{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,7]],"date-time":"2026-07-07T23:37:56Z","timestamp":1783467476729,"version":"3.55.0"},"reference-count":173,"publisher":"MathDoc\/Centre Mersenne","issue":"10","license":[{"start":{"date-parts":[[2014,9,22]],"date-time":"2014-09-22T00:00:00Z","timestamp":1411344000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["em-consulte.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":[],"abstract":"<jats:p id=\"spar0005\">Lactoferrin (LF) is an 80-kDa globular glycoprotein with high affinity for metal ions, particularly for iron. This protein possesses many biological functions, including the binding and release of iron and serves as one of the important components of the innate immune system, where it acts as a potent inhibitor of several pathogens. LF has efficacious antibacterial and antiviral activities against a wide range of Gram-positive and Gram-negative bacteria and against both naked and enveloped DNA and RNA viruses. In its antiviral pursuit, LF acts predominantly at the acute phase of the viral infection or even at the intracellular stage, as in hepatitis C virus infection. LF inhibits the entry of viral particles into host cells, either by direct attachment to the viral particles or by blocking their cellular receptors. This wide range of activities may be attributed to the capacity of LF to bind iron and its ability to interfere with the cellular receptors of both hosts and pathogenic microbes.<\/jats:p>","DOI":"10.1016\/j.crvi.2014.08.003","type":"journal-article","created":{"date-parts":[[2014,9,21]],"date-time":"2014-09-21T22:45:30Z","timestamp":1411339530000},"page":"581-595","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":106,"title":["Potential lactoferrin activity against pathogenic viruses"],"prefix":"10.5802","volume":"337","author":[{"given":"Elrashdy M.","family":"Redwan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vladimir N.","family":"Uversky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Esmail M.","family":"El-Fakharany","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hussein","family":"Al-Mehdar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"3842","published-online":{"date-parts":[[2014,9,22]]},"reference":[{"key":"key2025102316371552331_1","doi-asserted-by":"crossref","first-page":"1769","DOI":"10.1073\/pnas.84.7.1769","article-title":"Structure of human lactoferrin at 3.2\u2005A resolution","volume":"84","author":"Anderson, B.F.","year":"1987","unstructured":"[1] Anderson, B.F.; Baker, H.M.; Dodson, E.J.; Norris, G.E.; Rumball, S.V.; Waters, J.M.; Baker, E.N. Structure of human lactoferrin at 3.2\u2005A resolution, Proc. Natl. Acad. Sci. USA, Volume 84 (1987), pp. 1769-1773","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"key2025102316371552331_2","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1006\/jmbi.1997.1386","article-title":"Three-dimensional structure of diferric bovine lactoferrin at 2.8\u2005A resolution","volume":"274","author":"Moore, S.A.","year":"1997","unstructured":"[2] Moore, S.A.; Anderson, B.F.; Groom, C.R.; Haridas, M.; Baker, E.N. Three-dimensional structure of diferric bovine lactoferrin at 2.8\u2005A resolution, J. Mol. Biol., Volume 274 (1997), pp. 222-236","journal-title":"J. Mol. Biol."},{"key":"key2025102316371552331_3","first-page":"57","article-title":"Detecci\u00f3n de lysozima and lactoferrin por western blot enovas de <span class=\"italique\">Trucha arco\u00edris<\/span> (<span class=\"italique\">Oncorhynchus mykiss<\/span>)","volume":"2","author":"Torres, J.M.","year":"2006","unstructured":"[3] Torres, J.M.; Concepci\u00f3n, J.L.; Vielma, J.R. Detecci\u00f3n de lysozima and lactoferrin por western blot enovas de Trucha arco\u00edris (Oncorhynchus mykiss), Mundo Pecuario, Volume 2 (2006), pp. 57-59","journal-title":"Mundo Pecuario"},{"key":"key2025102316371552331_4","first-page":"73","author":"Russell, M.W.","year":"2005","unstructured":"[4] Russell, M.W.; Bobek, L.A.; Brock, J.H.; Hajishengallis, G.; Tenovuo, J. Innate humoral defense factors (Mestecky, J.; Bienenstock, J.; Lamm, M.E.; Mayer, L.; Strober, W.; McGhee, J.R., eds.), Mucosal Immunology, Academic Press\/Elsevier, San Diego, CA, USA, 2005, pp. 73-83","journal-title":"Innate humoral defense factors"},{"key":"key2025102316371552331_5","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1093\/infdis\/124.6.539","article-title":"Inhibition of growth of <span class=\"italique\">Candida albicans<\/span> by iron-unsaturated lactoferrin: relation to host-defense mechanisms in chronic mucocutaneous candidiasis","volume":"124","author":"Kirkpatrick, C.H.","year":"1971","unstructured":"[5] Kirkpatrick, C.H.; Green, I.; Rich, R.R.; Schade, A.L. Inhibition of growth of Candida albicans by iron-unsaturated lactoferrin: relation to host-defense mechanisms in chronic mucocutaneous candidiasis, J. Infect. Dis., Volume 124 (1971), pp. 539-544","journal-title":"J. Infect. Dis."},{"key":"key2025102316371552331_6","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1515\/CCLM.1999.049","article-title":"Lactoferrin: a multifunctional glycoprotein involved in the modulation of the inflammatory process","volume":"37","author":"Baveye, S.","year":"1999","unstructured":"[6] Baveye, S.; Elass, E.; Mazurier, J.; Spik, G.; Legrand, D. Lactoferrin: a multifunctional glycoprotein involved in the modulation of the inflammatory process, Clin. Chem. Lab. Med., Volume 37 (1999), pp. 281-286","journal-title":"Clin. Chem. Lab. Med."},{"key":"key2025102316371552331_7","first-page":"247","article-title":"Antimicrobial actions of lactoferrin","volume":"10","author":"Chierici, R.","year":"2001","unstructured":"[7] Chierici, R. Antimicrobial actions of lactoferrin, Adv. Nutr. Res., Volume 10 (2001), pp. 247-269","journal-title":"Adv. Nutr. Res."},{"key":"key2025102316371552331_8","first-page":"102","article-title":"Antimicrobial mechanisms and potencial clinical application of lactoferrin [in Spanish]","volume":"47","author":"Rodriguez, D.A.","year":"2005","unstructured":"[8] Rodriguez, D.A.; Velazquez, L.; Ramos, G. Antimicrobial mechanisms and potencial clinical application of lactoferrin [in Spanish], Rev. Latinoam. Microbiol., Volume 47 (2005), pp. 102-111","journal-title":"Rev. Latinoam. Microbiol."},{"issue":"2","key":"key2025102316371552331_9","first-page":"58","article-title":"Actividades antibacterianas de la lactoferrina","volume":"26","author":"Drago, S.M.E.","year":"2006","unstructured":"[9] Drago, S.M.E. Actividades antibacterianas de la lactoferrina, Enf. Inf. Microbiol., Volume 26 (2006) no. 2, pp. 58-63","journal-title":"Enf. Inf. Microbiol."},{"key":"key2025102316371552331_10","first-page":"55","article-title":"The proteins in whey","volume":"23","author":"Soerensen, M.","year":"1939","unstructured":"[10] Soerensen, M.; Soerensen, S.P.L. The proteins in whey, C. R. Trav. Lab. Carlsberg, Volume 23 (1939), pp. 55-99","journal-title":"C. R. Trav. Lab. Carlsberg"},{"key":"key2025102316371552331_11","doi-asserted-by":"crossref","first-page":"510","DOI":"10.3891\/acta.chem.scand.14-0510","article-title":"Isolation of an iron containing red protein from human milk","volume":"14","author":"Johansson, B.G.","year":"1960","unstructured":"[11] Johansson, B.G. Isolation of an iron containing red protein from human milk, Acta Chem. Scand., Volume 14 (1960), pp. 510-512","journal-title":"Acta Chem. Scand."},{"key":"key2025102316371552331_12","first-page":"252","article-title":"Lactoferrin: a general review","volume":"80","author":"Levay, P.F.","year":"1995","unstructured":"[12] Levay, P.F.; Viljoen, M. Lactoferrin: a general review, Haematologica, Volume 80 (1995), pp. 252-267","journal-title":"Haematologica"},{"key":"key2025102316371552331_13","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1146\/annurev.nu.15.070195.000521","article-title":"Lactoferrin: molecular structure and biological function","volume":"15","author":"Lonnerdal, B.","year":"1995","unstructured":"[13] Lonnerdal, B.; Iyer, S. Lactoferrin: molecular structure and biological function, Annu. Rev. Nutr., Volume 15 (1995), pp. 93-110","journal-title":"Annu. Rev. Nutr."},{"key":"key2025102316371552331_14","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1111\/j.1432-1033.1984.tb08607.x","article-title":"Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins","volume":"145","author":"Metz-Boutigue, M.H.","year":"1984","unstructured":"[14] Metz-Boutigue, M.H.; Jolles, J.; Mazurier, J.; Schoentgen, F.; Legrand, D.; Spik, G.; Montreuil, J.; Jolles, P. Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins, Eur. J. Biochem., Volume 145 (1984), pp. 659-676","journal-title":"Eur. J. Biochem."},{"key":"key2025102316371552331_15","doi-asserted-by":"crossref","first-page":"2531","DOI":"10.1007\/s00018-005-5368-9","article-title":"Molecular structure, binding properties and dynamics of lactoferrin","volume":"62","author":"Baker, E.N.","year":"2005","unstructured":"[15] Baker, E.N.; Baker, H.M. Molecular structure, binding properties and dynamics of lactoferrin, Cell Mol. Life Sci., Volume 62 (2005), pp. 2531-2539","journal-title":"Cell Mol. Life Sci."},{"key":"key2025102316371552331_16","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/978-1-4615-2548-6_1","article-title":"Three-dimensional structure of lactoferrin in various functional states","volume":"357","author":"Baker, E.N.","year":"1994","unstructured":"[16] Baker, E.N.; Anderson, B.F.; Baker, H.M.; Day, C.L.; Haridas, M.; Norris, G.E.; Rumball, S.V.; Smith, C.A.; Thomas, D.H. Three-dimensional structure of lactoferrin in various functional states, Adv. Exp. Med. Biol., Volume 357 (1994), pp. 1-12","journal-title":"Adv. Exp. Med. Biol."},{"key":"key2025102316371552331_17","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1016\/S0898-8838(08)60176-2","article-title":"Structure and reactivity of transferrins","volume":"41","author":"Baker, E.N.","year":"1994","unstructured":"[17] Baker, E.N. Structure and reactivity of transferrins, Adv. Inorg. Chem., Volume 41 (1994), pp. 389-463","journal-title":"Adv. Inorg. Chem."},{"key":"key2025102316371552331_18","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.biochi.2008.05.006","article-title":"A structural framework for understanding the multifunctional character of lactoferrin","volume":"91","author":"Baker, E.N.","year":"2009","unstructured":"[18] Baker, E.N.; Baker, H.M. A structural framework for understanding the multifunctional character of lactoferrin, Biochimie, Volume 91 (2009), pp. 3-10","journal-title":"Biochimie"},{"key":"key2025102316371552331_19","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/S0958-6946(99)00117-X","article-title":"Sequence analysis of camel (<span class=\"italique\">Camelus dromedarius<\/span>) lactoferrin","volume":"9","author":"Kappeler, S.R.","year":"1999","unstructured":"[19] Kappeler, S.R.; Ackermann, M.; Farah, Z.; Puhan, Z. Sequence analysis of camel (Camelus dromedarius) lactoferrin, Int. Dairy J., Volume 9 (1999), pp. 481-486","journal-title":"Int. Dairy J."},{"key":"key2025102316371552331_20","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1111\/j.1365-2141.1983.tb02113.x","article-title":"Receptor binding of lactoferrin by human monocytes","volume":"54","author":"Birgens, H.S.","year":"1983","unstructured":"[20] Birgens, H.S.; Hansen, N.E.; Karle, H.; Kristensen, L.O. Receptor binding of lactoferrin by human monocytes, Br. J. Haematol., Volume 54 (1983), pp. 383-391","journal-title":"Br. J. Haematol."},{"key":"key2025102316371552331_21","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1038\/373721a0","article-title":"Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA","volume":"373","author":"He, J.","year":"1995","unstructured":"[21] He, J.; Furmanski, P. Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA, Nature, Volume 373 (1995), pp. 721-724","journal-title":"Nature"},{"issue":"Pt 3","key":"key2025102316371552331_22","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1042\/bj3120839","article-title":"Lactoferrin-lipopolysaccharide interaction: involvement of the 28-34 loop region of human lactoferrin in the high affinity binding to <span class=\"italique\">Escherichia coli<\/span> 055B5 lipopolysaccharide","volume":"312","author":"Elass-Rochard, E.","year":"1995","unstructured":"[22] Elass-Rochard, E.; Roseanu, A.; Legrand, D.; Trif, M.; Salmon, V.; Motas, C.; Montreuil, J.; Spik, G. 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., Volume 312 (1995) no. Pt 3, pp. 839-845","journal-title":"Biochem. J."},{"key":"key2025102316371552331_23","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1128\/iai.35.3.792-799.1982","article-title":"Bactericidal activity of human lactoferrin: differentiation from the stasis of iron deprivation","volume":"35","author":"Arnold, R.R.","year":"1982","unstructured":"[23] Arnold, R.R.; Russell, J.E.; Champion, W.J.; Brewer, M.; Gauthier, J.J. Bactericidal activity of human lactoferrin: differentiation from the stasis of iron deprivation, Infect. Immunol., Volume 35 (1982), pp. 792-799","journal-title":"Infect. Immunol."},{"key":"key2025102316371552331_24","first-page":"177","article-title":"Isolation and structure-functional characterization of human colostral lactoferrin","volume":"17","author":"Aguila, A.","year":"2000","unstructured":"[24] Aguila, A.; Herrera, A.; Velzquez, W. Isolation and structure-functional characterization of human colostral lactoferrin, Biotecnologia Aplicada, Volume 17 (2000), pp. 177-182","journal-title":"Biotecnologia Aplicada"},{"key":"key2025102316371552331_25","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/S0166-3542(01)00195-4","article-title":"Antiviral activities of lactoferrin","volume":"52","author":"van der Strate, B.W.","year":"2001","unstructured":"[25] van der Strate, B.W.; Beljaars, L.; Molema, G.; Harmsen, M.C.; Meijer, D.K. Antiviral activities of lactoferrin, Antiviral Res., Volume 52 (2001), pp. 225-239","journal-title":"Antiviral Res."},{"key":"key2025102316371552331_26","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1182\/blood.V80.1.235.235","article-title":"Regulation of cytokine release from mononuclear cells by the iron-binding protein lactoferrin","volume":"80","author":"Crouch, S.P.","year":"1992","unstructured":"[26] Crouch, S.P.; Slater, K.J.; Fletcher, J. Regulation of cytokine release from mononuclear cells by the iron-binding protein lactoferrin, Blood, Volume 80 (1992), pp. 235-240","journal-title":"Blood"},{"key":"key2025102316371552331_27","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1136\/adc.67.5.657","article-title":"Biological role of lactoferrin","volume":"67","author":"Sanchez, L.","year":"1992","unstructured":"[27] Sanchez, L.; Calvo, M.; Brock, J.H. Biological role of lactoferrin, Arch. Dis. Child, Volume 67 (1992), pp. 657-661","journal-title":"Arch. Dis. Child"},{"key":"key2025102316371552331_28","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1016\/0167-4889(83)90099-X","article-title":"Identification of lactoferrin as an essential growth factor for human lymphocytic cell lines in serum-free medium","volume":"763","author":"Hashizume, S.","year":"1983","unstructured":"[28] Hashizume, S.; Kuroda, K.; Murakami, H. Identification of lactoferrin as an essential growth factor for human lymphocytic cell lines in serum-free medium, Biochim. Biophys. Acta, Volume 763 (1983), pp. 377-382","journal-title":"Biochim. Biophys. Acta"},{"key":"key2025102316371552331_29","first-page":"307","article-title":"Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor, Biochem","volume":"90","author":"Mariller, C.","year":"2012","unstructured":"[29] Mariller, C.; Hardiville, S.; Hoedt, E.; Huvent, I.; Pina-Canseco, S.; Pierce, A. Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor, Biochem, Cell Biol., Volume 90 (2012), pp. 307-319","journal-title":"Cell Biol."},{"issue":"5","key":"key2025102316371552331_30","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1007\/s10534-014-9744-5","article-title":"Delta-lactoferrin induces cell death via the mitochondrial death signaling pathway by upregulating bax expression","volume":"27","author":"Hardiville, S.","year":"2014","unstructured":"[30] Hardiville, S.; Escobar-Ramirez, A.; Pina-Canceco, S.; Elass, E.; Pierce, A. Delta-lactoferrin induces cell death via the mitochondrial death signaling pathway by upregulating bax expression, Biometals, Volume 27 (2014) no. 5, pp. 875-889","journal-title":"Biometals"},{"key":"key2025102316371552331_31","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1006\/jmbi.2001.4692","article-title":"Camel lactoferrin, a transferrin-cum-lactoferrin: crystal structure of camel apolactoferrin at 2.6\u2005A resolution and structural basis of its dual role","volume":"309","author":"Khan, J.A.","year":"2001","unstructured":"[31] Khan, J.A.; Kumar, P.; Paramasivam, M.; Yadav, R.S.; Sahani, M.S.; Sharma, S.; Srinivasan, A.; Singh, T.P. Camel lactoferrin, a transferrin-cum-lactoferrin: crystal structure of camel apolactoferrin at 2.6\u2005A resolution and structural basis of its dual role, J. Mol. Biol., Volume 309 (2001), pp. 751-761","journal-title":"J. Mol. Biol."},{"key":"key2025102316371552331_32","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1016\/0022-2836(89)90602-5","article-title":"Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8\u2005A resolution","volume":"209","author":"Anderson, B.F.","year":"1989","unstructured":"[32] Anderson, B.F.; Baker, H.M.; Norris, G.E.; Rice, D.W.; Baker, E.N. Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8\u2005A resolution, J. Mol. Biol., Volume 209 (1989), pp. 711-734","journal-title":"J. Mol. Biol."},{"key":"key2025102316371552331_33","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1107\/S0907444994013521","article-title":"Structure of human diferric lactoferrin refined at 2.2\u2005\u01fa resolution","volume":"51","author":"Haridas, M.","year":"1995","unstructured":"[33] Haridas, M.; Anderson, B.F.; Baker, E.N. Structure of human diferric lactoferrin refined at 2.2\u2005\u01fa resolution, Acta Crystallogr. D Biol. Crystallogr., Volume 51 (1995), pp. 629-646","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"key2025102316371552331_34","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1006\/jmbi.1999.2767","article-title":"Three-dimensional structure of mare diferric lactoferrin at 2.6\u2005A resolution","volume":"289","author":"Sharma, A.K.","year":"1999","unstructured":"[34] Sharma, A.K.; Paramasivam, M.; Srinivasan, A.; Yadav, M.P.; Singh, T.P. Three-dimensional structure of mare diferric lactoferrin at 2.6\u2005A resolution, J. Mol. Biol., Volume 289 (1999), pp. 303-317","journal-title":"J. Mol. Biol."},{"key":"key2025102316371552331_35","doi-asserted-by":"crossref","first-page":"1805","DOI":"10.1107\/S0907444999010951","article-title":"Structure of buffalo lactoferrin at 2.5\u2005A resolution using crystals grown at 303\u2005K shows different orientations of the N and C lobes","volume":"55","author":"Karthikeyan, S.","year":"1999","unstructured":"[35] Karthikeyan, S.; Paramasivam, M.; Yadav, S.; Srinivasan, A.; Singh, T.P. Structure of buffalo lactoferrin at 2.5\u2005A resolution using crystals grown at 303\u2005K shows different orientations of the N and C lobes, Acta Crystallogr. D Biol. Crystallogr., Volume 55 (1999), pp. 1805-1813","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"key2025102316371552331_36","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1038\/nsb1197-919","article-title":"Structure of Haemophilus influenzae Fe(3+)-binding protein reveals convergent evolution within a superfamily","volume":"4","author":"Bruns, C.M.","year":"1997","unstructured":"[36] Bruns, C.M.; Nowalk, A.J.; Arvai, A.S.; McTigue, M.A.; Vaughan, K.G.; Mietzner, T.A.; McRee, D.E. Structure of Haemophilus influenzae Fe(3+)-binding protein reveals convergent evolution within a superfamily, Nat. Struct. Biol., Volume 4 (1997), pp. 919-924","journal-title":"Nat. Struct. Biol."},{"key":"key2025102316371552331_37","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1017\/S0022029998003343","article-title":"Preparation and characterization of the N and C monoferric lobes of buffalo lactoferrin produced by proteolysis using proteinase K","volume":"66","author":"Sharma, S.","year":"1999","unstructured":"[37] Sharma, S.; Singh, T.P.; Bhatia, K.L. Preparation and characterization of the N and C monoferric lobes of buffalo lactoferrin produced by proteolysis using proteinase K, J. Dairy Res., Volume 66 (1999), pp. 81-90","journal-title":"J. Dairy Res."},{"key":"key2025102316371552331_38","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/S0022-2836(03)00717-4","article-title":"Crystal structure of a proteolytically generated functional monoferric C-lobe of bovine lactoferrin at 1.9\u2005A resolution","volume":"331","author":"Sharma, S.","year":"2003","unstructured":"[38] Sharma, S.; Jasti, J.; Kumar, J.; Mohanty, A.K.; Singh, T.P. Crystal structure of a proteolytically generated functional monoferric C-lobe of bovine lactoferrin at 1.9\u2005A resolution, J. Mol. Biol., Volume 331 (2003), pp. 485-496","journal-title":"J. Mol. Biol."},{"key":"key2025102316371552331_39","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1107\/S0907444905016069","article-title":"Structure of the zinc-saturated C-terminal lobe of bovine lactoferrin at 2.0\u2005\u01fa resolution","volume":"61","author":"Jabeen, T.","year":"2005","unstructured":"[39] Jabeen, T.; Sharma, S.; Singh, N.; Bhushan, A.; Singh, T.P. Structure of the zinc-saturated C-terminal lobe of bovine lactoferrin at 2.0\u2005\u01fa resolution, Acta Crystallogr. D Biol. Crystallogr., Volume 61 (2005), pp. 1107-1115","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"key2025102316371552331_40","doi-asserted-by":"crossref","first-page":"784","DOI":"10.1038\/344784a0","article-title":"Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins","volume":"344","author":"Anderson, B.F.","year":"1990","unstructured":"[40] Anderson, B.F.; Baker, H.M.; Norris, G.E.; Rumball, S.V.; Baker, E.N. Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins, Nature, Volume 344 (1990), pp. 784-787","journal-title":"Nature"},{"key":"key2025102316371552331_41","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1023\/B:BIOM.0000027694.40260.70","article-title":"Lactoferrin and iron: structural and dynamic aspects of binding and release","volume":"17","author":"Baker, H.M.","year":"2004","unstructured":"[41] Baker, H.M.; Baker, E.N. Lactoferrin and iron: structural and dynamic aspects of binding and release, Biometals, Volume 17 (2004), pp. 209-216","journal-title":"Biometals"},{"key":"key2025102316371552331_42","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1002\/1097-0134(20001115)41:3<415::AID-PROT130>3.0.CO;2-7","article-title":"Why are \u201cnatively unfolded\u201d proteins unstructured under physiologic conditions?","volume":"41","author":"Uversky, V.N.","year":"2000","unstructured":"[42] Uversky, V.N.; Gillespie, J.R.; Fink, A.L. Why are \u201cnatively unfolded\u201d proteins unstructured under physiologic conditions?, Proteins, Volume 41 (2000), pp. 415-427","journal-title":"Proteins"},{"key":"key2025102316371552331_43","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1006\/jmbi.1999.3110","article-title":"Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm","volume":"293","author":"Wright, P.E.","year":"1999","unstructured":"[43] Wright, P.E.; Dyson, H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm, J. Mol. Biol., Volume 293 (1999), pp. 321-331","journal-title":"J. Mol. Biol."