lactoferrin
    • 10.1016/j.biochi.2008.04.013 18534196
    • Haney E.F. Nazmi K. Lau F. Bolscher J.G. Vogel H.J. 2009. Novel lactoferrampin antimicrobial peptides derived from human lactoferrin. Biochimie, 91 (1): 141-154. 10.1016/j.biochi.2008.04.013 18534196
    • (2009) Biochimie , vol.91 , Issue.1 , pp. 141-154
    • Haney, E.F.1    Nazmi, K.2    Lau, F.3    Bolscher, J.G.4    Vogel, H.J.5
  • 52
    • 84855798186 scopus 로고    scopus 로고
    • Structural and biophysical characterization of an antimicrobial peptide chimera comprised of lactoferricin and lactoferrampin
    • 10.1016/j.bbamem.2011.11.023 22155682
    • Haney E.F. Nazmi K. Bolscher J.G. Vogel H.J. 2012. Structural and biophysical characterization of an antimicrobial peptide chimera comprised of lactoferricin and lactoferrampin. Biochim. Biophys. Acta, 1818 (3): 762-775. 10.1016/j.bbamem.2011.11.023 22155682
    • (2012) Biochim. Biophys. Acta , vol.1818 , Issue.3 , pp. 762-775
    • Haney, E.F.1    Nazmi, K.2    Bolscher, J.G.3    Vogel, H.J.4
  • 53
    • 33845973364 scopus 로고    scopus 로고
    • The medicinal chemistry of short lactoferricin-based antibacterial peptides
    • 10.2174/092986707779313435 17266565
    • Haug B.E. Strom M.B. Svendsen J.S. 2007. The medicinal chemistry of short lactoferricin-based antibacterial peptides. Curr. Med. Chem. 14 (1): 1-18. 10.2174/092986707779313435 17266565
    • (2007) Curr. Med. Chem. , vol.14 , Issue.1 , pp. 1-18
    • Haug, B.E.1    Strom, M.B.2    Svendsen, J.S.3
  • 54
    • 0028910517 scopus 로고
    • Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA
    • 10.1038/373721a0 7854459
    • He J. Furmanski P. 1995. Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA. Nature, 373 (6516): 721-724. 10.1038/373721a0 7854459
    • (1995) Nature , vol.373 , Issue.6516 , pp. 721-724
    • He, J.1    Furmanski, P.2
  • 55
    • 84861416827 scopus 로고    scopus 로고
    • Transgenic milk containing recombinant human lactoferrin modulates the intestinal flora in piglets
    • This issue. 10.1139/o2012-003 22400985
    • Hu W. Zhao J. Wang J. Yu T. Wang J. Li N. 2012. Transgenic milk containing recombinant human lactoferrin modulates the intestinal flora in piglets. Biochem. Cell Biol. This issue. 10.1139/o2012-003 22400985
    • (2012) Biochem. Cell Biol.
    • Hu, W.1    Zhao, J.2    Wang, J.3    Yu, T.4    Wang, J.5    Li, N.6
  • 56
    • 23044463641 scopus 로고    scopus 로고
    • Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent
    • 10.1128/AAC.49.8.3387-3395.2005 16048952
    • Hunter H.N. Demcoe A.R. Jenssen H. Gutteberg T.J. Vogel H.J. 2005. Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent. Antimicrob. Agents Chemother. 49 (8): 3387-3395. 10.1128/AAC.49.8.3387-3395.2005 16048952
    • (2005) Antimicrob. Agents Chemother. , vol.49 , Issue.8 , pp. 3387-3395
    • Hunter, H.N.1    Demcoe, A.R.2    Jenssen, H.3    Gutteberg, T.J.4    Vogel, H.J.5
  • 57
    • 84903421873 scopus 로고    scopus 로고
    • Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin
    • 10.1021/bi972323m 9521752
    • Hwang P.M. Zhou N. Shan X. Arrowsmith C.H. Vogel H.J. 1998. Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry, 37 (12): 4288-4298. 10.1021/bi972323m 9521752
    • (1998) Biochemistry , vol.37 , Issue.12 , pp. 4288-4298
    • Hwang, P.M.1    Zhou, N.2    Shan, X.3    Arrowsmith, C.H.4    Vogel, H.J.5
  • 58
    • 29344463703 scopus 로고    scopus 로고
    • Anti herpes simplex virus activity of lactoferrin/lactoferricin-an example of antiviral activity of antimicrobial protein/peptide
    • 10.1007/s00018-005-5228-7 16261265
    • Jenssen H. 2005. Anti herpes simplex virus activity of lactoferrin/lactoferricin-an example of antiviral activity of antimicrobial protein/peptide. Cell. Mol. Life Sci. 62 (24): 3002-3013. 10.1007/s00018-005- 5228-7 16261265
    • (2005) Cell. Mol. Life Sci. , vol.62 , Issue.24 , pp. 3002-3013
    • Jenssen, H.1
  • 59
    • 84861370079 scopus 로고    scopus 로고
    • Therapeutic approaches using host defence peptides to tackle herpes virus infections
    • 10.3390/v1030939 21994576
    • Jenssen H. 2009. Therapeutic approaches using host defence peptides to tackle herpes virus infections. Viruses, 1 (3): 939-964. 10.3390/v1030939 21994576
    • (2009) Viruses , vol.1 , Issue.3 , pp. 939-964
    • Jenssen, H.1
  • 60
    • 58149113170 scopus 로고    scopus 로고
    • Antimicrobial properties of lactoferrin
    • 10.1016/j.biochi.2008.05.015 18573312
    • Jenssen H. Hancock R.E. 2009. Antimicrobial properties of lactoferrin. Biochimie, 91 (1): 19-29. 10.1016/j.biochi.2008.05.015 18573312
    • (2009) Biochimie , vol.91 , Issue.1 , pp. 19-29
    • Jenssen, H.1    Hancock, R.E.2
  • 61
    • 0001618922 scopus 로고
    • Isolation of an iron-containing red protein from human milk
    • Johansson B. 1960. Isolation of an iron-containing red protein from human milk. Acta Chem. Scand. 14 (2): 510-512.
