Lactoferrin: a natural Glycoprotein involved in iron and inflammatory homeostasis
Open accessAbstract
Human lactoferrin (hLf), an iron-binding multifunctional cationic glycoprotein secreted by exocrine glands and by neutrophils, is a key element of host defenses. HLf and bovine Lf (bLf), possessing high sequence homology and identical functions, inhibit bacterial growth and biofilm dependently from iron binding ability while, independently, bacterial adhesion to and the entry into cells. In infected/inflamed host cells, bLf exerts an anti-inflammatory activity against interleukin-6 (IL-6), thus up-regulating ferroportin (Fpn) and transferrin receptor 1 (TfR1) and down-regulating ferritin (Ftn), pivotal actors of iron and inflammatory homeostasis (IIH). Consequently, bLf inhibits intracellular iron overload, an unsafe condition enhancing in vivo susceptibility to infections, as well as anemia of inflammation (AI), re-establishing IIH. In pregnant women, affected by AI, bLf oral administration decreases IL-6 and increases hematological parameters. This surprising effect is unrelated to iron supplementation by bLf (80 μg instead of 1-2 mg/day), but to its role on IIH. AI is unrelated to the lack of iron, but to iron delocalization: cellular/tissue overload and blood deficiency. BLf cures AI by restoring iron from cells to blood through Fpn up-expression. Indeed, anti-inflammatory activity of oral and intravaginal bLf prevents preterm delivery. Promising bLf treatments can prevent/cure transitory inflammation/anemia/oral pathologies in athletes.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
LF inhibits adhesion to and invasion of host cells, as demonstrated in studies with enteroinvasive E. coli, Listeria monocytogenes, Streptococcus pyogenes and S. aureus.
“Yet another antibacterial activity of LF is its ability to inhibit the adhesion to and invasion of host cells as demonstrated in studies with enteroinvasive E. coli, Listeria monocytogenes, Streptococcus pyogenes and S. aureus (Rosa et al., 2017).”
From Iron in infection and immunity (2020) · cites this paper as Rosa et al., 2017
Section 2.1 reports that lactoferrin inhibits bacterial adhesion to host cells and describes inhibition of invasion by L. monocytogenes, S. pyogenes, and S. aureus. For E. coli invasion, however, it describes HB101(pRI203), a recombinant strain made capable of entering cells by an inv gene, rather than identifying an enteroinvasive E. coli pathotype. (LLM, conf=0.83)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Targeting Hypoxia-Inducible Factors for the Treatment of Anemia in Chronic Kidney Disease Patients
Locatelli, F., Fishbane, S. N., Block, G. A., & Macdougall, I. C. (2017) · American Journal of Nephrology · doi:10.1159/000455166 · Cited by 4,834 · see citing works
Nemeth, E., Rivera, S., Gabayan, V., Keller, C., Taudorf, S., Pedersen, B. K., & Ganz, T. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420945 · Cited by 2,650 · see citing works
Hepcidin, a urinary antimicrobial peptide synthesized in the liver
Park, C. H., Valore, E. V., Waring, A. J., & Ganz, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008922200 · Cited by 2,168 · see citing works
Andrews, N. C. (1999) · New England Journal of Medicine · doi:10.1056/nejm199912233412607 · Cited by 2,130 · see citing works
LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity
Krause, A., Neitz, S., Mägert, H.-J., Schulz, A., Forssmann, W.-G., Schulz-Knappe, P., & Adermann, K. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01920-7 · Cited by 1,324 · see citing works
The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis
Donovan, A., Lima, C. A., Pinkus, J. L., Pinkus, G. S., Zon, L. I., Robine, S., & Andrews, N. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.003 · Cited by 1,275 · see citing works
A component of innate immunity prevents bacterial biofilm development
Singh, P. K., Parsek, M. R., Greenberg, E. P., & Welsh, M. J. (2002) · Nature · doi:10.1038/417552a · Cited by 1,026 · see citing works
Interleukin-6 induces hepcidin expression through STAT3
Wrighting, D. M., & Andrews, N. C. (2006) · Blood · doi:10.1182/blood-2006-06-027631 · Cited by 983 · see citing works
The role of reactive oxygen and antioxidant species in periodontal tissue destruction
Chapple, I., & Matthews, J. B. (2007) · Periodontology 2000 · doi:10.1111/j.1600-0757.2006.00178.x · Cited by 954 · see citing works
Regulation of Iron Metabolism by Hepcidin
Nemeth, E., & Ganz, T. (2006) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.26.061505.111303 · Cited by 756 · cited 1× · see citing works
“Therefore AI, characterized by hypoferremia in the blood despite suitable iron stores [27], is very difficult to cure in the absence of a contemporary decreasing of serum IL-6 levels.”
BackgroundCario, E., Rosenberg, I. M., Brandwein, S. L., Beck, P. L., Reinecker, H., & Podolsky, D. K. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.2.966 · Cited by 751 · see citing works
Bacterial vaginosis as a risk factor for preterm delivery: A meta-analysis
Leitich, H., Bodner‐Adler, B., Brunbauer, M., Kaider, A., Egarter, C., & Husslein, P. W. (2003) · American Journal of Obstetrics and Gynecology · doi:10.1067/mob.2003.339 · Cited by 735 · see citing works
LACTOFERRIN, AN IRON-BINBING PROTEIN NI NEUTROPHILIC LEUKOCYTES
Masson, P. L., Heremans, J. F., & Schonne, E. (1969) · The Journal of Experimental Medicine · doi:10.1084/jem.130.3.643 · Cited by 700 · see citing works
Iron Deficiency Anemia: A Common and Curable DiseasePreprint
Miller, J. L. (2013) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a011866 · Cited by 605 · see citing works
Anderson, B. F., Baker, H. M., Norris, G. E., Rice, D. W., & Baker, E. N. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90602-5 · Cited by 597 · see citing works
Bellamy, W., Takase, M., Wakabayashi, H., Kawase, K., & TOMITA, M. (1992) · Journal of Applied Bacteriology · doi:10.1111/j.1365-2672.1992.tb05007.x · Cited by 588 · see citing works
An iron-binding protein common to many external secretions
Masson, P. L., Heremans, J. F., & Dive, C. H. (1966) · Clinica Chimica Acta · doi:10.1016/0009-8981(66)90004-0 · Cited by 577 · see citing works
STAT3 mediates hepatic hepcidin expression and its inflammatory stimulation
Verga Falzacappa, M. V., Vujic Spasic, M., Kessler, R., Stolte, J., Hentze, M. W., & Muckenthaler, M. U. (2007) · Blood · doi:10.1182/blood-2006-07-033969 · Cited by 567 · see citing works
Regulation of hepcidin transcription by interleukin-1 and interleukin-6
Lee, P. L., Peng, H., Gelbart, T., Wang, L., & Beutler, E. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409808102 · Cited by 542 · see citing works
Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins
Metz‐Boutigue, M., Jollès, P., Mazurier, J., Schoentgen, F., Legrand, D., Spik, G., Montreuil, J., & Jollès, P. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08607.x · Cited by 537 · see citing works
Intracellular iron transport and storage: from molecular mechanisms to health implications
Mackenzie, E. L., Iwasaki, K., & Tsuji, Y. (2008) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1893 · Cited by 526 · see citing works
Valenti, P., & Antonini, G. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5372-0 · Cited by 470 · see citing works
Self-citationRegulation of iron acquisition and storage: consequences for iron-linked disorders
De Domenico, I., McVey Ward, D., & Kaplan, J. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2295 · Cited by 464 · see citing works
Potent Antibacterial Peptides Generated by Pepsin Digestion of Bovine Lactoferrin
TOMITA, M., Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., & Kawase, K. (1991) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(91)78608-6 · Cited by 445 · see citing works
Lactoferrin in milk from different species
Masson, P. L., & Heremans, J. F. (1971) · Comparative Biochemistry and Physiology Part B: Comparative Biochemistry · doi:10.1016/0305-0491(71)90258-6 · Cited by 444 · see citing works
Lactoferrin: Multifunctional roles of lactoferrin: a critical overview
Ward, P. P., Paz, E., & Conneely, O. M. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5369-8 · Cited by 443 · see citing works
Legrand, D., Elass, E., Carpentier, M., & Mazurier, J. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5370-2 · Cited by 421 · see citing works
Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution
Moore, S. A., Anderson, B. F., Groom, C. R., Haridas, M., & Baker, E. N. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1386 · Cited by 417 · see citing works
Hunter, H. N., Fulton, D. B., Ganz, T., & Vogel, H. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205305200 · Cited by 400 · see citing works
Baker, E. N., & Baker, H. M. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5368-9 · Cited by 387 · see citing works
Structure of human lactoferrin at 3.2-A resolution.
