{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T01:39:27Z","timestamp":1791337167879,"version":"4.3.1"},"reference-count":222,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2026,1,19]],"date-time":"2026-01-19T00:00:00Z","timestamp":1768780800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2026,1,19]],"date-time":"2026-01-19T00:00:00Z","timestamp":1768780800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/501100006769","name":"Russian Science Foundation","doi-asserted-by":"crossref","award":["25-26-00144"],"award-info":[{"award-number":["25-26-00144"]}],"id":[{"id":"10.13039\/501100006769","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Protein J"],"DOI":"10.1007\/s10930-025-10314-4","type":"journal-article","created":{"date-parts":[[2026,1,19]],"date-time":"2026-01-19T06:05:15Z","timestamp":1768802715000},"page":"83-99","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Non-specific Protein and Peptide Antibacterial Factors of Mammals"],"prefix":"10.1007","volume":"45","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6821-8888","authenticated-orcid":false,"given":"Pavel","family":"Levashov","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ilia","family":"Zaitsev","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergei","family":"Zaitsev","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daria","family":"Gasanova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,1,19]]},"reference":[{"issue":"5","key":"10314_CR1","doi-asserted-by":"publisher","first-page":"280","DOI":"10.1038\/s41579-022-00820-y","volume":"21","author":"EM Darby","year":"2023","unstructured":"Darby EM, Trampari E, Siasat P, Gaya MS, Alav I, Webber MA, Blair JMA (2023) Molecular mechanisms of antibiotic resistance revisited. Nat Rev Microbiol 21(5):280\u2013295. https:\/\/doi.org\/10.1038\/s41579-022-00820-y","journal-title":"Nat Rev Microbiol"},{"issue":"13","key":"10314_CR2","doi-asserted-by":"publisher","DOI":"10.3390\/healthcare11131946","volume":"11","author":"MA Salam","year":"2023","unstructured":"Salam MA, Al-Amin MY, Salam MT, Pawar JS, Akhter N, Rabaan AA, Alqumber MAA (2023) Antimicrobial resistance: a growing serious threat for global public health. Healthcare 11(13):1946. https:\/\/doi.org\/10.3390\/healthcare11131946","journal-title":"Healthcare"},{"key":"10314_CR3","doi-asserted-by":"publisher","first-page":"56","DOI":"10.1016\/j.coph.2014.09.006","volume":"18","author":"GM Rossolini","year":"2014","unstructured":"Rossolini GM, Arena F, Pecile P, Pollini S (2014) Update on the antibiotic resistance crisis. Curr Opin Pharmacol 18:56\u201360. https:\/\/doi.org\/10.1016\/j.coph.2014.09.006","journal-title":"Curr Opin Pharmacol"},{"issue":"2","key":"10314_CR4","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1038\/nrmicro2937","volume":"11","author":"PD Cotter","year":"2013","unstructured":"Cotter PD, Ross RP, Hill C (2013) Bacteriocins - a viable alternative to antibiotics? Nat Rev Microbiol 11(2):95\u2013105. https:\/\/doi.org\/10.1038\/nrmicro2937","journal-title":"Nat Rev Microbiol"},{"issue":"3","key":"10314_CR5","doi-asserted-by":"publisher","DOI":"10.3390\/ijms21031061","volume":"21","author":"CH Wang","year":"2020","unstructured":"Wang CH, Hsieh YH, Powers ZM, Kao CY (2020) Defeating antibiotic-resistant bacteria: exploring alternative therapies for a post-antibiotic era. Int J Mol Sci 21(3):1061. https:\/\/doi.org\/10.3390\/ijms21031061","journal-title":"Int J Mol Sci"},{"key":"10314_CR6","doi-asserted-by":"publisher","first-page":"1305294","DOI":"10.3389\/fphar.2023.1305294","volume":"14","author":"EM Halawa","year":"2024","unstructured":"Halawa EM, Fadel M, Al-Rabia MW, Behairy A, Nouh NA, Abdo M, Olga R, Fericean L, Atwa AM, El-Nablaway M, Abdeen A (2024) Antibiotic action and resistance: updated review of mechanisms, spread, influencing factors, and alternative approaches for combating resistance. Front Pharmacol 14:1305294. https:\/\/doi.org\/10.3389\/fphar.2023.1305294","journal-title":"Front Pharmacol"},{"key":"10314_CR7","doi-asserted-by":"publisher","DOI":"10.1016\/j.ejmech.2023.116072","volume":"265","author":"S Ji","year":"2024","unstructured":"Ji S, An F, Zhang T, Lou M, Guo J, Liu K, Zhu Y, Wu J, Wu R (2024) Antimicrobial peptides: an alternative to traditional antibiotics. Eur J Med Chem 265:116072. https:\/\/doi.org\/10.1016\/j.ejmech.2023.116072","journal-title":"Eur J Med Chem"},{"issue":"3","key":"10314_CR8","doi-asserted-by":"publisher","first-page":"167","DOI":"10.3390\/amh69030016","volume":"69","author":"A Elfadadny","year":"2024","unstructured":"Elfadadny A, Ragab RF, Abou Shehata MA, Elfadadny MR, Farag A, Abd El-Aziz AH, Khalifa HO (2024) Exploring bacteriophage applications in medicine and beyond. Acta Microbiol Hellen 69(3):167\u2013179. https:\/\/doi.org\/10.3390\/amh69030016","journal-title":"Acta Microbiol Hellen"},{"issue":"1","key":"10314_CR9","doi-asserted-by":"publisher","first-page":"30","DOI":"10.1186\/s12941-021-00433-y","volume":"20","author":"Z Chegini","year":"2021","unstructured":"Chegini Z, Khoshbayan A, Vesal S, Moradabadi A, Hashemi A, Shariati A (2021) Bacteriophage therapy for inhibition of multi drug-resistant uropathogenic bacteria: a narrative review. Ann Clin Microbiol Antimicrob 20(1):30. https:\/\/doi.org\/10.1186\/s12941-021-00433-y","journal-title":"Ann Clin Microbiol Antimicrob"},{"issue":"7","key":"10314_CR10","doi-asserted-by":"publisher","first-page":"1268","DOI":"10.3390\/v13071268","volume":"13","author":"D Liu","year":"2021","unstructured":"Liu D, Van Belleghem JD, de Vries CR, Burgener E, Chen Q, Manasherob R, Aronson JR, Amanatullah DF, Tamma PD, Suh GA (2021) The safety and toxicity of phage therapy: a review of animal and clinical studies. Viruses 13(7):1268. https:\/\/doi.org\/10.3390\/v13071268","journal-title":"Viruses"},{"issue":"10","key":"10314_CR11","doi-asserted-by":"publisher","first-page":"1058","DOI":"10.1016\/j.tim.2023.04.008","volume":"31","author":"K Champagne-Jorgensen","year":"2023","unstructured":"Champagne-Jorgensen K, Luong T, Darby T, Roach DR (2023) Immunogenicity of bacteriophages. Trends Microbiol 31(10):1058\u20131071. https:\/\/doi.org\/10.1016\/j.tim.2023.04.008","journal-title":"Trends Microbiol"},{"issue":"4","key":"10314_CR12","doi-asserted-by":"publisher","first-page":"419","DOI":"10.5114\/ceji.2016.65141","volume":"41","author":"P \u017belechowska","year":"2016","unstructured":"\u017belechowska P, Agier J, Brzezi\u0144ska-B\u0142aszczyk E (2016) Endogenous antimicrobial factors in the treatment of infectious diseases. Cent Eur J Immunol 41(4):419\u2013425. https:\/\/doi.org\/10.5114\/ceji.2016.65141","journal-title":"Cent Eur J Immunol"},{"key":"10314_CR13","doi-asserted-by":"publisher","DOI":"10.1038\/srep36692","volume":"6","author":"H Ottosson","year":"2016","unstructured":"Ottosson H, Nyl\u00e9n F, Sarker P, Miraglia E, Bergman P, Gudmundsson GH, Raqib R, Agerberth B, Str\u00f6mberg R (2016) Potent inducers of endogenous antimicrobial peptides for host directed therapy of infections. Sci Rep 6:36692. https:\/\/doi.org\/10.1038\/srep36692","journal-title":"Sci Rep"},{"issue":"9\u201310","key":"10314_CR14","doi-asserted-by":"publisher","first-page":"651","DOI":"10.1016\/j.biochi.2004.09.009","volume":"86","author":"B Powroznik","year":"2004","unstructured":"Powroznik B, Gharbi M, Dandrifosse G, Peulen O (2004) Enhancement of lysozyme stability and activity by polyamines. Biochimie 86(9\u201310):651\u2013656. https:\/\/doi.org\/10.1016\/j.biochi.2004.09.009","journal-title":"Biochimie"},{"key":"10314_CR15","doi-asserted-by":"publisher","first-page":"190","DOI":"10.1016\/j.procbio.2022.12.024","volume":"125","author":"NV Rastriga","year":"2023","unstructured":"Rastriga NV, Klimov DA, Gasanova DA, Levashov PA (2023) Comparison of the individual and combined actions of charged amino acids and glycine on the lysis of Escherichia coli cells by human and chicken lysozyme. Process Biochem 125:190\u2013197. https:\/\/doi.org\/10.1016\/j.procbio.2022.12.024","journal-title":"Process Biochem"},{"issue":"1","key":"10314_CR16","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1007\/s12038-010-0015-5","volume":"35","author":"L Callewaert","year":"2010","unstructured":"Callewaert L, Michiels CW (2010) Lysozymes in the animal kingdom. J Biosci 35(1):127\u2013160. https:\/\/doi.org\/10.1007\/s12038-010-0015-5","journal-title":"J Biosci"},{"issue":"2","key":"10314_CR17","doi-asserted-by":"publisher","first-page":"508","DOI":"10.1016\/j.dci.2014.06.007","volume":"46","author":"N Xu","year":"2014","unstructured":"Xu N, Pan J, Liu S, Xue Q, Zhang S (2014) Three in one: identification, expression and enzymatic activity of lysozymes in amphioxus. Dev Comp Immunol 46(2):508\u2013517. https:\/\/doi.org\/10.1016\/j.dci.2014.06.007","journal-title":"Dev Comp Immunol"},{"key":"10314_CR18","doi-asserted-by":"publisher","first-page":"166","DOI":"10.1186\/1471-2148-11-166","volume":"11","author":"DM Irwin","year":"2011","unstructured":"Irwin DM, Biegel JM, Stewart CB (2011) Evolution of the mammalian lysozyme gene family. BMC Evol Biol 11:166. https:\/\/doi.org\/10.1186\/1471-2148-11-166","journal-title":"BMC Evol Biol"},{"key":"10314_CR19","doi-asserted-by":"publisher","first-page":"188","DOI":"10.1186\/s12862-014-0188-x","volume":"14","author":"DM Irwin","year":"2014","unstructured":"Irwin DM (2014) Evolution of the vertebrate goose-type lysozyme gene family. BMC Evol Biol 14:188. https:\/\/doi.org\/10.1186\/s12862-014-0188-x","journal-title":"BMC Evol Biol"},{"issue":"9","key":"10314_CR20","doi-asserted-by":"publisher","DOI":"10.1093\/gbe\/evab201","volume":"13","author":"X Zhang","year":"2021","unstructured":"Zhang X, Chi H, Li G, Irwin DM, Zhang S, Rossiter SJ, Liu Y (2021) Parallel independent losses of G-type lysozyme genes in hairless aquatic mammals. Genome Biol Evol 13(9):evab201. https:\/\/doi.org\/10.1093\/gbe\/evab201","journal-title":"Genome Biol Evol"},{"key":"10314_CR21","doi-asserted-by":"publisher","first-page":"154","DOI":"10.1016\/j.dci.2017.04.017","volume":"74","author":"J Zhou","year":"2017","unstructured":"Zhou J, Zhao S, Fang WH, Zhou JF, Zhang JX, Ma H, Lan JF, Li XC (2017) Newly identified invertebrate-type lysozyme (Splys-i) in mud crab (Scylla paramamosain) exhibiting muramidase-deficient antimicrobial activity. Dev Comp Immunol 74:154\u2013166. https:\/\/doi.org\/10.1016\/j.dci.2017.04.017","journal-title":"Dev Comp Immunol"},{"key":"10314_CR22","doi-asserted-by":"publisher","DOI":"10.1016\/j.ecoenv.2020.110713","volume":"200","author":"A Gautam","year":"2020","unstructured":"Gautam A, Ray A, Manna S, Sarkar MP, Ghosh AR, Ray M, Ray S (2020) Shift in phagocytosis, lysosomal stability, lysozyme activity, apoptosis and cell cycle profile in the coelomocytes of earthworm of polluted soil near a tannery field of India. Ecotoxicol Environ Saf 200:110713. https:\/\/doi.org\/10.1016\/j.ecoenv.2020.110713","journal-title":"Ecotoxicol Environ Saf"},{"issue":"8","key":"10314_CR23","doi-asserted-by":"publisher","first-page":"2192","DOI":"10.1111\/j.1742-4658.2009.06948.x","volume":"276","author":"Y Nonaka","year":"2009","unstructured":"Nonaka Y, Akieda D, Aizawa T, Watanabe N, Kamiya M, Kumaki Y, Mizuguchi M, Kikukawa T, Demura M, Kawano K (2009) X-ray crystallography and structural stability of digestive lysozyme from cow stomach. FEBS J 276(8):2192\u20132200. https:\/\/doi.org\/10.1111\/j.1742-4658.2009.06948.x","journal-title":"FEBS J"},{"key":"10314_CR24","doi-asserted-by":"publisher","DOI":"10.1016\/j.cbpb.2024.110949","volume":"271","author":"N Barts","year":"2024","unstructured":"Barts N, Bhatt RH, Toner C, Meyer WK, Durrant JD, Kohl KD (2024) Functional convergence in gastric lysozymes of foregut-fermenting rodents, ruminants, and primates is not attributed to convergent molecular evolution. Comp Biochem Physiol B Biochem Mol Biol 271:110949. https:\/\/doi.org\/10.1016\/j.cbpb.2024.110949","journal-title":"Comp Biochem Physiol B Biochem Mol Biol"},{"key":"10314_CR25","doi-asserted-by":"publisher","first-page":"699","DOI":"10.1007\/s13594-013-0136-3","volume":"93","author":"K Shakir","year":"2013","unstructured":"Shakir K, Walsh MK, Mohammed SA (2013) Characterization of Iraqi sheep milk lysozyme with respect to molecular weight and hydrolytic activity. Dairy Sci Technol 93:699\u2013705. https:\/\/doi.org\/10.1007\/s13594-013-0136-3","journal-title":"Dairy Sci Technol"},{"issue":"1","key":"10314_CR26","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1111\/j.1574-6968.2006.00240.x","volume":"259","author":"D