    • (1960) Acta Chem. Scand. , vol.14 , Issue.2 , pp. 510-512
    • Johansson, B.1
  • 62
    • 0033052949 scopus 로고    scopus 로고
    • Human milk lactoferrin binds two DNA molecules with different affinities
    • 10.1016/S0014-5793(99)00579-7 10371196
    • Kanyshkova T.G. Semenov D.V. Buneva V.N. Nevinsky G.A. 1999. Human milk lactoferrin binds two DNA molecules with different affinities. FEBS Lett. 451 (3): 235-237. 10.1016/S0014-5793(99)00579-7 10371196
    • (1999) FEBS Lett. , vol.451 , Issue.3 , pp. 235-237
    • Kanyshkova, T.G.1    Semenov, D.V.2    Buneva, V.N.3    Nevinsky, G.A.4
  • 63
    • 34047262356 scopus 로고    scopus 로고
    • Why do we not all die of cancer at an early age?
    • 10.1016/S0065-230X(06)98001-4 17433906
    • Klein G. Imreh S. Zabarovsky E.R. 2007. Why do we not all die of cancer at an early age? Adv. Cancer Res. 98: 1-16. 10.1016/S0065-230X(06)98001-4 17433906
    • (2007) Adv. Cancer Res. , vol.98 , pp. 1-16
    • Klein, G.1    Imreh, S.2    Zabarovsky, E.R.3
  • 64
    • 74049157768 scopus 로고    scopus 로고
    • Effect of orally administered bovine lactoferrin on the growth of adenomatous colorectal polyps in a randomized, placebo-controlled clinical trial
    • 10.1158/1940-6207.CAPR-08-0208 19861543
    • Kozu T. Iinuma G. Ohashi Y. Saito Y. Akasu T. Saito D. et al. 2009. Effect of orally administered bovine lactoferrin on the growth of adenomatous colorectal polyps in a randomized, placebo-controlled clinical trial. Cancer Prev. Res. (Phila.), 2 (11): 975-983. 10.1158/1940-6207.CAPR-08-0208 19861543
    • (2009) Cancer Prev. Res. (Phila.) , vol.2 , Issue.11 , pp. 975-983
    • Kozu, T.1    Iinuma, G.2    Ohashi, Y.3    Saito, Y.4    Akasu, T.5    Saito, D.6
  • 65
    • 0028835226 scopus 로고
    • Crystal structure of diferric hen ovotransferrin at 2.4 A resolution
    • 10.1006/jmbi.1995.0611 7490743
    • Kurokawa H. Mikami B. Hirose M. 1995. Crystal structure of diferric hen ovotransferrin at 2.4 A resolution. J. Mol. Biol. 254 (2): 196-207. 10.1006/jmbi.1995.0611 7490743
    • (1995) J. Mol. Biol. , vol.254 , Issue.2 , pp. 196-207
    • Kurokawa, H.1    Mikami, B.2    Hirose, M.3
  • 66
    • 0032437146 scopus 로고    scopus 로고
    • Direct evidence of the generation in human stomach of an antimicrobial peptide domain (lactoferricin) from ingested lactoferrin
    • a. 10.1016/S0167-4838(98)00224-6 9920391
    • Kuwata H. Yip T.T. Tomita M. Hutchens T.W. 1998 a. Direct evidence of the generation in human stomach of an antimicrobial peptide domain (lactoferricin) from ingested lactoferrin. Biochim. Biophys. Acta, 1429 (1): 129-141. 10.1016/S0167-4838(98)00224-6 9920391
    • (1998) Biochim. Biophys. Acta , vol.1429 , Issue.1 , pp. 129-141
    • Kuwata, H.1    Yip, T.T.2    Tomita, M.3    Hutchens, T.W.4
  • 67
    • 0031716772 scopus 로고    scopus 로고
    • Direct detection and quantitative determination of bovine lactoferricin and lactoferrin fragments in human gastric contents by affinity mass spectrometry
    • b. 9781339
    • Kuwata H. Yip T.T. Yip C.L. Tomita M. Hutchens T.W. 1998 b. Direct detection and quantitative determination of bovine lactoferricin and lactoferrin fragments in human gastric contents by affinity mass spectrometry. Adv. Exp. Med. Biol. 443: 23-32. 9781339
    • (1998) Adv. Exp. Med. Biol. , vol.443 , pp. 23-32
    • Kuwata, H.1    Yip, T.T.2    Yip, C.L.3    Tomita, M.4    Hutchens, T.W.5
  • 68
    • 24344475974 scopus 로고    scopus 로고
    • Evolution of the transferrin family: Conservation of residues associated with iron and anion binding
    • 10.1016/j.cbpb.2005.07.007 16111909
    • Lambert L.A. Perri H. Halbrooks P.J. Mason A.B. 2005. Evolution of the transferrin family: conservation of residues associated with iron and anion binding. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 142 (2): 129-141. 10.1016/j.cbpb.2005.07.007 16111909
    • (2005) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.142 , Issue.2 , pp. 129-141
    • Lambert, L.A.1    Perri, H.2    Halbrooks, P.J.3    Mason, A.B.4
  • 69
    • 84858249372 scopus 로고    scopus 로고
    • Fecal lactoferrin as a noninvasive biomarker in inflammatory bowel diseases
    • 22384454
    • Langhorst J. Boone J. 2012. Fecal lactoferrin as a noninvasive biomarker in inflammatory bowel diseases. Drugs Today (Barc), 48 (2): 149-161. 22384454
    • (2012) Drugs Today (Barc) , vol.48 , Issue.2 , pp. 149-161
    • Langhorst, J.1    Boone, J.2
  • 70
    • 84861394265 scopus 로고    scopus 로고
    • LF immunomodulatory strategies: Mastering bacterial endotoxin
    • This issue. 10.1139/o11-059 22300429
    • Latorre D. Berlutti F. Valenti P. Gessani S. Puddu P. 2012. LF immunomodulatory strategies: mastering bacterial endotoxin. Biochem. Cell Biol.,. This issue. 10.1139/o11-059 22300429
    • (2012) Biochem. Cell Biol.