Anderson, B. F., Baker, H. M., Dodson, E. J., Norris, G. E., Rumball, S. V., Waters, J. M., & Baker, E. N. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.7.1769 · Cited by 386 · see citing works
Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins
Andersen, B. F., Baker, H. M., Morris, G. E., Rumball, S. V., & Baker, E. N. (1990) · Nature · doi:10.1038/344784a0 · Cited by 363 · see citing works
Lactoferrin is a lipid A-binding protein
Appelmelk, B. J., An, Y. Q., Geerts, M., Thijs, B. G., de Boer, H. A., MacLaren, D. M., Graaff, J., & Nuijens, J. H. (1994) · Infection and Immunity · doi:10.1128/iai.62.6.2628-2632.1994 · Cited by 362 · see citing works
β-Defensin-2 Expression Is Regulated by TLR Signaling in Intestinal Epithelial Cells
Vora, P., Youdim, A., Thomas, L. S., Fukata, M., Tesfay, S., Lukasek, K., Michelsen, K. S., Wada, A., Hirayama, T., Arditi, M., et al. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.9.5398 · Cited by 358 · see citing works
Antiviral properties of lactoferrin--a natural immunity molecule
Berlutti, F., Pantanella, F., Natalizi, T., Frioni, A., Paesano, R., Polimeni, A., & Valenti, P. (2011) · Molecules · doi:10.3390/molecules16086992 · Cited by 356 · see citing works
Self-citationThe Isolation of a Red Protein from Milk2
Groves, M. L. (1960) · Journal of the American Chemical Society · doi:10.1021/ja01498a029 · Cited by 350 · see citing works
Hepcidin-Induced Endocytosis of Ferroportin Is Dependent on Ferroportin Ubiquitination
Qiao, B., Sugianto, P., Fung, E., del-Castillo-Rueda, A., Moran-Jimenez, M.-J., Ganz, T., & Nemeth, E. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.03.018 · Cited by 334 · see citing works
Bacterial heme sources: the role of heme, hemoprotein receptors and hemophores
Wandersman, C., & Stojiljkovic, I. (2000) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(00)00078-3 · Cited by 318 · see citing works
Generation of inflammatory stimuli: how bacteria set up inflammatory responses in the gingiva
Madianos, P. N., Bobetsis, Y. A., & Kinane, D. F. (2005) · Journal Of Clinical Periodontology · doi:10.1111/j.1600-051x.2005.00821.x · Cited by 310 · see citing works
Inflammatory Cytokines and Spontaneous Preterm Birth in Asymptomatic Women
Wei, S. Q., Fraser, W. D., & Luo, Z. (2010) · Obstetrics and Gynecology · doi:10.1097/aog.0b013e3181e6dbc0 · Cited by 301 · see citing works
Isolation of an Iron-Containing Red Protein from Human Milk.
Johanson, B., Virtanen, A. I., Tweit, R. C., & Dodson, R. M. (1960) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.14-0510 · Cited by 301 · see citing works
Adlerova, L., Bartoskova, A., & Faldyna, M. (2008) · Veterinární Medicína · doi:10.17221/1978-vetmed · Cited by 285 · see citing works
A structural framework for understanding the multifunctional character of lactoferrin
Baker, E. N., & BAKER, H. (2008) · Biochimie · doi:10.1016/j.biochi.2008.05.006 · Cited by 279 · see citing works
Mazurier, J., & Spik, G. (1980) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(80)90112-9 · Cited by 278 · see citing works
Préparation et propriétés de la lactosidérophiline (lactotransferrine) du lait de femme
Montreuil, J., Tonnelat, J., & Mullet, S. (1960) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(60)91478-5 · Cited by 265 · see citing works
The Management of Inflammation in Periodontal Disease
Dyke, T. E. V. (2008) · Journal of Periodontology · doi:10.1902/jop.2008.080173 · Cited by 261 · see citing works
Iron metabolism and the innate immune response to infection
Johnson, E. E., & Wessling-Resnick, M. (2012) · Microbes and Infection · doi:10.1016/j.micinf.2011.10.001 · Cited by 253 · cited 1× · see citing works
“Iron supplementation in AI patients could heighten iron overload in tissues and secretions, thus increasing both susceptibility and severity of infections, especially in developing countries with a high incidence of microbial and parasitic infections [131].”
BackgroundMechanisms and control of pathologic bone loss in periodontitis
Bartold, P. M., Cantley, M. D., & Haynes, D. R. (2010) · Periodontology 2000 · doi:10.1111/j.1600-0757.2010.00347.x · Cited by 252 · see citing works
Interleukin-6 stimulates prostaglandin production by human amnion and decidual cells.
Mitchell, M. D., Dudley, D. J., Edwin, S. S., & Schiller, S. L. (1991) · European Journal of Pharmacology · doi:10.1016/0014-2999(91)90090-d · Cited by 228 · see citing works
MacGillivray, R. T. A., Moore, S. A., Chen, J., Anderson, B. F., Baker, H. M., Luo, Y., Bewley, M. C., Smith, C. A., Murphy, M. E. P., Wang, Y., et al. (1998) · Biochemistry · doi:10.1021/bi980355j · Cited by 227 · see citing works
Needleman, I. G., Ashley, P. F., Petrie, A., Fortune, F., Turner, W., Jones, J. C., Niggli, J., Engebretsen, L., Budgett, R., Donos, N., et al. (2013) · British Journal of Sports Medicine · doi:10.1136/bjsports-2013-092891 · Cited by 221 · see citing works
Structure and Reactivity of Transferrins
Baker, E. N. (1994) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60176-2 · Cited by 215 · see citing works
The orchestration of body iron intake: how and where do enterocytes receive their cues?
Frazer, D. M., & Anderson, G. J. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/s1079-9796(03)00039-1 · Cited by 211 · see citing works
Iron Metabolism: Iron Deficiency and Iron Overload
Andrews, N. C. (2000) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.1.1.75 · Cited by 209 · see citing works
Lactoferrin and transferrin: Functional variations on a common structural framework
Baker, E. N., Baker, H. M., & Kidd, R. D. (2002) · Biochemistry and Cell Biology · doi:10.1139/o01-153 · Cited by 205 · see citing works
Legrand, D. (2012) · Biochemistry and Cell Biology · doi:10.1139/o11-056 · Cited by 193 · see citing works
Iron homeostasis: An anthropocentric perspective
Coffey, R., & Ganz, T. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.781823 · Cited by 189 · see citing works
Ferumoxytol as an Intravenous Iron Replacement Therapy in Hemodialysis Patients
Provenzano, R., Schiller, B. M., Rao, M., Coyne, D. W., Brenner, L., & Pereira, B. J. G. (2009) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.02840608 · Cited by 187 · see citing works
Bruns, C. M., Nowalk, A. J., Arvai, A. S., McTigue, M. A., Vaughan, K. G., Mietzner, T. A., & McRee, D. E. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb1197-919 · Cited by 177 · see citing works
A kinetic study on the distribution of Cu(II)-ions between albumin and transferrin
Løvstad, R. A. (2004) · BioMetals · doi:10.1023/b:biom.0000018362.37471.0b · Cited by 175 · see citing works
Rogan, M. P., Taggart, C. C., Greene, C. M., Murphy, P. G., O’Neill, S. J., & McElvaney, N. G. (2004) · The Journal of Infectious Diseases · doi:10.1086/423821 · Cited by 171 · see citing works
Transferrins: insights into structure and function from studies on lactoferrin
Baker, E. N., Rumball, S. V., & Anderson, B. F. (1987) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(87)90163-0 · Cited by 168 · see citing works
Khalafallah, A. A., & Dennis, A. E. (2012) · Journal of Pregnancy · doi:10.1155/2012/630519 · Cited by 166 · see citing works
Studying Lactoferrin N-Glycosylation
Karav, S., German, J., Rouquié, C., Parc, A. L., & Barile, D. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18040870 · Cited by 166 · see citing works
Österlund, P., Pirhonen, J., Ikonen, N., Rönkkö, E., Strengell, M., Mäkelä, S. M., Broman, M., Hamming, O. J., Hartmann, R., Ziegler, T., et al. (2010) · Journal of Virology · doi:10.1128/jvi.01619-09 · Cited by 162 · see citing works
Sorokin, Y., Romero, R., Mele, L., Wapner, R., Iams, J., Dudley, D., Spong, C., Peaceman, A., Leveno, K., Harper, M., et al. (2010) · American Journal of Perinatology · doi:10.1055/s-0030-1249366 · Cited by 154 · see citing works
Gerstein, M., Anderson, B. F., Norris, G. E., Baker, E. N., Lesk, A. M., & Chothia, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1592 · Cited by 150 · see citing works
Thompson, A. B., Bohling, T., Payvandi, F., & Rennard, S. I. (1990) · PubMed · Cited by 149 · see citing works
Immunomodulatory effects of lactoferrin on antigen presenting cells
Puddu, P. E., Valenti, P., & Gessani, S. (2008) · Biochimie · doi:10.1016/j.biochi.2008.05.005 · Cited by 141 · see citing works
Self-citationBiophysical Characterization of Lipopolysaccharide and Lipid A Inactivation by Lactoferrin
Brandenburg, K., Jürgens, G., Müller, M., Fukuoka, S., & Koch, M. H. J. (2001) · Biological Chemistry · doi:10.1515/bc.2001.152 · Cited by 140 · see citing works
Iron supplementation generates hydroxyl radical in vivo. An ESR spin-trapping investigation.
