{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T14:47:32Z","timestamp":1791384452439,"version":"4.3.3"},"reference-count":111,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2026,3,9]],"date-time":"2026-03-09T00:00:00Z","timestamp":1773014400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Lysine lactylation represents a novel post-translational modification (PTM) involved in cellular functions including glycolysis and macrophage polarisation. It differs in form and mechanism from other PTMs such as acetylation, methylation, phosphorylation, ubiquitination, and SUMOylation. As a recently discovered modification, lactylation has been implicated in the progression of multiple diseases. Recent studies further indicate lactylation\u2019s association with multiple ocular pathologies. This review systematically summarises and discusses lactylation\u2019s involvement in prevalent eye diseases, including myopia, retinopathy, ocular melanoma, uveitis, and macular degeneration. We further collate emerging data suggesting lactylation signalling pathways may represent potential therapeutic targets for ocular pathologies. This review aims to provide a comprehensive overview for holistic intervention strategies and multidimensional assessment across various ocular conditions, while offering valuable insights for future research and development from a lactylation perspective.<\/jats:p>","DOI":"10.3390\/ijms27052516","type":"journal-article","created":{"date-parts":[[2026,3,9]],"date-time":"2026-03-09T15:49:42Z","timestamp":1773071382000},"page":"2516","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Focus on Lactate and Lactylation Modification: The Potential Role in Ophthalmic Disease Treatment"],"prefix":"10.3390","volume":"27","author":[{"given":"Mengyu","family":"Zong","sequence":"first","affiliation":[{"name":"Institute of Rehabilitation Medicine, Qilu Medical University, Zibo 255200, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yu","family":"Qiu","sequence":"additional","affiliation":[{"name":"Institute of Rehabilitation Medicine, Qilu Medical University, Zibo 255200, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7846-5989","authenticated-orcid":false,"given":"Changyong","family":"Li","sequence":"additional","affiliation":[{"name":"Institute of Rehabilitation Medicine, Qilu Medical University, Zibo 255200, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,3,9]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1038\/47412","article-title":"The language of covalent histone modifications","volume":"403","author":"Strahl","year":"2000","journal-title":"Nature"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1016","DOI":"10.1016\/j.cell.2011.08.008","article-title":"Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification","volume":"146","author":"Tan","year":"2011","journal-title":"Cell"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"458.e1","DOI":"10.1016\/j.cell.2014.09.037","article-title":"SnapShot: Histone modifications","volume":"159","author":"Huang","year":"2014","journal-title":"Cell"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1038\/nrm3890","article-title":"Histone core modifications regulating nucleosome structure and dynamics","volume":"15","author":"Tessarz","year":"2014","journal-title":"Nat. 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