    • Latorre, D.1    Berlutti, F.2    Valenti, P.3    Gessani, S.4    Puddu, P.5
  • 71
    • 37749004225 scopus 로고    scopus 로고
    • Protein therapeutics: A summary and pharmacological classification
    • 10.1038/nrd2399 18097458
    • Leader B. Baca Q.J. Golan D.E. 2008. Protein therapeutics: a summary and pharmacological classification. Nat. Rev. Drug Discov. 7 (1): 21-39. 10.1038/nrd2399 18097458
    • (2008) Nat. Rev. Drug Discov. , vol.7 , Issue.1 , pp. 21-39
    • Leader, B.1    Baca, Q.J.2    Golan, D.E.3
  • 72
    • 84861414827 scopus 로고    scopus 로고
    • Lactoferrin, a key molecule in immune and inflammatory processes
    • This issue. 10.1139/o11-056 22136726
    • Legrand D. 2011. Lactoferrin, a key molecule in immune and inflammatory processes. Biochem. Cell Biol.,. This issue. 10.1139/o11-056 22136726
    • (2011) Biochem. Cell Biol.
    • Legrand, D.1
  • 73
    • 77953286718 scopus 로고    scopus 로고
    • A critical review of the roles of host lactoferrin in immunity
    • 10.1007/s10534-010-9297-1 20143251
    • Legrand D. Mazurier J. 2010. A critical review of the roles of host lactoferrin in immunity. Biometals, 23 (3): 365-376. 10.1007/s10534-010-9297-1 20143251
    • (2010) Biometals , vol.23 , Issue.3 , pp. 365-376
    • Legrand, D.1    Mazurier, J.2
  • 75
    • 7644238048 scopus 로고    scopus 로고
    • Antimicrobial proteins and peptides: Anti-infective molecules of mammalian leukocytes
    • 10.1189/jlb.0604320 15292276
    • Levy O. 2004. Antimicrobial proteins and peptides: anti-infective molecules of mammalian leukocytes. J. Leukoc. Biol. 76 (5): 909-925. 10.1189/jlb.0604320 15292276
    • (2004) J. Leukoc. Biol. , vol.76 , Issue.5 , pp. 909-925
    • Levy, O.1
  • 76
    • 82355169684 scopus 로고    scopus 로고
    • Bovine lactoferrin can be taken up by the human intestinal lactoferrin receptor and exert bioactivities
    • 21832946
    • Lönnerdal B. Jiang R. Du X. 2011. Bovine lactoferrin can be taken up by the human intestinal lactoferrin receptor and exert bioactivities. J. Pediatr. Gastroenterol. Nutr. 53 (6): 606-614. 21832946
    • (2011) J. Pediatr. Gastroenterol. Nutr. , vol.53 , Issue.6 , pp. 606-614
    • Lönnerdal, B.1    Jiang, R.2    Du, X.3
  • 77
    • 38449119463 scopus 로고    scopus 로고
    • Human lactoferrin-derived peptide's antifungal activities against disseminated Candida albicans infection
    • 10.1086/522427 17922408
    • Lupetti A. Brouwer C.P. Bogaards S.J. Welling M.M. de Heer E. Campa M. et al. 2007. Human lactoferrin-derived peptide's antifungal activities against disseminated Candida albicans infection. J. Infect. Dis. 196 (9): 1416-1424. 10.1086/522427 17922408
    • (2007) J. Infect. Dis. , vol.196 , Issue.9 , pp. 1416-1424
    • Lupetti, A.1    Brouwer, C.P.2    Bogaards, S.J.3    Welling, M.M.4    De Heer, E.5    Campa, M.6
  • 78
    • 39549099917 scopus 로고    scopus 로고
    • Platelets, neutrophils, and neutrophil extracellular traps (NETs) in sepsis
    • 10.1111/j.1538-7836.2007.02865.x 18088344
    • Ma A.C. Kubes P. 2008. Platelets, neutrophils, and neutrophil extracellular traps (NETs) in sepsis. J. Thromb. Haemost. 6 (3): 415-420. 10.1111/j.1538-7836.2007.02865.x 18088344
    • (2008) J. Thromb. Haemost. , vol.6 , Issue.3 , pp. 415-420
    • Ma, A.C.1    Kubes, P.2
  • 79
    • 79954614799 scopus 로고    scopus 로고
    • Bovine lactoferrin improves bone status of ovariectomized mice via immune function modulation
    • 10.1016/j.bone.2011.02.002 21303707
    • Malet A. Bournaud E. Lan A. Mikogami T. Tome D. Blais A. 2011. Bovine lactoferrin improves bone status of ovariectomized mice via immune function modulation. Bone, 48 (5): 1028-1035. 10.1016/j.bone.2011.02.002 21303707
    • (2011) Bone , vol.48 , Issue.5 , pp. 1028-1035
    • Malet, A.1    Bournaud, E.2    Lan, A.3    Mikogami, T.4    Tome, D.5    Blais, A.6
  • 80
    • 84861363011 scopus 로고    scopus 로고
    • Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor
    • This issue. 10.1139/o11-070 22320386
    • Mariller C. Hardiville S. Hoedt E. Huvent I. Pina-Canseco S. Pierce A. 2012. delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor. Biochem. Cell Biol. This issue. 10.1139/o11-070 22320386
    • (2012) Biochem. Cell Biol.