Nakimbugwe","year":"2006","unstructured":"Nakimbugwe D, Masschalck B, Deckers D, Callewaert L, Aertsen A, Michiels CW (2006) Cell wall substrate specificity of six different lysozymes and lysozyme inhibitory activity of bacterial extracts. FEMS Microbiol Lett 259(1):41\u201346. https:\/\/doi.org\/10.1111\/j.1574-6968.2006.00240.x","journal-title":"FEMS Microbiol Lett"},{"issue":"6","key":"10314_CR27","doi-asserted-by":"publisher","first-page":"1053","DOI":"10.1007\/s00018-010-0507-3","volume":"68","author":"L Vanderkelen","year":"2011","unstructured":"Vanderkelen L, Van Herreweghe JM, Vanoirbeek KG, Baggerman G, Myrnes B, Declerck PJ, Nilsen IW, Michiels CW, Callewaert L (2011) Identification of a bacterial inhibitor against g-type lysozyme. Cell Mol Life Sci 68(6):1053\u20131064. https:\/\/doi.org\/10.1007\/s00018-010-0507-3","journal-title":"Cell Mol Life Sci"},{"issue":"1","key":"10314_CR28","doi-asserted-by":"publisher","first-page":"233","DOI":"10.1016\/S0021-9258(19)44466-9","volume":"248","author":"N Arnheim","year":"1973","unstructured":"Arnheim N, Inouye M, Law L, Laudin A (1973) Chemical studies on the enzymatic specificity of goose egg white lysozyme. J Biol Chem 248(1):233\u2013236. https:\/\/doi.org\/10.1016\/S0021-9258(19)44466-9","journal-title":"J Biol Chem"},{"issue":"6","key":"10314_CR29","doi-asserted-by":"publisher","first-page":"753","DOI":"10.1093\/jb\/mvn133","volume":"144","author":"H Hirakawa","year":"2008","unstructured":"Hirakawa H, Ochi A, Kawahara Y, Kawamura S, Torikata T, Kuhara S (2008) Catalytic reaction mechanism of goose egg-white lysozyme by molecular modelling of enzyme-substrate complex. J Biochem 144(6):753\u2013761. https:\/\/doi.org\/10.1093\/jb\/mvn133","journal-title":"J Biochem"},{"issue":"9","key":"10314_CR30","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1006512","volume":"13","author":"SA Ragland","year":"2017","unstructured":"Ragland SA, Criss AK (2017) From bacterial killing to immune modulation: recent insights into the functions of lysozyme. PLoS Pathog 13(9):e1006512. https:\/\/doi.org\/10.1371\/journal.ppat.1006512","journal-title":"PLoS Pathog"},{"key":"10314_CR31","doi-asserted-by":"publisher","first-page":"79","DOI":"10.1007\/s10989-025-10742-x","volume":"31","author":"M Matwiejczyk","year":"2025","unstructured":"Matwiejczyk M, Zambrowicz A, Besman M (2025) Lysozyme monomer, dimer, and oligomers: a review with a focus on immunological potential. Int J Pept Res Ther 31:79. https:\/\/doi.org\/10.1007\/s10989-025-10742-x","journal-title":"Int J Pept Res Ther"},{"issue":"3","key":"10314_CR32","doi-asserted-by":"publisher","first-page":"1663","DOI":"10.1007\/s12602-024-10226-2","volume":"17","author":"AM Abdou","year":"2025","unstructured":"Abdou AM, Awad DAB (2025) Lysozyme peptides as a novel nutra-preservative to control some food poisoning and food spoilage microorganisms. Probiotics Antimicrob Proteins 17(3):1663\u20131673. https:\/\/doi.org\/10.1007\/s12602-024-10226-2","journal-title":"Probiotics Antimicrob Proteins"},{"issue":"9","key":"10314_CR33","doi-asserted-by":"publisher","first-page":"1210","DOI":"10.3390\/biom10091210","volume":"10","author":"EA Permyakov","year":"2020","unstructured":"Permyakov EA (2020) \u03b1-Lactalbumin, amazing calcium-binding protein. Biomolecules 10(9):1210. https:\/\/doi.org\/10.3390\/biom10091210","journal-title":"Biomolecules"},{"key":"10314_CR34","doi-asserted-by":"publisher","first-page":"153","DOI":"10.1016\/j.rvsc.2019.11.011","volume":"128","author":"YH Zhang","year":"2020","unstructured":"Zhang YH, Bai J, Jiang WN, Zhao CR, Ji JJ, Wang JZ, Liu YW (2020) Promising hen egg-derived proteins\/peptides (EDPs) for food engineering, natural products and precision medicines. Res Vet Sci 128:153\u2013161. https:\/\/doi.org\/10.1016\/j.rvsc.2019.11.011","journal-title":"Res Vet Sci"},{"issue":"4660","key":"10314_CR35","doi-asserted-by":"publisher","first-page":"548","DOI":"10.1038\/183548a0","volume":"183","author":"R Ferrari","year":"1959","unstructured":"Ferrari R, Callerio C, Podio G (1959) Antiviral activity of lysozyme. Nature 183(4660):548. https:\/\/doi.org\/10.1038\/183548a0","journal-title":"Nature"},{"issue":"1","key":"10314_CR36","doi-asserted-by":"publisher","first-page":"318","DOI":"10.1186\/s12917-019-2067-6","volume":"15","author":"J Ma\u0142aczewska","year":"2019","unstructured":"Ma\u0142aczewska J, Kaczorek-\u0141ukowska E, W\u00f3jcik R, Siwicki AK (2019) Antiviral effects of nisin, lysozyme, lactoferrin and their mixtures against bovine viral diarrhoea virus. BMC Vet Res 15(1):318. https:\/\/doi.org\/10.1186\/s12917-019-2067-6","journal-title":"BMC Vet Res"},{"issue":"3","key":"10314_CR37","doi-asserted-by":"publisher","first-page":"652","DOI":"10.3390\/molecules29030652","volume":"29","author":"A Bergamo","year":"2024","unstructured":"Bergamo A, Sava G (2024) Lysozyme: a natural product with multiple and useful antiviral properties. Molecules 29(3):652. https:\/\/doi.org\/10.3390\/molecules29030652","journal-title":"Molecules"},{"issue":"9","key":"10314_CR38","doi-asserted-by":"publisher","first-page":"3296","DOI":"10.1128\/JCM.39.9.3296-3302.2001","volume":"39","author":"YH Samaranayake","year":"2001","unstructured":"Samaranayake YH, Samaranayake LP, Pow EH, Beena VT, Yeung KW (2001) Antifungal effects of lysozyme and lactoferrin against genetically similar, sequential Candida albicans isolates from a human immunodeficiency virus-infected southern Chinese cohort. J Clin Microbiol 39(9):3296\u20133302. https:\/\/doi.org\/10.1128\/JCM.39.9.3296-3302.2001","journal-title":"J Clin Microbiol"},{"issue":"3","key":"10314_CR39","first-page":"583","volume":"9","author":"G Sava","year":"1989","unstructured":"Sava G, Benetti A, Ceschia V, Pacor S (1989) Lysozyme and cancer: role of exogenous lysozyme as anticancer agent (review). Anticancer Res 9(3):583\u2013591","journal-title":"Anticancer Res"},{"issue":"2","key":"10314_CR40","doi-asserted-by":"publisher","first-page":"117","DOI":"10.1007\/s12262-012-0738-7","volume":"77","author":"MP Daniel","year":"2015","unstructured":"Daniel MP, Gaikwad V, Verghese M, Abraham R, Kapoor R (2015) Serum lysozyme (muramidase) levels in intra-abdominal abscesses: an experimental study. Indian J Surg 77(2):117\u2013119. https:\/\/doi.org\/10.1007\/s12262-012-0738-7","journal-title":"Indian J Surg"},{"key":"10314_CR41","doi-asserted-by":"publisher","DOI":"10.1016\/j.btre.2019.e00381","volume":"24","author":"PA Levashov","year":"2019","unstructured":"Levashov PA, Matolygina DA, Dmitrieva OA, Ovchinnikova ED, Adamova IY, Karelina NV, Nelyub VA, Eremeev NL, Levashov AV (2019) Covalently immobilized chemically modified lysozyme as a sorbent for bacterial endotoxins (lipopolysaccharides). Biotechnol Rep 24:e00381. https:\/\/doi.org\/10.1016\/j.btre.2019.e00381","journal-title":"Biotechnol Rep"},{"issue":"1","key":"10314_CR42","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1134\/S0006297919010048","volume":"84","author":"PA Levashov","year":"2019","unstructured":"Levashov PA, Matolygina DA, Ovchinnikova ED, Adamova IY, Dmitrieva OA, Nuzhdina AV, Pokrovsky NS, Eremeev NL (2019) New sorbent on the basis of covalently immobilized lysozyme for removal of bacterial lipopolysaccharide (endotoxin) from biological fluids. Biochemistry (Mosc) 84(1):33\u201339. https:\/\/doi.org\/10.1134\/S0006297919010048","journal-title":"Biochemistry (Mosc)"},{"issue":"1","key":"10314_CR43","doi-asserted-by":"publisher","DOI":"10.63096\/medtigo3092112","volume":"1","author":"AA Sumaiya","year":"2024","unstructured":"Sumaiya AA (2024) Recent advances in sepsis management: from early goal-directed therapy to biomarker-driven approaches. Medtigo J Emerg Med 1(1):e3092112. https:\/\/doi.org\/10.63096\/medtigo3092112","journal-title":"Medtigo J Emerg Med"},{"issue":"1","key":"10314_CR44","doi-asserted-by":"publisher","first-page":"400","DOI":"10.1186\/s13054-023-04690-5","volume":"27","author":"JA Kellum","year":"2023","unstructured":"Kellum JA, Ronco C (2023) The role of endotoxin in septic shock. Crit Care 27(1):400. https:\/\/doi.org\/10.1186\/s13054-023-04690-5","journal-title":"Crit Care"},{"issue":"1","key":"10314_CR45","doi-asserted-by":"publisher","DOI":"10.1002\/adhm.202001378","volume":"10","author":"L Papafilippou","year":"2021","unstructured":"Papafilippou L, Claxton A, Dark P, Kostarelos K, Hadjidemetriou M (2021) Nanotools for sepsis diagnosis and treatment. Adv Healthc Mater 10(1):e2001378. https:\/\/doi.org\/10.1002\/adhm.202001378","journal-title":"Adv Healthc Mater"},{"issue":"1","key":"10314_CR46","doi-asserted-by":"publisher","first-page":"8333","DOI":"10.1038\/s41598-025-93010-8","volume":"15","author":"W Xiong","year":"2025","unstructured":"Xiong W, Zhan Y, Xiao R, Liu F (2025) Advancing sepsis diagnosis and immunotherapy machine learning-driven identification of stable molecular biomarkers and therapeutic targets. Sci Rep 15(1):8333. https:\/\/doi.org\/10.1038\/s41598-025-93010-8","journal-title":"Sci Rep"},{"issue":"1","key":"10314_CR47","doi-asserted-by":"publisher","first-page":"432","DOI":"10.1186\/s13054-024-05220-7","volume":"28","author":"G Bottari","year":"2024","unstructured":"Bottari G, Ranieri VM, Ince C, Pesenti A, Aucella F, Scandroglio AM, Ronco C, Vincent JL (2024) Use of extracorporeal blood purification therapies in sepsis: the current paradigm, available evidence, and future perspectives. Crit Care 28(1):432. https:\/\/doi.org\/10.1186\/s13054-024-05220-7","journal-title":"Crit Care"},{"issue":"7","key":"10314_CR48","doi-asserted-by":"publisher","first-page":"1684","DOI":"10.3390\/biomedicines13071684","volume":"13","author":"M Guarino","year":"2025","unstructured":"Guarino M, Costanzini A, Luppi F, Maritati M, Contini C, De Giorgio R, Spampinato MD (2025) Extracorporeal cytokine adsorption in sepsis: current evidence and future perspectives. Biomedicines 13(7):1684. https:\/\/doi.org\/10.3390\/biomedicines13071684","journal-title":"Biomedicines"},{"issue":"2","key":"10314_CR49","doi-asserted-by":"publisher","first-page":"82","DOI":"10.32607\/20758251-2017-9-2-82-87","volume":"9","author":"PA Levashov","year":"2017","unstructured":"Levashov PA, Matolygina DA, Ovchinnikova ED, Atroshenko DL, Savin SS, Belogurova NG, Smirnov SA, Tishkov VI, Levashov AV (2017) Bacteriolytic activity of human interleukin-2, chicken egg lysozyme in the presence of potential effectors. Acta Naturae 9(2):82\u201387. https:\/\/doi.org\/10.32607\/20758251-2017-9-2-82-87","journal-title":"Acta Naturae"},{"issue":"1","key":"10314_CR50","doi-asserted-by":"publisher","first-page":"58","DOI":"10.52547\/ibj.3614","volume":"27","author":"TA Pankratov","year":"2023","unstructured":"Pankratov TA, Gannesen AV, Nikolaev YA (2023) Regulation of lysozyme activity by human hormones. Iran Biomed J 27(1):58\u201365. https:\/\/doi.org\/10.52547\/ibj.3614","journal-title":"Iran Biomed J"},{"issue":"3","key":"10314_CR51","doi-asserted-by":"publisher","first-page":"510","DOI":"10.1002\/2211-5463.12591","volume":"9","author":"PA Levashov","year":"2019","unstructured":"Levashov PA, Matolygina DA, Ovchinnikova ED, Adamova IY, Gasanova DA, Smirnov SA, Nelyub VA, Belogurova NG, Tishkov VI, Eremeev NL, Levashov AV (2019) The bacteriolytic activity of native and covalently immobilized lysozyme against Gram-positive and Gram-negative bacteria is differentially affected by charged amino acids and glycine. FEBS Open Bio 9(3):510\u2013518. https:\/\/doi.org\/10.1002\/2211-5463.12591","journal-title":"FEBS Open Bio"},{"issue":"3","key":"10314_CR52","doi-asserted-by":"publisher","DOI":"10.3390\/antibiotics8030094","volume":"8","author":"AS Brott","year":"2019","unstructured":"Brott AS, Clarke AJ (2019) Peptidoglycan o-acetylation as a virulence factor: its effect on lysozyme in the innate immune system. Antibiotics 8(3):94. https:\/\/doi.org\/10.3390\/antibiotics8030094","journal-title":"Antibiotics"},{"key":"10314_CR53","doi-asserted-by":"publisher","first-page":"156","DOI":"10.1016\/j.mib.2021.11.010","volume":"65","author":"H Coullon","year":"2022","unstructured":"Coullon H, Candela T (2022) Clostridioides difficile peptidoglycan modifications. Curr Opin Microbiol 65:156\u2013161. https:\/\/doi.org\/10.1016\/j.mib.2021.11.010","journal-title":"Curr Opin Microbiol"},{"issue":"20","key":"10314_CR54","doi-asserted-by":"publisher","first-page":"7071","DOI":"10.3390\/molecules28207071","volume":"28","author":"L Vanderkelen","year":"2023","unstructured":"Vanderkelen L, Van Herreweghe JM, Michiels CW (2023) Lysozyme inhibitors as tools for lysozyme