Kadiiska, M. B., Burkitt, M. J., Xiang, Q.-H., & Mason, R. P. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118205 · Cited by 140 · see citing works
Wakabayashi, H., Yamauchi, K., Kobayashi, T., Yaeshima, T., Iwatsuki, K., & Yoshie, H. (2009) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01688-08 · Cited by 136 · see citing works
Goepfert, A. R., Goldenberg, R. L., Andrews, W. W., Hauth, J. C., Mercer, B. M., Iams, J. D., Meis, P. J., Moawad, A., Thom, E. A., VanDorsten, J. P., et al. (2001) · American Journal of Obstetrics and Gynecology · doi:10.1067/mob.2001.109653 · Cited by 134 · see citing works
Qiu, J., Hendrixson, D. R., Baker, E. N., Murphy, T. F., Geme, J. W. S., & Plaut, A. G. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12641 · Cited by 133 · see citing works
Baker, H. M., & Baker, E. N. (2012) · Biochemistry and Cell Biology · doi:10.1139/o11-071 · Cited by 130 · cited 1× · see citing works
“The iron-saturated closed form is highly stable and more resistant to digestion by proteases compared to the unsaturated open one [51].”
BackgroundGotsch, F., Gotsch, F., Romero, R. J., Erez, O., Vaisbuch, E., Kusanovic, J. P., Mazaki‐Tovi, S., Kim, S. K., Hassan, S. S., & Yeo, L. (2009) · The Journal of Maternal-Fetal & Neonatal Medicine · doi:10.1080/14767050902860690 · Cited by 130 · see citing works
Nanomedicine as an emerging approach against intracellular pathogens
Li, B., & Armstead (2011) · International Journal of Nanomedicine · doi:10.2147/ijn.s27285 · Cited by 130 · see citing works
Siderophores for molecular imaging applications
Petřík, M., Zhai, C., Haas, H., & Decristoforo, C. (2016) · Clinical and Translational Imaging · doi:10.1007/s40336-016-0211-x · Cited by 129 · see citing works
Sociobehavioral aspects of periodontal disease
Thomson, W. M., Sheiham, A., & Spencer, A. J. (2012) · Periodontology 2000 · doi:10.1111/j.1600-0757.2011.00405.x · Cited by 125 · see citing works
Berlutti, F., Morea, C., Battistoni, A., Sarli, S., Cipriani, P., Superti, F., Ammendolia, M. G., & Valenti, P. (2005) · International Journal of Immunopathology and Pharmacology · doi:10.1177/039463200501800407 · Cited by 122 · see citing works
Self-citationTreatment of chlamydial infections: 2014 update
Kohlhoff, S. A., & Hammerschlag, M. R. (2015) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.2015.999041 · Cited by 122 · see citing works
Hematologic, iron-related, and acute-phase protein responses to sustained strenuous exercise
Taylor, C. B., Rogers, G. G., Goodman, C. A., Baynes, R. D., Bothwell, T. H., Bezwoda, W. R., Kramer, F., & Hattingh, J. (1987) · Journal of Applied Physiology · doi:10.1152/jappl.1987.62.2.464 · Cited by 121 · see citing works
Cellular internalization of lactoferrin in intestinal epithelial cells
Ashida, K., Sasaki, H., Suzuki, Y. A., & Lönnerdal, B. (2004) · BioMetals · doi:10.1023/b:biom.0000027710.13543.3f · Cited by 117 · see citing works
Susceptibility of Porphyromonas gingivalis in biofilms to amoxicillin, doxycycline and metronidazole
Larsen, T. (2002) · Oral Microbiology and Immunology · doi:10.1034/j.1399-302x.2002.170501.x · Cited by 117 · see citing works
Ji, Z. S., & Mahley, R. W. (1994) · Arteriosclerosis and Thrombosis A Journal of Vascular Biology · doi:10.1161/01.atv.14.12.2025 · Cited by 117 · see citing works
Hendrixson, D. R., Qiu, J., Shewry, S. C., Fink, D. L., Petty, S., Baker, E. N., Plaut, A. G., & Geme, J. W. S. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03327.x · Cited by 115 · see citing works
Dental erosive wear and salivary flow rate in physically active young adults
Mulic, A., Tveit, A. B., Songe, D., Sivertsen, H., & Skaare, A. B. (2012) · BMC Oral Health · doi:10.1186/1472-6831-12-8 · Cited by 114 · see citing works
Superti, F., Siciliano, R. A., Rega, B., Giansanti, F., Valenti, P., & Antonini, G. (2001) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(01)00178-7 · Cited by 112 · see citing works
Self-citationLactoferrin Impairs Type III Secretory System Function in EnteropathogenicEscherichia coli
Ochoa, T. J., Noguera-Obenza, M., Ebel, F., Guzmán, C. A., Gomez, H. F., & Cleary, T. G. (2003) · Infection and Immunity · doi:10.1128/iai.71.9.5149-5155.2003 · Cited by 111 · see citing works
Ceruloplasmin-ferroportin system of iron traffic in vertebrates
Musci, G. (2014) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v5.i2.204 · Cited by 108 · see citing works
Papapanou, P. N. (2015) · International Dental Journal · doi:10.1111/idj.12185 · Cited by 105 · see citing works
Extracellular Heme Uptake and the Challenge of Bacterial Cell Membranes
Huang, W., & Wilks, A. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014214 · Cited by 105 · see citing works
Characterization of the Glycosaminoglycan-Binding Region of Lactoferrin
Wu, H. F., Monroe, D. M., & Church, F. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1139 · Cited by 104 · see citing works
Human Lactoferrin Impairs Virulence ofShigella flexneri
Gomez, H. F., Ochoa, T. J., Carlin, L. G., & Cleary, T. G. (2002) · The Journal of Infectious Diseases · doi:10.1086/345875 · Cited by 101 · see citing works
Puddu, P., Latorre, D., Carollo, M., Catizone, A., Ricci, G., Valenti, P., & Gessani, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022504 · Cited by 100 · see citing works
Self-citationCutone, A., Rosa, L., Lepanto, M. S., Scotti, M. J., Berlutti, F., di Patti, M. C. B., Musci, G., & Valenti, P. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00705 · Cited by 99 · see citing works
Self-citationStites, S. W., Walters, B., O'Brien-Ladner, A. R., Bailey, K., & Wesselius, L. (1998) · CHEST Journal · doi:10.1378/chest.114.3.814 · Cited by 95 · see citing works
Paesano, R., Torcia, F., Berlutti, F., Pacifici, E., Ebano, V., Moscarini, M., & Valenti, P. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-040 · Cited by 95 · see citing works
Self-citationThe Effects of Acute Exercise Bouts on Hepcidin in Women
Newlin, M. K., Williams, S., McNamara, T., Tjalsma, H., Swinkels, D. W., & Haymes, E. M. (2012) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.22.2.79 · Cited by 91 · see citing works
Uptake and release of metal ions by transferrin and interaction with receptor 1
Chahine, J. E. H., Hémadi, M., & Duong, N.-T. H. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.07.008 · Cited by 90 · see citing works
Targeted disruption of hepcidin in the liver recapitulates the hemochromatotic phenotype
Zumerle, S., Mathieu, J. R. R., Delga, S., Heinis, M., Viatte, L., Vaulont, S., & Peyssonnaux, C. (2014) · Blood · doi:10.1182/blood-2014-01-550467 · Cited by 87 · see citing works
Rossi, P., Giansanti, F., Boffi, A., Ajello, M., Valenti, P., Chiancone, E., & Antonini, G. (2002) · Biochemistry and Cell Biology · doi:10.1139/o01-209 · Cited by 86 · see citing works
Self-citationHouben, M. L., Nikkels, P. G. J., van Bleek, G. M., Visser, G. H. A., Rovers, M. M., van Kessel, H. I., de Waal, W. J., Schuijff, L. S., Evers, A. C. C., Kimpen, J. L. L., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006572 · Cited by 86 · see citing works
Berlutti, F., Schippa, S., Morea, C., Sarli, S., Perfetto, B., Donnarumma, G., & Valenti, P. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-039 · Cited by 82 · see citing works