    • Mariller, C.1    Hardiville, S.2    Hoedt, E.3    Huvent, I.4    Pina-Canseco, S.5    Pierce, A.6
  • 81
    • 0014574791 scopus 로고
    • Lactoferrin, an iron-binding protein in neutrophilic leukocytes
    • 10.1084/jem.130.3.643 4979954
    • Masson P.L. Heremans J.F. Schonne E. 1969. Lactoferrin, an iron-binding protein in neutrophilic leukocytes. J. Exp. Med. 130 (3): 643-658. 10.1084/jem.130.3.643 4979954
    • (1969) J. Exp. Med. , vol.130 , Issue.3 , pp. 643-658
    • Masson, P.L.1    Heremans, J.F.2    Schonne, E.3
  • 82
    • 0001213833 scopus 로고
    • Pŕparation et proprít́s de la lactosid́ rophiline (lactotransferrine) du lait de femme
    • 13772242
    • Montreuil J. Tonnelat J. Mullet S. 1960. Pŕparation et proprít́s de la lactosid́rophiline (lactotransferrine) du lait de femme. Biochim. Biophys. Acta., 45: 413-421. 13772242
    • (1960) Biochim. Biophys. Acta. , vol.45 , pp. 413-421
    • Montreuil, J.1    Tonnelat, J.2    Mullet, S.3
  • 83
    • 37849045369 scopus 로고    scopus 로고
    • Identification of angiogenin as the osteoclastic bone resorption-inhibitory factor in bovine milk
    • 10.1016/j.bone.2007.10.012 18055286
    • Morita Y. Matsuyama H. Serizawa A. Takeya T. Kawakami H. 2008. Identification of angiogenin as the osteoclastic bone resorption-inhibitory factor in bovine milk. Bone, 42 (2): 380-387. 10.1016/j.bone.2007.10.012 18055286
    • (2008) Bone , vol.42 , Issue.2 , pp. 380-387
    • Morita, Y.1    Matsuyama, H.2    Serizawa, A.3    Takeya, T.4    Kawakami, H.5
  • 84
    • 25844442224 scopus 로고    scopus 로고
    • Lactoferrin- A novel bone growth factor
    • 10.3121/cmr.3.2.93 16012127
    • Naot D. Grey A. Reid I.R. Cornish J. 2005. Lactoferrin- A novel bone growth factor. Clin. Med. Res. 3 (2): 93-101. 10.3121/cmr.3.2.93 16012127
    • (2005) Clin. Med. Res. , vol.3 , Issue.2 , pp. 93-101
    • Naot, D.1    Grey, A.2    Reid, I.R.3    Cornish, J.4
  • 85
    • 77958581350 scopus 로고    scopus 로고
    • Serum stabilities of short tryptophan-and arginine-rich antimicrobial peptide analogs
    • 10.1371/journal.pone.0012684 20844765
    • Nguyen L.T. Chau J.K. Perry N.A. de Boer L. Zaat S.A. Vogel H.J. 2010. Serum stabilities of short tryptophan-and arginine-rich antimicrobial peptide analogs. PLoS ONE, 5 (9): e12684. 10.1371/journal.pone.0012684 20844765
    • (2010) PLoS ONE , vol.5 , Issue.9 , pp. 12684
    • Nguyen, L.T.1    Chau, J.K.2    Perry, N.A.3    De Boer, L.4    Zaat, S.A.5    Vogel, H.J.6
  • 86
    • 1542609189 scopus 로고    scopus 로고
    • 99mTc-Labeled UBI 29-41 peptide for monitoring the efficacy of antibacterial agents in mice infected with Staphylococcus aureus
    • 14960656
    • Nibbering P.H. Welling M.M. Paulusma-Annema A. Brouwer C.P. Lupetti A. Pauwels E.K. 2004. 99mTc-Labeled UBI 29-41 peptide for monitoring the efficacy of antibacterial agents in mice infected with Staphylococcus aureus. J. Nucl. Med. 45 (2): 321-326. 14960656
    • (2004) J. Nucl. Med. , vol.45 , Issue.2 , pp. 321-326
    • Nibbering, P.H.1    Welling, M.M.2    Paulusma-Annema, A.3    Brouwer, C.P.4    Lupetti, A.5    Pauwels, E.K.6
  • 87
    • 84857783784 scopus 로고    scopus 로고
    • Structural basis for iron piracy by pathogenic Neisseria
    • 10.1038/nature10823 22327295
    • Noinaj N. Easley N.C. Oke M. Mizuno N. Gumbart J. Boura E. et al. 2012. Structural basis for iron piracy by pathogenic Neisseria. Nature, 483 (7387): 53-58. 10.1038/nature10823 22327295
    • (2012) Nature , vol.483 , Issue.7387 , pp. 53-58
    • Noinaj, N.1    Easley, N.C.2    Oke, M.3    Mizuno, N.4    Gumbart, J.5    Boura, E.6
  • 90
    • 80755143443 scopus 로고    scopus 로고
    • Randomized, double-blind, placebo-controlled phase II study of single-agent oral talactoferrin in patients with locally advanced or metastatic non-small-cell lung cancer that progressed after chemotherapy
    • 10.1200/JCO.2010.34.4127 21969509
    • Parikh P.M. Vaid A. Advani S.H. Digumarti R. Madhavan J. Nag S. et al. 2011. Randomized, double-blind, placebo-controlled phase II study of single-agent oral talactoferrin in patients with locally advanced or metastatic non-small-cell lung cancer that progressed after chemotherapy. J. Clin. Oncol. 29 (31): 4129-4136. 10.1200/JCO.2010.34.4127 21969509