profiling: identification and antibacterial function of lysozymes in the hemolymph of the blue mussel. Molecules 28(20):7071. https:\/\/doi.org\/10.3390\/molecules28207071","journal-title":"Molecules"},{"issue":"1","key":"10314_CR55","doi-asserted-by":"publisher","first-page":"666","DOI":"10.1080\/21505594.2018.1433979","volume":"9","author":"Y Bao","year":"2018","unstructured":"Bao Y, Zhang H, Huang X, Ma J, Logue CM, Nolan LK, Li G (2018) O-specific polysaccharide confers lysozyme resistance to extraintestinal pathogenic Escherichia coli. Virulence 9(1):666\u2013680. https:\/\/doi.org\/10.1080\/21505594.2018.1433979","journal-title":"Virulence"},{"issue":"1","key":"10314_CR56","doi-asserted-by":"publisher","first-page":"266","DOI":"10.1093\/emph\/eoac022","volume":"10","author":"A Santos-Lopez","year":"2022","unstructured":"Santos-Lopez A, Fritz MJ, Lombardo JB, Burr AHP, Heinrich VA, Marshall CW, Cooper VS (2022) Evolved resistance to a novel cationic peptide antibiotic requires high mutation supply. Evol Med Public Health 10(1):266\u2013276. https:\/\/doi.org\/10.1093\/emph\/eoac022","journal-title":"Evol Med Public Health"},{"issue":"3","key":"10314_CR57","doi-asserted-by":"publisher","first-page":"188","DOI":"10.1016\/j.bbagen.2011.10.013","volume":"1820","author":"K Gkouvatsos","year":"2012","unstructured":"Gkouvatsos K, Papanikolaou G, Pantopoulos K (2012) Regulation of iron transport and the role of transferrin. Biochim Biophys Acta 1820(3):188\u2013202. https:\/\/doi.org\/10.1016\/j.bbagen.2011.10.013","journal-title":"Biochim Biophys Acta"},{"issue":"4","key":"10314_CR58","doi-asserted-by":"publisher","first-page":"301.e1","DOI":"10.1016\/j.ijantimicag.2008.07.020","volume":"33","author":"SA Gonz\u00e1lez-Ch\u00e1vez","year":"2009","unstructured":"Gonz\u00e1lez-Ch\u00e1vez SA, Ar\u00e9valo-Gallegos S, Rasc\u00f3n-Cruz Q (2009) Lactoferrin: structure, function and applications. Int J Antimicrob Agents 33(4):301.e1\u20138. https:\/\/doi.org\/10.1016\/j.ijantimicag.2008.07.020","journal-title":"Int J Antimicrob Agents"},{"key":"10314_CR59","doi-asserted-by":"publisher","DOI":"10.1016\/j.jinorgbio.2020.111101","volume":"210","author":"CM Petersen","year":"2020","unstructured":"Petersen CM, Edwards KC, Gilbert NC, Vincent JB, Thompson MK (2020) X-ray structure of chromium (III)-containing transferrin: first structure of a physiological Cr (III)-binding protein. J Inorg Biochem 210:111101. https:\/\/doi.org\/10.1016\/j.jinorgbio.2020.111101","journal-title":"J Inorg Biochem"},{"issue":"5","key":"10314_CR60","doi-asserted-by":"publisher","first-page":"800","DOI":"10.1007\/s13361-015-1082-5","volume":"26","author":"S Wang","year":"2015","unstructured":"Wang S, Kaltashov IA (2015) Identification of reduction-susceptible disulfide bonds in transferrin by differential alkylation using O(16)\/O(18) labeled iodoacetic acid. J Am Soc Mass Spectrom 26(5):800\u2013807. https:\/\/doi.org\/10.1007\/s13361-015-1082-5","journal-title":"J Am Soc Mass Spectrom"},{"issue":"3","key":"10314_CR61","doi-asserted-by":"publisher","first-page":"244","DOI":"10.1016\/j.bbagen.2011.06.002","volume":"1820","author":"LA Lambert","year":"2012","unstructured":"Lambert LA (2012) Molecular evolution of the transferrin family and associated receptors. Biochim Biophys Acta 1820(3):244\u2013255. https:\/\/doi.org\/10.1016\/j.bbagen.2011.06.002","journal-title":"Biochim Biophys Acta"},{"issue":"4","key":"10314_CR62","doi-asserted-by":"publisher","first-page":"369","DOI":"10.1111\/j.1600-0625.2010.01218.x","volume":"20","author":"JH Park","year":"2011","unstructured":"Park JH, Park GT, Cho IH, Sim SM, Yang JM, Lee DY (2011) An antimicrobial protein, lactoferrin exists in the sweat: proteomic analysis of sweat. Exp Dermatol 20(4):369\u2013371. https:\/\/doi.org\/10.1111\/j.1600-0625.2010.01218.x","journal-title":"Exp Dermatol"},{"issue":"3","key":"10314_CR63","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1016\/j.bbagen.2011.09.003","volume":"1820","author":"YS Rahmanto","year":"2012","unstructured":"Rahmanto YS, Bal S, Loh KH, Yu Y, Richardson DR (2012) Melanotransferrin: search for a function. Biochim Biophys Acta 1820(3):237\u2013243. https:\/\/doi.org\/10.1016\/j.bbagen.2011.09.003","journal-title":"Biochim Biophys Acta"},{"issue":"9","key":"10314_CR64","doi-asserted-by":"publisher","first-page":"1616","DOI":"10.1002\/pro.439","volume":"19","author":"BE Eckenroth","year":"2010","unstructured":"Eckenroth BE, Mason AB, McDevitt ME, Lambert LA, Everse SJ (2010) The structure and evolution of the murine inhibitor of carbonic anhydrase: a member of the transferrin superfamily. Protein Sci 19(9):1616\u20131626. https:\/\/doi.org\/10.1002\/pro.439","journal-title":"Protein Sci"},{"issue":"2","key":"10314_CR65","doi-asserted-by":"publisher","first-page":"261","DOI":"10.1016\/0305-0491(90)90074-4","volume":"95","author":"GS Baldwin","year":"1990","unstructured":"Baldwin GS, Bacic T, Chandler R, Grego B, Pedersen J, Simpson RJ, Toh BH, Weinstock J (1990) Isolation of transferrin from porcine gastric mucosa: comparison with porcine serum transferrin. Comp Biochem Physiol B 95(2):261\u2013268. https:\/\/doi.org\/10.1016\/0305-0491(90)90074-4","journal-title":"Comp Biochem Physiol B"},{"issue":"6","key":"10314_CR66","doi-asserted-by":"publisher","first-page":"726","DOI":"10.1182\/blood.2019002907","volume":"136","author":"Y Yu","year":"2020","unstructured":"Yu Y, Jiang L, Wang H, Shen Z, Cheng Q, Zhang P, Wang J, Wu Q, Fang X, Duan L, Wang S, Wang K, An P, Shao T, Chung RT, Zheng S, Min J, Wang F (2020) Hepatic transferrin plays a role in systemic iron homeostasis and liver ferroptosis. Blood 136(6):726\u2013739. https:\/\/doi.org\/10.1182\/blood.2019002907","journal-title":"Blood"},{"issue":"1","key":"10314_CR67","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1016\/0305-0491(91)90305-w","volume":"98","author":"RC Penhallow","year":"1991","unstructured":"Penhallow RC, Mason AB, Woodworth RC (1991) Electrophoretic characterization of human, equine and bovine transferrins. Comp Biochem Physiol B 98(1):41\u201345. https:\/\/doi.org\/10.1016\/0305-0491(91)90305-w","journal-title":"Comp Biochem Physiol B"},{"key":"10314_CR68","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1007\/978-1-4615-9200-6_8","volume":"135","author":"A Bezkorovainy","year":"1981","unstructured":"Bezkorovainy A (1981) Antimicrobial properties of iron-binding proteins. Adv Exp Med Biol 135:139\u2013154. https:\/\/doi.org\/10.1007\/978-1-4615-9200-6_8","journal-title":"Adv Exp Med Biol"},{"issue":"Suppl.1","key":"10314_CR69","doi-asserted-by":"publisher","first-page":"72","DOI":"10.1002\/2211-5463.12675","volume":"9","author":"PA Levashov","year":"2019","unstructured":"Levashov PA, Matolygina DA, Ovchinnikova ED, Ushakova DA, Burmakin VV, Cherdyntseva TA, Eremeev NL, Tishkov VI, Levashov AV (2019) Bacteriolytic activity of human blood plasma serotransferrin. FEBS Open Bio 9(Suppl.1):72. https:\/\/doi.org\/10.1002\/2211-5463.12675","journal-title":"FEBS Open Bio"},{"key":"10314_CR70","doi-asserted-by":"publisher","DOI":"10.3390\/molecules27092941","author":"P Kowalczyk","year":"2022","unstructured":"Kowalczyk P, Kaczy\u0144ska K, Kleczkowska P, Bukowska-O\u015bko I, Kramkowski K, Sulejczak D (2022) The lactoferrin phenomenon - a miracle molecule. Molecules. https:\/\/doi.org\/10.3390\/molecules27092941","journal-title":"Molecules"},{"issue":"2","key":"10314_CR71","first-page":"85","volume":"3","author":"SM Sohrabi","year":"2014","unstructured":"Sohrabi SM, Niazi A, Chahardoli M, Hortamani A, Setoodeh P (2014) In silico investigation of lactoferrin protein characterizations for the prediction of anti-microbial properties. Mol Biol Res Commun 3(2):85\u2013100","journal-title":"Mol Biol Res Commun"},{"issue":"8","key":"10314_CR72","doi-asserted-by":"publisher","first-page":"778","DOI":"10.2174\/1389203715666140919124530","volume":"15","author":"AH Albar","year":"2014","unstructured":"Albar AH, Almehdar HA, Uversky VN, Redwan EM (2014) Structural heterogeneity and multifunctionality of lactoferrin. Curr Protein Pept Sci 15(8):778\u2013797. https:\/\/doi.org\/10.2174\/1389203715666140919124530","journal-title":"Curr Protein Pept Sci"},{"issue":"14","key":"10314_CR73","doi-asserted-by":"publisher","first-page":"813","DOI":"10.1089\/ars.2015.6458","volume":"24","author":"S Mayeur","year":"2016","unstructured":"Mayeur S, Spahis S, Pouliot Y, Levy E (2016) Lactoferrin, a pleiotropic protein in health and disease. Antioxid Redox Signal 24(14):813\u2013836. https:\/\/doi.org\/10.1089\/ars.2015.6458","journal-title":"Antioxid Redox Signal"},{"issue":"2","key":"10314_CR74","doi-asserted-by":"publisher","first-page":"171","DOI":"10.2298\/BAH1702171A","volume":"33","author":"FE Akumbugu","year":"2017","unstructured":"Akumbugu FE, Olusegun OA (2017) Genetic diversity of lactoferrin gene in-silico on selected mammalian species. Biotechnol Anim Husb 33(2):171\u2013180. https:\/\/doi.org\/10.2298\/BAH1702171A","journal-title":"Biotechnol Anim Husb"},{"issue":"2","key":"10314_CR75","doi-asserted-by":"publisher","first-page":"139","DOI":"10.2174\/1389203719666180514150921","volume":"20","author":"L Hao","year":"2019","unstructured":"Hao L, Shan Q, Wei J, Ma F, Sun P (2019) Lactoferrin: major physiological functions and applications. Curr Protein Pept Sci 20(2):139\u2013144. https:\/\/doi.org\/10.2174\/1389203719666180514150921","journal-title":"Curr Protein Pept Sci"},{"key":"10314_CR76","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1007\/s10989-023-10541-2","volume":"29","author":"C Coccolini","year":"2023","unstructured":"Coccolini C, Berselli E, Blanco-Llamero C, Fathi F, Oliveira M, Krambeck K, Souto EB (2023) Biomedical and nutritional applications of lactoferrin. Int J Pept Res Ther 29:71. https:\/\/doi.org\/10.1007\/s10989-023-10541-2","journal-title":"Int J Pept Res Ther"},{"key":"10314_CR77","doi-asserted-by":"publisher","first-page":"2633","DOI":"10.3389\/fmicb.2017.02633","volume":"8","author":"E Acosta-Smith","year":"2018","unstructured":"Acosta-Smith E, Viveros-Jim\u00e9nez K, Canizalez-Rom\u00e1n A, Reyes-Lopez M, Bolscher JGM, Nazmi K, Flores-Villase\u00f1or H, Alapizco-Castro G, de la Garza M, Mart\u00ednez-Garcia JJ, Velazquez-Roman J, Leon-Sicairos N (2018) Bovine lactoferrin and lactoferrin-derived peptides inhibit the growth of Vibrio cholerae and other Vibrio species. Front Microbiol 8:2633. https:\/\/doi.org\/10.3389\/fmicb.2017.02633","journal-title":"Front Microbiol"},{"issue":"4","key":"10314_CR78","doi-asserted-by":"publisher","first-page":"1080","DOI":"10.1172\/JCI115407","volume":"88","author":"RT Ellison","year":"1991","unstructured":"Ellison RT, Giehl TJ (1991) Killing of gram-negative bacteria by lactoferrin and lysozyme. J Clin Invest 88(4):1080\u20131091. https:\/\/doi.org\/10.1172\/JCI115407","journal-title":"J Clin Invest"},{"issue":"12","key":"10314_CR79","doi-asserted-by":"publisher","first-page":"1117","DOI":"10.1080\/14728222.2024.2441705","volume":"28","author":"Y Zhang","year":"2024","unstructured":"Zhang Y, Song D, Han X, Liu H, Wang Y, Wang X, Dou C (2024) Unlocking the potential of melanotransferrin (CD228): implications for targeted drug development and novel therapeutic avenues. Expert Opin Ther Targets 28(12):1117\u20131129. https:\/\/doi.org\/10.1080\/14728222.2024.2441705","journal-title":"Expert Opin Ther Targets"},{"issue":"7","key":"10314_CR80","doi-asserted-by":"publisher","first-page":"1580","DOI":"10.7150\/ijms.53650","volume":"18","author":"M Dubon","year":"2021","unstructured":"Dubon M, Lee S, Park JH, Lee JY, Kang D (2021) The role of melanotransferrin (CD228) in the regulation of the differentiation of human bone marrow-derived mesenchymal stem cells (hBM-MSC). Int J Med Sci 18(7):1580\u20131591. https:\/\/doi.org\/10.7150\/ijms.53650","journal-title":"Int J Med Sci"},{"issue":"9","key":"10314_CR81","doi-asserted-by":"publisher","first-page":"3277","DOI":"10.1021\/jf053031s","volume":"54","author":"HL Chen","year":"2006","unstructured":"Chen HL, Yen CC, Lu CY, Yu CH, Chen CM (2006) Synthetic porcine lactoferricin with a 20-residue peptide exhibits antimicrobial activity against Escherichia coli, Staphylococcus aureus, and Candida albicans. J Agric Food Chem 54(9):3277\u20133282. https:\/\/doi.org\/10.1021\/jf053031s","journal-title":"J Agric Food Chem"},{"key":"10314_CR82","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2020.606489","volume":"11","author":"MR Walter","year":"2020","unstructured":"Walter MR (2020) The role of structure in the biology