Self-citationThe Development of Awareness of Iron-Withholding Defense
Weinberg, E. D. (1993) · Perspectives in biology and medicine · doi:10.1353/pbm.1993.0063 · Cited by 81 · see citing works
Iron Supplementation May Aggravate Inflammatory Status of Colitis in a Rat Model
Reifen, R. M., Matas, Z., Zeidel, L., Berkovich, Z., & Bujanover, Y. (2000) · Digestive Diseases and Sciences · doi:10.1023/a:1005437331967 · Cited by 80 · see citing works
Lyon, D., Cheng, C., Howland, L. C., Rattican, D., Jallo, N., Pickler, R. H., Brown, L., & McGrath, J. M. (2009) · Biological Research For Nursing · doi:10.1177/1099800409344620 · Cited by 80 · see citing works
Smith, C. A., Anderson, B. F., Baker, H. M., & Baker, E. N. (1992) · Biochemistry · doi:10.1021/bi00133a020 · Cited by 77 · see citing works
Elite Athletes and Oral Health
Bryant, S., McLaughlin, K., Morgaine, K. C., & Drummond, B. (2011) · International Journal of Sports Medicine · doi:10.1055/s-0031-1277192 · Cited by 77 · see citing works
Li, L., Hangoc, G., Oliff, A. I., Chen, L. T., Shen, R., & Broxmeyer, H. E. (1987) · PubMed · Cited by 76 · see citing works
Suzuki, Y. A., Wong, H., Ashida, K.-Y., Schryvers, A. B., & Lönnerdal, B. (2008) · Biochemistry · doi:10.1021/bi8012164 · Cited by 75 · see citing works
Three-dimensional structure of mare diferric lactoferrin at 2.6 Å resolution
Sharma, A. K., Paramasivam, M., Srinivasan, A., Yadav, M. P., & Singh, T. P. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2767 · Cited by 74 · see citing works
The effect of lactoferrin on oral bacterial attachment
Arslan, S. Y., Leung, K. P., & Wu, C. D. (2009) · Oral Microbiology and Immunology · doi:10.1111/j.1399-302x.2009.00537.x · Cited by 72 · see citing works
Rose, J. E., Meyer, D. H., & Fives-Taylor, P. M. (2003) · Infection and Immunity · doi:10.1128/iai.71.5.2384-2393.2003 · Cited by 71 · see citing works
de Araújo, A. N., & Giugliano, L. G. (2001) · BMC Microbiology · doi:10.1186/1471-2180-1-25 · Cited by 70 · see citing works
Paesano, R., Berlutti, F., Pietropaoli, M., Pantanella, F., Pacifici, E., Goolsbee, W., & Valenti, P. (2010) · BioMetals · doi:10.1007/s10534-010-9335-z · Cited by 69 · see citing works
Self-citationFrioni, A., Conte, M. P., Cutone, A., Longhi, C., Musci, G., di Patti, M. C. B., Natalizi, T., Marazzato, M., Lepanto, M. S., Puddu, P., et al. (2014) · BioMetals · doi:10.1007/s10534-014-9740-9 · Cited by 69 · see citing works
Self-citationPaesano, R., Berlutti, F., Pietropaoli, M., Goolsbee, W., Pacifici, E., & Valenti, P. (2010) · International Journal of Immunopathology and Pharmacology · doi:10.1177/039463201002300220 · Cited by 69 · see citing works
Self-citationMaternal Serum Interleukin-6 Concentration as a Marker for Impending Preterm Delivery
Murtha, A. P. (1998) · Obstetrics and Gynecology · doi:10.1016/s0029-7844(97)00602-9 · Cited by 68 · see citing works
He, C.-S., Tsai, M.-L., Ko, M.-H., Chang, C.-K., & Fang, S.-H. (2010) · European Journal of Applied Physiology · doi:10.1007/s00421-010-1574-8 · Cited by 67 · see citing works
Ortiz, R., Toblli, J. E., Romero, J. D., Monterrosa, B., Frer, C., Macagno, E., & Breymann, C. (2011) · The Journal of Maternal-Fetal & Neonatal Medicine · doi:10.3109/14767058.2011.599080 · Cited by 66 · see citing works
Periodontitis, periodontopathic bacteria and lactoferrin
Wakabayashi, H., Kondo, I., Kobayashi, T., Yamauchi, K., Toida, T., Iwatsuki, K., & Yoshie, H. (2010) · BioMetals · doi:10.1007/s10534-010-9304-6 · Cited by 66 · see citing works
Properties of a Heparin-binding Peptide Derived from Bovine Lactoferrin
SHIMAZAKI, K., Tazume, T., Uji, K., Tanaka, M., Kumura, H., Mikawa, K., & Shimo‐Oka, T. (1998) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(98)75843-6 · Cited by 66 · see citing works
The effect of protein-coated contact lenses on the adhesion and viability of gram negative bacteria
Williams, T. J., Schneider, R. P., & Willcox, M. D. P. (2003) · Current Eye Research · doi:10.1076/ceyr.27.4.227.16602 · Cited by 65 · see citing works
Enhanced antimicrobial activity of lactoferrin by binding to the bacterial surface.
Dalmastri, C., Valenti, P., Visca, P., Vittorioso, P., & Orsi, N. (1988) · PubMed · Cited by 63 · see citing works
Self-citationCutone, A., Frioni, A., Berlutti, F., Valenti, P., Musci, G., & di Patti, M. C. B. (2014) · BioMetals · doi:10.1007/s10534-014-9742-7 · Cited by 63 · see citing works
Self-citationKawasaki, Y., Tazume, S., Shimizu, K., Matsuzawa, H., Dosako, S., Isoda, H., Tsukiji, M., FUJIMURA, R., Muranaka, Y., & ISIHIDA, H. (2000) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.64.348 · Cited by 60 · see citing works
The Chlamydia trachomatis Ctad1 invasin exploits the human integrin β1 receptor for host cell entry
Stallmann, S., & Hegemann, J. H. (2015) · Cellular Microbiology · doi:10.1111/cmi.12549 · Cited by 60 · see citing works
Paesano, R., Pacifici, E., Benedetti, S., Berlutti, F., Frioni, A., Polimeni, A., & Valenti, P. (2014) · BioMetals · doi:10.1007/s10534-014-9723-x · Cited by 59 · see citing works
Self-citationPaesano, R., Pietropaoli, M., Gessani, S., & Valenti, P. (2008) · Biochimie · doi:10.1016/j.biochi.2008.06.004 · Cited by 58 · see citing works
Self-citationInfluence of lactoferrin on the entry process of Escherichia coli HB101(pRI203) in HeLa cells
Longhi, C., Conte, M. P., Seganti, L., Polidoro, M., Alfsen, A., & Valenti, P. (1993) · Medical Microbiology and Immunology · doi:10.1007/bf00195948 · Cited by 57 · see citing works
Self-citationLactoferrin and oral diseases: current status and perspective in periodontitis.
Berlutti, F., Pilloni, A., Pietropaoli, M., Polimeni, A., & Valenti, P. (2011) · PubMed Central · Cited by 55 · see citing works
Self-citationAnti-invasive activity of bovine lactoferrin towards group A streptococci
Ajello, M., Greco, R., Giansanti, F., Massucci, M. T., Antonini, G., & Valenti, P. (2002) · Biochemistry and Cell Biology · doi:10.1139/o01-211 · Cited by 55 · see citing works
Self-citationLactoferrin against Staphylococcus aureus Mastitis
Diarra, M. S., Petitclerc, D., Deschênes, É., Lessard, N., Grondin, G., Talbot, B. G., & Lacasse, P. (2003) · Veterinary Immunology and Immunopathology · doi:10.1016/s0165-2427(03)00098-9 · Cited by 54 · see citing works
Lindenmüller, I. H., & Lambrecht, J. T. (2011) · Current problems in dermatology · doi:10.1159/000321060 · Cited by 53 · see citing works
Ochoa, T. J., Brown, E. L., Guion, C. E., Chen, J. Z., McMahon, R. J., & Cleary, T. G. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-053 · Cited by 51 · see citing works
Effect of lactoferrin on Helicobacter felis induced gastritis
Dial, E. J., & Lichtenberger, L. M. (2002) · Biochemistry and Cell Biology · doi:10.1139/o01-205 · Cited by 51 · see citing works
Plaut, A. G., Qiu, J., & Geme, J. W. S. (2000) · Vaccine · doi:10.1016/s0264-410x(00)00296-6 · Cited by 50 · see citing works
Oho, T., Mitoma, M., & Koga, T. (2002) · Infection and Immunity · doi:10.1128/iai.70.9.5279-5282.2002 · Cited by 50 · cited 1× · see citing works
“mutans to HA through residues 473–538 of its C-lobe confirmed that this activity is unrelated to Lf iron-binding properties [79].”