    • (2011) J. Clin. Oncol. , vol.29 , Issue.31 , pp. 4129-4136
    • Parikh, P.M.1    Vaid, A.2    Advani, S.H.3    Digumarti, R.4    Madhavan, J.5    Nag, S.6
  • 91
    • 79952722634 scopus 로고    scopus 로고
    • An antimicrobial protein, lactoferrin exists in the sweat: Proteomic analysis of sweat
    • 10.1111/j.1600-0625.2010.01218.x 21366701
    • Park J.H. Park G.T. Cho I.H. Sim S.M. Yang J.M. Lee D.Y. 2011. An antimicrobial protein, lactoferrin exists in the sweat: proteomic analysis of sweat. Exp. Dermatol. 20 (4): 369-371. 10.1111/j.1600-0625.2010.01218.x 21366701
    • (2011) Exp. Dermatol. , vol.20 , Issue.4 , pp. 369-371
    • Park, J.H.1    Park, G.T.2    Cho, I.H.3    Sim, S.M.4    Yang, J.M.5    Lee, D.Y.6
  • 92
    • 69949150585 scopus 로고    scopus 로고
    • Intracellular delivery of bovine lactoferricin's antimicrobial core (RRWQWR) kills T-leukemia cells
    • 10.1016/j.bbrc.2009.08.083 19699713
    • Richardson A. de Antueno R. Duncan R. Hoskin D.W. 2009. Intracellular delivery of bovine lactoferricin's antimicrobial core (RRWQWR) kills T-leukemia cells. Biochem. Biophys. Res. Commun. 388 (4): 736-741. 10.1016/j.bbrc.2009.08. 083 19699713
    • (2009) Biochem. Biophys. Res. Commun. , vol.388 , Issue.4 , pp. 736-741
    • Richardson, A.1    De Antueno, R.2    Duncan, R.3    Hoskin, D.W.4
  • 93
    • 44649149642 scopus 로고    scopus 로고
    • RNase A ribonucleases and host defense: An evolving story
    • 18211964
    • Rosenberg H.F. 2008. RNase A ribonucleases and host defense: an evolving story. J. Leukoc. Biol. 83 (5): 1079-1087. 18211964
    • (2008) J. Leukoc. Biol. , vol.83 , Issue.5 , pp. 1079-1087
    • Rosenberg, H.F.1
  • 94
    • 80051513696 scopus 로고    scopus 로고
    • Quadrupolar central transition and carbon-13 NMR competition studies of metal ion binding to ovotransferrin
    • 10.1139/v11-019
    • Saponja J. Vogel H.J. 2011. Quadrupolar central transition and carbon-13 NMR competition studies of metal ion binding to ovotransferrin. Can. J. Chem. 89: 779-788. 10.1139/v11-019
    • (2011) Can. J. Chem. , vol.89 , pp. 779-788
    • Saponja, J.1    Vogel, H.J.2
  • 95
  • 96
    • 84856429829 scopus 로고    scopus 로고
    • Lactoferricin but not lactoferrin inhibit herpes simplex virus type 2 infection in mice
    • 10.1016/j.antiviral.2012.01.003 22269645
    • Shestakov A. Jenssen H. Nordstrom I. Eriksson K. 2012. Lactoferricin but not lactoferrin inhibit herpes simplex virus type 2 infection in mice. Antiviral Res. 93 (3): 340-345. 10.1016/j.antiviral.2012.01.003 22269645
    • (2012) Antiviral Res. , vol.93 , Issue.3 , pp. 340-345
    • Shestakov, A.1    Jenssen, H.2    Nordstrom, I.3    Eriksson, K.4
  • 97
    • 0030946524 scopus 로고    scopus 로고
    • Identification of an alternative form of human lactoferrin mRNA that is expressed differentially in normal tissues and tumor-derived cell lines
    • 10.1073/pnas.94.6.2198 9122171
    • Siebert P.D. Huang B.C. 1997. Identification of an alternative form of human lactoferrin mRNA that is expressed differentially in normal tissues and tumor-derived cell lines. Proc. Natl. Acad. Sci. U.S.A. 94 (6): 2198-2203. 10.1073/pnas.94.6.2198 9122171
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , Issue.6 , pp. 2198-2203
    • Siebert, P.D.1    Huang, B.C.2
  • 98
    • 0037198693 scopus 로고    scopus 로고
    • A component of innate immunity prevents bacterial biofilm development
    • 10.1038/417552a 12037568
    • Singh P.K. Parsek M.R. Greenberg E.P. Welsh M.J. 2002. A component of innate immunity prevents bacterial biofilm development. Nature, 417 (6888): 552-555. 10.1038/417552a 12037568
    • (2002) Nature , vol.417 , Issue.6888 , pp. 552-555
    • Singh, P.K.1    Parsek, M.R.2    Greenberg, E.P.3    Welsh, M.J.4
  • 99
    • 0033796465 scopus 로고    scopus 로고
    • Zinc-reversible antimicrobial activity of recombinant calprotectin (migration inhibitory factor-related proteins 8 and 14)
    • 10.1086/315810 10979933