},{"key":"key2025102316371552331_44","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/S1093-3263(00)00138-8","article-title":"Intrinsically disordered protein","volume":"19","author":"Dunker, A.K.","year":"2001","unstructured":"[44] Dunker, A.K.; Lawson, J.D.; Brown, C.J.; Williams, R.M.; Romero, P.; Oh, J.S.; Oldfield, C.J.; Campen, A.M.; Ratliff, C.M.; Hipps, K.W. et al. Intrinsically disordered protein, J. Mol. Graph. Model., Volume 19 (2001), pp. 26-59","journal-title":"J. Mol. Graph. Model."},{"key":"key2025102316371552331_45","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1016\/S0968-0004(02)02169-2","article-title":"Intrinsically unstructured proteins","volume":"27","author":"Tompa, P.","year":"2002","unstructured":"[45] Tompa, P. Intrinsically unstructured proteins, Trends Biochem. Sci., Volume 27 (2002), pp. 527-533","journal-title":"Trends Biochem. Sci."},{"key":"key2025102316371552331_46","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1016\/j.bbapap.2010.01.017","article-title":"Understanding protein non-folding","volume":"1804","author":"Uversky, V.N.","year":"2010","unstructured":"[46] Uversky, V.N.; Dunker, A.K. Understanding protein non-folding, Biochim. Biophys. Acta, Volume 1804 (2010), pp. 1231-1264","journal-title":"Biochim. Biophys. Acta"},{"key":"key2025102316371552331_47","doi-asserted-by":"crossref","first-page":"1011","DOI":"10.1006\/jmbi.2001.4750","article-title":"Calculation of ensembles of structures representing the unfolded state of an SH3 domain","volume":"308","author":"Choy, W.Y.","year":"2001","unstructured":"[47] Choy, W.Y.; Forman-Kay, J.D. Calculation of ensembles of structures representing the unfolded state of an SH3 domain, J. Mol. Biol., Volume 308 (2001), pp. 1011-1032","journal-title":"J. Mol. Biol."},{"key":"key2025102316371552331_48","doi-asserted-by":"crossref","first-page":"e1000155","DOI":"10.1371\/journal.pcbi.1000155","article-title":"The effect of a DeltaK280 mutation on the unfolded state of a microtubule-binding repeat in Tau","volume":"4","author":"Huang, A.","year":"2008","unstructured":"[48] Huang, A.; Stultz, C.M. The effect of a DeltaK280 mutation on the unfolded state of a microtubule-binding repeat in Tau, PLoS Comput. Biol., Volume 4 (2008), p. e1000155","journal-title":"PLoS Comput. Biol."},{"key":"key2025102316371552331_49","doi-asserted-by":"crossref","first-page":"8390","DOI":"10.1073\/pnas.0507916103","article-title":"Alternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organisms","volume":"103","author":"Romero, P.R.","year":"2006","unstructured":"[49] Romero, P.R.; Zaidi, S.; Fang, Y.Y.; Uversky, V.N.; Radivojac, P.; Oldfield, C.J.; Cortese, M.S.; Sickmeier, M.; LeGall, T.; Obradovic, Z.; Dunker, A.K. Alternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organisms, Proc. Natl. Acad. Sci. USA, Volume 103 (2006), pp. 8390-8395","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"key2025102316371552331_50","doi-asserted-by":"crossref","first-page":"S1","DOI":"10.1186\/1471-2164-9-S1-S1","article-title":"Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners","volume":"9Suppl1","author":"Oldfield, C.J.","year":"2008","unstructured":"[50] Oldfield, C.J.; Meng, J.; Yang, J.Y.; Yang, M.Q.; Uversky, V.N.; Dunker, A.K. Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners, BMC Genomics, Volume 9Suppl1 (2008), p. S1","journal-title":"BMC Genomics"},{"key":"key2025102316371552331_51","doi-asserted-by":"crossref","first-page":"4191","DOI":"10.2174\/1381612811319230005","article-title":"Intrinsic disorder-based protein interactions and their modulators","volume":"19","author":"Uversky, V.N.","year":"2013","unstructured":"[51] Uversky, V.N. Intrinsic disorder-based protein interactions and their modulators, Curr. Pharm. Des., Volume 19 (2013), pp. 4191-4213","journal-title":"Curr. Pharm. Des."},{"key":"key2025102316371552331_52","first-page":"1","article-title":"The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure F1000","volume":"5","author":"Uversky, V.N.","year":"2013","unstructured":"[52] Uversky, V.N.; Dunker, A.K. The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure F1000, Biol. Rep., Volume 5 (2013), p. 1","journal-title":"Biol. Rep."},{"key":"key2025102316371552331_53","doi-asserted-by":"crossref","DOI":"10.1146\/annurev-biochem-072711-164947","article-title":"Intrinsically disordered proteins and intrinsically disordered protein regions","author":"Oldfield, C.J.","year":"2014","unstructured":"[53] Oldfield, C.J.; Dunker, A.K. Intrinsically disordered proteins and intrinsically disordered protein regions, Annu. Rev. Biochem. (2014)","journal-title":"Annu. Rev. Biochem."},{"key":"key2025102316371552331_54","first-page":"161","article-title":"Intrinsic protein disorder in complete genomes","volume":"11","author":"Dunker, A.K.","year":"2000","unstructured":"[54] Dunker, A.K.; Obradovic, Z.; Romero, P.; Garner, E.C.; Brown, C.J. Intrinsic protein disorder in complete genomes, Gen. Inform. Ser. Workshop, Volume 11 (2000), pp. 161-171","journal-title":"Gen. Inform. Ser. Workshop"},{"key":"key2025102316371552331_55","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.tibs.2008.10.009","article-title":"Do viral proteins possess unique biophysical features?","volume":"34","author":"Tokuriki, N.","year":"2009","unstructured":"[55] Tokuriki, N.; Oldfield, C.J.; Uversky, V.N.; Berezovsky, I.N.; Tawfik, D.S. Do viral proteins possess unique biophysical features?, Trends Biochem. Sci., Volume 34 (2009), pp. 53-59","journal-title":"Trends Biochem. Sci."},{"key":"key2025102316371552331_56","doi-asserted-by":"crossref","first-page":"568068","DOI":"10.1155\/2010\/568068","article-title":"The mysterious unfoldome: structureless, underappreciated, yet vital part of any given proteome","volume":"2010","author":"Uversky, V.N.","year":"2010","unstructured":"[56] Uversky, V.N. The mysterious unfoldome: structureless, underappreciated, yet vital part of any given proteome, J. Biomed. Biotechnol., Volume 2010 (2010), p. 568068","journal-title":"J. Biomed. Biotechnol."},{"key":"key2025102316371552331_57","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1016\/j.jmb.2004.02.002","article-title":"Prediction and functional analysis of native disorder in proteins from the three kingdoms of life","volume":"337","author":"Ward, J.J.","year":"2004","unstructured":"[57] Ward, J.J.; Sodhi, J.S.; McGuffin, L.J.; Buxton, B.F.; Jones, D.T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life, J. Mol. Biol., Volume 337 (2004), pp. 635-645","journal-title":"J. Mol. Biol."},{"key":"key2025102316371552331_58","doi-asserted-by":"crossref","first-page":"1211","DOI":"10.1007\/s00018-011-0859-3","article-title":"Protein intrinsic disorder as a flexible armor and a weapon of HIV-1","volume":"69","author":"Xue, B.","year":"2012","unstructured":"[58] Xue, B.; Mizianty, M.J.; Kurgan, L.; Uversky, V.N. Protein intrinsic disorder as a flexible armor and a weapon of HIV-1, Cell. Mol. Life Sci., Volume 69 (2012), pp. 1211-1259","journal-title":"Cell. Mol. Life Sci."},{"issue":"Suppl. 1","key":"key2025102316371552331_59","doi-asserted-by":"crossref","first-page":"S1","DOI":"10.1186\/1752-0509-4-S1-S1","article-title":"Archaic chaos: intrinsically disordered proteins in Archaea","volume":"4","author":"Xue, B.","year":"2010","unstructured":"[59] Xue, B.; Williams, R.W.; Oldfield, C.J.; Dunker, A.K.; Uversky, V.N. Archaic chaos: intrinsically disordered proteins in Archaea, BMC Syst. Biol., Volume 4 (2010) no. Suppl. 1, p. S1","journal-title":"BMC Syst. Biol."},{"key":"key2025102316371552331_60","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1002\/jmr.747","article-title":"Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling","volume":"18","author":"Uversky, V.N.","year":"2005","unstructured":"[60] Uversky, V.N.; Oldfield, C.J.; Dunker, A.K. Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling, J. Mol. Recognit., Volume 18 (2005), pp. 343-384","journal-title":"J. Mol. Recognit."},{"key":"key2025102316371552331_61","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/S0065-3233(02)62004-2","article-title":"Identification and functions of usefully disordered proteins","volume":"62","author":"Dunker, A.K.","year":"2002","unstructured":"[61] Dunker, A.K.; Brown, C.J.; Obradovic, Z. Identification and functions of usefully disordered proteins, Adv. Protein Chem., Volume 62 (2002), pp. 25-49","journal-title":"Adv. Protein Chem."},{"key":"key2025102316371552331_62","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1002\/pro.2207","article-title":"Exploring the binding diversity of intrinsically disordered proteins involved in one-to-many binding","volume":"22","author":"Hsu, W.L.","year":"2013","unstructured":"[62] Hsu, W.L.; Oldfield, C.J.; Xue, B.; Meng, J.; Huang, F.; Romero, P.; Uversky, V.N.; Dunker, A.K. Exploring the binding diversity of intrinsically disordered proteins involved in one-to-many binding, Protein Sci., Volume 22 (2013), pp. 258-273","journal-title":"Protein Sci."},{"issue":"Suppl.\u00a01","key":"key2025102316371552331_63","doi-asserted-by":"crossref","first-page":"S12","DOI":"10.1186\/1471-2164-10-S1-S12","article-title":"Protein disorder in the human diseasome: unfoldomics of human genetic diseases","volume":"10","author":"Midic, U.","year":"2009","unstructured":"[63] Midic, U.; Oldfield, C.J.; Dunker, A.K.; Obradovic, Z.; Uversky, V.N. Protein disorder in the human diseasome: unfoldomics of human genetic diseases, BMC Genomics, Volume 10 (2009) no. Suppl.\u00a01, p. S12","journal-title":"BMC Genomics"},{"key":"key2025102316371552331_64","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.2174\/092986609789839377","article-title":"Unfoldomics of human genetic diseases: illustrative examples of ordered and intrinsically disordered members of the human diseasome","volume":"16","author":"Midic, U.","year":"2009","unstructured":"[64] Midic, U.; Oldfield, C.J.; Dunker, A.K.; Obradovic, Z.; Uversky, V.N. Unfoldomics of human genetic diseases: illustrative examples of ordered and intrinsically disordered members of the human diseasome, Protein Pept. Lett., Volume 16 (2009), pp. 1533-1547","journal-title":"Protein Pept. Lett."},{"key":"key2025102316371552331_65","doi-asserted-by":"crossref","first-page":"5188","DOI":"10.2741\/3594","article-title":"Intrinsic disorder in proteins associated with neurodegenerative diseases","volume":"14","author":"Uversky, V.N.","year":"2009","unstructured":"[65] Uversky, V.N. Intrinsic disorder in proteins associated with neurodegenerative diseases, Front. Biosci., Volume 14 (2009), pp. 5188-5238","journal-title":"Front. Biosci."},{"key":"key2025102316371552331_66","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1517\/17460441.2012.686489","article-title":"Intrinsically disordered proteins and novel strategies for drug discovery","volume":"7","author":"Uversky, V.N.","year":"2012","unstructured":"[66] Uversky, V.N. Intrinsically disordered proteins and novel strategies for drug discovery, Expert Opin. Drug Discov., Volume 7 (2012), pp. 475-488","journal-title":"Expert Opin. Drug Discov."},{"key":"key2025102316371552331_67","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1146\/annurev.biophys.37.032807.125924","article-title":"Intrinsically disordered proteins in human diseases: introducing the D2 concept","volume":"37","author":"Uversky, V.N.","year":"2008","unstructured":"[67] Uversky, V.N.; Oldfield, C.J.; Dunker, A.K. Intrinsically disordered proteins in human diseases: introducing the D2 concept, Annu. Rev. Biophys., Volume 37 (2008), pp. 215-246","journal-title":"Annu. Rev. Biophys."},{"issue":"Suppl.