of interferon signaling. Front Immunol 11:606489. https:\/\/doi.org\/10.3389\/fimmu.2020.606489","journal-title":"Front Immunol"},{"issue":"3","key":"10314_CR83","doi-asserted-by":"publisher","first-page":"299","DOI":"10.1016\/j.pharmthera.2004.12.002","volume":"106","author":"CD Krause","year":"2005","unstructured":"Krause CD, Pestka S (2005) Evolution of the class 2 cytokines and receptors, and discovery of new friends and relatives. Pharmacol Ther 106(3):299\u2013346. https:\/\/doi.org\/10.1016\/j.pharmthera.2004.12.002","journal-title":"Pharmacol Ther"},{"issue":"14","key":"10314_CR84","doi-asserted-by":"publisher","DOI":"10.15252\/embj.2022112907","volume":"42","author":"L Dalskov","year":"2023","unstructured":"Dalskov L, Gad HH, Hartmann R (2023) Viral recognition and the antiviral interferon response. EMBO J 42(14):e112907. https:\/\/doi.org\/10.15252\/embj.2022112907","journal-title":"EMBO J"},{"issue":"2","key":"10314_CR85","doi-asserted-by":"publisher","first-page":"87","DOI":"10.1038\/nri3787","volume":"15","author":"F McNab","year":"2015","unstructured":"McNab F, Mayer-Barber K, Sher A, Wack A, O\u2019Garra A (2015) Type I interferons in infectious disease. Nat Rev Immunol 15(2):87\u2013103. https:\/\/doi.org\/10.1038\/nri3787","journal-title":"Nat Rev Immunol"},{"key":"10314_CR86","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2016.00652","volume":"7","author":"P Kovarik","year":"2016","unstructured":"Kovarik P, Castiglia V, Ivin M, Ebner F (2016) Type I interferons in bacterial infections: a balancing act. Front Immunol 7:652. https:\/\/doi.org\/10.3389\/fimmu.2016.00652","journal-title":"Front Immunol"},{"issue":"10","key":"10314_CR87","doi-asserted-by":"publisher","first-page":"4036","DOI":"10.4049\/jimmunol.1601226","volume":"198","author":"A Kaplan","year":"2017","unstructured":"Kaplan A, Lee MW, Wolf AJ, Limon JJ, Becker CA, Ding M, Murali R, Lee EY, Liu GY, Wong GCL, Underhill DM (2017) Direct antimicrobial activity of IFN-\u03b2. J Immunol 198(10):4036\u20134045. https:\/\/doi.org\/10.4049\/jimmunol.1601226","journal-title":"J Immunol"},{"issue":"44","key":"10314_CR88","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2409684121","volume":"121","author":"X Xiao","year":"2024","unstructured":"Xiao X, Wang J, Ma J, Peng X, Wu S, Chen X, Lu H, Tan C, Fang L, Xiao S (2024) Interferon lambda 4 is a gut antimicrobial protein. Proc Natl Acad Sci U S A 121(44):e2409684121. https:\/\/doi.org\/10.1073\/pnas.2409684121","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"9","key":"10314_CR89","doi-asserted-by":"publisher","first-page":"675","DOI":"10.1038\/nri1684","volume":"5","author":"T Decker","year":"2005","unstructured":"Decker T, M\u00fcller M, Stockinger S (2005) The yin and yang of type I interferon activity in bacterial infection. Nat Rev Immunol 5(9):675\u2013687. https:\/\/doi.org\/10.1038\/nri1684","journal-title":"Nat Rev Immunol"},{"issue":"6","key":"10314_CR90","doi-asserted-by":"publisher","first-page":"760","DOI":"10.1016\/j.chom.2016.05.016","volume":"19","author":"GM Boxx","year":"2016","unstructured":"Boxx GM, Cheng G (2016) The roles of type I interferon in bacterial infection. Cell Host Microbe 19(6):760\u2013769. https:\/\/doi.org\/10.1016\/j.chom.2016.05.016","journal-title":"Cell Host Microbe"},{"issue":"1","key":"10314_CR91","doi-asserted-by":"publisher","first-page":"1929005","DOI":"10.1080\/2162402X.2021.1929005","volume":"10","author":"X Zhang","year":"2021","unstructured":"Zhang X, Wang S, Zhu Y, Zhang M, Zhao Y, Yan Z, Wang Q, Li X (2021) Double-edged effects of interferons on the regulation of cancer-immunity cycle. Oncoimmunology 10(1):1929005. https:\/\/doi.org\/10.1080\/2162402X.2021.1929005","journal-title":"Oncoimmunology"},{"issue":"8","key":"10314_CR92","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1010740","volume":"18","author":"M Pekmezovic","year":"2022","unstructured":"Pekmezovic M, Dietschmann A, Gresnigt MS (2022) Type I interferons during host-fungus interactions: is antifungal immunity going viral? PLoS Pathog 18(8):e1010740. https:\/\/doi.org\/10.1371\/journal.ppat.1010740","journal-title":"PLoS Pathog"},{"issue":"12","key":"10314_CR93","doi-asserted-by":"publisher","first-page":"687","DOI":"10.1089\/jir.2004.24.687","volume":"24","author":"J Chen","year":"2004","unstructured":"Chen J, Baig E, Fish EN (2004) Diversity and relatedness among the type I interferons. J Interferon Cytokine Res 24(12):687\u2013698. https:\/\/doi.org\/10.1089\/jir.2004.24.687","journal-title":"J Interferon Cytokine Res"},{"key":"10314_CR94","doi-asserted-by":"publisher","first-page":"187","DOI":"10.1186\/1471-2164-10-187","volume":"10","author":"AM Walker","year":"2009","unstructured":"Walker AM, Roberts RM (2009) Characterization of the bovine type I IFN locus: rearrangements, expansions, and novel subfamilies. BMC Genomics 10:187. https:\/\/doi.org\/10.1186\/1471-2164-10-187","journal-title":"BMC Genomics"},{"key":"10314_CR95","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2020.528854","volume":"11","author":"Y Guo","year":"2020","unstructured":"Guo Y, Song Z, Li C, Yu Y, Dai H, Luo X, Wang Y, Wang J, Gao M (2020) A novel type-I interferon family, bovine interferon-chi, is involved in positive-feedback regulation of interferon production. Front Immunol 11:528854. https:\/\/doi.org\/10.3389\/fimmu.2020.528854","journal-title":"Front Immunol"},{"issue":"1\u20132","key":"10314_CR96","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1016\/j.gene.2007.03.018","volume":"397","author":"CH Woelk","year":"2007","unstructured":"Woelk CH, Frost SD, Richman DD, Higley PE, Kosakovsky Pond SL (2007) Evolution of the interferon alpha gene family in eutherian mammals. Gene 397(1\u20132):38\u201350. https:\/\/doi.org\/10.1016\/j.gene.2007.03.018","journal-title":"Gene"},{"issue":"2","key":"10314_CR97","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1016\/j.pep.2008.0","volume":"60","author":"A Ghosalkar","year":"2008","unstructured":"Ghosalkar A, Sahai V, Srivastava A (2008) Secretory expression of interferon-alpha 2b in recombinant Pichia pastoris using three different secretion signals. Protein Expr Purif 60(2):103\u2013109. https:\/\/doi.org\/10.1016\/j.pep.2008.0","journal-title":"Protein Expr Purif"},{"issue":"2","key":"10314_CR98","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1046\/j.0818-9641.2004.01230.x","volume":"82","author":"GA Harrison","year":"2004","unstructured":"Harrison GA, McNicol KA, Deane EM (2004) Type I interferon genes from the egg-laying mammal, Tachyglossus aculeatus (short-beaked echidna). Immunol Cell Biol 82(2):112\u2013118. https:\/\/doi.org\/10.1046\/j.0818-9641.2004.01230.x","journal-title":"Immunol Cell Biol"},{"key":"10314_CR99","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1016\/j.intimp.2017.08.028","volume":"52","author":"SF Li","year":"2017","unstructured":"Li SF, Zhao FR, Shao JJ, Xie YL, Chang HY, Zhang YG (2017) Interferon-omega: current status in clinical applications. Int Immunopharmacol 52:253\u2013260. https:\/\/doi.org\/10.1016\/j.intimp.2017.08.028","journal-title":"Int Immunopharmacol"},{"issue":"3","key":"10314_CR100","doi-asserted-by":"publisher","first-page":"335","DOI":"10.3390\/v12030335","volume":"12","author":"X Wang","year":"2020","unstructured":"Wang X, Li F, Han M, Jia S, Wang L, Qiao X, Jiang Y, Cui W, Tang L, Li Y, Xu YG (2020) Cloning, prokaryotic soluble expression, and analysis of antiviral activity of two novel feline IFN-\u03c9 proteins. Viruses 12(3):335. https:\/\/doi.org\/10.3390\/v12030335","journal-title":"Viruses"},{"issue":"1","key":"10314_CR101","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1089\/jir.1992.12.1","volume":"12","author":"DW Leaman","year":"1992","unstructured":"Leaman DW, Roberts RM (1992) Genes for the trophoblast interferons in sheep, goat, and musk ox and distribution of related genes among mammals. J Interferon Res 12(1):1\u201311. https:\/\/doi.org\/10.1089\/jir.1992.12.1","journal-title":"J Interferon Res"},{"issue":"5","key":"10314_CR102","doi-asserted-by":"publisher","first-page":"F1","DOI":"10.1530\/REP-17-0292","volume":"154","author":"AD Ealy","year":"2017","unstructured":"Ealy AD, Wooldridge LK (2017) The evolution of interferon-tau. Reproduction 154(5):F1\u2013F10. https:\/\/doi.org\/10.1530\/REP-17-0292","journal-title":"Reproduction"},{"issue":"1\u20132","key":"10314_CR103","doi-asserted-by":"publisher","first-page":"88","DOI":"10.1016\/j.gene.2008.11.026","volume":"433","author":"M Cochet","year":"2009","unstructured":"Cochet M, Vaiman D, Lef\u00e8vre F (2009) Novel interferon delta genes in mammals: cloning of one gene from the sheep, two genes expressed by the horse conceptus and discovery of related sequences in several taxa by genomic database screening. Gene 433(1\u20132):88\u201399. https:\/\/doi.org\/10.1016\/j.gene.2008.11.026","journal-title":"Gene"},{"issue":"2","key":"10314_CR104","doi-asserted-by":"publisher","first-page":"297","DOI":"10.1016\/j.molimm.2014.07.019","volume":"63","author":"J Alsemgeest","year":"2015","unstructured":"Alsemgeest J, Old JM, Young LJ (2015) The macropod type 2 interferon gene shares important regulatory and functionally relevant regions with eutherian IFN-\u03b3. Mol Immunol 63(2):297\u2013304. https:\/\/doi.org\/10.1016\/j.molimm.2014.07.019","journal-title":"Mol Immunol"},{"issue":"1","key":"10314_CR105","doi-asserted-by":"publisher","first-page":"317","DOI":"10.1111\/imr.12001","volume":"250","author":"J Piehler","year":"2012","unstructured":"Piehler J, Thomas C, Garcia KC, Schreiber G (2012) Structural and dynamic determinants of type I interferon receptor assembly and their functional interpretation. Immunol Rev 250(1):317\u2013334. https:\/\/doi.org\/10.1111\/imr.12001","journal-title":"Immunol Rev"},{"issue":"5","key":"10314_CR106","doi-asserted-by":"publisher","first-page":"483","DOI":"10.1038\/icb.2012.9","volume":"90","author":"NA de Weerd","year":"2012","unstructured":"de Weerd NA, Nguyen T (2012) The interferons and their receptors - distribution and regulation. Immunol Cell Biol 90(5):483\u2013491. https:\/\/doi.org\/10.1038\/icb.2012.9","journal-title":"Immunol Cell Biol"},{"issue":"1","key":"10314_CR107","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1089\/jir.2012.0160","volume":"34","author":"Z Ping","year":"2014","unstructured":"Ping Z, Qi J, Sun Y, Lu G, Shi Y, Wang X, Gao GF, Wang M (2014) Crystal structure of the interferon gamma receptor alpha chain from chicken reveals an undetected extra helix compared with the human counterparts. J Interferon Cytokine Res 34(1):41\u201351. https:\/\/doi.org\/10.1089\/jir.2012.0160","journal-title":"J Interferon Cytokine Res"},{"key":"10314_CR108","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2013.00267","volume":"4","author":"CM Blouin","year":"2013","unstructured":"Blouin CM, Lamaze C (2013) Interferon gamma receptor: the beginning of the journey. Front Immunol 4:267. https:\/\/doi.org\/10.3389\/fimmu.2013.00267","journal-title":"Front Immunol"},{"key":"10314_CR109","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2017.00119","volume":"8","author":"M Syedbasha","year":"2017","unstructured":"Syedbasha M, Egli A (2017) Interferon lambda: modulating immunity in infectious diseases. Front Immunol 8:119. https:\/\/doi.org\/10.3389\/fimmu.2017.00119","journal-title":"Front Immunol"},{"issue":"5","key":"10314_CR110","doi-asserted-by":"publisher","first-page":"525","DOI":"10.1007\/s10930-019-09833-8","volume":"38","author":"U Roy","year":"2019","unstructured":"Roy U (2019) Structure and function of an inflammatory cytokine, interleukin-2, analyzed using the bioinformatic approach. Protein J 38(5):525\u2013536. https:\/\/doi.org\/10.1007\/s10930-019-09833-8","journal-title":"Protein J"},{"issue":"25","key":"10314_CR111","doi-asserted-by":"publisher","DOI":"10.1126\/sciimmunol.aat1482","volume":"3","author":"AK Abbas","year":"2018","unstructured":"Abbas AK, Trotta E, Simeonov DR, Marson A, Bluestone JA (2018) Revisiting IL-2: biology and therapeutic prospects. Sci Immunol 3(25):eaat1482. https:\/\/doi.org\/10.1126\/sciimmunol.aat1482","journal-title":"Sci Immunol"},{"issue":"10","key":"10314_CR112","doi-asserted-by":"publisher","first-page":"648","DOI":"10.1038\/s41577-018-0046-y","volume":"18","author":"R Spolski","year":"2018","unstructured":"Spolski R, Li P, Leonard WJ (2018) Biology and regulation of IL-2: from molecular mechanisms to human therapy. Nat Rev Immunol 18(10):648\u2013659. https:\/\/doi.org\/10.1038\/s41577-018-0046-y","journal-title":"Nat