    • Sohnle P.G. Hunter M.J. Hahn B. Chazin W.J. 2000. Zinc-reversible antimicrobial activity of recombinant calprotectin (migration inhibitory factor-related proteins 8 and 14). J. Infect. Dis. 182 (4): 1272-1275. 10.1086/315810 10979933
    • (2000) J. Infect. Dis. , vol.182 , Issue.4 , pp. 1272-1275
    • Sohnle, P.G.1    Hunter, M.J.2    Hahn, B.3    Chazin, W.J.4
  • 101
    • 48749104758 scopus 로고    scopus 로고
    • Lactoferrin, a major defense protein of innate immunity, is a novel maturation factor for human dendritic cells
    • 10.1096/fj.07-098038 18364398
    • Spadaro M. Caorsi C. Ceruti P. Varadhachary A. Forni G. Pericle F. Giovarelli M. 2008. Lactoferrin, a major defense protein of innate immunity, is a novel maturation factor for human dendritic cells. FASEB J. 22 (8): 2747-2757. 10.1096/fj.07-098038 18364398
    • (2008) FASEB J. , vol.22 , Issue.8 , pp. 2747-2757
    • Spadaro, M.1    Caorsi, C.2    Ceruti, P.3    Varadhachary, A.4    Forni, G.5    Pericle, F.6    Giovarelli, M.7
  • 102
    • 27944438079 scopus 로고    scopus 로고
    • Histatin and lactoferrin derived peptides: Antimicrobial properties and effects on mammalian cells
    • 10.1016/j.peptides.2005.05.014 15979203
    • Stallmann H.P. Faber C. Bronckers A.L. de Blieck-Hogervorst J.M. Brouwer C.P. Amerongen A.V. Wuisman P.I. 2005. Histatin and lactoferrin derived peptides: antimicrobial properties and effects on mammalian cells. Peptides, 26 (12): 2355-2359. 10.1016/j.peptides.2005.05.014 15979203
    • (2005) Peptides , vol.26 , Issue.12 , pp. 2355-2359
    • Stallmann, H.P.1    Faber, C.2    Bronckers, A.L.3    De Blieck-Hogervorst, J.M.4    Brouwer, C.P.5    Amerongen, A.V.6    Wuisman, P.I.7
  • 103
    • 0038064554 scopus 로고    scopus 로고
    • Important structural features of 15-residue lactoferricin derivatives and methods for improvement of antimicrobial activity
    • 10.1139/o01-236 11908644
    • Strøm M.B. Haug B.E. Rekdal O. Skar M.L. Stensen W. Svendsen J.S. 2002. Important structural features of 15-residue lactoferricin derivatives and methods for improvement of antimicrobial activity. Biochem. Cell Biol. 80 (1): 65-74. 10.1139/o01-236 11908644
    • (2002) Biochem. Cell Biol. , vol.80 , Issue.1 , pp. 65-74
    • Strøm, M.B.1    Haug, B.E.2    Rekdal, O.3    Skar, M.L.4    Stensen, W.5    Svendsen, J.S.6
  • 104
    • 74549124200 scopus 로고    scopus 로고
    • A rice-derived recombinant human lactoferrin stimulates fibroblast proliferation, migration, and sustains cell survival
    • a. 10.1111/j.1524-475X.2009.00563.x 20082685
    • Tang L. Cui T. Wu J.J. Liu-Mares W. Huang N. Li J. 2010 a. A rice-derived recombinant human lactoferrin stimulates fibroblast proliferation, migration, and sustains cell survival. Wound Repair Regen. 18 (1): 123-131. 10.1111/j.1524-475X.2009.00563.x 20082685
    • (2010) Wound Repair Regen. , vol.18 , Issue.1 , pp. 123-131
    • Tang, L.1    Cui, T.2    Wu, J.J.3    Liu-Mares, W.4    Huang, N.5    Li, J.6
  • 105
    • 77953987745 scopus 로고    scopus 로고
    • Human lactoferrin stimulates skin keratinocyte function and wound re-epithelialization
    • b. 20222924
    • Tang L. Wu J.J. Ma Q. Cui T. Andreopoulos F.M. Gil J. et al. 2010 b. Human lactoferrin stimulates skin keratinocyte function and wound re-epithelialization. Br. J. Dermatol. 163 (1): 38-47. 20222924
    • (2010) Br. J. Dermatol. , vol.163 , Issue.1 , pp. 38-47
    • Tang, L.1    Wu, J.J.2    Ma, Q.3    Cui, T.4    Andreopoulos, F.M.5    Gil, J.6
  • 106
    • 0034868442 scopus 로고    scopus 로고
    • Non-invasive investigation of inflammatory bowel disease
    • 11819811
    • Tibble J.A. Bjarnason I. 2001. Non-invasive investigation of inflammatory bowel disease. World J. Gastroenterol. 7 (4): 460-465. 11819811
    • (2001) World J. Gastroenterol. , vol.7 , Issue.4 , pp. 460-465
    • Tibble, J.A.1    Bjarnason, I.2
  • 108
    • 77953270296 scopus 로고    scopus 로고
    • Cancer prevention by bovine lactoferrin: From animal studies to human trial
    • 10.1007/s10534-010-9331-3 20407806
    • Tsuda H. Kozu T. Iinuma G. Ohashi Y. Saito Y. Saito D. et al. 2010. Cancer prevention by bovine lactoferrin: from animal studies to human trial. Biometals, 23 (3): 399-409. 10.1007/s10534-010-9331-3 20407806
    • (2010) Biometals , vol.23 , Issue.3 , pp. 399-409