\u00a01","key":"key2025102316371552331_68","doi-asserted-by":"crossref","first-page":"S7","DOI":"10.1186\/1471-2164-10-S1-S7","article-title":"Unfoldomics of human diseases: linking protein intrinsic disorder with diseases","volume":"10","author":"Uversky, V.N.","year":"2009","unstructured":"[68] Uversky, V.N.; Oldfield, C.J.; Midic, U.; Xie, H.; Xue, B.; Vucetic, S.; Iakoucheva, L.M.; Obradovic, Z.; Dunker, A.K. Unfoldomics of human diseases: linking protein intrinsic disorder with diseases, BMC Genomics, Volume 10 (2009) no. Suppl.\u00a01, p. S7","journal-title":"BMC Genomics"},{"issue":"13","key":"key2025102316371552331_69","doi-asserted-by":"crossref","first-page":"6844","DOI":"10.1021\/cr400713r","article-title":"Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases","volume":"114","author":"Uversky, V.N.","year":"2014","unstructured":"[69] Uversky, V.N.; Dave, V.; Iakoucheva, L.M.; Malaney, P.; Metallo, S.J.; Pathak, R.R.; Joerger, A.C. Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases, Chem. Rev., Volume 114 (2014) no. 13, pp. 6844-6879","journal-title":"Chem. Rev."},{"key":"key2025102316371552331_70","doi-asserted-by":"crossref","first-page":"1829","DOI":"10.1021\/pr0602388","article-title":"Protein intrinsic disorder and human papillomaviruses: increased amount of disorder in E6 and E7 oncoproteins from high risk HPVs","volume":"5","author":"Uversky, V.N.","year":"2006","unstructured":"[70] Uversky, V.N.; Roman, A.; Oldfield, C.J.; Dunker, A.K. Protein intrinsic disorder and human papillomaviruses: increased amount of disorder in E6 and E7 oncoproteins from high risk HPVs, J. Proteome Res., Volume 5 (2006), pp. 1829-1842","journal-title":"J. Proteome Res."},{"key":"key2025102316371552331_71","doi-asserted-by":"crossref","first-page":"932","DOI":"10.2174\/092986610791498984","article-title":"Viral disorder or disordered viruses: do viral proteins possess unique features?","volume":"17","author":"Xue, B.","year":"2010","unstructured":"[71] Xue, B.; Williams, R.W.; Oldfield, C.J.; Goh, G.K.; Dunker, A.K.; Uversky, V.N. Viral disorder or disordered viruses: do viral proteins possess unique features?, Protein Pept. Lett., Volume 17 (2010), pp. 932-951","journal-title":"Protein Pept. Lett."},{"key":"key2025102316371552331_72","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1093\/gbe\/evt026","article-title":"Rapid evolutionary dynamics of structural disorder as a potential driving force for biological divergence in flaviviruses","volume":"5","author":"Ortiz, J.F.","year":"2013","unstructured":"[72] Ortiz, J.F.; MacDonald, M.L.; Masterson, P.; Uversky, V.N.; Siltberg-Liberles, J. Rapid evolutionary dynamics of structural disorder as a potential driving force for biological divergence in flaviviruses, Genome Biol. Evol., Volume 5 (2013), pp. 504-513","journal-title":"Genome Biol. Evol."},{"key":"key2025102316371552331_73","doi-asserted-by":"crossref","first-page":"1274","DOI":"10.2174\/13816128113199990072","article-title":"Disordered interactome of human papillomavirus","volume":"20","author":"Xue, B.","year":"2014","unstructured":"[73] Xue, B.; Ganti, K.; Rabionet, A.; Banks, L.; Uversky, V.N. Disordered interactome of human papillomavirus, Curr. Pharm. Des., Volume 20 (2014), pp. 1274-1292","journal-title":"Curr. Pharm. Des."},{"key":"key2025102316371552331_74","doi-asserted-by":"crossref","first-page":"1345","DOI":"10.1039\/C4MB00027G","article-title":"The intrinsic disorder status of the human hepatitis C virus proteome","volume":"10","author":"Fan, X.","year":"2014","unstructured":"[74] Fan, X.; Xue, B.; Dolan, P.T.; Lacount, D.J.; Kurgan, L.; Uversky, V.N. The intrinsic disorder status of the human hepatitis C virus proteome, Mol. Biosyst., Volume 10 (2014), pp. 1345-1363","journal-title":"Mol. Biosyst."},{"issue":"13","key":"key2025102316371552331_75","doi-asserted-by":"crossref","first-page":"6880","DOI":"10.1021\/cr4005692","article-title":"Structural disorder in viral proteins","volume":"114","author":"Xue, B.","year":"2014","unstructured":"[75] Xue, B.; Blocquel, D.; Habchi, J.; Uversky, A.V.; Kurgan, L.; Uversky, V.N.; Longhi, S. Structural disorder in viral proteins, Chem. Rev., Volume 114 (2014) no. 13, pp. 6880-6911","journal-title":"Chem. Rev."},{"key":"key2025102316371552331_76","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1039\/b719168e","article-title":"Intrinsic disorder in pathogenic and non-pathogenic microbes: discovering and analyzing the unfoldomes of early-branching eukaryotes","volume":"4","author":"Mohan, A.","year":"2008","unstructured":"[76] Mohan, A.; Sullivan, W.J. Jr.; Radivojac, P.; Dunker, A.K.; Uversky, V.N. Intrinsic disorder in pathogenic and non-pathogenic microbes: discovering and analyzing the unfoldomes of early-branching eukaryotes, Mol. Biosyst., Volume 4 (2008), pp. 328-340","journal-title":"Mol. Biosyst."},{"key":"key2025102316371552331_77","doi-asserted-by":"crossref","first-page":"e9762","DOI":"10.1371\/journal.pone.0097625","article-title":"Identifying novel cell cycle proteins in apicomplexa parasites through co-expression decision analysis","volume":"9","author":"Butler, C.L.","year":"2014","unstructured":"[77] Butler, C.L.; Lucas, O.; Wuchty, S.; Xue, B.; Uversky, V.N.; White, M. Identifying novel cell cycle proteins in apicomplexa parasites through co-expression decision analysis, PLoS One, Volume 9 (2014), p. e9762-e9765","journal-title":"PLoS One"},{"key":"key2025102316371552331_78","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1016\/j.jmb.2013.10.030","article-title":"Intrinsic disorder in proteins involved in the innate antiviral immunity: another flexible side of a molecular arms race","volume":"426","author":"Xue, B.","year":"2014","unstructured":"[78] Xue, B.; Uversky, V.N. Intrinsic disorder in proteins involved in the innate antiviral immunity: another flexible side of a molecular arms race, J. Mol. Biol., Volume 426 (2014), pp. 1322-1330","journal-title":"J. Mol. Biol."},{"key":"key2025102316371552331_79","doi-asserted-by":"crossref","first-page":"D508","DOI":"10.1093\/nar\/gks1226","article-title":"D(2)P(2): database of disordered protein predictions","volume":"41","author":"Oates, M.E.","year":"2013","unstructured":"[79] Oates, M.E.; Romero, P.; Ishida, T.; Ghalwash, M.; Mizianty, M.J.; Xue, B.; Dosztanyi, Z.; Uversky, V.N.; Obradovic, Z.; Kurgan, L. et al. D(2)P(2): database of disordered protein predictions, Nucleic Acids Res., Volume 41 (2013), p. D508-D516","journal-title":"Nucleic Acids Res."},{"key":"key2025102316371552331_80","doi-asserted-by":"crossref","first-page":"36099","DOI":"10.1074\/jbc.M109.036426","article-title":"A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency","volume":"284","author":"Duchardt, F.","year":"2009","unstructured":"[80] Duchardt, F.; Ruttekolk, I.R.; Verdurmen, W.P.; Lortat-Jacob, H.; Burck, J.; Hufnagel, H.; Fischer, R.; van den Heuvel, M.; Lowik, D.W.; Vuister, G.W. et al. A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency, J. Biol. Chem., Volume 284 (2009), pp. 36099-36100","journal-title":"J. Biol. Chem."},{"key":"key2025102316371552331_81","doi-asserted-by":"crossref","first-page":"4288","DOI":"10.1021\/bi972323m","article-title":"Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin","volume":"37","author":"Hwang, P.M.","year":"1998","unstructured":"[81] Hwang, P.M.; Zhou, N.; Shan, X.; Arrowsmith, C.H.; Vogel, H.J. Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin, Biochemistry, Volume 37 (1998), pp. 4288-4290","journal-title":"Biochemistry"},{"key":"key2025102316371552331_82","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1023\/B:BIOM.0000027695.99874.ea","article-title":"Molecular dynamics simulations of bovine lactoferricin: turning a helix into a sheet","volume":"17","author":"Zhou, N.","year":"2004","unstructured":"[82] Zhou, N.; Tieleman, D.P.; Vogel, H.J. Molecular dynamics simulations of bovine lactoferricin: turning a helix into a sheet, Biometals, Volume 17 (2004), pp. 217-223","journal-title":"Biometals"},{"key":"key2025102316371552331_83","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1002\/prot.21285","article-title":"Analysis of chameleon sequences and their implications in biological processes","volume":"67","author":"Guo, J.T.","year":"2007","unstructured":"[83] Guo, J.T.; Jaromczyk, J.W.; Xu, Y. Analysis of chameleon sequences and their implications in biological processes, Proteins, Volume 67 (2007), pp. 548-558","journal-title":"Proteins"},{"key":"key2025102316371552331_84","doi-asserted-by":"crossref","first-page":"367","DOI":"10.6026\/97320630003367","article-title":"Analysis of protein chameleon sequence characteristics","volume":"3","author":"Ghozlane, A.","year":"2009","unstructured":"[84] Ghozlane, A.; Joseph, A.P.; Bornot, A.; de Brevern, A.G. Analysis of protein chameleon sequence characteristics, Bioinformation, Volume 3 (2009), pp. 367-369","journal-title":"Bioinformation"},{"key":"key2025102316371552331_85","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1002\/pro.590","article-title":"Discordant and chameleon sequences: their distribution and implications for amyloidogenicity","volume":"20","author":"Gendoo, D.M.","year":"2011","unstructured":"[85] Gendoo, D.M.; Harrison, P.M. Discordant and chameleon sequences: their distribution and implications for amyloidogenicity, Protein Sci., Volume 20 (2011), pp. 567-579","journal-title":"Protein Sci."},{"key":"key2025102316371552331_86","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/j.ijbiomac.2011.04.017","article-title":"Certain heptapeptide and large sequences representing an entire helix, strand or coil conformation in proteins are associated as chameleon sequences","volume":"49","author":"Krishna, N.","year":"2011","unstructured":"[86] Krishna, N.; Guruprasad K: Certain heptapeptide and large sequences representing an entire helix, strand or coil conformation in proteins are associated as chameleon sequences, Int. J. Biol. Macromol., Volume 49 (2011), pp. 218-222","journal-title":"Int. J. Biol. Macromol."},{"key":"key2025102316371552331_87","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1139\/o01-230","article-title":"Bovine lactoferrin and lactoferricin derived from milk: production and applications","volume":"80","author":"Tomita, M.","year":"2002","unstructured":"[87] Tomita, M.; Wakabayashi, H.; Yamauchi, K.; Teraguchi, S.; Hayasawa, H. Bovine lactoferrin and lactoferricin derived from milk: production and applications, Biochem. Cell Biol., Volume 80 (2002), pp. 109-112","journal-title":"Biochem. Cell Biol."},{"key":"key2025102316371552331_88","doi-asserted-by":"crossref","first-page":"1457","DOI":"10.1111\/j.1939-1676.2006.tb00766.x","article-title":"Serum lactoferrin and immunoglobulin G concentrations in healthy or ill neonatal foals and healthy adult horses","volume":"20","author":"Barton, M.H.","year":"2006","unstructured":"[88] Barton, M.H.; Hurley, D.; Norton, N.; Heusner, G.; Costa, L.; Jones, S.; Byars, D.; Watanabe, K. Serum lactoferrin and immunoglobulin G concentrations in healthy or ill neonatal foals and healthy adult horses, J. Vet. Intern. Med., Volume 20 (2006), pp. 1457-1462","journal-title":"J. Vet. Intern. Med."},{"key":"key2025102316371552331_89","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1080\/15321810701454839","article-title":"Camel lactoferrin markedly inhibits hepatitis C virus genotype 4 infection of human peripheral blood leukocytes","volume":"28","author":"Redwan el, R.M.","year":"2007","unstructured":"[89] Redwan el, R.M.; Tabll, A. Camel lactoferrin markedly inhibits hepatitis C virus genotype 4 infection of human peripheral blood leukocytes, J. Immunoassay Immunochem., Volume 28 (2007), pp. 267-277","journal-title":"J. Immunoassay Immunochem."