Rev Immunol"},{"issue":"2","key":"10314_CR113","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1089\/jir.2017.0101","volume":"38","author":"JM Wrangle","year":"2018","unstructured":"Wrangle JM, Patterson A, Johnson CB, Neitzke DJ, Mehrotra S, Denlinger CE, Paulos CM, Li Z, Cole DJ, Rubinstein MP (2018) IL-2 and beyond in cancer immunotherapy. J Interferon Cytokine Res 38(2):45\u201368. https:\/\/doi.org\/10.1089\/jir.2017.0101","journal-title":"J Interferon Cytokine Res"},{"issue":"10","key":"10314_CR114","doi-asserted-by":"publisher","first-page":"614","DOI":"10.1038\/s41577-022-00680-w","volume":"22","author":"R Hernandez","year":"2022","unstructured":"Hernandez R, P\u00f5der J, LaPorte KM, Malek TR (2022) Engineering IL-2 for immunotherapy of autoimmunity and cancer. Nat Rev Immunol 22(10):614\u2013628. https:\/\/doi.org\/10.1038\/s41577-022-00680-w","journal-title":"Nat Rev Immunol"},{"issue":"9","key":"10314_CR115","doi-asserted-by":"publisher","first-page":"1900","DOI":"10.1038\/s12276-024-01301-3","volume":"56","author":"SJ Im","year":"2024","unstructured":"Im SJ, Lee K, Ha SJ (2024) Harnessing IL-2 for immunotherapy against cancer and chronic infection: a historical perspective and emerging trends. Exp Mol Med 56(9):1900\u20131908. https:\/\/doi.org\/10.1038\/s12276-024-01301-3","journal-title":"Exp Mol Med"},{"key":"10314_CR116","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2024.1433989","volume":"15","author":"S Rokade","year":"2024","unstructured":"Rokade S, Damani AM, Oft M, Emmerich J (2024) IL-2 based cancer immunotherapies: an evolving paradigm. Front Immunol 15:1433989. https:\/\/doi.org\/10.3389\/fimmu.2024.1433989","journal-title":"Front Immunol"},{"issue":"6","key":"10314_CR117","doi-asserted-by":"publisher","DOI":"10.1080\/2162402X.2016.1163462","volume":"5","author":"T Jiang","year":"2016","unstructured":"Jiang T, Zhou C, Ren S (2016) Role of IL-2 in cancer immunotherapy. Oncoimmunology 5(6):e1163462. https:\/\/doi.org\/10.1080\/2162402X.2016.1163462","journal-title":"Oncoimmunology"},{"key":"10314_CR118","doi-asserted-by":"publisher","first-page":"1312","DOI":"10.1134\/S0006297912110107","volume":"77","author":"PA Levashov","year":"2012","unstructured":"Levashov PA, Sedov SA, Belogurova NG, Shipovskov SV, Levashov AV (2012) Bacteriolytic activity of human interleukin-2. Biochemistry Moscow 77:1312\u20131314. https:\/\/doi.org\/10.1134\/S0006297912110107","journal-title":"Biochemistry Moscow"},{"key":"10314_CR119","doi-asserted-by":"publisher","first-page":"274","DOI":"10.1134\/S1068162012030132","volume":"38","author":"SA Sedov","year":"2012","unstructured":"Sedov SA, Belogurova NG, Shipovskov SV, Semenova MV, Gitinov MM, Levashov AV, Levashov PA (2012) Bacteriolytic enzymes from the blood plasma of the sheep. Russ J Bioorg Chem 38:274\u2013281. https:\/\/doi.org\/10.1134\/S1068162012030132","journal-title":"Russ J Bioorg Chem"},{"key":"10314_CR120","doi-asserted-by":"publisher","first-page":"287","DOI":"10.3103\/S0027131415060048","volume":"70","author":"PA Levashov","year":"2015","unstructured":"Levashov PA, Matolygina DA, Osipova HE, Savin SS, Zaharova GS, Gasanova DA, Belogurova NG, Ovchinnikova ED, Smirnov SA, Tishkov VI, Levashov AV (2015) Comparison of bacteriolytic activity of human interleukin-2 and chicken egg lysozyme on Lactobacillus plantarum and Escherichia coli cells. Moscow Univ Chem Bull 70:287\u2013291. https:\/\/doi.org\/10.3103\/S0027131415060048","journal-title":"Moscow Univ Chem Bull"},{"issue":"1","key":"10314_CR121","doi-asserted-by":"publisher","first-page":"98","DOI":"10.32607\/20758251-2016-8-1-98-102","volume":"8","author":"PA Levashov","year":"2016","unstructured":"Levashov PA, Ovchinnikova ED, Morozova OA, Matolygina DA, Osipova HE, Cherdyntseva TA, Savin SS, Zakharova GS, Alekseeva AA, Belogurova NG, Smirnov SA, Tishkov VI, Levashov AV (2016) Human interleukin-2 and hen egg white lysozyme: screening for bacteriolytic activity against various bacterial cells. Acta Naturae 8(1):98\u2013102. https:\/\/doi.org\/10.32607\/20758251-2016-8-1-98-102","journal-title":"Acta Naturae"},{"issue":"6","key":"10314_CR122","doi-asserted-by":"publisher","first-page":"1037","DOI":"10.1080\/03007995.2022.2065145","volume":"38","author":"JQ Zhang","year":"2022","unstructured":"Zhang JQ, Zhang SX, Wang J, Qiao J, Qiu MT, Wu XY, Chen JW, Gao C, Li XF (2022) Low-dose IL-2 therapy limits the reduction in absolute numbers of peripheral lymphocytes in systemic lupus erythematosus patients with infection. Curr Med Res Opin 38(6):1037\u20131044. https:\/\/doi.org\/10.1080\/03007995.2022.2065145","journal-title":"Curr Med Res Opin"},{"issue":"4","key":"10314_CR123","doi-asserted-by":"publisher","first-page":"753","DOI":"10.47278\/journal.ijab\/2024.185","volume":"13","author":"O Gizinger","year":"2024","unstructured":"Gizinger O, Radzinskiy V, Sorokin Y, Sachivkina N, Letifov G, Gaziev A, Kornova N, Burgasova O, Taranova M, Ibragimova A, Bobunova A (2024) The effects of interleukin-2 substances (glutamate, glycine, arginine) on biofilm formation in multidrug-resistant uropathogenic Escherichia coli in women with previous reproductive losses. Int Journ Agric Biosci 13(4):753\u2013762. https:\/\/doi.org\/10.47278\/journal.ijab\/2024.185","journal-title":"Int Journ Agric Biosci"},{"issue":"50","key":"10314_CR124","doi-asserted-by":"publisher","first-page":"42361","DOI":"10.1074\/jbc.M112.382028","volume":"287","author":"JS Oeemig","year":"2012","unstructured":"Oeemig JS, Lynggaard C, Knudsen DH, Hansen FT, N\u00f8rgaard KD, Schneider T, Vad BS, Sandvang DH, Nielsen LA, Neve S, Kristensen HH, Sahl HG, Otzen DE, Wimmer R (2012) Eurocin, a new fungal defensin: structure, lipid binding, and its mode of action. J Biol Chem 287(50):42361\u201342372. https:\/\/doi.org\/10.1074\/jbc.M112.382028","journal-title":"J Biol Chem"},{"issue":"50","key":"10314_CR125","doi-asserted-by":"publisher","first-page":"34953","DOI":"10.1074\/jbc.M114.599878","volume":"289","author":"A Essig","year":"2014","unstructured":"Essig A, Hofmann D, M\u00fcnch D, Gayathri S, K\u00fcnzler M, Kallio PT, Sahl HG, Wider G, Schneider T, Aebi M (2014) Copsin, a novel peptide-based fungal antibiotic interfering with the peptidoglycan synthesis. J Biol Chem 289(50):34953\u201334964. https:\/\/doi.org\/10.1074\/jbc.M114.599878","journal-title":"J Biol Chem"},{"issue":"5","key":"10314_CR126","doi-asserted-by":"publisher","first-page":"507","DOI":"10.1094\/MPMI-08-18-0229-CR","volume":"32","author":"AE Sathoff","year":"2019","unstructured":"Sathoff AE, Samac DA (2019) Antibacterial Activity of Plant Defensins. Mol Plant Microbe Interact 32(5):507\u2013514. https:\/\/doi.org\/10.1094\/MPMI-08-18-0229-CR","journal-title":"Mol Plant Microbe Interact"},{"key":"10314_CR127","doi-asserted-by":"publisher","first-page":"758","DOI":"10.3389\/fimmu.2020.00758","volume":"11","author":"M Gerdol","year":"2020","unstructured":"Gerdol M, Schmitt P, Venier P, Rocha G, Rosa RD, Destoumieux-Garz\u00f3n D (2020) Functional insights from the evolutionary diversification of big defensins. Front Immunol 11:758. https:\/\/doi.org\/10.3389\/fimmu.2020.00758","journal-title":"Front Immunol"},{"issue":"4","key":"10314_CR128","doi-asserted-by":"publisher","first-page":"663","DOI":"10.1007\/s00018-016-2344-5","volume":"74","author":"TM Shafee","year":"2017","unstructured":"Shafee TM, Lay FT, Phan TK, Anderson MA, Hulett MD (2017) Convergent evolution of defensin sequence, structure and function. Cell Mol Life Sci 74(4):663\u2013682. https:\/\/doi.org\/10.1007\/s00018-016-2344-5","journal-title":"Cell Mol Life Sci"},{"issue":"1","key":"10314_CR129","doi-asserted-by":"publisher","first-page":"61","DOI":"10.1007\/s00251-018-1086-y","volume":"71","author":"W Zhou","year":"2019","unstructured":"Zhou W, Gao B, Zhu S (2019) Did cis- and trans-defensins derive from a common ancestor? Immunogenetics 71(1):61\u201369. https:\/\/doi.org\/10.1007\/s00251-018-1086-y","journal-title":"Immunogenetics"},{"issue":"5","key":"10314_CR130","doi-asserted-by":"publisher","first-page":"743","DOI":"10.1093\/bioinformatics\/bty697","volume":"35","author":"T Shafee","year":"2019","unstructured":"Shafee T, Anderson MA (2019) A quantitative map of protein sequence space for the cis-defensin superfamily. Bioinformatics 35(5):743\u2013752. https:\/\/doi.org\/10.1093\/bioinformatics\/bty697","journal-title":"Bioinformatics"},{"issue":"5","key":"10314_CR131","doi-asserted-by":"publisher","first-page":"446","DOI":"10.2174\/138920307782411446","volume":"8","author":"JH Wong","year":"2007","unstructured":"Wong JH, Xia L, Ng TB (2007) A review of defensins of diverse origins. Curr Protein Pept Sci 8(5):446\u2013459. https:\/\/doi.org\/10.2174\/138920307782411446","journal-title":"Curr Protein Pept Sci"},{"issue":"40","key":"10314_CR132","doi-asserted-by":"publisher","first-page":"10612","DOI":"10.1002\/anie.201402167","volume":"53","author":"AC Conibear","year":"2014","unstructured":"Conibear AC, Craik DJ (2014) The chemistry and biology of theta defensins. Angew Chem Int Ed Engl 53(40):10612\u201310623. https:\/\/doi.org\/10.1002\/anie.201402167","journal-title":"Angew Chem Int Ed Engl"},{"issue":"21","key":"10314_CR133","doi-asserted-by":"publisher","DOI":"10.3390\/ijms222111691","volume":"22","author":"A Bin Hafeez","year":"2021","unstructured":"Bin Hafeez A, Jiang X, Bergen PJ, Zhu Y (2021) Antimicrobial peptides: an update on classifications and databases. Int J Mol Sci 22(21):11691. https:\/\/doi.org\/10.3390\/ijms222111691","journal-title":"Int J Mol Sci"},{"issue":"3","key":"10314_CR134","doi-asserted-by":"publisher","first-page":"1563","DOI":"10.1007\/s12602-024-10436-8","volume":"17","author":"M Nagib","year":"2025","unstructured":"Nagib M, Sayed AM, Korany AH, Abdelkader K, Shari FH, Mackay WG, Rateb ME (2025) Human Defensins: Structure, Function, and Potential as Therapeutic Antimicrobial Agents with Highlights Against SARS CoV-2. Probiotics Antimicrob Proteins 17(3):1563\u20131583. https:\/\/doi.org\/10.1007\/s12602-024-10436-8","journal-title":"Probiotics Antimicrob Proteins"},{"issue":"1\u20132","key":"10314_CR135","doi-asserted-by":"publisher","first-page":"94","DOI":"10.1007\/s000180050010","volume":"56","author":"AL Hughes","year":"1999","unstructured":"Hughes AL (1999) Evolutionary diversification of the mammalian defensins. Cell Mol Life Sci 56(1\u20132):94\u2013103. https:\/\/doi.org\/10.1007\/s000180050010","journal-title":"Cell Mol Life Sci"},{"key":"10314_CR136","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1016\/j.cytogfr.2015.11.002","volume":"28","author":"EH Mattar","year":"2016","unstructured":"Mattar EH, Almehdar HA, Yacoub HA, Uversky VN, Redwan EM (2016) Antimicrobial potentials and structural disorder of human and animal defensins. Cytokine Growth Factor Rev 28:95\u2013111. https:\/\/doi.org\/10.1016\/j.cytogfr.2015.11.002","journal-title":"Cytokine Growth Factor Rev"},{"issue":"1","key":"10314_CR137","doi-asserted-by":"publisher","first-page":"300","DOI":"10.1038\/s41392-023-01553-x","volume":"8","author":"J Fu","year":"2023","unstructured":"Fu J, Zong X, Jin M, Min J, Wang F, Wang Y (2023) Mechanisms and regulation of defensins in host defense. Signal Transduct Target Ther 8(1):300. https:\/\/doi.org\/10.1038\/s41392-023-01553-x","journal-title":"Signal Transduct Target Ther"},{"key":"10314_CR138","doi-asserted-by":"publisher","first-page":"45282","DOI":"10.1038\/srep45282","volume":"7","author":"HJ Min","year":"2017","unstructured":"Min HJ, Yun H, Ji S, Rajasekaran G, Kim JI, Kim JS, Shin SY, Lee CW (2017) Rattusin structure reveals a novel defensin scaffold formed by intermolecular disulfide exchanges. Sci Rep 7:45282. https:\/\/doi.org\/10.1038\/srep45282","journal-title":"Sci Rep"},{"issue":"13","key":"10314_CR139","doi-asserted-by":"publisher","first-page":"2069","DOI":"10.1007\/s00018-008-8035-0","volume":"65","author":"AM Aerts","year":"2008","unstructured":"Aerts AM, Fran\u00e7ois IE, Cammue BP, Thevissen K (2008) The mode of antifungal action of plant, insect and human defensins. Cell Mol Life Sci 65(13):2069\u20132079. https:\/\/doi.org\/10.1007\/s00018-008-8035-0","journal-title":"Cell Mol Life Sci"},{"issue":"24","key":"10314_CR140","doi-asserted-by":"publisher","first-page":"4965","DOI":"10.1016\/j.jmb.2013.09.038","volume":"425","author":"SS Wilson","year":"2013","unstructured":"Wilson SS, Wiens ME, Smith JG (2013) Antiviral mechanisms of human defensins. J Mol Biol 425(24):4965\u20134980. https:\/\/doi.org\/10.1016\/j.jmb.2013.09.038","journal-title":"J