BackgroundRizvi, S. H., & Schoen, R. E. (2011) · The American Journal of Gastroenterology · doi:10.1038/ajg.2011.232 · Cited by 49 · see citing works
Effect of bovine lactoferrin on Chlamydia trachomatis infection and inflammation
Sessa, R., Pietro, M. D., Filardo, S., Bressan, A., Rosa, L., Cutone, A., Frioni, A., Berlutti, F., Paesano, R., & Valenti, P. (2016) · Biochemistry and Cell Biology · doi:10.1139/bcb-2016-0049 · Cited by 48 · see citing works
Self-citationEstrada‐Gutiérrez, G., Gomez‐Lopez, N., Zaga‐Clavellina, V., Giono-Cerezo, S., Espejel-Núñez, A., González-Jiménez, M. A., y Sosa, S. E., Olson, D. M., & Vadillo‐Ortega, F. (2010) · Infection and Immunity · doi:10.1128/iai.00522-10 · Cited by 46 · see citing works
Puddu, P., Carollo, M., Belardelli, F., Valenti, P., & Gessani, S. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.1106688 · Cited by 45 · see citing works
Self-citationThe lactoferrin receptor complex in Gram negative bacteria
Beddek, A. J., & Schryvers, A. B. (2010) · BioMetals · doi:10.1007/s10534-010-9299-z · Cited by 43 · see citing works
de Araújo, A. N., & Giugliano, L. G. (2000) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2000.tb08996.x · Cited by 42 · see citing works
Karthikeyan, S., Paramasivam, M., Yadav, S., Srinivasan, A., & Singh, T. P. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444999010951 · Cited by 42 · see citing works
Paesano, R., Natalizi, T., Berlutti, F., & Valenti, P. (2012) · Pathogens and Global Health · doi:10.1179/2047773212y.0000000043 · Cited by 42 · see citing works
Self-citationIron acquisition through the bacterial transferrin receptor
Pogoutse, A. K., & Moraes, T. F. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2017.1293606 · Cited by 42 · see citing works
Latorre, D., Berlutti, F., Valenti, P., Gessani, S., & Puddu, P. (2012) · Biochemistry and Cell Biology · doi:10.1139/o11-059 · Cited by 41 · see citing works
Self-citationWiller, E. M., Lima, R. D. L., & Giugliano, L. G. (2004) · BMC Microbiology · doi:10.1186/1471-2180-4-18 · Cited by 40 · see citing works
Visca, P., Berlutti, F., Vittorioso, P., Dalmastri, C., Thaller, M. C., & Valenti, P. (1989) · Medical Microbiology and Immunology · doi:10.1007/bf00203302 · Cited by 40 · see citing works
Self-citationSports Drinks and Dental Erosion
Noble, W. H., Donovan, T. E., & Geissberger, M. J. (2011) · Journal of the California Dental Association · doi:10.1080/19424396.2011.12221890 · Cited by 36 · see citing works
Fujita, T., Yumoto, H., Shiba, H., Ouhara, K., Miyagawa, T., Nagahara, T., Matsuda, S., Kawaguchi, H., Matsuo, T., Murakami, S., et al. (2011) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.2011.01404.x · Cited by 36 · see citing works
Kim, C. W., Lee, T. H., Park, K. H., Choi, S.-Y., & Kim, J. (2012) · FEBS Letters · doi:10.1016/j.febslet.2011.12.011 · Cited by 35 · see citing works
Valenti, P., Catizone, A., Pantanella, F., Frioni, A., Natalizi, T., Tendini, M., & Berlutti, F. (2011) · International Journal of Immunopathology and Pharmacology · doi:10.1177/039463201102400423 · Cited by 35 · see citing works
Self-citationEffect of bovine lactoferricin on enteropathogenic Yersinia adhesion and invasion in HEp-2 cells
Biase, A. M. D., Tinari, A., Pietrantoni, A., Antonini, G., Valenti, P., Conte, M. P., & Superti, F. (2004) · Journal of Medical Microbiology · doi:10.1099/jmm.0.05410-0 · Cited by 34 · see citing works
Self-citationThe effects of tetracycline, minocycline, doxycycline and ofloxacin on Prevotella intermedia biofilm
Takahashi, N., Ishihara, K., Kimizuka, R., Okuda, K., & Kato, T. (2006) · Oral Microbiology and Immunology · doi:10.1111/j.1399-302x.2006.00305.x · Cited by 33 · see citing works
Berlutti, F., Catizone, A., Ricci, G., Frioni, A., Natalizi, T., Valenti, P., & Polimeni, A. (2010) · International Journal of Immunopathology and Pharmacology · doi:10.1177/039463201002300430 · Cited by 32 · see citing works
Self-citationHayworth, J. L., Kasper, K. J., Leon‐Ponte, M., Herfst, C. A., Yue, D., Brintnell, W. C., Mazzuca, D. M., Heinrichs, D. E., Cairns, E., Madrenas, J., et al. (2009) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2009.03963.x · Cited by 30 · see citing works
Berlutti, F., Superti, F., Nicoletti, M., Morea, C., Frioni, A., Ammendolia, M. G., Battistoni, A., & Valenti, P. (2008) · International Journal of Immunopathology and Pharmacology · doi:10.1177/039463200802100107 · Cited by 29 · see citing works
Self-citationThe expressions of claudin-1 and E-cadherin in junctional epithelium
Fujita, T., Hayashida, K., Shiba, H., Kishimoto, A., Matsuda, S., Takeda, K., Kawaguchi, H., & Kurihara, H. (2010) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.2009.01258.x · Cited by 26 · see citing works
The dual role of Escherichia coli in the course of ulcerative colitis
Pilarczyk-Żurek, M., Strus, M., Adamski, P., & Heczko, P. B. (2016) · BMC Gastroenterology · doi:10.1186/s12876-016-0540-2 · Cited by 26 · see citing works
The prevalence of oral health problems in participants of the 1992 Olympic Games in Barcelona.
Badia, D. S., Batchelor, P., & Sheiham, A. (1994) · PubMed · Cited by 25 · see citing works
Zaïm, M., Piselli, L., Fioravanti, P., & Kanony-Truc, C. (2011) · European Journal of Nutrition · doi:10.1007/s00394-011-0210-7 · Cited by 24 · see citing works
The management of iron deficiency in menometrorrhagia
Palacios, S. (2011) · Gynecological Endocrinology · doi:10.3109/09513590.2012.636916 · Cited by 20 · see citing works
de Araújo, A. N. (2000) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(00)00028-8 · Cited by 19 · see citing works
The dental condition of Olympic Games contestants--a pilot study, 1968.
Forrest, J. O. (1969) · PubMed · Cited by 17 · see citing works
Anti-Invasive Activity of Bovine Lactoferrin against Listeria monocytogenes
Antonini, G., Catania, M. R., Greco, R., Longhi, C., Pisciotta, M. G., Seganti, L., & Valenti, P. (1997) · Journal of Food Protection · doi:10.4315/0362-028x-60.3.267 · Cited by 16 · see citing works
Self-citationBovine lactoferrin interacts with cable pili of Burkholderia cenocepacia
Ammendolia, M. G., Bertuccini, L., Iosi, F., Minelli, F., Berlutti, F., Valenti, P., & Superti, F. (2010) · BioMetals · doi:10.1007/s10534-010-9333-1 · Cited by 15 · see citing works
Self-citationFujita, T., Ashikaga, A., Shiba, H., Kajiya, M., Kishimoto, A., Hirata, R., Tsunekuni, N., Hirono, C., Kawaguchi, H., Shiba, Y., et al. (2007) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.2007.01000.x · Cited by 13 · see citing works
Crystallographic Studies on Metal and Anion Substituted Human Lactoferrin
Smith, C. A., Baker, H. M., Shongwe, M. S., Anderson, B. F., & Baker, E. N. (1994) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-2548-6_29 · Cited by 5 · see citing works
Kumar, H., Wen, J., Shaw, J., Cornish, J., & Bunt, C. R. (2013) · Current Drug Delivery · doi:10.2174/15672018113109990043 · Cited by 4 · see citing works
Antiinvasive activity of bovine lactoferrin towards Listeria monocytogenes.