},{"key":"key2025102316371552331_90","doi-asserted-by":"crossref","first-page":"8802","DOI":"10.1074\/jbc.272.13.8802","article-title":"Characterization of recombinant human lactoferrin secreted in milk of transgenic mice","volume":"272","author":"Nuijens, J.H.","year":"1997","unstructured":"[90] Nuijens, J.H.; van Berkel, P.H.; Geerts, M.E.; Hartevelt, P.P.; de Boer, H.A.; van Veen, H.A.; Pieper, F.R. Characterization of recombinant human lactoferrin secreted in milk of transgenic mice, J. Biol. Chem., Volume 272 (1997), pp. 8802-8807","journal-title":"J. Biol. Chem."},{"key":"key2025102316371552331_91","first-page":"101","article-title":"Potential activity of camel milk-amylase and lactoferrin against hepatitis C virus infectivity in HepG2 and lymphocytes","volume":"8","author":"El-Fakharany, E.M.","year":"2008","unstructured":"[91] El-Fakharany, E.M.; Tabll, A.; Abd El-Wahab, A.; Haroun, B.M.; Redwan, E.M. Potential activity of camel milk-amylase and lactoferrin against hepatitis C virus infectivity in HepG2 and lymphocytes, Hepat. Mon., Volume 8 (2008), pp. 101-109","journal-title":"Hepat. Mon."},{"key":"key2025102316371552331_92","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1099\/jmm.0.033894-0","article-title":"Inhibitory effects of native and recombinant full-length camel lactoferrin and its N and C lobes on hepatitis C virus infection of Huh7.5 cells","volume":"61","author":"Liao, Y.","year":"2012","unstructured":"[92] Liao, Y.; El-Fakkarany, E.; Lonnerdal, B.; Redwan, E.M. Inhibitory effects of native and recombinant full-length camel lactoferrin and its N and C lobes on hepatitis C virus infection of Huh7.5 cells, J. Med. Microbiol., Volume 61 (2012), pp. 375-383","journal-title":"J. Med. Microbiol."},{"key":"key2025102316371552331_93","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1016\/j.biotechadv.2010.07.002","article-title":"Recombinant human lactoferrin: a valuable protein for pharmaceutical products and functional foods","volume":"28","author":"Conesa, C.","year":"2010","unstructured":"[93] Conesa, C.; Calvo, M.; Sanchez, L. Recombinant human lactoferrin: a valuable protein for pharmaceutical products and functional foods, Biotechnol. Adv., Volume 28 (2010), pp. 831-838","journal-title":"Biotechnol. Adv."},{"issue":"Pt 2","key":"key2025102316371552331_94","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1042\/bj2760349","article-title":"Expression of cloned human lactoferrin in baby-hamster kidney cells","volume":"276","author":"Stowell, K.M.","year":"1991","unstructured":"[94] Stowell, K.M.; Rado, T.A.; Funk, W.D.; Tweedie, J.W. Expression of cloned human lactoferrin in baby-hamster kidney cells, Biochem. J., Volume 276 (1991) no. Pt 2, pp. 349-355","journal-title":"Biochem. J."},{"issue":"9","key":"key2025102316371552331_95","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1002\/cbin.10304","article-title":"Plant-based biopharming of recombinant human lactoferrin","volume":"38","author":"Yemets, A.I.","year":"2014","unstructured":"[95] Yemets, A.I.; Tanasienko, I.V.; Krasylenko, Y.A.; Blume YB: Plant-based biopharming of recombinant human lactoferrin, Cell Biol. Int., Volume 38 (2014) no. 9, pp. 989-1002","journal-title":"Cell Biol. Int."},{"key":"key2025102316371552331_96","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1016\/j.bbagen.2011.06.018","article-title":"Lactoferrin a multiple bioactive protein: an overview","volume":"1820","author":"Garcia-Montoya, I.A.","year":"2012","unstructured":"[96] Garcia-Montoya, I.A.; Cendon, T.S.; Arevalo-Gallegos, S.; Rascon-Cruz, Q. Lactoferrin a multiple bioactive protein: an overview, Biochim. Biophys. Acta, Volume 1820 (2012), pp. 226-236","journal-title":"Biochim. Biophys. Acta"},{"key":"key2025102316371552331_97","doi-asserted-by":"crossref","first-page":"e301","DOI":"10.1016\/j.ijantimicag.2008.07.020","article-title":"Lactoferrin: structure, function and applications","volume":"33","author":"Gonzalez-Chavez, S.A.","year":"2009","unstructured":"[97] Gonzalez-Chavez, S.A.; Arevalo-Gallegos, S.; Rascon-Cruz, Q. Lactoferrin: structure, function and applications, Int. J. Antimicrob. Agents, Volume 33 (2009), p. e301-e308","journal-title":"Int. J. Antimicrob. Agents"},{"key":"key2025102316371552331_98","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1046\/j.1365-3083.2003.01162.x","article-title":"Anti-inflammatory activities of human lactoferrin in acute dextran sulphate-induced colitis in mice","volume":"57","author":"Haversen, L.A.","year":"2003","unstructured":"[98] Haversen, L.A.; Baltzer, L.; Dolphin, G.; Hanson, L.A.; Mattsby-Baltzer, I. Anti-inflammatory activities of human lactoferrin in acute dextran sulphate-induced colitis in mice, Scand. J. Immunol., Volume 57 (2003), pp. 2-10","journal-title":"Scand. J. Immunol."},{"key":"key2025102316371552331_99","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1016\/S0161-5890(03)00152-4","article-title":"Lactoferrin\u00a0\u2013\u00a0a multifunctional protein with antimicrobial properties","volume":"40","author":"Farnaud, S.","year":"2003","unstructured":"[99] Farnaud, S.; Evans, R.W. Lactoferrin\u00a0\u2013\u00a0a multifunctional protein with antimicrobial properties, Mol. Immunol., Volume 40 (2003), pp. 395-405","journal-title":"Mol. Immunol."},{"key":"key2025102316371552331_100","first-page":"199","author":"Valenti, P.","year":"1998","unstructured":"[100] Valenti, P.; Marchetti, M.; Superti, F.; Ammendolia, M.G.; Puddu, P.; Gessani, S.; Borghi, P.; Belardelli, F.; Antonini, G.; Seganti, L.; Spik, G.; Legrand, D. Mazurier Antiviral activity of lactoferrin (Pierce, J.; Perraudin, A.J.P., eds.), Advances in lactoferrin research, Plenum Press, New York, 1998, pp. 199-203","journal-title":"Mazurier Antiviral activity of lactoferrin"},{"key":"key2025102316371552331_101","doi-asserted-by":"crossref","first-page":"2576","DOI":"10.1007\/s00018-005-5372-0","article-title":"Lactoferrin: an important host defence against microbial and viral attack","volume":"62","author":"Valenti, P.","year":"2005","unstructured":"[101] Valenti, P.; Antonini, G. Lactoferrin: an important host defence against microbial and viral attack, Cell. Mol. Life Sci., Volume 62 (2005), pp. 2576-2587","journal-title":"Cell. Mol. Life Sci."},{"key":"key2025102316371552331_102","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1139\/m89-174","article-title":"Bactericidal effect of lactoferrin on <span class=\"italique\">Legionella pneumophila<\/span>: effect of the physiological state of the organism","volume":"35","author":"Bortner, C.A.","year":"1989","unstructured":"[102] Bortner, C.A.; Arnold, R.R.; Miller, R.D. Bactericidal effect of lactoferrin on Legionella pneumophila: effect of the physiological state of the organism, Can. J. Microbiol., Volume 35 (1989), pp. 1048-1051","journal-title":"Can. J. Microbiol."},{"key":"key2025102316371552331_103","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1128\/iai.51.2.373-377.1986","article-title":"Bactericidal effect of lactoferrin on <span class=\"italique\">Legionella pneumophila<\/span>","volume":"51","author":"Bortner, C.A.","year":"1986","unstructured":"[103] Bortner, C.A.; Miller, R.D.; Arnold, R.R. Bactericidal effect of lactoferrin on Legionella pneumophila, Infect. Immunol., Volume 51 (1986), pp. 373-377","journal-title":"Infect. Immunol."},{"key":"key2025102316371552331_104","first-page":"291","article-title":"Bovine lactoferrin: benefits and mechanism of action against infections","volume":"84","author":"Yamauchi, K.","year":"2006","unstructured":"[104] Yamauchi, K.; Wakabayashi, H.; Shin, K.; Takase, M. Bovine lactoferrin: benefits and mechanism of action against infections, Biochem. Cell Biol., Volume 84 (2006), pp. 291-296","journal-title":"Biochem. Cell Biol."},{"key":"key2025102316371552331_105","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1023\/B:BIOM.0000027706.51112.62","article-title":"Neonatal small bowel epithelia: enhancing anti-bacterial defense with lactoferrin and Lactobacillus GG","volume":"17","author":"Sherman, M.P.","year":"2004","unstructured":"[105] Sherman, M.P.; Bennett, S.H.; Hwang, F.F.; Yu, C. Neonatal small bowel epithelia: enhancing anti-bacterial defense with lactoferrin and Lactobacillus GG, Biometals, Volume 17 (2004), pp. 285-289","journal-title":"Biometals"},{"key":"key2025102316371552331_106","first-page":"4184","article-title":"Protective influence of lactoferrin on mice infected with the polycythemia-inducing strain of Friend virus complex","volume":"47","author":"Lu, L.","year":"1987","unstructured":"[106] Lu, L.; Hangoc, G.; Oliff, A.; Chen, L.T.; Shen, R.N.; Broxmeyer, H.E. Protective influence of lactoferrin on mice infected with the polycythemia-inducing strain of Friend virus complex, Cancer Res., Volume 47 (1987), pp. 4184-4188","journal-title":"Cancer Res."},{"key":"key2025102316371552331_107","doi-asserted-by":"crossref","first-page":"73","DOI":"10.7883\/yoken1952.47.73","article-title":"Inhibition with lactoferrin of in vitro infection with human herpes virus","volume":"47","author":"Hasegawa, K.","year":"1994","unstructured":"[107] Hasegawa, K.; Motsuchi, W.; Tanaka, S.; Dosako, S. Inhibition with lactoferrin of in vitro infection with human herpes virus, Jpn. J. Med. Sci. Biol., Volume 47 (1994), pp. 73-85","journal-title":"Jpn. J. Med. Sci. Biol."},{"key":"key2025102316371552331_108","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/S1386-6346(02)00088-8","article-title":"Lactoferrin inhibits hepatitis B virus infection in cultured human hepatocytes","volume":"24","author":"Hara, K.","year":"2002","unstructured":"[108] Hara, K.; Ikeda, M.; Saito, S.; Matsumoto, S.; Numata, K.; Kato, N.; Tanaka, K.; Sekihara, H. Lactoferrin inhibits hepatitis B virus infection in cultured human hepatocytes, Hepatol. Res., Volume 24 (2002), p. 228","journal-title":"Hepatol. Res."},{"key":"key2025102316371552331_109","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1002\/jmv.20171","article-title":"Anti-HSV activity of lactoferrin and lactoferricin is dependent on the presence of heparan sulphate at the cell surface","volume":"74","author":"Andersen, J.H.","year":"2004","unstructured":"[109] Andersen, J.H.; Jenssen, H.; Sandvik, K.; Gutteberg, T.J. Anti-HSV activity of lactoferrin and lactoferricin is dependent on the presence of heparan sulphate at the cell surface, J. Med. Virol., Volume 74 (2004), pp. 262-271","journal-title":"J. Med. Virol."},{"key":"key2025102316371552331_110","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1016\/j.virol.2005.01.010","article-title":"Antiviral activity of human lactoferrin: inhibition of alphavirus interaction with heparan sulfate","volume":"333","author":"Waarts, B.L.","year":"2005","unstructured":"[110] Waarts, B.L.; Aneke, O.J.; Smit, J.M.; Kimata, K.; Bittman, R.; Meijer, D.K.; Wilschut, J. Antiviral activity of human lactoferrin: inhibition of alphavirus interaction with heparan sulfate, Virology, Volume 333 (2005), pp. 284-292","journal-title":"Virology"},{"key":"key2025102316371552331_111","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1186\/1743-422X-10-199","article-title":"Effectiveness of human, camel, bovine and sheep lactoferrin on the hepatitis C virus cellular infectivity: comparison study","volume":"10","author":"El-Fakharany, E.M.","year":"2013","unstructured":"[111] El-Fakharany, E.M.; Sanchez, L.; Al-Mehdar, H.A.; Redwan, E.M. Effectiveness of human, camel, bovine and sheep lactoferrin on the hepatitis C virus cellular infectivity: comparison study, Virol. J., Volume 10 (2013), p. 199","journal-title":"Virol. J."},{"key":"key2025102316371552331_112","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1046\/j.1463-5224.2003.00301.x","article-title":"Effects of bovine lactoferrin on in vitro replication of feline herpesvirus","volume":"6","author":"Beaumont, S.L.","year":"2003","unstructured":"[112] Beaumont, S.L.; Maggs, D.J.; Clarke, H.E. Effects of bovine lactoferrin on in vitro replication of feline herpesvirus, Vet. Ophthalmol., Volume 6 (2003), pp. 245-250","journal-title":"Vet. Ophthalmol."