{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,3]],"date-time":"2026-07-03T07:13:25Z","timestamp":1783062805400,"version":"3.54.6"},"reference-count":57,"publisher":"MDPI AG","issue":"14","license":[{"start":{"date-parts":[[2023,7,19]],"date-time":"2023-07-19T00:00:00Z","timestamp":1689724800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea (NRF)","doi-asserted-by":"publisher","award":["2021R1A2C3010505"],"award-info":[{"award-number":["2021R1A2C3010505"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea (NRF)","doi-asserted-by":"publisher","award":["322017\u20133"],"award-info":[{"award-number":["322017\u20133"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Ministry of Agriculture, Food and Rural Affairs (MAFRA)","award":["2021R1A2C3010505"],"award-info":[{"award-number":["2021R1A2C3010505"]}]},{"name":"Ministry of Agriculture, Food and Rural Affairs (MAFRA)","award":["322017\u20133"],"award-info":[{"award-number":["322017\u20133"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Antimicrobial peptides (AMPs) are promising alternatives to existing treatments for multidrug-resistant bacteria-infected wounds. Therefore, the effect of protegrin-1 (PG1), a potent porcine AMP with broad-spectrum activity, on wound healing was evaluated. PG1-overexpressing transgenic mice were used as an in vivo model to evaluate its healing efficiency against Staphylococcus aureus-infected (106 colony forming units) wounds. We analyzed the wounds under four specific conditions in the presence or absence of antibiotic treatment. We observed the resolution of bacterial infection and formation of neo-epithelium in S. aureus-infected wounds of the mice, even without antibiotic treatment, whereas all wild-type mice with bacterial infection died within 8 to 10 days due to uncontrolled bacterial proliferation. Interestingly, the wound area on day 7 was smaller (p &lt; 0.01) in PG1 transgenic mice than that in the other groups, including antibiotic-treated mice, suggesting that PG1 exerts biological effects other than bactericidal effect. Additionally, we observed that the treatment of primary epidermal keratinocytes with recombinant PG1 enhanced cell migration in in vitro scratch and cell migration assays. This study contributes to the understanding of broad-spectrum endogenous cathelicidins with potent antimicrobial activities, such as PG1, on wound healing. Furthermore, our findings suggest that PG1 is a potent therapeutic candidate for wound healing.<\/jats:p>","DOI":"10.3390\/ijms241411658","type":"journal-article","created":{"date-parts":[[2023,7,19]],"date-time":"2023-07-19T21:20:14Z","timestamp":1689801614000},"page":"11658","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Effective Healing of Staphylococcus aureus-Infected Wounds in Pig Cathelicidin Protegrin-1-Overexpressing Transgenic Mice"],"prefix":"10.3390","volume":"24","author":[{"given":"Nagasundarapandian","family":"Soundrarajan","sequence":"first","affiliation":[{"name":"Department of Stem Cells and Regenerative Biology, Konkuk University, Hwayang-dong, Seoul 05029, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4910-4623","authenticated-orcid":false,"given":"Prathap","family":"Somasundaram","sequence":"additional","affiliation":[{"name":"Department of Stem Cells and Regenerative Biology, Konkuk University, Hwayang-dong, Seoul 05029, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dohun","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of Stem Cells and Regenerative Biology, Konkuk University, Hwayang-dong, Seoul 05029, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hye-Sun","family":"Cho","sequence":"additional","affiliation":[{"name":"Department of Stem Cells and Regenerative Biology, Konkuk University, Hwayang-dong, Seoul 05029, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hyoim","family":"Jeon","sequence":"additional","affiliation":[{"name":"Department of Stem Cells and Regenerative Biology, Konkuk University, Hwayang-dong, Seoul 05029, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Byeonyong","family":"Ahn","sequence":"additional","affiliation":[{"name":"Department of Stem Cells and Regenerative Biology, Konkuk University, Hwayang-dong, Seoul 05029, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mingue","family":"Kang","sequence":"additional","affiliation":[{"name":"Department of Stem Cells and Regenerative Biology, Konkuk University, Hwayang-dong, Seoul 05029, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9258-8304","authenticated-orcid":false,"given":"Hyuk","family":"Song","sequence":"additional","affiliation":[{"name":"Department of Stem Cells and Regenerative Biology, Konkuk University, Hwayang-dong, Seoul 05029, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4855-2210","authenticated-orcid":false,"given":"Chankyu","family":"Park","sequence":"additional","affiliation":[{"name":"Department of Stem Cells and Regenerative Biology, Konkuk University, Hwayang-dong, Seoul 05029, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,7,19]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Nguyen, A.V., and Soulika, A.M. (2019). The Dynamics of the Skin\u2019s Immune System. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20081811"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1494","DOI":"10.1007\/s10439-014-1010-z","article-title":"Tissue engineering and regenerative repair in wound healing","volume":"42","author":"Hu","year":"2014","journal-title":"Ann. Biomed. Eng."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1089\/wound.2017.0761","article-title":"Immune Regulation of Skin Wound Healing: Mechanisms and Novel Therapeutic Targets","volume":"7","author":"Larouche","year":"2018","journal-title":"Adv. Wound Care"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1186\/s13756-019-0533-3","article-title":"Antibiotics versus biofilm: An emerging battleground in microbial communities","volume":"8","author":"Sharma","year":"2019","journal-title":"Antimicrob. Resist. Infect. Control"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.jbiotec.2014.09.003","article-title":"Antibiotic resistance in Pseudomonas aeruginosa biofilms: Towards the development of novel anti-biofilm therapies","volume":"191","author":"Taylor","year":"2014","journal-title":"J. Biotechnol."},{"key":"ref_6","first-page":"352","article-title":"Wound biofilms: Lessons learned from oral biofilms","volume":"21","author":"Mancl","year":"2013","journal-title":"Wound Repair Regen. Off. Publ. Wound Health Soc. Eur. Tissue Repair Soc."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1038\/sj.clpt.6100247","article-title":"The challenge of treating biofilm-associated bacterial infections","volume":"82","author":"Patel","year":"2007","journal-title":"Clin. Pharmacol. Ther."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"35S","DOI":"10.1016\/j.amjsurg.2003.10.006","article-title":"Skin and soft-tissue infections: Impact of resistant gram-positive bacteria","volume":"186","author":"Wilson","year":"2003","journal-title":"Am. J. Surg."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1186\/s13049-019-0596-4","article-title":"Sepsis: Mechanisms of bacterial injury to the patient","volume":"27","author":"Minasyan","year":"2019","journal-title":"Scand. J. Trauma Resusc. Emerg. Med."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1186\/1476-9255-9-7","article-title":"Induction of intestinal pro-inflammatory immune responses by lipoteichoic acid","volume":"9","author":"Zadeh","year":"2012","journal-title":"J. Inflamm."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1189\/jlb.0403147","article-title":"Cathelicidins, multifunctional peptides of the innate immunity","volume":"75","author":"Zanetti","year":"2004","journal-title":"J. Leukoc. Biol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/S0196-9781(03)00114-1","article-title":"Antimicrobial peptides in the first line defence of human colon mucosa","volume":"24","author":"Tollin","year":"2003","journal-title":"Peptides"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1007\/s00726-021-02948-2","article-title":"Cathelicidin \u0394Pb-CATH4 derived from Python bivittatus accelerates the healing of Staphylococcus aureus-infected wounds in mice","volume":"53","author":"Nagasundarapandian","year":"2021","journal-title":"Amino Acids"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"2206","DOI":"10.1128\/AAC.42.9.2206","article-title":"Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils","volume":"42","author":"Turner","year":"1998","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"331","DOI":"10.3389\/fcimb.2018.00331","article-title":"Protegrin 1 Enhances Innate Cellular Defense via the Insulin-Like Growth Factor 1 Receptor Pathway","volume":"8","author":"Penney","year":"2018","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"347","DOI":"10.3389\/fimmu.2020.00347","article-title":"Opossum Cathelicidins Exhibit Antimicrobial Activity Against a Broad Spectrum of Pathogens Including West Nile Virus","volume":"11","author":"Cho","year":"2020","journal-title":"Front. Immunol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1159\/000495320","article-title":"The Designer Antimicrobial Peptide A-hBD-2 Facilitates Skin Wound Healing by Stimulating Keratinocyte Migration and Proliferation","volume":"51","author":"Mi","year":"2018","journal-title":"Cell. Physiol. Biochem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1665","DOI":"10.1172\/JCI17545","article-title":"An angiogenic role for the human peptide antibiotic LL-37\/hCAP-18","volume":"111","author":"Koczulla","year":"2003","journal-title":"J. Clin. Investig."