Mol Biol"},{"key":"10314_CR141","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2020.00764","volume":"11","author":"D Xu","year":"2020","unstructured":"Xu D, Lu W (2020) Defensins: a double-edged sword in host immunity. Front Immunol 11:764. https:\/\/doi.org\/10.3389\/fimmu.2020.00764","journal-title":"Front Immunol"},{"issue":"2","key":"10314_CR142","doi-asserted-by":"publisher","first-page":"179","DOI":"10.21775\/cimb.007.179","volume":"7","author":"M Zanetti","year":"2005","unstructured":"Zanetti M (2005) The role of cathelicidins in the innate host defenses of mammals. Curr Issues Mol Biol 7(2):179\u2013196. https:\/\/doi.org\/10.21775\/cimb.007.179","journal-title":"Curr Issues Mol Biol"},{"issue":"12","key":"10314_CR143","doi-asserted-by":"publisher","first-page":"10957","DOI":"10.1007\/s11033-012-1997-x","volume":"39","author":"EM Ko\u015bciuczuk","year":"2012","unstructured":"Ko\u015bciuczuk EM, Lisowski P, Jarczak J, Strza\u0142kowska N, J\u00f3\u017awik A, Horba\u0144czuk J, Krzy\u017cewski J, Zwierzchowski L, Bagnicka E (2012) Cathelicidins: family of antimicrobial peptides. A review. Mol Biol Rep 39(12):10957\u201310970. https:\/\/doi.org\/10.1007\/s11033-012-1997-x","journal-title":"Mol Biol Rep"},{"issue":"1","key":"10314_CR144","doi-asserted-by":"publisher","first-page":"31","DOI":"10.1002\/1097-0282(2000)55:1<31::AID-BIP40>3.0.CO;2-9","volume":"55","author":"R Gennaro","year":"2000","unstructured":"Gennaro R, Zanetti M (2000) Structural features and biological activities of the cathelicidin-derived antimicrobial peptides. Biopolymers 55(1):31\u201349. https:\/\/doi.org\/10.1002\/1097-0282(2000)55:1%3c31::AID-BIP40%3e3.0.CO;2-9","journal-title":"Biopolymers"},{"issue":"3","key":"10314_CR145","doi-asserted-by":"publisher","first-page":"796","DOI":"10.1007\/s12602-023-10070-w","volume":"16","author":"N Farzi","year":"2024","unstructured":"Farzi N, Oloomi M, Bahramali G, Siadat SD, Bouzari S (2024) Antibacterial properties and efficacy of LL-37 fragment GF-17D3 and scolopendin A2 peptides against resistant clinical strains of Staphylococcus aureus, Pseudomonas aeruginosa, and Acinetobacter baumannii in vitro and in vivo model studies. Probiotics Antimicrob Proteins 16(3):796\u2013814. https:\/\/doi.org\/10.1007\/s12602-023-10070-w","journal-title":"Probiotics Antimicrob Proteins"},{"issue":"5","key":"10314_CR146","doi-asserted-by":"publisher","first-page":"958","DOI":"10.1016\/j.bbamem.2015.10.011","volume":"1858","author":"P Schmitt","year":"2016","unstructured":"Schmitt P, Rosa RD, Destoumieux-Garz\u00f3n D (2016) An intimate link between antimicrobial peptide sequence diversity and binding to essential components of bacterial membranes. Biochim Biophys Acta 1858(5):958\u2013970. https:\/\/doi.org\/10.1016\/j.bbamem.2015.10.011","journal-title":"Biochim Biophys Acta"},{"issue":"3","key":"10314_CR147","doi-asserted-by":"publisher","first-page":"361","DOI":"10.1016\/s1286-4579(02)01549-6","volume":"4","author":"B Ramanathan","year":"2002","unstructured":"Ramanathan B, Davis EG, Ross CR, Blecha F (2002) Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity. Microbes Infect 4(3):361\u2013372. https:\/\/doi.org\/10.1016\/s1286-4579(02)01549-6","journal-title":"Microbes Infect"},{"issue":"3","key":"10314_CR148","doi-asserted-by":"publisher","DOI":"10.3390\/vaccines6030063","volume":"6","author":"RM van Harten","year":"2018","unstructured":"van Harten RM, van Woudenbergh E, van Dijk A, Haagsman HP (2018) Cathelicidins: immunomodulatory antimicrobials. Vaccines 6(3):63. https:\/\/doi.org\/10.3390\/vaccines6030063","journal-title":"Vaccines"},{"key":"10314_CR149","doi-asserted-by":"publisher","DOI":"10.1016\/j.peptides.2023.171011","volume":"165","author":"ML Leite","year":"2023","unstructured":"Leite ML, Duque HM, Rodrigues GR, da Cunha NB, Franco OL (2023) The LL-37 domain: a clue to cathelicidin immunomodulatory response? Peptides 165:171011. https:\/\/doi.org\/10.1016\/j.peptides.2023.171011","journal-title":"Peptides"},{"key":"10314_CR150","doi-asserted-by":"publisher","DOI":"10.1007\/s10989-024-10595-w","volume":"30","author":"M Bashi","year":"2024","unstructured":"Bashi M, Baharlou R, Haghmorad D, Lashkari R, Yousefi B, Madanchi H (2024) Peptide derivatives of human and rabbit cathelicidin reduce inflammatory cytokines in peripheral blood mononuclear cells of rheumatoid arthritis patients. Int J Pept Res Ther 30:18. https:\/\/doi.org\/10.1007\/s10989-024-10595-w","journal-title":"Int J Pept Res Ther"},{"issue":"4","key":"10314_CR151","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0124706","volume":"10","author":"S Tripathi","year":"2015","unstructured":"Tripathi S, Wang G, White M, Qi L, Taubenberger J, Hartshorn KL (2015) Antiviral activity of the human cathelicidin, LL-37, and derived peptides on seasonal and pandemic influenza A viruses. PLoS ONE 10(4):e0124706. https:\/\/doi.org\/10.1371\/journal.pone.0124706","journal-title":"PLoS ONE"},{"key":"10314_CR152","doi-asserted-by":"publisher","DOI":"10.1007\/s10989-025-10698-y","volume":"31","author":"GE Metz","year":"2025","unstructured":"Metz GE, Azcurra MB, de Souza GS, Brasil M, Cilli E, Lorenz\u00f3n E (2025) Inactivation of equine arteritis virus by indolicidin peptide. Int J Pept Res Ther 31:39. https:\/\/doi.org\/10.1007\/s10989-025-10698-y","journal-title":"Int J Pept Res Ther"},{"issue":"1","key":"10314_CR153","doi-asserted-by":"publisher","DOI":"10.1007\/s11274-023-03852-5","volume":"40","author":"M Memariani","year":"2023","unstructured":"Memariani M, Memariani H (2023) Antifungal properties of cathelicidin LL-37: current knowledge and future research directions. World J Microbiol Biotechnol 40(1):34. https:\/\/doi.org\/10.1007\/s11274-023-03852-5","journal-title":"World J Microbiol Biotechnol"},{"issue":"1","key":"10314_CR154","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1007\/s00005-015-0359-5","volume":"64","author":"E Piktel","year":"2016","unstructured":"Piktel E, Niemirowicz K, Wnorowska U, W\u0105tek M, Wollny T, G\u0142uszek K, G\u00f3\u017ad\u017a S, Levental I, Bucki R (2016) The role of cathelicidin LL-37 in cancer development. Arch Immunol Ther Exp (Warsz) 64(1):33\u201346. https:\/\/doi.org\/10.1007\/s00005-015-0359-5","journal-title":"Arch Immunol Ther Exp (Warsz)"},{"issue":"1","key":"10314_CR155","doi-asserted-by":"publisher","first-page":"23","DOI":"10.2174\/1389203053027520","volume":"6","author":"L Tomasinsig","year":"2005","unstructured":"Tomasinsig L, Zanetti M (2005) The cathelicidins - structure, function and evolution. Curr Protein Pept Sci 6(1):23\u201334. https:\/\/doi.org\/10.2174\/1389203053027520","journal-title":"Curr Protein Pept Sci"},{"issue":"4","key":"10314_CR156","doi-asserted-by":"publisher","first-page":"461","DOI":"10.3390\/antibiotics3040461","volume":"3","author":"KL Nawrocki","year":"2014","unstructured":"Nawrocki KL, Crispell EK, McBride SM (2014) Antimicrobial peptide resistance mechanisms of Gram-Positive bacteria. Antibiotics (Basel) 3(4):461\u2013492. https:\/\/doi.org\/10.3390\/antibiotics3040461","journal-title":"Antibiotics (Basel)"},{"key":"10314_CR157","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2020.593215","volume":"11","author":"L Assoni","year":"2020","unstructured":"Assoni L, Milani B, Carvalho MR, Nepomuceno LN, Waz NT, Guerra MES, Converso TR, Darrieux M (2020) Resistance mechanisms to antimicrobial peptides in Gram-Positive bacteria. Front Microbiol 11:593215. https:\/\/doi.org\/10.3389\/fmicb.2020.593215","journal-title":"Front Microbiol"},{"issue":"7","key":"10314_CR158","doi-asserted-by":"publisher","first-page":"1259","DOI":"10.3390\/microorganisms12071259","volume":"12","author":"L Tajer","year":"2024","unstructured":"Tajer L, Paillart JC, Dib H, Sabatier JM, Fajloun Z, Abi Khattar Z (2024) Molecular mechanisms of bacterial resistance to antimicrobial peptides in the modern era: an updated review. Microorganisms 12(7):1259. https:\/\/doi.org\/10.3390\/microorganisms12071259","journal-title":"Microorganisms"},{"issue":"3","key":"10314_CR159","doi-asserted-by":"publisher","DOI":"10.3390\/jof6030124","volume":"6","author":"HL Norris","year":"2020","unstructured":"Norris HL, Kumar R, Ong CY, Xu D, Edgerton M (2020) Zinc binding by histatin 5 promotes fungicidal membrane disruption in C. albicans and C. glabrata. J Fungi 6(3):124. https:\/\/doi.org\/10.3390\/jof6030124","journal-title":"J Fungi"},{"issue":"3","key":"10314_CR160","doi-asserted-by":"publisher","first-page":"657","DOI":"10.1111\/febs.12612","volume":"281","author":"S Melino","year":"2014","unstructured":"Melino S, Santone C, Di Nardo P, Sarkar B (2014) Histatins: salivary peptides with copper(II)- and zinc(II)-binding motifs: perspectives for biomedical applications. FEBS J 281(3):657\u2013672. https:\/\/doi.org\/10.1111\/febs.12612","journal-title":"FEBS J"},{"issue":"1","key":"10314_CR161","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-019-52676-7","volume":"9","author":"TG McCaslin","year":"2019","unstructured":"McCaslin TG, Pagba CV, Yohannan J, Barry BA (2019) Specific metallo-protein interactions and antimicrobial activity in Histatin-5, an intrinsically disordered salivary peptide. Sci Rep 9(1):17303. https:\/\/doi.org\/10.1038\/s41598-019-52676-7","journal-title":"Sci Rep"},{"issue":"Suppl 01","key":"10314_CR162","doi-asserted-by":"publisher","first-page":"S177","DOI":"10.1055\/s-0040-1715708","volume":"14","author":"K Nasiri","year":"2020","unstructured":"Nasiri K (2020) COVID-19 and the antiviral effect of saliva. Eur J Dent 14(Suppl 01):S177\u2013S178. https:\/\/doi.org\/10.1055\/s-0040-1715708","journal-title":"Eur J Dent"},{"issue":"7","key":"10314_CR163","doi-asserted-by":"publisher","first-page":"1087","DOI":"10.1016\/j.chom.2023.05.026","volume":"31","author":"AS Luis","year":"2023","unstructured":"Luis AS, Hansson G (2023) Intestinal mucus and their glycans: a habitat for thriving microbiota. Cell Host Microbe 31(7):1087\u20131100. https:\/\/doi.org\/10.1016\/j.chom.2023.05.026","journal-title":"Cell Host Microbe"},{"issue":"3","key":"10314_CR164","doi-asserted-by":"publisher","DOI":"10.3390\/microorganisms4030034","volume":"4","author":"K Nishiyama","year":"2016","unstructured":"Nishiyama K, Sugiyama M, Mukai T (2016) Adhesion properties of lactic acid bacteria on intestinal mucin. Microorganisms 4(3):34. https:\/\/doi.org\/10.3390\/microorganisms4030034","journal-title":"Microorganisms"},{"issue":"24","key":"10314_CR165","doi-asserted-by":"publisher","first-page":"2325","DOI":"10.1016\/j.cub.2012.10.028","volume":"22","author":"M Caldara","year":"2012","unstructured":"Caldara M, Friedlander RS, Kavanaugh NL, Aizenberg J, Foster KR, Ribbeck K (2012) Mucin biopolymers prevent bacterial aggregation by retaining cells in the free-swimming state. Curr Biol 22(24):2325\u20132330. https:\/\/doi.org\/10.1016\/j.cub.2012.10.028","journal-title":"Curr Biol"},{"key":"10314_CR166","doi-asserted-by":"publisher","DOI":"10.1016\/j.carres.2024.109309","volume":"546","author":"I Brockhausen","year":"2024","unstructured":"Brockhausen I, Falconer D, Sara S (2024) Relationships between bacteria and the mucus layer. Carbohydr Res 546:109309. https:\/\/doi.org\/10.1016\/j.carres.2024.109309","journal-title":"Carbohydr Res"},{"key":"10314_CR167","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2020.02054","volume":"11","author":"JA Grondin","year":"2020","unstructured":"Grondin JA, Kwon YH, Far PM, Haq S, Khan WI (2020) Mucins in intestinal mucosal defense and inflammation: learning from clinical and experimental studies. Front Immunol 11:2054. https:\/\/doi.org\/10.3389\/fimmu.2020.02054","journal-title":"Front Immunol"},{"issue":"3","key":"10314_CR168","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1159\/000453594","volume":"9","author":"JPM van Putten","year":"2017","unstructured":"van Putten JPM, Strijbis K (2017) Transmembrane mucins: signaling receptors at the intersection of inflammation and cancer. J Innate Immun 9(3):281\u2013299. https:\/\/doi.org\/10.1159\/000453594","journal-title":"J Innate Immun"},{"issue":"6","key":"10314_CR169","doi-asserted-by":"publisher","DOI":"10.3390\/cimb47060406","volume":"47","author":"C Chen","year":"2025","unstructured":"Chen C, Patel A, Demirkhanyan L, Gondi CS (2025) The role of mucins in cancer and cancer progression: a comprehensive review. Curr Issues Mol Biol 47(6):406. https:\/\/doi.org\/10.3390\/cimb47060406","journal-title":"Curr Issues Mol Biol"},{"issue":"6","key":"10314_CR170","doi-asserted-by":"publisher","DOI":"10.1128\/mBio.01984-19","volume":"10","author":"GMF