{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T07:38:54Z","timestamp":1792654734523,"version":"4.5.0"},"reference-count":40,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T00:00:00Z","timestamp":1792540800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,10,21]],"date-time":"2026-10-21T00:00:00Z","timestamp":1792540800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Oral Diseases"],"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Objective<\/jats:title>\n                    <jats:p>Periodontitis drives persistent inflammation, alveolar bone loss, mitochondrial dysfunction and fibroblast programmed cell death. Receptor\u2010interacting protein kinase 3 (RIPK3) regulates inflammation and cell fate, while its role in modulating FUNDC1\u2010associated mitophagy and cell death in periodontitis remains poorly defined.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>Clinical gingival tissues, a ligature\u2010induced rat periodontitis model, and Pg.LPS\u2010stimulated human gingival fibroblasts were used. RIPK3 function was verified via pharmacological inhibition and siRNA\u2010mediated knockdown, combined with mitophagy intervention and detection of mitochondrial damage, apoptosis and necroptosis.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>RIPK3 and pTyr18\u2010FUNDC1 were upregulated while LC3\u2010II was downregulated in periodontitis tissues. RIPK3 inhibition restored defective mitophagic flux, alleviated mitochondrial dysfunction, apoptosis and MLKL\u2010mediated necroptosis. Mitophagy activation reversed LPS\u2010induced injuries, whereas autophagy inhibition abrogated RIPK3\u2010related protection. RIPK3 acts as an upstream regulator of FUNDC1 Tyr18 phosphorylation, without confirming direct catalytic activity or specific FUNDC1 dependency.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion<\/jats:title>\n                    <jats:p>RIPK3 elevation exacerbates periodontal damage via mitophagy impairment and dual activation of apoptosis and necroptosis. RIPK3 inhibition improves mitophagy, though its direct targeting of FUNDC1 requires further validation. RIPK3 serves as a promising therapeutic candidate for periodontitis.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/odi.70555","type":"journal-article","created":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T06:55:17Z","timestamp":1792652117000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["<scp>RIPK3<\/scp>\n                    Promotes Gingival Fibroblast Apoptosis and Periodontal Inflammatory Injury by Impairing Mitophagy"],"prefix":"10.1111","author":[{"ORCID":"https:\/\/orcid.org\/0009-0003-5673-058X","authenticated-orcid":false,"given":"Yuwen","family":"Huang","sequence":"first","affiliation":[{"name":"School of Stomatology Southwest Medical University  Luzhou China"},{"name":"Luzhou Key Laboratory of Oral &amp; Maxillofacial Reconstruction and Regeneration  Luzhou China"},{"name":"Department of Prosthodontics The Affiliated Stomatological Hospital of Southwest Medical University  Luzhou 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