},{"key":"key2025102316371552331_113","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1023\/B:BIOM.0000027707.82911.be","article-title":"The antiviral activity of the milk protein lactoferrin against the human immunodeficiency virus type 1","volume":"17","author":"Berkhout, B.","year":"2004","unstructured":"[113] Berkhout, B.; Floris, R.; Recio, I.; Visser, S. The antiviral activity of the milk protein lactoferrin against the human immunodeficiency virus type 1, Biometals, Volume 17 (2004), pp. 291-294","journal-title":"Biometals"},{"key":"key2025102316371552331_114","doi-asserted-by":"crossref","first-page":"2688","DOI":"10.1128\/AAC.47.8.2688-2691.2003","article-title":"Bovine lactoferrin inhibits adenovirus infection by interacting with viral structural polypeptides","volume":"47","author":"Pietrantoni, A.","year":"2003","unstructured":"[114] Pietrantoni, A.; Di Biase, A.M.; Tinari, A.; Marchetti, M.; Valenti, P.; Seganti, L.; Superti, F. Bovine lactoferrin inhibits adenovirus infection by interacting with viral structural polypeptides, Antimicrob. Agents Chemother., Volume 47 (2003), pp. 2688-2691","journal-title":"Antimicrob. Agents Chemother."},{"key":"key2025102316371552331_115","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.antiviral.2003.09.001","article-title":"Anti-HSV activity of lactoferricin analogues is only partly related to their affinity for heparan sulfate","volume":"61","author":"Jenssen, H.","year":"2004","unstructured":"[115] Jenssen, H.; Andersen, J.H.; Uhlin-Hansen, L.; Gutteberg, T.J.; Rekdal, O. Anti-HSV activity of lactoferricin analogues is only partly related to their affinity for heparan sulfate, Antiviral Res., Volume 61 (2004), pp. 101-109","journal-title":"Antiviral Res."},{"key":"key2025102316371552331_116","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/j.virol.2003.09.029","article-title":"Inhibition of herpes simplex virus infection by lactoferrin is dependent on interference with the virus binding to glycosaminoglycans","volume":"318","author":"Marchetti, M.","year":"2004","unstructured":"[116] Marchetti, M.; Trybala, E.; Superti, F.; Johansson, M.; Bergstrom, T. Inhibition of herpes simplex virus infection by lactoferrin is dependent on interference with the virus binding to glycosaminoglycans, Virology, Volume 318 (2004), pp. 405-413","journal-title":"Virology"},{"key":"key2025102316371552331_117","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/j.virol.2014.01.022","article-title":"Inhibition of Mayaro virus infection by bovine lactoferrin","volume":"452\u2013453","author":"Carvalho, C.A.","year":"2014","unstructured":"[117] Carvalho, C.A.; Sousa, I.P. Jr.; Silva, J.L.; Oliveira, A.C.; Goncalves, R.B.; Gomes, A.M. Inhibition of Mayaro virus infection by bovine lactoferrin, Virology, Volume 452\u2013453 (2014), pp. 297-302","journal-title":"Virology"},{"key":"key2025102316371552331_118","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1002\/jmv.23549","article-title":"Characterization of the anti-HBV activity of HLP1-23, a human lactoferrin-derived peptide","volume":"85","author":"Florian, P.E.","year":"2013","unstructured":"[118] Florian, P.E.; Macovei, A.; Lazar, C.; Milac, A.L.; Sokolowska, I.; Darie, C.C.; Evans, R.W.; Roseanu, A.; Branza-Nichita, N. Characterization of the anti-HBV activity of HLP1-23, a human lactoferrin-derived peptide, J. Med. Virol., Volume 85 (2013), pp. 780-788","journal-title":"J. Med. Virol."},{"key":"key2025102316371552331_119","doi-asserted-by":"crossref","DOI":"10.1016\/j.siny.2013.02.001","article-title":"Lactoferrin: antimicrobial activity and therapeutic potential","author":"Embleton, N.D.","year":"2013","unstructured":"[119] Embleton, N.D.; Berrington, J.E.; McGuire, W.; Stewart, C.J.; Cummings, S.P. Lactoferrin: antimicrobial activity and therapeutic potential, Semin. Fetal Neonatal Med. (2013) (PII: S1744-165X(13)00009-7)","journal-title":"Semin. Fetal Neonatal Med."},{"key":"key2025102316371552331_120","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1016\/j.bbrc.2013.04.013","article-title":"The protective effects of lactoferrin against murine norovirus infection through inhibition of both viral attachment and replication","volume":"434","author":"Ishikawa, H.","year":"2013","unstructured":"[120] Ishikawa, H.; Awano, N.; Fukui, T.; Sasaki, H.; Kyuwa, S. The protective effects of lactoferrin against murine norovirus infection through inhibition of both viral attachment and replication, Biochem. Biophys. Res. Commun., Volume 434 (2013), pp. 791-796","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"key2025102316371552331_121","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1292\/jvms.09-0324","article-title":"PEGylated lactoferrin enhances its hepatoprotective effects on acute liver injury induced by D-galactosamine and lipopolysaccharide in rats","volume":"72","author":"Sugiyama, A.","year":"2010","unstructured":"[121] Sugiyama, A.; Sato, A.; Shimizu, H.; Ando, K.; Takeuchi, T. PEGylated lactoferrin enhances its hepatoprotective effects on acute liver injury induced by D-galactosamine and lipopolysaccharide in rats, J. Vet. Med. Sci., Volume 72 (2010), pp. 173-180","journal-title":"J. Vet. Med. Sci."},{"key":"key2025102316371552331_122","doi-asserted-by":"crossref","first-page":"97","DOI":"10.5650\/jos.62.97","article-title":"Bovine lactoferrin reduces visceral fat and liver triglycerides in ICR mice","volume":"62","author":"Morishita, S.","year":"2013","unstructured":"[122] Morishita, S.; Ono, T.; Fujisaki, C.; Ishihara, Y.; Murakoshi, M.; Kato, H.; Hosokawa, M.; Miyashita, K.; Sugiyama, K.; Nishino, H. Bovine lactoferrin reduces visceral fat and liver triglycerides in ICR mice, J. Oleo Sci., Volume 62 (2013), pp. 97-103","journal-title":"J. Oleo Sci."},{"key":"key2025102316371552331_123","doi-asserted-by":"crossref","first-page":"1801","DOI":"10.1017\/S0007114513004315","article-title":"Bovine lactoferrin ingestion protects against inflammation via IL-11 induction in the small intestine of mice with hepatitis","volume":"111","author":"Kuhara, T.","year":"2014","unstructured":"[123] Kuhara, T.; Tanaka, A.; Yamauchi, K.; Iwatsuki, K. Bovine lactoferrin ingestion protects against inflammation via IL-11 induction in the small intestine of mice with hepatitis, Br. J. Nutr., Volume 111 (2014), pp. 1801-1810","journal-title":"Br. J. Nutr."},{"key":"key2025102316371552331_124","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1078\/0171-2985-00115","article-title":"Immunoregulatory activities of lactoferrin in the delayed type hypersensitivity in mice are mediated by a receptor with affinity to mannose","volume":"205","author":"Zimecki, M.","year":"2002","unstructured":"[124] Zimecki, M.; Kocieba, M.; Kruzel, M. Immunoregulatory activities of lactoferrin in the delayed type hypersensitivity in mice are mediated by a receptor with affinity to mannose, Immunobiology, Volume 205 (2002), pp. 120-131","journal-title":"Immunobiology"},{"key":"key2025102316371552331_125","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/0165-2478(91)90099-V","article-title":"Immunostimulatory activity of lactotransferrin and maturation of CD4\u2013 CD8\u2013 murine thymocytes","volume":"30","author":"Zimecki, M.","year":"1991","unstructured":"[125] Zimecki, M.; Mazurier, J.; Machnicki, M.; Wieczorek, Z.; Montreuil, J.; Spik, G. Immunostimulatory activity of lactotransferrin and maturation of CD4\u2013 CD8\u2013 murine thymocytes, Immunol. Lett., Volume 30 (1991), pp. 119-123","journal-title":"Immunol. Lett."},{"key":"key2025102316371552331_126","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1080\/15321810903084400","article-title":"Animal-derived pharmaceutical proteins","volume":"30","author":"Redwan El, R.M.","year":"2009","unstructured":"[126] Redwan El, R.M. Animal-derived pharmaceutical proteins, J. Immunoassay Immunochem., Volume 30 (2009), pp. 262-290","journal-title":"J. Immunoassay Immunochem."},{"key":"key2025102316371552331_127","doi-asserted-by":"crossref","first-page":"137","DOI":"10.3233\/HAB-2007-163-408","article-title":"Cumulative updating of approved biopharmaceuticals","volume":"16","author":"Redwan El, R.M.","year":"2007","unstructured":"[127] Redwan El, R.M. Cumulative updating of approved biopharmaceuticals, Hum. Antibodies, Volume 16 (2007), pp. 137-158","journal-title":"Hum. Antibodies"},{"key":"key2025102316371552331_128","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1006\/bbrc.1998.8481","article-title":"Lactoferrin markedly inhibits hepatitis C virus infection in cultured human hepatocytes","volume":"245","author":"Ikeda, M.","year":"1998","unstructured":"[128] Ikeda, M.; Sugiyama, K.; Tanaka, T.; Tanaka, K.; Sekihara, H.; Shimotohno, K.; Kato, N. Lactoferrin markedly inhibits hepatitis C virus infection in cultured human hepatocytes, Biochem. Biophys. Res. Commun., Volume 245 (1998), pp. 549-553","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"key2025102316371552331_129","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/S0168-1702(99)00121-5","article-title":"Characterization of antiviral activity of lactoferrin against hepatitis C virus infection in human cultured cells","volume":"66","author":"Ikeda, M.","year":"2000","unstructured":"[129] Ikeda, M.; Nozaki, A.; Sugiyama, K.; Tanaka, T.; Naganuma, A.; Tanaka, K.; Sekihara, H.; Shimotohno, K.; Saito, M.; Kato, N. Characterization of antiviral activity of lactoferrin against hepatitis C virus infection in human cultured cells, Virus Res., Volume 66 (2000), pp. 51-63","journal-title":"Virus Res."},{"key":"key2025102316371552331_130","doi-asserted-by":"crossref","first-page":"10162","DOI":"10.1074\/jbc.M207879200","article-title":"Identification of a lactoferrin-derived peptide possessing binding activity to hepatitis C virus E2 envelope protein","volume":"278","author":"Nozaki, A.","year":"2003","unstructured":"[130] Nozaki, A.; Ikeda, M.; Naganuma, A.; Nakamura, T.; Inudoh, M.; Tanaka, K.; Kato, N. Identification of a lactoferrin-derived peptide possessing binding activity to hepatitis C virus E2 envelope protein, J. Biol. Chem., Volume 278 (2003), pp. 10162-10173","journal-title":"J. Biol. Chem."},{"key":"key2025102316371552331_131","doi-asserted-by":"crossref","first-page":"5997","DOI":"10.1128\/jvi.71.8.5997-6002.1997","article-title":"Hepatitis C virus envelope proteins bind lactoferrin","volume":"71","author":"Yi, M.","year":"1997","unstructured":"[131] Yi, M.; Kaneko, S.; Yu, D.Y.; Murakami, S. Hepatitis C virus envelope proteins bind lactoferrin, J. Virol., Volume 71 (1997), pp. 5997-6002","journal-title":"J. Virol."},{"key":"key2025102316371552331_132","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.cbpb.2008.02.005","article-title":"Isolation of lactoferrin from milk of different species: calorimetric and antimicrobial studies","volume":"150","author":"Conesa, C.","year":"2008","unstructured":"[132] Conesa, C.; Sanchez, L.; Rota, C.; Perez, M.D.; Calvo, M.; Farnaud, S.; Evans, R.W. Isolation of lactoferrin from milk of different species: calorimetric and antimicrobial studies, Comp. Biochem. Physiol. B Biochem. Mol. Biol., Volume 150 (2008), pp. 131-139","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"key":"key2025102316371552331_133","doi-asserted-by":"crossref","first-page":"724","DOI":"10.5812\/kowsar.1735143X.1367","article-title":"Examination of the activity of camel milk casein against hepatitis C virus (genotype-4a) and its apoptotic potential in hepatoma and hela cell lines","volume":"11","author":"Almahdy, O.","year":"2011","unstructured":"[133] Almahdy, O.; El-Fakharany, E.M.; El-Dabaa, E.; Ng, T.B.; Redwan, E.M. Examination of the activity of camel milk casein against hepatitis C virus (genotype-4a) and its apoptotic potential in hepatoma and hela cell lines, Hepat. Mon., Volume 11 (2011), pp. 724-730","journal-title":"Hepat. Mon."