    • Tsuda, H.1    Kozu, T.2    Iinuma, G.3    Ohashi, Y.4    Saito, Y.5    Saito, D.6
  • 109
    • 28344457682 scopus 로고    scopus 로고
    • Lactoferrin: An important host defence against microbial and viral attack
    • 10.1007/s00018-005-5372-0 16261253
    • Valenti P. Antonini G. 2005. Lactoferrin: an important host defence against microbial and viral attack. Cell. Mol. Life Sci. 62 (22): 2576-2587. 10.1007/s00018-005-5372-0 16261253
    • (2005) Cell. Mol. Life Sci. , vol.62 , Issue.22 , pp. 2576-2587
    • Valenti, P.1    Antonini, G.2
  • 110
    • 77953234577 scopus 로고    scopus 로고
    • The human lactoferrin-derived peptide hLF1-11 primes monocytes for an enhanced TLR-mediated immune response
    • 10.1007/s10534-010-9322-4 20238236
    • van der Does A.M. Bogaards S.J. Jonk L. Wulferink M. Velders M.P. Nibbering P.H. 2010. The human lactoferrin-derived peptide hLF1-11 primes monocytes for an enhanced TLR-mediated immune response. Biometals, 23 (3): 493-505. 10.1007/s10534-010-9322-4 20238236
    • (2010) Biometals , vol.23 , Issue.3 , pp. 493-505
    • Van Der Does, A.M.1    Bogaards, S.J.2    Jonk, L.3    Wulferink, M.4    Velders, M.P.5    Nibbering, P.H.6
  • 111
    • 84859896286 scopus 로고    scopus 로고
    • The antimicrobial peptide hLF1-11 drives monocyte-dendritic cell differentiation toward dendritic cells that promote antifungal responses and enhance Th17 polarization
    • a. 10.1159/000332941 22261275
    • van der Does A.M. Joosten S.A. Vroomans E. Bogaards S.J. van Meijgaarden K.E. Ottenhoff T.H. et al. 2012 a. The antimicrobial peptide hLF1-11 drives monocyte-dendritic cell differentiation toward dendritic cells that promote antifungal responses and enhance Th17 polarization. J. Innate Immun., 4 (3): 284-292. 10.1159/000332941 22261275
    • (2012) J. Innate Immun. , vol.4 , Issue.3 , pp. 284-292
    • Van Der Does, A.M.1    Joosten, S.A.2    Vroomans, E.3    Bogaards, S.J.4    Van Meijgaarden, K.E.5    Ottenhoff, T.H.6
  • 112
    • 84861137566 scopus 로고    scopus 로고
    • The human lactoferrin-derived peptide hLF1-11 exerts immunomodulatory effects by specific inhibition of myeloperoxidase activity
    • b. In press. 10.4049/jimmunol.1102777 22523385
    • van der Does A.M. Hensbergen P.J. Bogaards S.J. Cansoy M. Deelder A.M. van Leeuwen H.C. et al. 2012 b. The human lactoferrin-derived peptide hLF1-11 exerts immunomodulatory effects by specific inhibition of myeloperoxidase activity. J. Immunol. In press. 10.4049/jimmunol.1102777 22523385
    • (2012) J. Immunol.
    • Van Der Does, A.M.1    Hensbergen, P.J.2    Bogaards, S.J.3    Cansoy, M.4    Deelder, A.M.5    Van Leeuwen, H.C.6
  • 113
    • 1942452255 scopus 로고    scopus 로고
    • Lactoferrampin: A novel antimicrobial peptide in the N1-domain of bovine lactoferrin
    • 10.1016/j.peptides.2003.12.006 15062998
    • van der Kraan M.I.A. Groenink J. Nazmi K. Veerman E.C.I. Bolscher J.G.M. Amerongen A.V.N. 2004. Lactoferrampin: a novel antimicrobial peptide in the N1-domain of bovine lactoferrin. Peptides, 25 (2): 177-183. 10.1016/j.peptides. 2003.12.006 15062998
    • (2004) Peptides , vol.25 , Issue.2 , pp. 177-183
    • Van Der Kraan, M.I.A.1    Groenink, J.2    Nazmi, K.3    Veerman, E.C.I.4    Bolscher, J.G.M.5    Amerongen, A.V.N.6
  • 114
    • 14944369298 scopus 로고    scopus 로고
    • Lactoferrampin, an antimicrobial peptide of bovine lactoferrin, exerts its candidacidal activity by a cluster of positively charged residues at the C-terminus in combination with a helix-facilitating N-terminal part
    • 10.1515/BC.2005.017 15843157
    • van der Kraan M.I.A. Nazmi K. Teeken A. Groenink J. van't Hof W. Veerman E.C.I. et al. 2005. Lactoferrampin, an antimicrobial peptide of bovine lactoferrin, exerts its candidacidal activity by a cluster of positively charged residues at the C-terminus in combination with a helix-facilitating N-terminal part. Biol. Chem. 386 (2): 137-142. 10.1515/BC.2005.017 15843157
    • (2005) Biol. Chem. , vol.386 , Issue.2 , pp. 137-142
    • Van Der Kraan, M.I.A.1    Nazmi, K.2    Teeken, A.3    Groenink, J.4    Van'T Hof, W.5    Veerman, E.C.I.6
  • 115
