{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T14:47:27Z","timestamp":1791384447478,"version":"4.3.3"},"reference-count":99,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2025,12,29]],"date-time":"2025-12-29T00:00:00Z","timestamp":1766966400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2025,12,29]],"date-time":"2025-12-29T00:00:00Z","timestamp":1766966400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/501100001809","name":"the National Natural Science Foundation of China","doi-asserted-by":"crossref","award":["82571575"],"award-info":[{"award-number":["82571575"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"name":"the Natural Science Foundation of Shandong Province","award":["ZR2024YQ074"],"award-info":[{"award-number":["ZR2024YQ074"]}]},{"name":"Joint TCM Science & Technology Projects of National Demonstration Zones for Comprehensive TCM Reform","award":["GZY-KJS-SD-2024-021"],"award-info":[{"award-number":["GZY-KJS-SD-2024-021"]}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Neurochem Res"],"published-print":{"date-parts":[[2026,2]]},"DOI":"10.1007\/s11064-025-04631-4","type":"journal-article","created":{"date-parts":[[2025,12,29]],"date-time":"2025-12-29T05:42:09Z","timestamp":1766986929000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Regulatory Landscapes of Protein Acylations in Neuroinflammation: From Molecular Mechanisms to Therapeutic Targets"],"prefix":"10.1007","volume":"51","author":[{"given":"Jinxuan","family":"Han","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jingjing","family":"Han","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shuangshuang","family":"Duan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chunlei","family":"Xin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pei","family":"Jiang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,12,29]]},"reference":[{"key":"4631_CR1","doi-asserted-by":"publisher","DOI":"10.1016\/j.arr.2021.101336","volume":"68","author":"R Gupta","year":"2021","unstructured":"Gupta R, Sahu M, Srivastava D et al (2021) Post-translational modifications: regulators of neurodegenerative proteinopathies. Ageing Res Rev 68:101336. https:\/\/doi.org\/10.1016\/j.arr.2021.101336","journal-title":"Ageing Res Rev"},{"key":"4631_CR2","doi-asserted-by":"publisher","first-page":"244","DOI":"10.1016\/j.gpb.2018.06.004","volume":"16","author":"H Xu","year":"2018","unstructured":"Xu H, Wang Y, Lin S et al (2018) PTMD: a database of human disease-associated post-translational modifications. Genomic Proteom Bioinform 16:244\u2013251. https:\/\/doi.org\/10.1016\/j.gpb.2018.06.004","journal-title":"Genomic Proteom Bioinform"},{"key":"4631_CR3","doi-asserted-by":"publisher","first-page":"1016","DOI":"10.1016\/j.cell.2011.08.008","volume":"146","author":"M Tan","year":"2011","unstructured":"Tan M, Luo H, Lee S et al (2011) Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell 146:1016\u20131028. https:\/\/doi.org\/10.1016\/j.cell.2011.08.008","journal-title":"Cell"},{"key":"4631_CR4","doi-asserted-by":"publisher","DOI":"10.3389\/fnut.2023.1171806","volume":"10","author":"D Xie","year":"2023","unstructured":"Xie D, Zhang Y, Guo Y et al (2023) The impact of high-glucose or high-fat diets on the metabolomic profiling of mice. Front Nutr 10:1171806. https:\/\/doi.org\/10.3389\/fnut.2023.1171806","journal-title":"Front Nutr"},{"key":"4631_CR5","doi-asserted-by":"publisher","first-page":"361","DOI":"10.1016\/j.cmet.2024.10.015","volume":"37","author":"R Zhu","year":"2025","unstructured":"Zhu R, Ye X, Lu X et al (2025) ACSS2 acts as a lactyl-CoA synthetase and couples KAT2A to function as a lactyltransferase for