Almeida","year":"2019","unstructured":"Almeida GMF, Laanto E, Ashrafi R, Sundberg LR (2019) Bacteriophage adherence to mucus mediates preventive protection against pathogenic bacteria. MBio 10(6):e01984-19. https:\/\/doi.org\/10.1128\/mBio.01984-19","journal-title":"MBio"},{"issue":"6","key":"10314_CR171","doi-asserted-by":"publisher","DOI":"10.1007\/s00705-025-06322-5","volume":"170","author":"J Jakin Lazar","year":"2025","unstructured":"Jakin Lazar J, \u0160imunovi\u0107 K, Dog\u0161a I, Mandi\u0107 Mulec I, Middelboe M, Drago\u0161 A (2025) Distinct effects of mucin on phage-host interactions in model systems of beneficial and pathogenic bacteria. Arch Virol 170(6):133. https:\/\/doi.org\/10.1007\/s00705-025-06322-5","journal-title":"Arch Virol"},{"issue":"3","key":"10314_CR172","doi-asserted-by":"publisher","first-page":"270","DOI":"10.1093\/glycob\/cwp186","volume":"20","author":"TK Dam","year":"2010","unstructured":"Dam TK, Brewer CF (2010) Lectins as pattern recognition molecules: the effects of epitope density in innate immunity. Glycobiology 20(3):270\u2013279. https:\/\/doi.org\/10.1093\/glycob\/cwp186","journal-title":"Glycobiology"},{"issue":"1","key":"10314_CR173","doi-asserted-by":"publisher","DOI":"10.1038\/s41392-021-00687-0","volume":"6","author":"D Li","year":"2021","unstructured":"Li D, Wu M (2021) Pattern recognition receptors in health and diseases. Signal Transduct Target Ther 6(1):291. https:\/\/doi.org\/10.1038\/s41392-021-00687-0","journal-title":"Signal Transduct Target Ther"},{"key":"10314_CR174","doi-asserted-by":"publisher","first-page":"234","DOI":"10.1016\/j.ijbiomac.2019.08.059","volume":"140","author":"PM Dos Santos Silva","year":"2019","unstructured":"Dos Santos Silva PM, de Oliveira WF, Albuquerque PBS, Dos Santos Correia MT, Coelho LCBB (2019) Insights into anti-pathogenic activities of mannose lectins. Int J Biol Macromol 140:234\u2013244. https:\/\/doi.org\/10.1016\/j.ijbiomac.2019.08.059","journal-title":"Int J Biol Macromol"},{"key":"10314_CR175","doi-asserted-by":"publisher","DOI":"10.1016\/j.fct.2019.110827","volume":"134","author":"A Mishra","year":"2019","unstructured":"Mishra A, Behura A, Mawatwal S, Kumar A, Naik L, Mohanty SS, Manna D, Dokania P, Mishra A, Patra SK, Dhiman R (2019) Structure-function and application of plant lectins in disease biology and immunity. Food Chem Toxicol 134:110827. https:\/\/doi.org\/10.1016\/j.fct.2019.110827","journal-title":"Food Chem Toxicol"},{"issue":"2","key":"10314_CR176","doi-asserted-by":"publisher","first-page":"188","DOI":"10.3390\/biom11020188","volume":"11","author":"CD Raposo","year":"2021","unstructured":"Raposo CD, Canelas AB, Barros MT (2021) Human lectins, their carbohydrate affinities and where to find them. Biomolecules 11(2):188. https:\/\/doi.org\/10.3390\/biom11020188","journal-title":"Biomolecules"},{"key":"10314_CR177","doi-asserted-by":"publisher","first-page":"421","DOI":"10.1007\/978-1-4939-1396-1_27","volume":"1207","author":"CM Arthur","year":"2015","unstructured":"Arthur CM, Cummings RD, Stowell SR (2015) Evaluation of the bactericidal activity of galectins. Methods Mol Biol 1207:421\u2013430. https:\/\/doi.org\/10.1007\/978-1-4939-1396-1_27","journal-title":"Methods Mol Biol"},{"issue":"6","key":"10314_CR178","doi-asserted-by":"publisher","first-page":"1501","DOI":"10.1007\/s12602-022-10001-1","volume":"15","author":"S Sharma","year":"2023","unstructured":"Sharma S, Raj K, Riyaz M, Singh DD (2023) Antimicrobial studies on garlic lectin. Probiotics Antimicrob Proteins 15(6):1501\u20131512. https:\/\/doi.org\/10.1007\/s12602-022-10001-1","journal-title":"Probiotics Antimicrob Proteins"},{"key":"10314_CR179","doi-asserted-by":"publisher","DOI":"10.1016\/j.biopha.2022.113735","volume":"155","author":"EHE Konozy","year":"2022","unstructured":"Konozy EHE, Osman MEM, Dirar AI, Ghartey-Kwansah G (2022) Plant lectins: a new antimicrobial frontier. Biomed Pharmacother 155:113735. https:\/\/doi.org\/10.1016\/j.biopha.2022.113735","journal-title":"Biomed Pharmacother"},{"issue":"2","key":"10314_CR180","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1007\/s12602-021-09837-w","volume":"15","author":"SP da Silva","year":"2023","unstructured":"da Silva SP, da Silva JDF, da Costa CBL, da Silva PM, de Freitas AFS, da Silva CES, da Silva AR, de Oliveira AM, S\u00e1 RA, Peixoto AR, de Oliveira APS, Paiva PMG, Napole\u00e3o TH (2023) Purification, characterization, and assessment of antimicrobial activity and toxicity of Portulaca elatior leaf lectin (PeLL). Probiotics Antimicrob Proteins 15(2):287\u2013299. https:\/\/doi.org\/10.1007\/s12602-021-09837-w","journal-title":"Probiotics Antimicrob Proteins"},{"issue":"3","key":"10314_CR181","doi-asserted-by":"publisher","first-page":"964","DOI":"10.1007\/s12602-023-10078-2","volume":"16","author":"S Li","year":"2024","unstructured":"Li S, Li N, Wang Y, Zhang X, Wang J, Zhang M, Chen H (2024) Structural characterization of the Staphylococcus aureus targeting lectin peptides from garlic (Allium sativum L) by liquid nitrogen grinding coupled with the proteomic and antimicrobial mechanism analysis. Probiotics Antimicrob Proteins 16(3):964\u2013978. https:\/\/doi.org\/10.1007\/s12602-023-10078-2","journal-title":"Probiotics Antimicrob Proteins"},{"issue":"3","key":"10314_CR182","doi-asserted-by":"publisher","first-page":"3791","DOI":"10.3390\/molecules20033791","volume":"20","author":"T Yau","year":"2015","unstructured":"Yau T, Dan X, Ng CC, Ng TB (2015) Lectins with potential for anti-cancer therapy. Molecules 20(3):3791\u20133810. https:\/\/doi.org\/10.3390\/molecules20033791","journal-title":"Molecules"},{"issue":"12","key":"10314_CR183","doi-asserted-by":"publisher","first-page":"12239","DOI":"10.1007\/s11033-022-07854-8","volume":"49","author":"S Naik","year":"2022","unstructured":"Naik S, Kumar S (2022) Lectins from plants and algae act as anti-viral against HIV, influenza and coronaviruses. Mol Biol Rep 49(12):12239\u201312246. https:\/\/doi.org\/10.1007\/s11033-022-07854-8","journal-title":"Mol Biol Rep"},{"issue":"10","key":"10314_CR184","doi-asserted-by":"publisher","DOI":"10.3390\/md21100515","volume":"21","author":"C Alvarez","year":"2023","unstructured":"Alvarez C, F\u00e9lix C, Lemos MFL (2023) The antiviral potential of algal lectins. Mar Drugs 21(10):515. https:\/\/doi.org\/10.3390\/md21100515","journal-title":"Mar Drugs"},{"issue":"1","key":"10314_CR185","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1186\/s11658-022-00338-4","volume":"27","author":"M Nabi-Afjadi","year":"2022","unstructured":"Nabi-Afjadi M, Heydari M, Zalpoor H, Arman I, Sadoughi A, Sahami P, Aghazadeh S (2022) Lectins and lectibodies: potential promising antiviral agents. Cell Mol Biol Lett 27(1):37. https:\/\/doi.org\/10.1186\/s11658-022-00338-4","journal-title":"Cell Mol Biol Lett"},{"issue":"8","key":"10314_CR186","doi-asserted-by":"publisher","first-page":"2085","DOI":"10.1111\/febs.15772","volume":"289","author":"O Fatoba","year":"2022","unstructured":"Fatoba O, Itokazu T, Yamashita T (2022) Complement cascade functions during brain development and neurodegeneration. FEBS J 289(8):2085\u20132109. https:\/\/doi.org\/10.1111\/febs.15772","journal-title":"FEBS J"},{"issue":"7","key":"10314_CR187","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2024.107467","volume":"300","author":"AC Goodrich","year":"2024","unstructured":"Goodrich AC, Le Clair NP, Shillova N, Morton WD, Wittwer AJ, Loyet KM, Hannoush RN (2024) Reconstitution of the alternative pathway of the complement system enables rapid delineation of the mechanism of action of novel inhibitors. J Biol Chem 300(7):107467. https:\/\/doi.org\/10.1016\/j.jbc.2024.107467","journal-title":"J Biol Chem"},{"key":"10314_CR188","doi-asserted-by":"publisher","first-page":"42532","DOI":"10.1038\/srep42532","volume":"7","author":"N Shahini","year":"2017","unstructured":"Shahini N, Michelsen AE, Nilsson PH, Ekholt K, Gullestad L, Broch K, Dahl CP, Aukrust P, Ueland T, Mollnes TE, Yndestad A, Louwe MC (2017) The alternative complement pathway is dysregulated in patients with chronic heart failure. Sci Rep 7:42532. https:\/\/doi.org\/10.1038\/srep42532","journal-title":"Sci Rep"},{"issue":"4","key":"10314_CR189","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1007\/s00232-025-00343-6","volume":"258","author":"BHT Ho","year":"2025","unstructured":"Ho BHT, Spicer BA, Dunstone MA (2025) Action of the terminal complement pathway on cell membranes. J Membr Biol 258(4):269\u2013304. https:\/\/doi.org\/10.1007\/s00232-025-00343-6","journal-title":"J Membr Biol"},{"key":"10314_CR190","unstructured":"www.uniprot.org\/uniprot\/A5YBU8"},{"issue":"40","key":"10314_CR191","doi-asserted-by":"publisher","first-page":"25996","DOI":"10.1074\/jbc.273.40.25996","volume":"273","author":"DE Hourcade","year":"1998","unstructured":"Hourcade DE, Mitchell LM, Oglesby TJ (1998) A conserved element in the serine protease domain of complement factor B. J Biol Chem 273(40):25996\u201326000. https:\/\/doi.org\/10.1074\/jbc.273.40.25996","journal-title":"J Biol Chem"},{"key":"10314_CR192","doi-asserted-by":"publisher","DOI":"10.1016\/j.intimp.2025.114427","volume":"152","author":"H Xu","year":"2025","unstructured":"Xu H, Yin L, Zou L, Zhang E, Cheng Y, Zhang W, Liu Y, Han J, Zhao Y (2025) Lysozyme modulates inflammatory responses to exacerbate the severity of rheumatoid arthritis. Int Immunopharmacol 152:114427. https:\/\/doi.org\/10.1016\/j.intimp.2025.114427","journal-title":"Int Immunopharmacol"},{"issue":"4","key":"10314_CR193","doi-asserted-by":"publisher","first-page":"469","DOI":"10.1111\/ped.14431","volume":"63","author":"R Muramatsu","year":"2021","unstructured":"Muramatsu R, Saga M, Muramatsu K (2021) First anaphylaxis case from a deodorant spray including lysozyme chloride. Pediatr Int 63(4):469\u2013470. https:\/\/doi.org\/10.1111\/ped.14431","journal-title":"Pediatr Int"},{"issue":"3","key":"10314_CR194","doi-asserted-by":"publisher","first-page":"209","DOI":"10.1016\/j.arcped.2023.12.005","volume":"31","author":"C Elbany","year":"2024","unstructured":"Elbany C, de Boissieu D, Karila C, Alyanakian MA, Ponvert C, Lageix F, Lezmi G (2024) A rare case of lysozyme-induced anaphylaxis in a child with egg allergy. Arch Pediatr 31(3):209\u2013211. https:\/\/doi.org\/10.1016\/j.arcped.2023.12.005","journal-title":"Arch Pediatr"},{"key":"10314_CR195","doi-asserted-by":"publisher","first-page":"143","DOI":"10.1016\/j.redox.2017.11.026","volume":"15","author":"N De Gregorio-Rocasolano","year":"2018","unstructured":"De Gregorio-Rocasolano N, Mart\u00ed-Sistac O, Ponce J, Castell\u00f3-Ruiz M, Mill\u00e1n M, Guirao V, Garc\u00eda-Y\u00e9benes I, Salom JB, Ramos-Cabrer P, Alborch E, Lizasoain I, Castillo J, D\u00e1valos A, Gasull T (2018) Iron-loaded transferrin (Tf) is detrimental whereas iron-free Tf confers protection against brain ischemia by modifying blood Tf saturation and subsequent neuronal damage. Redox Biol 15:143\u2013158. https:\/\/doi.org\/10.1016\/j.redox.2017.11.026","journal-title":"Redox Biol"},{"issue":"12","key":"10314_CR196","doi-asserted-by":"publisher","DOI":"10.3390\/ijms241210115","volume":"24","author":"P Mertowska","year":"2023","unstructured":"Mertowska P, Smolak K, Mertowski S, Grywalska E (2023) Immunomodulatory role of interferons in viral and bacterial infections. Int J Mol Sci 24(12):10115. https:\/\/doi.org\/10.3390\/ijms241210115","journal-title":"Int J Mol Sci"},{"issue":"8","key":"10314_CR197","doi-asserted-by":"publisher","DOI":"10.3390\/ijms24086887","volume":"24","author":"A Kamyshnyi","year":"2023","unstructured":"Kamyshnyi A, Koval H, Kobevko O, Buchynskyi M, Oksenych V, Kainov D, Lyubomirskaya K, Kamyshna I, Potters G, Moshynets O (2023) Therapeutic effectiveness of interferon-\u03b12b against COVID-19 with community-acquired pneumonia: the Ukrainian experience. Int J Mol Sci 24(8):6887. https:\/\/doi.org\/10.3390\/ijms24086887","journal-title":"Int J Mol Sci"},{"issue":"5","key":"10314_CR198","doi-asserted-by":"publisher","first-page":"684","DOI":"10.5152\/dir.2021.20503","volume":"27","author":"NR Shah","year":"2021","unstructured":"Shah NR, Declouette B, Ansari-Gilani K, Alhomoud MS, Hoimes C, Ramaiya NH, G\u00fcler E (2021) High-dose interleukin-2 therapy related adverse events and implications on imaging. Diagn Interv Radiol 27(5):684\u2013689. https:\/\/doi.org\/10.5152\/dir.2021.20503","journal-title":"Diagn Interv Radiol"},{"key":"10314_CR199","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2021.780610","volume":"12","author":"D