ANTONINI, G., CATANIA, M., GRECO, R., Pisciotta, M. G., Longhi, C., Seganti, L., & VALENTI, P. (1997) · IRIS Research product catalog (Sapienza University of Rome) · Cited by 2 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Bhol, N. K., Bhanjadeo, M. M., Singh, A. K., Dash, U. C., Ojha, R. R., Majhi, S., Duttaroy, A. K., & Jena, A. B. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117177 · Cited by 531 · see citing works
Kell, D. B., Heyden, E. L., & Pretorius, E. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01221 · Cited by 460 · see citing works
Iron in infection and immunity
Nairz, M., & Weiss, G. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2020.100864 · Cited by 359 · see citing works
Mrityunjaya, M., Pavithra, V., Neelam, R., Janhavi, P., Halami, P. M., & Veeranna, R. P. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.570122 · Cited by 337 · see citing works
Iron Metabolism in Obesity and Metabolic Syndrome
González-Domínguez, Á., Visiedo-García, F. M., Domínguez-Riscart, J., González-Domínguez, R., Mateos, R. M., & Lechuga-Sancho, A. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155529 · Cited by 227 · see citing works
Role of Lactobacilli and Lactoferrin in the Mucosal Cervicovaginal Defense
Valenti, P., Rosa, L., Capobianco, D., Lepanto, M. S., Schiavi, E., Cutone, A., Paesano, R., & Mastromarino, P. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00376 · Cited by 218 · see citing works
Self-citationLactoferrin’s Anti-Cancer Properties: Safety, Selectivity, and Wide Range of Action
Cutone, A., Rosa, L., Ianiro, G., Lepanto, M. S., di Patti, M. C. B., Valenti, P., & Musci, G. (2020) · Biomolecules · doi:10.3390/biom10030456 · Cited by 212 · see citing works
Self-citationKontoghiorghes, G. J., & Kontoghiorghe, C. (2020) · Cells · doi:10.3390/cells9061456 · Cited by 197 · see citing works
Gruden, Š., & Ulrih, N. P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011264 · Cited by 187 · see citing works
The Lactoferrin Phenomenon—A Miracle Molecule
Kowalczyk, P., Kaczyńska, K., Kleczkowska, P., Bukowska‐Ośko, I., Kramkowski, K., & Sulejczak, D. (2022) · Molecules · doi:10.3390/molecules27092941 · Cited by 185 · see citing works
Invited review: Acid whey trends and health benefits
Rocha-Mendoza, D., Kosmerl, E., Krentz, A., Zhang, L., Badiger, S., Miyagusuku-Cruzado, G., Mayta-Apaza, A. C., Giusti, M. M., Jiménez‐Flores, R., & García‐Cano, I. (2020) · Journal of Dairy Science · doi:10.3168/jds.2020-19038 · Cited by 177 · see citing works
The Iron Tug-of-War between Bacterial Siderophores and Innate Immunity
Golonka, R. M., Yeoh, B. S., & Vijay–Kumar, M. (2019) · Journal of Innate Immunity · doi:10.1159/000494627 · Cited by 171 · see citing works
Lactoferrin as potential preventative and adjunct treatment for COVID-19
Chang, R. Y., Ng, T. B., & Sun, W. (2020) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2020.106118 · Cited by 160 · see citing works
Lactoferrin in aseptic and septic inflammation
Lepanto, M. S., Rosa, L., Paesano, R., Valenti, P., & Cutone, A. (2019) · Molecules · doi:10.3390/molecules24071323 · Cited by 147 · see citing works
Self-citationLactoferrin: A Glycoprotein Involved in Immunomodulation, Anticancer, and Antimicrobial Processes
Rascón-Cruz, Q., Espinoza-Sánchez, E. A., Siqueiros-Cendón, T., Nakamura-Bencomo, S. I., Arévalo‐Gallegos, S., & Iglesias-Figueroa, B. F. (2021) · Molecules · doi:10.3390/molecules26010205 · Cited by 129 · see citing works
Sienkiewicz, M., Jaśkiewicz, A., Tarasiuk, A., & Fichna, J. (2021) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1895063 · Cited by 125 · see citing works
Lactoferrin: A Critical Player in Neonatal Host Defense
Telang, S. (2018) · Nutrients · doi:10.3390/nu10091228 · Cited by 127 · see citing works
Regulation of zinc-dependent enzymes by metal carrier proteins
Thompson, M. W. (2022) · BioMetals · doi:10.1007/s10534-022-00373-w · Cited by 121 · see citing works
Iron supplementation and iron-fortified foods: a review
Man, Y., Xu, T., Adhikari, B., Zhou, C., Wang, Y., & Wang, B. (2021) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1876623 · Cited by 126 · see citing works
Decreased salivary lactoferrin levels are specific to Alzheimer's disease
González‐Sánchez, M., Bartolomé, F. B., Antequera, D., Puertas‐Martín, V., González, P., Gómez‐Grande, A., Velasco, S. L., Martín, A. H. S., Pérez-Martínez, D. A., Villarejo‐Galende, A., et al. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2020.102834 · Cited by 116 · see citing works
Iron: An Essential Element of Cancer Metabolism
Hsu, M. Y., Mina, E., Roetto, A., & Porporato, P. E. (2020) · Cells · doi:10.3390/cells9122591 · Cited by 116 · see citing works
Zarzosa-Moreno, D., Ávalos-Gómez, C., Ramírez-Texcalco, L. S., Torres-López, E., Ramírez-Mondragón, R., Hernández-Ramírez, J. O., Serrano‐Luna, J., & de la Garza, M. (2020) · Molecules · doi:10.3390/molecules25245763 · Cited by 112 · see citing works
Iron homeostasis and disorders revisited in the sepsis
Liu, Q., Wu, J., Zhang, X., Wu, X., Zhao, Y., & Ren, J. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.01.025 · Cited by 112 · see citing works
Campione, E., Cosio, T., Rosa, L., Lanna, C., Girolamo, S. D., Gaziano, R., Valenti, P., & Bianchi, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21144903 · Cited by 108 · see citing works
Self-citationWhey proteins and peptides in health-promoting functions – A review
Zhao, C., Chen, N., & Ashaolu, T. J. (2021) · International Dairy Journal · doi:10.1016/j.idairyj.2021.105269 · Cited by 107 · see citing works
Lactoferrin Against SARS-CoV-2: In Vitro and In Silico Evidences
Campione, E., Lanna, C., Cosio, T., Rosa, L., Conte, M. P., Iacovelli, F., Romeo, A., Falconi, M., Vecchio, C. D., Franchin, E., et al. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.666600 · Cited by 98 · see citing works
Self-citationMarchetti, M., Bei, O. D., Bettati, S., Campanini, B., Kovachka, S., Gianquinto, E., Spyrakis, F., & Ronda, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062145 · Cited by 92 · see citing works
The role of ferroptosis in acute lung injury
Liu, X., Zhang, J., & Xie, W. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-021-04327-7 · Cited by 93 · see citing works
Lepanto, M. S., Rosa, L., Cutone, A., Conte, M. P., Paesano, R., & Valenti, P. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02123 · Cited by 90 · see citing works
Self-citationA Review on Lactoferrin and Central Nervous System Diseases
Li, Y.-Q., & Guo, C. (2021) · Cells · doi:10.3390/cells10071810 · Cited by 91 · see citing works
Lactoferrin in Human Milk of Prolonged Lactation
Czosnykowska-Łukacka, M., Orczyk‐Pawiłowicz, M., Broers, B., & Królak‐Olejnik, B. (2019) · Nutrients · doi:10.3390/nu11102350 · Cited by 88 · see citing works
Dyrda-Terniuk, T., & Pomastowski, P. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c06887 · Cited by 85 · see citing works
El-Aidie, S. A.-A. M., & Khalifa, G. S. A. (2024) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.13319 · Cited by 80 · see citing works
Chang, S., Kim, Y.-H., Kim, Y.-J., Kim, Y., Moon, S., Lee, Y. Y., Jung, J. S., Kim, Y., Jung, H.-E., Kim, T.-J., et al. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01984 · Cited by 80 · see citing works
Lactoferrin as Antiviral Treatment in COVID-19 Management: Preliminary Evidence
Campione, E., Lanna, C., Cosio, T., Rosa, L., Conte, M., Iacovelli, F., Romeo, A., Falconi, M., Vecchio, C. D., Franchin, E., et al. (2021) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph182010985 · Cited by 66 · see citing works
Self-citationLópez-Machado, A., Díaz‐Garrido, N., Cano, A. C., Espina, M., Badı́a, J., Baldomà, L., Calpena, A. C., Souto, E. B., García, M. L., & Sánchez‐López, E. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13101698 · Cited by 78 · see citing works
Kaur, N., Sharma, P., Jaimni, S., Kehinde, B. A., & Kaur, S. (2019) · Chemical Engineering Communications · doi:10.1080/00986445.2019.1573169 · Cited by 71 · see citing works