    • 0034972589 scopus 로고    scopus 로고
    • Mechanism of extracellular release of human neutrophil calprotectin complex
    • 11435495
    • Voganatsi A. Panyutich A. Miyasaki K.T. Murthy R.K. 2001. Mechanism of extracellular release of human neutrophil calprotectin complex. J. Leukoc. Biol. 70 (1): 130-134. 11435495
    • (2001) J. Leukoc. Biol. , vol.70 , Issue.1 , pp. 130-134
    • Voganatsi, A.1    Panyutich, A.2    Miyasaki, K.T.3    Murthy, R.K.4
  • 116
    • 33748325910 scopus 로고    scopus 로고
    • Lactoferrin research, technology and applications
    • 10.1016/j.idairyj.2006.06.013
    • Wakabayashi H. Yamauchi K. Takase M. 2006. Lactoferrin research, technology and applications. Int. Dairy J. 16: 1241-1251. 10.1016/j.idairyj. 2006.06.013
    • (2006) Int. Dairy J. , vol.16 , pp. 1241-1251
    • Wakabayashi, H.1    Yamauchi, K.2    Takase, M.3
  • 117
    • 0037214319 scopus 로고    scopus 로고
    • Iron status in mice carrying a targeted disruption of lactoferrin
    • 10.1128/MCB.23.1.178-185.2003 12482971
    • Ward P.P. Mendoza-Meneses M. Cunningham G.A. Conneely O.M. 2003. Iron status in mice carrying a targeted disruption of lactoferrin. Mol. Cell. Biol. 23 (1): 178-185. 10.1128/MCB.23.1.178-185.2003 12482971
    • (2003) Mol. Cell. Biol. , vol.23 , Issue.1 , pp. 178-185
    • Ward, P.P.1    Mendoza-Meneses, M.2    Cunningham, G.A.3    Conneely, O.M.4
  • 118
    • 28344447990 scopus 로고    scopus 로고
    • Multifunctional roles of lactoferrin: A critical overview
    • 10.1007/s00018-005-5369-8 16261256
    • Ward P.P. Paz E. Conneely O.M. 2005. Multifunctional roles of lactoferrin: a critical overview. Cell Mol Life Sci. 62 (22): 2540-2548. 10.1007/s00018-005-5369-8 16261256
    • (2005) Cell Mol Life Sci. , vol.62 , Issue.22 , pp. 2540-2548
    • Ward, P.P.1    Paz, E.2    Conneely, O.M.3
  • 119
    • 0034744067 scopus 로고    scopus 로고
    • 99mTc-labeled antimicrobial peptides for detection of bacterial and Candida albicans infections
    • 11337578
    • Welling M.M. Lupetti A. Balter H.S. Lanzzeri S. Souto B. Rey A.M. et al. 2001. 99mTc-labeled antimicrobial peptides for detection of bacterial and Candida albicans infections. J. Nucl. Med. 42 (5): 788-794. 11337578
    • (2001) J. Nucl. Med. , vol.42 , Issue.5 , pp. 788-794
    • Welling, M.M.1    Lupetti, A.2    Balter, H.S.3    Lanzzeri, S.4    Souto, B.5    Rey, A.M.6
  • 120
    • 67349118128 scopus 로고    scopus 로고
    • Thermodynamic characterization of the interactions between the immunoregulatory proteins osteopontin and lactoferrin
    • 10.1016/j.molimm.2009.04.024 19477017
    • Yamniuk A.P. Burling H. Vogel H.J. 2009. Thermodynamic characterization of the interactions between the immunoregulatory proteins osteopontin and lactoferrin. Mol. Immunol. 46 (11-12): 2395-2402. 10.1016/j.molimm.2009.04.024 19477017
    • (2009) Mol. Immunol. , vol.46 , Issue.1112 , pp. 2395-2402
    • Yamniuk, A.P.1    Burling, H.2    Vogel, H.J.3
  • 121
    • 0033400204 scopus 로고    scopus 로고
    • A 1-Mb PAC contig spanning the common eliminated region 1 (CER1) in microcell hybrid-derived SCID tumors
    • 10.1006/geno.1999.5952 10610706
    • Yang Y. Kiss H. Kost-Alimova M. Kedra D. Fransson I. Seroussi E. et al. 1999. A 1-Mb PAC contig spanning the common eliminated region 1 (CER1) in microcell hybrid-derived SCID tumors. Genomics, 62 (2): 147-155. 10.1006/geno.1999.5952 10610706
    • (1999) Genomics , vol.62 , Issue.2 , pp. 147-155
    • Yang, Y.1    Kiss, H.2    Kost-Alimova, M.3    Kedra, D.4    Fransson, I.5    Seroussi, E.6
  • 122
    • 79960087671 scopus 로고    scopus 로고
    • Lactoferrin: An iron-binding antimicrobial protein against Escherichia coli infection
    • 10.1007/s10534-011-9423-8 21327478
    • Yen C.C. Shen C.J. Hsu W.H. Chang Y.H. Lin H.T. Chen H.L. Chen C.M. 2011. Lactoferrin: an iron-binding antimicrobial protein against Escherichia coli infection. Biometals, 24 (4): 585-594. 10.1007/s10534-011-9423-8 21327478
    • (2011) Biometals , vol.24 , Issue.4 , pp. 585-594
    • Yen, C.C.1    Shen, C.J.2    Hsu, W.H.3    Chang, Y.H.4    Lin, H.T.5    Chen, H.L.6    Chen, C.M.7


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