Kaur","year":"2021","unstructured":"Kaur D, Patiyal S, Arora C, Singh R, Lodhi G, Raghava GPS (2021) In-Silico tool for predicting, scanning, and designing defensins. Front Immunol 12:780610. https:\/\/doi.org\/10.3389\/fimmu.2021.780610","journal-title":"Front Immunol"},{"issue":"6","key":"10314_CR200","doi-asserted-by":"publisher","first-page":"1095","DOI":"10.24272\/j.issn.2095-8137.2023.246","volume":"44","author":"J Mwangi","year":"2023","unstructured":"Mwangi J, Kamau PM, Thuku RC, Lai R (2023) Design methods for antimicrobial peptides with improved performance. Zool Res 44(6):1095\u20131114. https:\/\/doi.org\/10.24272\/j.issn.2095-8137.2023.246","journal-title":"Zool Res"},{"issue":"11","key":"10314_CR201","doi-asserted-by":"publisher","DOI":"10.3390\/jfb15110320","volume":"15","author":"DP Verma","year":"2024","unstructured":"Verma DP, Tripathi AK, Thakur AK (2024) Innovative strategies and methodologies in antimicrobial peptide design. J Funct Biomater 15(11):320. https:\/\/doi.org\/10.3390\/jfb15110320","journal-title":"J Funct Biomater"},{"issue":"1","key":"10314_CR202","doi-asserted-by":"publisher","DOI":"10.1515\/jib-2023-0053","volume":"22","author":"Z Mosalanejad","year":"2025","unstructured":"Mosalanejad Z, Faraji SN, Rahbar MR, Gholami A (2025) Designing an optimized theta-defensin peptide for HIV therapy using in-silico approaches. J Integr Bioinform 22(1):20230053. https:\/\/doi.org\/10.1515\/jib-2023-0053","journal-title":"J Integr Bioinform"},{"key":"10314_CR203","doi-asserted-by":"publisher","first-page":"93","DOI":"10.3389\/fimmu.2020.00093","volume":"11","author":"L Koeninger","year":"2020","unstructured":"Koeninger L, Armbruster NS, Brinch KS, Kjaerulf S, Andersen B, Langnau C, Autenrieth SE, Schneidawind D, Stange EF, Malek NP, Nordkild P, Jensen BAH, Wehkamp J (2020) Human \u03b2-defensin 2 mediated immune modulation as treatment for experimental colitis. Front Immunol 11:93. https:\/\/doi.org\/10.3389\/fimmu.2020.00093","journal-title":"Front Immunol"},{"key":"10314_CR204","doi-asserted-by":"publisher","DOI":"10.1016\/j.micpath.2021.104930","volume":"155","author":"SS Solanki","year":"2021","unstructured":"Solanki SS, Singh P, Kashyap P, Sansi MS, Ali SA (2021) Promising role of defensins peptides as therapeutics to combat against viral infection. Microb Pathog 155:104930. https:\/\/doi.org\/10.1016\/j.micpath.2021.104930","journal-title":"Microb Pathog"},{"issue":"1","key":"10314_CR205","doi-asserted-by":"publisher","first-page":"28","DOI":"10.1016\/j.immuni.2014.12.028","volume":"42","author":"S Mukherjee","year":"2015","unstructured":"Mukherjee S, Hooper LV (2015) Antimicrobial defense of the intestine. Immunity 42(1):28\u201339. https:\/\/doi.org\/10.1016\/j.immuni.2014.12.028","journal-title":"Immunity"},{"key":"10314_CR206","doi-asserted-by":"publisher","DOI":"10.1155\/2017\/8392523","volume":"2017","author":"L Coretti","year":"2017","unstructured":"Coretti L, Natale A, Cuomo M, Florio E, Keller S, Lembo F, Chiariotti L, Pero R (2017) The interplay between defensins and microbiota in Crohn\u2019s disease. Mediators Inflamm 2017:8392523. https:\/\/doi.org\/10.1155\/2017\/8392523","journal-title":"Mediators Inflamm"},{"key":"10314_CR207","doi-asserted-by":"publisher","first-page":"1137","DOI":"10.3389\/fimmu.2020.01137","volume":"11","author":"MR Scheenstra","year":"2020","unstructured":"Scheenstra MR, van Harten RM, Veldhuizen EJA, Haagsman HP, Coorens M (2020) Cathelicidins modulate TLR-activation and inflammation. Front Immunol 11:1137. https:\/\/doi.org\/10.3389\/fimmu.2020.01137","journal-title":"Front Immunol"},{"key":"10314_CR208","doi-asserted-by":"publisher","first-page":"387","DOI":"10.3389\/fcimb.2017.00387","volume":"7","author":"JF Sicard","year":"2017","unstructured":"Sicard JF, Le Bihan G, Vogeleer P, Jacques M, Harel J (2017) Interactions of intestinal bacteria with components of the intestinal mucus. Front Cell Infect Microbiol 7:387. https:\/\/doi.org\/10.3389\/fcimb.2017.00387","journal-title":"Front Cell Infect Microbiol"},{"key":"10314_CR209","doi-asserted-by":"publisher","DOI":"10.1016\/j.biopha.2023.115878","volume":"169","author":"YJ Ma","year":"2023","unstructured":"Ma YJ, Parente R, Zhong H, Sun Y, Garlanda C, Doni A (2023) Complement-pentraxins synergy: navigating the immune battlefield and beyond. Biomed Pharmacother 169:115878. https:\/\/doi.org\/10.1016\/j.biopha.2023.115878","journal-title":"Biomed Pharmacother"},{"issue":"3","key":"10314_CR210","doi-asserted-by":"publisher","DOI":"10.3390\/ijms25031566","volume":"25","author":"J Dob\u00f3","year":"2024","unstructured":"Dob\u00f3 J, Kocsis A, Farkas B, Demeter F, Cervenak L, G\u00e1l P (2024) The lectin pathway of the complement system-activation, regulation, disease connections and interplay with other (proteolytic) systems. Int J Mol Sci 25(3):1566. https:\/\/doi.org\/10.3390\/ijms25031566","journal-title":"Int J Mol Sci"},{"issue":"6","key":"10314_CR211","doi-asserted-by":"publisher","first-page":"1214","DOI":"10.1093\/jn\/132.6.1214","volume":"132","author":"BD Humphrey","year":"2002","unstructured":"Humphrey BD, Huang N, Klasing KC (2002) Rice expressing lactoferrin and lysozyme has antibiotic-like properties when fed to chicks. J Nutr 132(6):1214\u20131218. https:\/\/doi.org\/10.1093\/jn\/132.6.1214","journal-title":"J Nutr"},{"issue":"11","key":"10314_CR212","doi-asserted-by":"publisher","first-page":"1470","DOI":"10.3390\/antibiotics11111470","volume":"11","author":"X Xu","year":"2022","unstructured":"Xu X, Huang P, Cui X, Li X, Sun J, Ji Q, Wei Q, Huang Y, Li Z, Bao G, Liu Y (2022) Effects of dietary coated lysozyme on the growth performance, antioxidant activity, immunity and gut health of weaned piglets. Antibiotics (Basel) 11(11):1470. https:\/\/doi.org\/10.3390\/antibiotics11111470","journal-title":"Antibiotics (Basel)"},{"issue":"1","key":"10314_CR213","doi-asserted-by":"publisher","first-page":"284","DOI":"10.1016\/j.apsb.2022.03.024","volume":"13","author":"Y Wang","year":"2023","unstructured":"Wang Y, Lv Q, Chen Y, Xu L, Feng M, Xiong Z, Li J, Ren J, Liu J, Liu B (2023) Bilayer hydrogel dressing with lysozyme-enhanced photothermal therapy for biofilm eradication and accelerated chronic wound repair. Acta Pharm Sin B 13(1):284\u2013297. https:\/\/doi.org\/10.1016\/j.apsb.2022.03.024","journal-title":"Acta Pharm Sin B"},{"issue":"4","key":"10314_CR214","doi-asserted-by":"publisher","first-page":"401","DOI":"10.1002\/bjs.1800770415","volume":"77","author":"PG Horgan","year":"1990","unstructured":"Horgan PG, Mannick JA, Dubravec DB, Rodrick ML (1990) Effect of low dose recombinant interleukin 2 plus indomethacin on mortality after sepsis in a murine burn model. Br J Surg 77(4):401\u2013404. https:\/\/doi.org\/10.1002\/bjs.1800770415","journal-title":"Br J Surg"},{"issue":"4","key":"10314_CR215","doi-asserted-by":"publisher","first-page":"477","DOI":"10.1007\/s10517-013-2183-4","volume":"155","author":"LM Somova","year":"2013","unstructured":"Somova LM, Kondrashova NM, Plekhova NG, Drobot EI, Lyapun IN (2013) Pathomorphosis of experimental infection in mice, infected by Streptococcus pneumoniae, under the effect of immunotropic drugs. Bull Exp Biol Med 155(4):477\u2013483. https:\/\/doi.org\/10.1007\/s10517-013-2183-4","journal-title":"Bull Exp Biol Med"},{"issue":"8","key":"10314_CR216","doi-asserted-by":"publisher","first-page":"3642","DOI":"10.7150\/thno.53089","volume":"11","author":"G Luo","year":"2021","unstructured":"Luo G, Sun Y, Zhang J, Xu Z, Lu W, Wang H, Zhang Y, Li H, Mao Z, Ye S, Cheng B, Fang X (2021) Nanodefensin-encased hydrogel with dual bactericidal and pro-regenerative functions for advanced wound therapy. Theranostics 11(8):3642\u20133660. https:\/\/doi.org\/10.7150\/thno.53089","journal-title":"Theranostics"},{"issue":"4","key":"10314_CR217","doi-asserted-by":"publisher","first-page":"830","DOI":"10.1007\/s10266-023-00789-x","volume":"111","author":"Y Hiroshima","year":"2023","unstructured":"Hiroshima Y, Kido JI, Kido R, Yoshida K, Bando M, Kajimoto K, Yumoto H, Shinohara Y (2023) \u03b2-defensin 2 synthesized by a cell-free protein synthesis system and encapsulated in liposomes inhibits adhesion of Porphyromonas gingivalis to oral epithelial cells. Odontology 111(4):830\u2013838. https:\/\/doi.org\/10.1007\/s10266-023-00789-x","journal-title":"Odontology"},{"key":"10314_CR218","doi-asserted-by":"publisher","first-page":"58","DOI":"10.1016\/j.jconrel.2017.07.007","volume":"262","author":"M Comune","year":"2017","unstructured":"Comune M, Rai A, Chereddy KK, Pinto S, Aday S, Ferreira AF, Zonari A, Blersch J, Cunha R, Rodrigues R, Lerma J, Sim\u00f5es PN, Pr\u00e9at V, Ferreira L (2017) Antimicrobial peptide-gold nanoscale therapeutic formulation with high skin regenerative potential. J Control Release 262:58\u201371. https:\/\/doi.org\/10.1016\/j.jconrel.2017.07.007","journal-title":"J Control Release"},{"issue":"13","key":"10314_CR219","doi-asserted-by":"publisher","first-page":"1647","DOI":"10.2217\/nnm-2018-0337","volume":"14","author":"N Matougui","year":"2019","unstructured":"Matougui N, Groo AC, Umerska A, Cassisa V, Saulnier P (2019) A comparison of different strategies for antimicrobial peptides incorporation onto\/into lipid nanocapsules. Nanomedicine (Lond) 14(13):1647\u20131662. https:\/\/doi.org\/10.2217\/nnm-2018-0337","journal-title":"Nanomedicine (Lond)"},{"issue":"3","key":"10314_CR220","doi-asserted-by":"publisher","first-page":"260","DOI":"10.3390\/antibiotics14030260","volume":"14","author":"MD Kaleva","year":"2025","unstructured":"Kaleva MD, Kermedchiev M, Velkova L, Zaharieva MM, Dolashki A, Todorova M, Guncheva M, Dolashka P, Najdenski HM (2025) Synergistic antibacterial effect of mucus fraction from Cornu aspersum and Cirpofloxacin against pathogenic bacteria isolated from wounds of diabetic patients. Antibiotics (Basel) 14(3):260. https:\/\/doi.org\/10.3390\/antibiotics14030260","journal-title":"Antibiotics (Basel)"},{"issue":"1","key":"10314_CR221","doi-asserted-by":"publisher","first-page":"27071","DOI":"10.1038\/s41598-025-10496-y","volume":"15","author":"G Guagliano","year":"2025","unstructured":"Guagliano G, Peluso E, Butnarasu CS, Restivo E, Sardelli L, Frasca E, Petrini P, Tirelli N, Sganga S, Visai L, Visentin S (2025) Mucosomes as next-generation drug carriers for treating mucus-resident bacterial infections and biofilms. Sci Rep 15(1):27071. https:\/\/doi.org\/10.1038\/s41598-025-10496-y","journal-title":"Sci Rep"},{"issue":"11","key":"10314_CR222","doi-asserted-by":"publisher","DOI":"10.1002\/mbo3.869","volume":"8","author":"TF Proc\u00f3pio","year":"2019","unstructured":"Proc\u00f3pio TF, Moura MC, Bento EFL, Soares T, Coelho LCBB, Bezerra RP, Mota RA, Porto ALF, Paiva PMG, Napole\u00e3o TH (2019) Looking for alternative treatments for bovine and caprine mastitis: evaluation of the potential of Calliandra surinamensis leaf pinnulae lectin (CasuL), both alone and in combination with antibiotics. Microbiologyopen 8(11):e869. https:\/\/doi.org\/10.1002\/mbo3.869","journal-title":"Microbiologyopen"}],"container-title":["The Protein Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s10930-025-10314-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s10930-025-10314-4","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s10930-025-10314-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,3,3]],"date-time":"2026-03-03T14:01:00Z","timestamp":1772546460000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s10930-025-10314-4"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,1,19]]},"references-count":222,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,2]]}},"alternative-id":["10314"],"URL":"https:\/\/doi.org\/10.1007\/s10930-025-10314-4","relation":{},"ISSN":["1875-8355"],"issn-type":[{"value":"1875-8355","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,1,19]]},"assertion":[{"value":"28 July 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"14 December 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"19 January 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Not applicable.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethical Approval"}},{"value":"Not applicable.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent to Participate"}},{"value":"All authors reviewed the results and approved the final version of the manuscript.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for Publication"}},{"value":"The authors declare no competing interests.","order":5,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}}]}}