Iglesias-Figueroa, B. F., Siqueiros-Cendón, T., Gutiérrez, D. A., Aguilera, R. J., Espinoza-Sánchez, E. A., Arévalo‐Gallegos, S., Varela-Ramı́rez, A., & Rascón-Cruz, Q. (2019) · APOPTOSIS · doi:10.1007/s10495-019-01539-7 · Cited by 71 · see citing works
Cutone, A., Lepanto, M. S., Rosa, L., Scotti, M. J., Rossi, A., Ranucci, S., Fino, I. D., Bragonzi, A., Valenti, P., Musci, G., et al. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092128 · Cited by 65 · see citing works
Self-citationMann, J. K., & Ndung’u, T. (2020) · Future Virology · doi:10.2217/fvl-2020-0170 · Cited by 65 · see citing works
The First-Row Transition Metals in the Periodic Table of Medicine
Cleave, C. V., & Crans, D. C. (2019) · Inorganics · doi:10.3390/inorganics7090111 · Cited by 67 · see citing works
di Patti, M. C. B., Cutone, A., Polticelli, F., Rosa, L., Lepanto, M. S., Valenti, P., & Musci, G. (2018) · BioMetals · doi:10.1007/s10534-018-0087-5 · Cited by 64 · see citing works
Self-citationHarnessing biomolecules for bioinspired dental biomaterials
Fischer, N., Münchow, E., Tamerler, C., Bottino, M. C., & Aparicio, C. (2020) · Journal of materials chemistry. B · doi:10.1039/d0tb01456g · Cited by 50 · see citing works
Berthon, B. S., Williams, L. M., Williams, E. J., & Wood, L. G. (2022) · Advances in Nutrition · doi:10.1093/advances/nmac047 · Cited by 62 · see citing works
Erythropoietin and Nrf2: key factors in the neuroprotection provided by apo-lactoferrin
Zakharova, E. T., Av, S., Павличенко, Н. Н., Kostevich, V. A., Abdurasulova, I. N., Владимирович, Ч. А., Voynova, I. V., Elizarova, A. Y., Kolmakov, N. N., Bass, M. G., et al. (2018) · BioMetals · doi:10.1007/s10534-018-0111-9 · Cited by 60 · see citing works
Artym, J., Zimecki, M., & Kruzel, M. L. (2021) · Biomedicines · doi:10.3390/biomedicines9080898 · Cited by 58 · see citing works
Viral Hepatitis and Iron Dysregulation: Molecular Pathways and the Role of Lactoferrin
Mancinelli, R., Rosa, L., Cutone, A., Lepanto, M. S., Franchitto, A., Onori, P., Gaudio, E., & Valenti, P. (2020) · Molecules · doi:10.3390/molecules25081997 · Cited by 55 · see citing works
Self-citationConvolutions in the rendition of nose to brain therapeutics from bench to bedside: Feats & fallacies
Goel, H., Kalra, V., Verma, S. K., Dubey, S. K., & Tiwary, A. K. (2021) · Journal of Controlled Release · doi:10.1016/j.jconrel.2021.12.009 · Cited by 52 · see citing works
Wotring, J. W., Fursmidt, R. M., Ward, L. S., & Sexton, J. Z. (2022) · Journal of Dairy Science · doi:10.3168/jds.2021-21247 · Cited by 52 · see citing works
Rosa, L., Tripepi, G. L., Naldi, E., Aimati, M., Santangeli, S., Venditto, F., Caldarelli, M., & Valenti, P. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10184276 · Cited by 51 · see citing works
Self-citationIron Pathways and Iron Chelation Approaches in Viral, Microbial, and Fungal Infections
Chhabra, R., Saha, A., Chamani, A., Schneider, N., Shah, R., & Nanjundan, M. (2020) · Pharmaceuticals · doi:10.3390/ph13100275 · Cited by 51 · see citing works
Nutraceuticals and Dietary Supplements for Older Adults with Long COVID-19
Tosato, M., Ciciarello, F., Zazzara, M. B., Pais, C., Savera, G., Picca, A., Galluzzo, V., Coelho‐Júnior, H. J., Calvani, R., Marzetti, E., et al. (2022) · Clinics in Geriatric Medicine · doi:10.1016/j.cger.2022.04.004 · Cited by 50 · see citing works
Arain, M. A., Khaskheli, G. B., Barham, G. S., & Marghazani, I. B. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e34051 · Cited by 49 · see citing works
Zhu, C., Li, L., Yang, G. H., Irfan, M., Wang, Z., Fang, S., & Qu, F. (2019) · Talanta · doi:10.1016/j.talanta.2019.06.088 · Cited by 49 · see citing works
Could nutritional supplements act as therapeutic adjuvants in COVID-19?
Costagliola, G., Spada, E., Comberiati, P., & Peroni, D. G. (2021) · The Italian Journal of Pediatrics/Italian journal of pediatrics · doi:10.1186/s13052-021-00990-0 · Cited by 49 · see citing works
Beverly, R. L., Underwood, M. A., & Dallas, D. C. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00604 · Cited by 47 · see citing works
Targeting cancer with lactoferrin nanoparticles: recent advances.
Kondapi, A. (2020) · Nanomedicine · doi:10.2217/nnm-2020-0090 · Cited by 42 · see citing works
Rahman, M. M., Islam, M. R., Akash, S., Mim, S. A., Rahaman, M. S., Emran, T. B., Akkol, E. K., Sharma, R., Alhumaydhi, F. A., Sweilam, S. H., et al. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.929430 · Cited by 49 · see citing works
Cutone, A., Colella, B., Pagliaro, A., Rosa, L., Lepanto, M. S., di Patti, M. C. B., Valenti, P., Bartolomeo, S. D., & Musci, G. (2019) · Cellular Signalling · doi:10.1016/j.cellsig.2019.109461 · Cited by 45 · see citing works
Self-citationCOVID-19 Infection in Children and Infants: Current Status on Therapies and Vaccines
Malcangi, G., Inchingolo, A. D., Inchingolo, A. M., Piras, F., Settanni, V., Garofoli, G., Palmieri, G., Ceci, S., Patano, A., Mancini, A., et al. (2022) · Children · doi:10.3390/children9020249 · Cited by 44 · see citing works
Nutraceuticals in Viral Infections: An Overview of the Immunomodulating Properties
Costagliola, G., Nuzzi, G., Spada, E., Comberiati, P., Verduci, E., & Peroni, D. G. (2021) · Nutrients · doi:10.3390/nu13072410 · Cited by 43 · see citing works
Filardo, S., Pietro, M. D., Tranquilli, G., Latino, M. A., Recine, N., Porpora, M. G., & Sessa, R. (2019) · mSystems · doi:10.1128/msystems.00094-19 · Cited by 41 · see citing works
Wuersching, S. N., Huth, K. C., Hickel, R., & Kollmuß, M. (2020) · Anaerobe · doi:10.1016/j.anaerobe.2020.102301 · Cited by 42 · see citing works
The 15-Months Clinical Experience of SARS-CoV-2: A Literature Review of Therapies and Adjuvants
Inchingolo, A. D., Dipalma, G., Inchingolo, A. M., Malcangi, G., Santacroce, L., D’Oria, M. T., Isacco, C. G., Bordea, I. R., Candrea, S., Scarano, A., et al. (2021) · Antioxidants · doi:10.3390/antiox10060881 · Cited by 40 · see citing works
Kontoghiorghes, G. J., Kolnagou, A., Demetriou, T., Neocleous, M., & Kontoghiorghe, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115546 · Cited by 41 · see citing works
Lactoferrin: from the structure to the functional orchestration of iron homeostasis
Ianiro, G., Rosa, L., di Patti, M. C. B., Valenti, P., Musci, G., & Cutone, A. (2022) · BioMetals · doi:10.1007/s10534-022-00453-x · Cited by 42 · see citing works
Self-citationRosa, L., Cutone, A., Conte, M. P., Campione, E., Bianchi, L., & Valenti, P. (2022) · BioMetals · doi:10.1007/s10534-022-00427-z · Cited by 39 · see citing works
Self-citationCutone, A., Ianiro, G., Lepanto, M. S., Rosa, L., Valenti, P., di Patti, M. C. B., & Musci, G. (2020) · Cancers · doi:10.3390/cancers12123806 · Cited by 39 · see citing works
Self-citationLópez-Machado, A., Díaz‐Garrido, N., Cano, A. C., Espina, M., Badı́a, J., Baldomà, L., Calpena, A. C., Biancardi, M., Souto, E. B., García, M. L., et al. (2021) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2021.121188 · Cited by 39 · see citing works
Physico-chemical properties influence the functions and efficacy of commercial bovine lactoferrins
Rosa, L., Cutone, A., Lepanto, M. S., Scotti, M. J., Conte, M. P., Paesano, R., & Valenti, P. (2018) · BioMetals · doi:10.1007/s10534-018-0092-8 · Cited by 38 · see citing works
Self-citationAntimicrobial Activity of the Peptide LfcinB15 against Candida albicans
Chang, C.-K., Kao, M., & Lan, C. (2021) · Journal of Fungi · doi:10.3390/jof7070519 · Cited by 38 · see citing works
Therapeutic Implications of Ferroptosis in Renal Fibrosis
Zhang, Y., Mou, Y., Zhang, J., Suo, C., Zhou, H., Gu, M. J., Wang, Z., & Tan, R. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.890766 · Cited by 37 · see citing works
Naidu, S. A. G., Clemens, R., & Naidu, A. S. (2022) · Journal of Dietary Supplements · doi:10.1080/19390211.2022.2075072 · Cited by 38 · see citing works
Lactoferrin: Cytokine Modulation and Application in Clinical Practice
Presti, S., Manti, S., Parisi, G. F., Papale, M. R., Barbagallo, I. A., Volti, G. L., & Leonardi, S. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10235482 · Cited by 34 · see citing works
Short-chain fatty acids—a key link between the gut microbiome and T-lymphocytes in neonates?