},{"key":"key2025102316371552331_134","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.2174\/092986610791498948","article-title":"Oyster mushroom laccase inhibits hepatitis C virus entry into peripheral blood cells and hepatoma cells","volume":"17","author":"El-Fakharany, E.M.","year":"2010","unstructured":"[134] El-Fakharany, E.M.; Haroun, B.M.; Ng, T.B.; Redwan, E.R. Oyster mushroom laccase inhibits hepatitis C virus entry into peripheral blood cells and hepatoma cells, Protein Pept. Lett., Volume 17 (2010), pp. 1031-1039","journal-title":"Protein Pept. Lett."},{"key":"key2025102316371552331_135","first-page":"107","article-title":"Quantitative method of intracellular hepatitis C virus RNA using LightCycler PCR","volume":"56","author":"Nozaki, A.","year":"2002","unstructured":"[135] Nozaki, A.; Kato, N. Quantitative method of intracellular hepatitis C virus RNA using LightCycler PCR, Acta Med. Okayama, Volume 56 (2002), pp. 107-110","journal-title":"Acta Med. Okayama"},{"key":"key2025102316371552331_136","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1111\/j.1348-0421.2007.tb03882.x","article-title":"Tandem repeats of lactoferrin-derived anti-hepatitis C virus peptide enhance antiviral activity in cultured human hepatocytes","volume":"51","author":"Abe, K.","year":"2007","unstructured":"[136] Abe, K.; Nozaki, A.; Tamura, K.; Ikeda, M.; Naka, K.; Dansako, H.; Hoshino, H.O.; Tanaka, K.; Kato, N. Tandem repeats of lactoferrin-derived anti-hepatitis C virus peptide enhance antiviral activity in cultured human hepatocytes, Microbiol. Immunol., Volume 51 (2007), pp. 117-125","journal-title":"Microbiol. Immunol."},{"key":"key2025102316371552331_137","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1111\/j.1747-0285.2008.00715.x","article-title":"Helical peptides derived from lactoferrin bind hepatitis C virus envelope protein E2","volume":"72","author":"Beleid, R.","year":"2008","unstructured":"[137] Beleid, R.; Douglas, D.; Kneteman, N.; Kaur, K. Helical peptides derived from lactoferrin bind hepatitis C virus envelope protein E2, Chem. Biol. Drug Des., Volume 72 (2008), pp. 436-443","journal-title":"Chem. Biol. Drug Des."},{"key":"key2025102316371552331_138","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1139\/o2012-016","article-title":"Lactoferrin, a bird's eye view","volume":"90","author":"Vogel, H.J.","year":"2012","unstructured":"[138] Vogel, H.J. Lactoferrin, a bird's eye view, Biochem. Cell Biol., Volume 90 (2012), pp. 233-244","journal-title":"Biochem. Cell Biol."},{"key":"key2025102316371552331_139","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/0166-3542(95)00840-3","article-title":"Lactoferrin inhibits herpes simplex virus type 1 adsorption to Vero cells","volume":"29","author":"Marchetti, M.","year":"1996","unstructured":"[139] Marchetti, M.; Longhi, C.; Conte, M.P.; Pisani, S.; Valenti, P.; Seganti, L. Lactoferrin inhibits herpes simplex virus type 1 adsorption to Vero cells, Antiviral Res., Volume 29 (1996), pp. 221-231","journal-title":"Antiviral Res."},{"key":"key2025102316371552331_140","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1023\/A:1009217709851","article-title":"Metal complexes of bovine lactoferrin inhibit in vitro replication of herpes simplex virus type 1 and 2","volume":"11","author":"Marchetti, M.","year":"1998","unstructured":"[140] Marchetti, M.; Pisani, S.; Antonini, G.; Valenti, P.; Seganti, L.; Orsi, N. Metal complexes of bovine lactoferrin inhibit in vitro replication of herpes simplex virus type 1 and 2, Biometals, Volume 11 (1998), pp. 89-94","journal-title":"Biometals"},{"key":"key2025102316371552331_141","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1007\/978-1-4757-9068-9_23","article-title":"Antiviral activity of lactoferrin","volume":"443","author":"Valenti, P.","year":"1998","unstructured":"[141] Valenti, P.; Marchetti, M.; Superti, F.; Amendolia, M.G.; Puddu, P.; Gessani, S.; Borghi, P.; Belardelli, F.; Antonini, G.; Seganti, L. Antiviral activity of lactoferrin, Adv. Exp. Med. Biol., Volume 443 (1998), pp. 199-203","journal-title":"Adv. Exp. Med. Biol."},{"key":"key2025102316371552331_142","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1006\/bbrc.1999.1318","article-title":"Bovine lactoferrin peptidic fragments involved in inhibition of herpes simplex virus type 1 infection","volume":"264","author":"Siciliano, R.","year":"1999","unstructured":"[142] Siciliano, R.; Rega, B.; Marchetti, M.; Seganti, L.; Antonini, G.; Valenti, P. Bovine lactoferrin peptidic fragments involved in inhibition of herpes simplex virus type 1 infection, Biochem. Biophys. Res. Commun., Volume 264 (1999), pp. 19-23","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"key2025102316371552331_143","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.biochi.2008.05.016","article-title":"Bovine lactoferrin and lactoferricin interfere with intracellular trafficking of Herpes simplex virus-1","volume":"91","author":"Marr, A.K.","year":"2009","unstructured":"[143] Marr, A.K.; Jenssen, H.; Moniri, M.R.; Hancock, R.E.; Pante, N. Bovine lactoferrin and lactoferricin interfere with intracellular trafficking of Herpes simplex virus-1, Biochimie, Volume 91 (2009), pp. 160-164","journal-title":"Biochimie"},{"key":"key2025102316371552331_144","first-page":"239","author":"Hammer, J.","year":"2000","unstructured":"[144] Hammer, J.; Haaheim, H.; Gutteberg, T.J. Bovine lactoferrin is more efficient than bovine lactoferricin in inhibiting HSV-I\/-II replication in vitro (Shimazaki, K., ed.), Lactoferrin: Structure, Functions and Applications, Elsevier, Amsterdam, 2000, pp. 239-243","journal-title":"Bovine lactoferrin is more efficient than bovine lactoferricin in inhibiting HSV-I\/-II replication in vitro"},{"key":"key2025102316371552331_145","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1093\/infdis\/172.2.380","article-title":"Antiviral effects of plasma and milk proteins: lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro","volume":"172","author":"Harmsen, M.C.","year":"1995","unstructured":"[145] Harmsen, M.C.; Swart, P.J.; de Bethune, M.P.; Pauwels, R.; De Clercq, E.; The, T.H.; Meijer, D.K. Antiviral effects of plasma and milk proteins: lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro, J. Infect. Dis., Volume 172 (1995), pp. 380-388","journal-title":"J. Infect. Dis."},{"key":"key2025102316371552331_146","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1016\/S1357-2725(98)00066-1","article-title":"Antiviral effect of bovine lactoferrin saturated with metal ions on early steps of human immunodeficiency virus type 1 infection","volume":"30","author":"Puddu, P.","year":"1998","unstructured":"[146] Puddu, P.; Borghi, P.; Gessani, S.; Valenti, P.; Belardelli, F.; Seganti, L. Antiviral effect of bovine lactoferrin saturated with metal ions on early steps of human immunodeficiency virus type 1 infection, Int. J. Biochem. Cell Biol., Volume 30 (1998), pp. 1055-1062","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"key2025102316371552331_147","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1002\/(SICI)1099-1387(199912)5:12<563::AID-PSC226>3.0.CO;2-3","article-title":"Charge modification of plasma and milk proteins results in antiviral active compounds","volume":"5","author":"Swart, P.J.","year":"1999","unstructured":"[147] Swart, P.J.; Harmsen, M.C.; Kuipers, M.E.; Van Dijk, A.A.; Van Der Strate, B.W.; Van Berkel, P.H.; Nuijens, J.H.; Smit, C.; Witvrouw, M.; De Clercq, E. et al. Charge modification of plasma and milk proteins results in antiviral active compounds, J. Pept. Sci., Volume 5 (1999), pp. 563-576","journal-title":"J. Pept. Sci."},{"key":"key2025102316371552331_148","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1006\/smim.1998.0127","article-title":"Structural interactions between chemokine receptors, gp120 Env and CD4","volume":"10","author":"Choe, H.","year":"1998","unstructured":"[148] Choe, H.; Martin, K.A.; Farzan, M.; Sodroski, J.; Gerard, N.P.; Gerard, C. Structural interactions between chemokine receptors, gp120 Env and CD4, Semin. Immunol., Volume 10 (1998), pp. 249-257","journal-title":"Semin. Immunol."},{"key":"key2025102316371552331_149","doi-asserted-by":"crossref","first-page":"1645","DOI":"10.1128\/JVI.73.2.1645-1648.1999","article-title":"CCR5-Mediated human immunodeficiency virus entry depends on an amino-terminal gp120-binding site and on the conformational integrity of all four extracellular domains","volume":"73","author":"Genoud, S.","year":"1999","unstructured":"[149] Genoud, S.; Kajumo, F.; Guo, Y.; Thompson, D.; Dragic, T. CCR5-Mediated human immunodeficiency virus entry depends on an amino-terminal gp120-binding site and on the conformational integrity of all four extracellular domains, J. Virol., Volume 73 (1999), pp. 1645-1648","journal-title":"J. Virol."},{"key":"key2025102316371552331_150","doi-asserted-by":"crossref","first-page":"23499","DOI":"10.1074\/jbc.274.33.23499","article-title":"Roles of CD4 and co-receptors in binding, endocytosis, and proteolysis of gp120 envelope glycoproteins derived from human immunodeficiency virus type 1","volume":"274","author":"Kozak, S.L.","year":"1999","unstructured":"[150] Kozak, S.L.; Kuhmann, S.E.; Platt, E.J.; Kabat, D. Roles of CD4 and co-receptors in binding, endocytosis, and proteolysis of gp120 envelope glycoproteins derived from human immunodeficiency virus type 1, J. Biol. Chem., Volume 274 (1999), pp. 23499-23507","journal-title":"J. Biol. Chem."},{"key":"key2025102316371552331_151","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1046\/j.1432-1033.2003.03929.x","article-title":"Surface nucleolin participates in both the binding and endocytosis of lactoferrin in target cells","volume":"271","author":"Legrand, D.","year":"2004","unstructured":"[151] Legrand, D.; Vigie, K.; Said, E.A.; Elass, E.; Masson, M.; Slomianny, M.C.; Carpentier, M.; Briand, J.P.; Mazurier, J.; Hovanessian, A.G. Surface nucleolin participates in both the binding and endocytosis of lactoferrin in target cells, Eur. J. Biochem., Volume 271 (2004), pp. 303-317","journal-title":"Eur. J. Biochem."},{"key":"key2025102316371552331_152","doi-asserted-by":"crossref","first-page":"3009","DOI":"10.1128\/JVI.79.5.3009-3015.2005","article-title":"Lactoferrin prevents dendritic cell-mediated human immunodeficiency virus type 1 transmission by blocking the DC-SIGN\u00a0\u2013\u00a0gp120 interaction","volume":"79","author":"Groot, F.","year":"2005","unstructured":"[152] Groot, F.; Geijtenbeek, T.B.; Sanders, R.W.; Baldwin, C.E.; Sanchez-Hernandez, M.; Floris, R.; van Kooyk, Y.; de Jong, E.C.; Berkhout, B. Lactoferrin prevents dendritic cell-mediated human immunodeficiency virus type 1 transmission by blocking the DC-SIGN\u00a0\u2013\u00a0gp120 interaction, J. Virol., Volume 79 (2005), pp. 3009-3015","journal-title":"J. Virol."},{"key":"key2025102316371552331_153","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/S0304-4165(01)00178-7","article-title":"Involvement of bovine lactoferrin metal saturation, sialic acid and protein fragments in the inhibition of rotavirus infection","volume":"1528","author":"Superti, F.","year":"2001","unstructured":"[153] Superti, F.; Siciliano, R.; Rega, B.; Giansanti, F.; Valenti, P.; Antonini, G. Involvement of bovine lactoferrin metal saturation, sialic acid and protein fragments in the inhibition of rotavirus infection, Biochim. Biophys. Acta, Volume 1528 (2001), pp. 107-115","journal-title":"Biochim. Biophys. Acta"},{"key":"key2025102316371552331_154","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1007\/s004300050093","article-title":"Inhibition of poliovirus type 1 infection by iron-, manganese- and zinc-saturated lactoferrin","volume":"187","author":"Marchetti, M.","year":"1999","unstructured":"[154] Marchetti, M.; Superti, F.; Ammendolia, M.G.; Rossi, P.; Valenti, P.; Seganti, L. Inhibition of poliovirus type 1 infection by iron-, manganese- and zinc-saturated lactoferrin, Med. Microbiol. Immunol., Volume 187 (1999), pp. 199-204","journal-title":"Med. Microbiol. Immunol."