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1046\/j.1523-1747.2003.12069.x","article-title":"The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium","volume":"120","author":"Heilborn","year":"2003","journal-title":"J. Investig. Dermatol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"23","DOI":"10.2174\/1389203053027520","article-title":"The cathelicidins--structure, function and evolution","volume":"6","author":"Tomasinsig","year":"2005","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1007\/0-306-46831-X_17","article-title":"Structure and biology of cathelicidins","volume":"479","author":"Zanetti","year":"2000","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1097\/00062752-200201000-00004","article-title":"Cathelicidins: A family of endogenous antimicrobial peptides","volume":"9","author":"Lehrer","year":"2002","journal-title":"Curr. Opin. Hematol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"143","DOI":"10.3389\/fimmu.2013.00143","article-title":"The Human Cathelicidin Antimicrobial Peptide LL-37 as a Potential Treatment for Polymicrobial Infected Wounds","volume":"4","author":"Duplantier","year":"2013","journal-title":"Front. Immunol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"5420","DOI":"10.1111\/febs.13072","article-title":"Defining the genetic relationship of protegrin-related sequences and the in vivo expression of protegrins","volume":"281","author":"Choi","year":"2014","journal-title":"FEBS J."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"10957","DOI":"10.1007\/s11033-012-1997-x","article-title":"Cathelicidins: Family of antimicrobial peptides. A review","volume":"39","author":"Lisowski","year":"2012","journal-title":"Mol. Biol. Rep."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1046\/j.1523-1747.2001.01340.x","article-title":"Cutaneous injury induces the release of cathelicidin anti-microbial peptides active against group A Streptococcus","volume":"117","author":"Dorschner","year":"2001","journal-title":"J. Investig. Dermatol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1016\/j.peptides.2011.06.005","article-title":"Wound healing activity of the human antimicrobial peptide LL37","volume":"32","author":"Ramos","year":"2011","journal-title":"Peptides"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1038\/s41598-018-19486-9","article-title":"Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing","volume":"8","author":"Cao","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1038\/nm1407","article-title":"The antimicrobial peptide cathelicidin protects the urinary tract against invasive bacterial infection","volume":"12","author":"Chromek","year":"2006","journal-title":"Nat. Med."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"105552","DOI":"10.1016\/j.jsbmb.2019.105552","article-title":"A mouse model for vitamin D-induced human cathelicidin antimicrobial peptide gene expression","volume":"198","author":"Lowry","year":"2020","journal-title":"J. Steroid Biochem. Mol. Biol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"3750","DOI":"10.1073\/pnas.0500268102","article-title":"Expression of an additional cathelicidin antimicrobial peptide protects against bacterial skin infection","volume":"102","author":"Lee","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.peptides.2012.04.005","article-title":"Subacute toxicity of antimicrobial peptide S-thanatin in ICR mice","volume":"36","author":"Wu","year":"2012","journal-title":"Peptides"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.bsheal.2022.02.003","article-title":"Biosynthesis, bioactivity, biotoxicity and applications of antimicrobial peptides for human health","volume":"4","author":"Wei","year":"2022","journal-title":"Biosaf. Health"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"11569","DOI":"10.1038\/s41598-019-47955-2","article-title":"Protegrin-1 cytotoxicity towards mammalian cells positively correlates with the magnitude of conformational changes of the unfolded form upon cell interaction","volume":"9","author":"Soundrarajan","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/0014-5793(94)00493-5","article-title":"Identification of a new member of the protegrin family by cDNA cloning","volume":"346","author":"Zhao","year":"1994","journal-title":"FEBS Lett."},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Maystrenko, A., Feng, Y., Akhtar, N., and Li, J. (2020). The Addition of a Synthetic LPS-Targeting Domain Improves Serum Stability While Maintaining Antimicrobial, Antibiofilm, and Cell Stimulating Properties of an Antimicrobial Peptide. Biomolecules, 10.","DOI":"10.3390\/biom10071014"},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Choi, M.K., Le, M.T., Cho, H.S., Lee, J., Jeon, H., Cha, S.Y., Na, M., Chun, T., Kim, J.H., and Song, H. (2021). Transgenic Mice Overexpressing PG1 Display Corneal Opacity and Severe Inflammation in the Eye. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22041586"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1812","DOI":"10.1128\/AAC.01530-07","article-title":"Enhanced Resistance to Bacterial Infection in Protegrin-1 Transgenic Mice","volume":"52","author":"Cheung","year":"2008","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"20661","DOI":"10.1038\/srep20661","article-title":"Green fluorescent protein as a scaffold for high efficiency production of functional bacteriotoxic proteins in Escherichia coli","volume":"6","author":"Soundrarajan","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1089\/wound.2014.0540","article-title":"The Roles of Growth Factors in Keratinocyte Migration","volume":"4","author":"Seeger","year":"2015","journal-title":"Adv. Wound Care"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1038\/sj.jid.5700599","article-title":"Antimicrobial peptides human beta-defensins stimulate epidermal keratinocyte migration, proliferation and production of proinflammatory cytokines and chemokines","volume":"127","author":"Niyonsaba","year":"2007","journal-title":"J. Investig. Dermatol."