Bui, T., Paul, A., Guleria, S., O'Sullivan, J. M., & Toldi, G. (2025) · Pediatric Research · doi:10.1038/s41390-025-04075-0 · Cited by 33 · see citing works
Trauma-induced heme release increases susceptibility to bacterial infection
Lee, G. R., Gallo, D. J., de Souza, R. W. A., Tiwari‐Heckler, S., Csizmadia, E., Harbison, J., Shankar, S., Banner‐Goodspeed, V., Yaffe, M. B., Longhi, M. S., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.150813 · Cited by 32 · see citing works
Biomedical and Nutritional Applications of Lactoferrin
Coccolini, C., Berselli, E., Blanco-Llamero, C., Fathi, F., Oliveira, M. B. P., Krambeck, K., & Souto, E. B. (2023) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-023-10541-2 · Cited by 33 · see citing works
COVID-19 during Pregnancy and Postpartum:
Naidu, S. A. G., Clemens, R., Pressman, P., Zaigham, M., Davies, K. J. A., & Naidu, A. S. (2020) · Journal of Dietary Supplements · doi:10.1080/19390211.2020.1834047 · Cited by 31 · see citing works
Bukowska‐Ośko, I., Popiel, M., & Kowalczyk, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115799 · Cited by 32 · see citing works
The effect of lactoferrin in aging: role and potential
Li, B., Zhang, B., Liu, X., Zheng, Y., Han, K., Liu, H., Wu, C., Li, J., Fan, S., Peng, W., et al. (2021) · Food & Function · doi:10.1039/d1fo02750f · Cited by 31 · see citing works
Absolute and functional iron deficiency: Biomarkers, impact on immune system, and therapy
Iriarte‐Gahete, M., Tarancón‐Díez, L., Garrido‐Rodríguez, V., Leal, M., & Pacheco, Y. M. (2024) · Blood Reviews · doi:10.1016/j.blre.2024.101227 · Cited by 35 · see citing works
Ng, T. K. S., Udeh‐Momoh, C. T., Lim, M. A., Gleerup, H. S., Leifert, W. R., Ajalo, C., Ashton, N. J., Zetterberg, H., Rissman, R. A., Winston, C. N., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14420 · Cited by 30 · see citing works
Barakat, S. H., Meheissen, M. A., Omar, O. M., & Elbana, D. A. (2019) · Journal of Tropical Pediatrics · doi:10.1093/tropej/fmz029 · Cited by 32 · see citing works
Lactoferrin and oral pathologies: a therapeutic treatment
Rosa, L., Lepanto, M. S., Cutone, A., Ianiro, G., Pernarella, S., Sangermano, R., Musci, G., Ottolenghi, L., & Valenti, P. (2020) · Biochemistry and Cell Biology · doi:10.1139/bcb-2020-0052 · Cited by 32 · see citing works
Self-citationRosa, L., Lepanto, M. S., Cutone, A., Siciliano, R. A., Paesano, R., Costi, R., Musci, G., & Valenti, P. (2020) · BioMetals · doi:10.1007/s10534-020-00236-2 · Cited by 30 · see citing works
Self-citationKontoghiorghes, G. J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25094654 · Cited by 31 · see citing works
Too much iron: A masked foe for leukemias
Brissot, É., Bernard, D. G., Loréal, O., Brissot, P., & Troadec, M. (2019) · Blood Reviews · doi:10.1016/j.blre.2019.100617 · Cited by 28 · see citing works
Chen, K. G., Jin, S., Chen, H., Cao, Y., Dong, X., Li, H., Zhou, Z., & Liu, C. (2021) · Nutrition · doi:10.1016/j.nut.2021.111288 · Cited by 29 · see citing works
Li, D., Qian, H., Yang, H., Du, Y., Yu, K., Yang, J., Tong, X., Guo, Y., Xu, J., & Qin, L. (2021) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202100253 · Cited by 29 · see citing works
Alexander, M. R., Norlander, A. E., Elijovich, F., Atreya, R. V., Gaye, A., Gnecco, J. S., Laffer, C. L., Galindo, C. L., & Madhur, M. S. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14364 · Cited by 28 · see citing works
Niu, Z., Thielen, I., Barnett, A. M., Loveday, S. M., & Singh, H. (2019) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2019.03.006 · Cited by 28 · see citing works
Role of lactoferrin and its receptors on biliary epithelium
Mancinelli, R., Olivero, F., Carpino, G., Overi, D., Rosa, L., Lepanto, M. S., Cutone, A., Franchitto, A., Alpini, G. D., Onori, P., et al. (2018) · BioMetals · doi:10.1007/s10534-018-0094-6 · Cited by 27 · see citing works
Self-citationCrohn’s disease IRGM risk alleles are associated with altered gene expression in human tissues
Ajayi, T. A., Innes, C. L., Grimm, S. A., Rai, P., Finethy, R., Coers, J., Wang, X., Bell, D. A., McGrath, J. A., Schurman, S. H., et al. (2018) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00196.2018 · Cited by 27 · see citing works
Potential Protective Protein Components of Cow’s Milk against Certain Tumor Entities
Leischner, C., Egert, S., Burkard, M., & Venturelli, S. (2021) · Nutrients · doi:10.3390/nu13061974 · Cited by 29 · see citing works
Understanding the Potential and Risk of Bacterial Siderophores in Cancer
Pita-Grisanti, V., Chasser, K. M., Sobol, T., & Cruz-Monserrate, Z. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.867271 · Cited by 24 · see citing works
Potential of Lactoferrin in the Treatment of Lung Diseases
Kaczyńska, K., Jampolska, M., Wojciechowski, P., Sulejczak, D., Andrzejewski, K., & Zając, D. (2023) · Pharmaceuticals · doi:10.3390/ph16020192 · Cited by 28 · see citing works
Matino, E., Tavella, E., Rizzi, M., Avanzi, G. C., Azzolina, D., Battaglia, A., Becco, P., Bellan, M., Bertinieri, G., Bertoletti, M., et al. (2023) · Nutrients · doi:10.3390/nu15051285 · Cited by 27 · see citing works
Self-citationChibanda, Y., Brookes, M., Churchill, D. N., & Al-Hassi, H. O. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713323 · Cited by 30 · see citing works
Naidu, A. S., Wang, C., Rao, P., Mancini, F., Clemens, R., Wirakartakusumah, A., Chiu, H., Yen, C., Porretta, S., Mathai, I., et al. (2024) · npj Science of Food · doi:10.1038/s41538-024-00261-2 · Cited by 30 · see citing works
Characterization of recombinant human lactoferrin expressed in Komagataella phaffii
Lu, X., Cummings, C., Osuala, U. A., Yennawar, N. H., Namitz, K. E. W., Hellner, B., Besada‐Lombana, P. B., Peterson, R., & Clark, A. J. (2024) · The Analyst · doi:10.1039/d4an00333k · Cited by 27 · see citing works
- Authors
- Rosa, L., Cutone, A., Lepanto, M., Paesano, R., & Valenti, P.
- Affiliations
- Sapienza University of Rome (IT)
- Corresponding author
- Valenti, Piera
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2017-09-15
- Volume
- 18
- Issue
- 9
- Pages
- 1985
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC5618634
- OpenAlex
- W2755877600
- Cited by
- 376
- References
- 173
- Citations by year
- 2026: 34 · 2025: 42 · 2024: 47 · 2023: 35 · 2022: 62 · 2021: 55 · 2020: 44 · 2019: 34 · 2018: 22 · 2017: 1
- FWCI
- 4.36
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- IRIS Research product catalog (Sapienza University of Rome) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Archivio Istituzionale della Ricerca - Università degli Studi del Molise (submittedVersion)
- Funders
- Sapienza Università di Roma
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Nursing › Nutrition and Dietetics › Infant Nutrition and Health
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Keywords
- lactoferrin, bovine lactoferrin, iron homeostasis, anemia of chronic disease, interleukin-6, ferroportin, transferrin receptor 1, ferritin, antibacterial activity, bacterial biofilms, bacterial adhesion, preterm birth
- MeSH terms
- Anemia, Animals, Anti-Infective Agents, Anti-Inflammatory Agents, Female, Glycoproteins, Homeostasis, Humans, Inflammation, Iron, Lactoferrin, Oral Health, Pregnancy, Protein Binding, Structure-Activity Relationship, Anemia, Iron-Deficiency, Premature Birth
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review