},{"key":"key2025102316371552331_155","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0166-3542(01)00197-8","article-title":"Antiadenovirus activity of milk proteins: lactoferrin prevents viral infection","volume":"53","author":"Arnold, D.","year":"2002","unstructured":"[155] Arnold, D.; Di Biase, A.M.; Marchetti, M.; Pietrantoni, A.; Valenti, P.; Seganti, L.; Superti, F. Antiadenovirus activity of milk proteins: lactoferrin prevents viral infection, Antiviral Res., Volume 53 (2002), pp. 153-158","journal-title":"Antiviral Res."},{"key":"key2025102316371552331_156","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1002\/jmv.10337","article-title":"Heparin-interacting sites of bovine lactoferrin are involved in anti-adenovirus activity","volume":"69","author":"Di Biase, A.M.","year":"2003","unstructured":"[156] Di Biase, A.M.; Pietrantoni, A.; Tinari, A.; Siciliano, R.; Valenti, P.; Antonini, G.; Seganti, L.; Superti, F. Heparin-interacting sites of bovine lactoferrin are involved in anti-adenovirus activity, J. Med. Virol., Volume 69 (2003), pp. 495-502","journal-title":"J. Med. Virol."},{"key":"key2025102316371552331_157","first-page":"77","article-title":"[Cell receptors for human adenoviruses]","volume":"193","author":"Boulanger, P.","year":"1999","unstructured":"[157] Boulanger, P. [Cell receptors for human adenoviruses], J. Soc. Biol., Volume 193 (1999), pp. 77-84","journal-title":"J. Soc. Biol."},{"issue":"Suppl.\u00a01","key":"key2025102316371552331_158","doi-asserted-by":"crossref","first-page":"S127","DOI":"10.1017\/S000711450000235X","article-title":"In vivo antimicrobial and antiviral activity of components in bovine milk and colostrum involved in non-specific defence","volume":"84","author":"van Hooijdonk, A.C.","year":"2000","unstructured":"[158] van Hooijdonk, A.C.; Kussendrager, K.D.; Steijns, J.M. In vivo antimicrobial and antiviral activity of components in bovine milk and colostrum involved in non-specific defence, Br. J. Nutr., Volume 84 (2000) no. Suppl.\u00a01, p. S127-S134","journal-title":"Br. J. Nutr."},{"key":"key2025102316371552331_159","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/j.antiviral.2013.05.013","article-title":"Lack of effect of bovine lactoferrin in respiratory syncytial virus replication and clinical disease severity in the mouse model","volume":"99","author":"Gualdi, L.","year":"2013","unstructured":"[159] Gualdi, L.; Mertz, S.; Gomez, A.M.; Ramilo, O.; Wittke, A.; Mejias, A. Lack of effect of bovine lactoferrin in respiratory syncytial virus replication and clinical disease severity in the mouse model, Antiviral Res., Volume 99 (2013), pp. 188-195","journal-title":"Antiviral Res."},{"key":"key2025102316371552331_160","first-page":"122","article-title":"Human lactoferrin induces phenotypic and functional changes in murine splenic B cells","volume":"86","author":"Zimecki, M.","year":"1995","unstructured":"[160] Zimecki, M.; Mazurier, J.; Spik, G.; Kapp, J.A. Human lactoferrin induces phenotypic and functional changes in murine splenic B cells, Immunology, Volume 86 (1995), pp. 122-127","journal-title":"Immunology"},{"key":"key2025102316371552331_161","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1111\/j.1365-2567.2007.02719.x","article-title":"Immunological decision-making: how does the immune system decide to mount a helper T-cell response?","volume":"123","author":"Kaiko, G.E.","year":"2008","unstructured":"[161] Kaiko, G.E.; Horvat, J.C.; Beagley, K.W.; Hansbro, P.M. Immunological decision-making: how does the immune system decide to mount a helper T-cell response?, Immunology, Volume 123 (2008), pp. 326-338","journal-title":"Immunology"},{"key":"key2025102316371552331_162","first-page":"303","article-title":"Regulation of physiological and pathological Th1 and Th2 responses by lactoferrin","volume":"84","author":"Fischer, R.","year":"2006","unstructured":"[162] Fischer, R.; Debbabi, H.; Dubarry, M.; Boyaka, P.; Tome, D. Regulation of physiological and pathological Th1 and Th2 responses by lactoferrin, Biochem. Cell Biol., Volume 84 (2006), pp. 303-311","journal-title":"Biochem. Cell Biol."},{"key":"key2025102316371552331_163","doi-asserted-by":"crossref","first-page":"1956","DOI":"10.2174\/138161209788453202","article-title":"Lactoferrin as a natural immune modulator","volume":"15","author":"Actor, J.K.","year":"2009","unstructured":"[163] Actor, J.K.; Hwang, S.A.; Kruzel, M.L. Lactoferrin as a natural immune modulator, Curr. Pharm. Des., Volume 15 (2009), pp. 1956-1973","journal-title":"Curr. Pharm. Des."},{"key":"key2025102316371552331_164","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1046\/j.1365-3083.1997.d01-165.x","article-title":"Activated human gamma delta T lymphocytes express functional lactoferrin receptors","volume":"46","author":"Mincheva-Nilsson, L.","year":"1997","unstructured":"[164] Mincheva-Nilsson, L.; Hammarstrom, S.; Hammarstrom, M.L. Activated human gamma delta T lymphocytes express functional lactoferrin receptors, Scand. J. Immunol., Volume 46 (1997), pp. 609-618","journal-title":"Scand. J. Immunol."},{"key":"key2025102316371552331_165","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1292\/jvms.66.865","article-title":"Detection of bovine lactoferrin binding protein on Jurkat human lymphoblastic T cell line","volume":"66","author":"Tanaka, T.","year":"2004","unstructured":"[165] Tanaka, T.; Morita, H.; Yoo, Y.C.; Kim, W.S.; Kumura, H.; Shimazaki, K. Detection of bovine lactoferrin binding protein on Jurkat human lymphoblastic T cell line, J. Vet. Med. Sci., Volume 66 (2004), pp. 865-869","journal-title":"J. Vet. Med. Sci."},{"issue":"Pt 3","key":"key2025102316371552331_166","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1042\/bj3270841","article-title":"The N-terminal Arg2, Arg3 and Arg4 of human lactoferrin interact with sulphated molecules but not with the receptor present on Jurkat human lymphoblastic T-cells","volume":"327","author":"Legrand, D.","year":"1997","unstructured":"[166] Legrand, D.; van Berkel, P.H.; Salmon, V.; van Veen, H.A.; Slomianny, M.C.; Nuijens, J.H.; Spik, G. The N-terminal Arg2, Arg3 and Arg4 of human lactoferrin interact with sulphated molecules but not with the receptor present on Jurkat human lymphoblastic T-cells, Biochem. J., Volume 327 (1997) no. Pt 3, pp. 841-846","journal-title":"Biochem. J."},{"key":"key2025102316371552331_167","first-page":"288","article-title":"Internalization of human lactoferrin by the Jurkat human lymphoblastic T-cell line","volume":"69","author":"Bi, B.Y.","year":"1996","unstructured":"[167] Bi, B.Y.; Liu, J.L.; Legrand, D.; Roche, A.C.; Capron, M.; Spik, G.; Mazurier J: Internalization of human lactoferrin by the Jurkat human lymphoblastic T-cell line, Eur. J. Cell Biol., Volume 69 (1996), pp. 288-296","journal-title":"Eur. J. Cell Biol."},{"key":"key2025102316371552331_168","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1146\/annurev.immunol.15.1.297","article-title":"Induction of Th1 and Th2 CD4+ T cell responses: the alternative approaches","volume":"15","author":"Constant, S.L.","year":"1997","unstructured":"[168] Constant, S.L.; Bottomly K: Induction of Th1 and Th2 CD4+ T cell responses: the alternative approaches, Annu. Rev. Immunol., Volume 15 (1997), pp. 297-322","journal-title":"Annu. Rev. Immunol."},{"key":"key2025102316371552331_169","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/j.bbi.2005.08.005","article-title":"Epigenetic regulation of Th1 and Th2 cell development","volume":"20","author":"Sanders, V.M.","year":"2006","unstructured":"[169] Sanders, V.M. Epigenetic regulation of Th1 and Th2 cell development, Brain Behav. Immun., Volume 20 (2006), pp. 317-324","journal-title":"Brain Behav. Immun."},{"key":"key2025102316371552331_170","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1111\/j.1349-7006.2000.tb00880.x","article-title":"Activation of intestinal mucosal immunity in tumor-bearing mice by lactoferrin","volume":"91","author":"Wang, W.P.","year":"2000","unstructured":"[170] Wang, W.P.; Iigo, M.; Sato, J.; Sekine, K.; Adachi, I.; Tsuda, H. Activation of intestinal mucosal immunity in tumor-bearing mice by lactoferrin, Jpn. J. Cancer Res., Volume 91 (2000), pp. 1022-1027","journal-title":"Jpn. J. Cancer Res."},{"key":"key2025102316371552331_171","doi-asserted-by":"crossref","first-page":"6868","DOI":"10.4049\/jimmunol.180.10.6868","article-title":"Lactoferrin acts as an alarmin to promote the recruitment and activation of APCs and antigen-specific immune responses","volume":"180","author":"de la Rosa, G.","year":"2008","unstructured":"[171] de la Rosa, G.; Yang, D.; Tewary, P.; Varadhachary, A.; Oppenheim, J.J. Lactoferrin acts as an alarmin to promote the recruitment and activation of APCs and antigen-specific immune responses, J. Immunol., Volume 180 (2008), pp. 6868-6876","journal-title":"J. Immunol."},{"key":"key2025102316371552331_172","doi-asserted-by":"crossref","first-page":"e42094","DOI":"10.1371\/journal.pone.0042094","article-title":"Ribavirin exerts differential effects on functions of Cd4+ Th1, Th2, and regulatory T cell clones in hepatitis C","volume":"7","author":"Langhans, B.","year":"2012","unstructured":"[172] Langhans, B.; Nischalke, H.D.; Arndt, S.; Braunschweiger, I.; Nattermann, J.; Sauerbruch, T.; Spengler, U. Ribavirin exerts differential effects on functions of Cd4+ Th1, Th2, and regulatory T cell clones in hepatitis C, PLoS One, Volume 7 (2012), p. e42094","journal-title":"PLoS One"},{"key":"key2025102316371552331_173","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1139\/o06-056","article-title":"Influences of orally administered lactoferrin on IFN-gamma and IL-10 production by intestinal intraepithelial lymphocytes and mesenteric lymph-node cells","volume":"84","author":"Takakura, N.","year":"2006","unstructured":"[173] Takakura, N.; Wakabayashi, H.; Yamauchi, K.; Takase, M. Influences of orally administered lactoferrin on IFN-gamma and IL-10 production by intestinal intraepithelial lymphocytes and mesenteric lymph-node cells, Biochem. Cell Biol., Volume 84 (2006), pp. 363-368","journal-title":"Biochem. Cell Biol."}],"container-title":["Comptes Rendus. Biologies"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/comptes-rendus.academie-sciences.fr\/biologies\/item\/10.1016\/j.crvi.2014.08.003.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,23]],"date-time":"2025-10-23T14:51:01Z","timestamp":1761231061000},"score":1,"resource":{"primary":{"URL":"https:\/\/comptes-rendus.academie-sciences.fr\/biologies\/articles\/10.1016\/j.crvi.2014.08.003\/"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,9,22]]},"references-count":173,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2014]]}},"alternative-id":["10.1016\/j.crvi.2014.08.003"],"URL":"https:\/\/doi.org\/10.1016\/j.crvi.2014.08.003","relation":{},"ISSN":["1631-0691","1768-3238"],"issn-type":[{"value":"1631-0691","type":"print"},{"value":"1768-3238","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,9,22]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Potential lactoferrin activity against pathogenic viruses","name":"articletitle","label":"Article Title"},{"value":"Comptes Rendus Biologies","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.crvi.2014.08.003","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 Acad\u00e9mie des sciences. Published by Elsevier Masson SAS All rights reserved.","name":"copyright","label":"Copyright"}]}}