},{"key":"ref_42","first-page":"585","article-title":"Growth factors and cytokines in wound healing","volume":"16","author":"Barrientos","year":"2008","journal-title":"Wound Repair Regen. Off. Publ. Wound Health Soc. Eur. Tissue Repair Soc."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1152\/physrev.2003.83.3.835","article-title":"Regulation of wound healing by growth factors and cytokines","volume":"83","author":"Werner","year":"2003","journal-title":"Physiol. Rev."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1083\/jcb.137.2.481","article-title":"Regulation of cell motility by mitogen-activated protein kinase","volume":"137","author":"Klemke","year":"1997","journal-title":"J. Cell Biol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"14398","DOI":"10.1038\/s41598-018-32851-y","article-title":"ERK activating peptide, AES16-2M promotes wound healing through accelerating migration of keratinocytes","volume":"8","author":"Lee","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1080\/19420862.2016.1160989","article-title":"XGFR*, a novel affinity-matured bispecific antibody targeting IGF-1R and EGFR with combined signaling inhibition and enhanced immune activation for the treatment of pancreatic cancer","volume":"8","author":"Schanzer","year":"2016","journal-title":"MAbs"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1124\/pr.109.002469","article-title":"Insulin-like growth factor-I regulation of immune function: A potential therapeutic target in autoimmune diseases?","volume":"62","author":"Smith","year":"2010","journal-title":"Pharmacol. Rev."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"2333","DOI":"10.1007\/s00726-014-1804-1","article-title":"Efficacy of the designer antimicrobial peptide SHAP1 in wound healing and wound infection","volume":"46","author":"Kim","year":"2014","journal-title":"Amino Acids"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1111\/exd.12929","article-title":"Antimicrobial peptides and wound healing: Biological and therapeutic considerations","volume":"25","author":"Mangoni","year":"2016","journal-title":"Exp. Derm."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1128\/AAC.00530-17","article-title":"Genomewide Analysis of the Antimicrobial Peptides in Python bivittatus and Characterization of Cathelicidins with Potent Antimicrobial Activity and Low Cytotoxicity","volume":"61","author":"Kim","year":"2017","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1007\/s10156-010-0094-0","article-title":"Antibacterial effects of brand-name teicoplanin and generic products against clinical isolates of methicillin-resistant Staphylococcus aureus","volume":"17","author":"Fujimura","year":"2011","journal-title":"J. Infect. Chemother."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1738","DOI":"10.1128\/AAC.41.8.1738","article-title":"Protegrin-1: A broad-spectrum, rapidly microbicidal peptide with in vivo activity","volume":"41","author":"Steinberg","year":"1997","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1038\/nmeth.2089","article-title":"NIH Image to ImageJ: 25 years of image analysis","volume":"9","author":"Schneider","year":"2012","journal-title":"Nat. Methods"},{"key":"ref_54","first-page":"56027","article-title":"Isolation and Culture of Primary Mouse Keratinocytes from Neonatal and Adult Mouse Skin","volume":"125","author":"Li","year":"2017","journal-title":"J. Vis. Exp. JoVE"},{"key":"ref_55","unstructured":"(2018). Performance Standards for Antimicrobial Susceptibility Testing, 28th ed (Standard No. CLSI Supplement M100-S28)."},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Choi, M., Cho, H.S., Ahn, B., Prathap, S., Nagasundarapandian, S., and Park, C. (2022). Genomewide Analysis and Biological Characterization of Cathelicidins with Potent Antimicrobial Activity and Low Cytotoxicity from Three Bat Species. Antibiotics, 11.","DOI":"10.3390\/antibiotics11080989"},{"key":"ref_57","first-page":"71","article-title":"An improvement of the 2\u02c6(-delta delta CT) method for quantitative real-time polymerase chain reaction data analysis","volume":"3","author":"Rao","year":"2013","journal-title":"Biostat. Bioinform. Biomath."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/14\/11658\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T20:15:04Z","timestamp":1760127304000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/24\/14\/11658"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,7,19]]},"references-count":57,"journal-issue":{"issue":"14","published-online":{"date-parts":[[2023,7]]}},"alternative-id":["ijms241411658"],"URL":"https:\/\/doi.org\/10.3390\/ijms241411658","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,7,19]]}}}