histone lactylation and tumor immune evasion. Cell Metab 37:361-376.e7. https:\/\/doi.org\/10.1016\/j.cmet.2024.10.015","journal-title":"Cell Metab"},{"key":"4631_CR6","doi-asserted-by":"publisher","first-page":"575","DOI":"10.1038\/s41586-019-1678-1","volume":"574","author":"D Zhang","year":"2019","unstructured":"Zhang D, Tang Z, Huang H et al (2019) Metabolic regulation of gene expression by histone lactylation. Nature 574:575\u2013580. https:\/\/doi.org\/10.1038\/s41586-019-1678-1","journal-title":"Nature"},{"key":"4631_CR7","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.abi6696","volume":"8","author":"C Moreno-Yruela","year":"2022","unstructured":"Moreno-Yruela C, Zhang D, Wei W et al (2022) Class I histone deacetylases (HDAC1-3) are histone lysine delactylases. Sci Adv 8:eabi6696. https:\/\/doi.org\/10.1126\/sciadv.abi6696","journal-title":"Sci Adv"},{"key":"4631_CR8","doi-asserted-by":"publisher","first-page":"273","DOI":"10.1038\/nature25003","volume":"552","author":"Y Wang","year":"2017","unstructured":"Wang Y, Guo YR, Liu K et al (2017) KAT2A coupled with the \u03b1-KGDH complex acts as a histone H3 succinyltransferase. Nature 552:273\u2013277. https:\/\/doi.org\/10.1038\/nature25003","journal-title":"Nature"},{"key":"4631_CR9","doi-asserted-by":"publisher","first-page":"105","DOI":"10.1038\/s41467-017-02651-5","volume":"9","author":"R Fellows","year":"2018","unstructured":"Fellows R, Denizot J, Stellato C et al (2018) Microbiota derived short chain fatty acids promote histone crotonylation in the colon through histone deacetylases. Nat Commun 9:105. https:\/\/doi.org\/10.1038\/s41467-017-02651-5","journal-title":"Nat Commun"},{"key":"4631_CR10","doi-asserted-by":"publisher","first-page":"138","DOI":"10.1158\/2159-8290.CD-RW2017-234","volume":"8","author":"Y Wang","year":"2018","unstructured":"Wang Y, Guo YR, Liu K et al (2018) KAT2A is a \u03b1-KGDH-dependent histone succinyltransferase. Cancer Discov 8:138. https:\/\/doi.org\/10.1158\/2159-8290.CD-RW2017-234","journal-title":"Cancer Discov"},{"key":"4631_CR11","doi-asserted-by":"publisher","first-page":"296","DOI":"10.1186\/s12974-024-03284-4","volume":"21","author":"X Zhao","year":"2024","unstructured":"Zhao X, Yang X, Du C et al (2024) Up-regulated succinylation modifications induce a senescence phenotype in microglia by altering mitochondrial energy metabolism. J Neuroinflammation 21:296. https:\/\/doi.org\/10.1186\/s12974-024-03284-4","journal-title":"J Neuroinflammation"},{"key":"4631_CR12","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.abe2771","volume":"7","author":"H Huang","year":"2021","unstructured":"Huang H, Zhang D, Weng Y et al (2021) The regulatory enzymes and protein substrates for the lysine \u03b2-hydroxybutyrylation pathway. Sci Adv 7:eabe2771. https:\/\/doi.org\/10.1126\/sciadv.abe2771","journal-title":"Sci Adv"},{"key":"4631_CR13","doi-asserted-by":"publisher","first-page":"694","DOI":"10.1038\/s41422-019-0211-2","volume":"29","author":"SM Abmayr","year":"2019","unstructured":"Abmayr SM, Workman JL (2019) Histone lysine de-\u03b2-hydroxybutyrylation by SIRT3. Cell Res 29:694\u2013695. https:\/\/doi.org\/10.1038\/s41422-019-0211-2","journal-title":"Cell Res"},{"key":"4631_CR14","doi-asserted-by":"publisher","first-page":"1342830","DOI":"10.3389\/fphar.2023.1342830","volume":"14","author":"D Liao","year":"2024","unstructured":"Liao D, Huang Y, Liu D et al (2024) The role of s-palmitoylation in neurological diseases: implication for zDHHC family. Front Pharmacol 14:1342830. https:\/\/doi.org\/10.3389\/fphar.2023.1342830","journal-title":"Front Pharmacol"},{"key":"4631_CR15","doi-asserted-by":"publisher","first-page":"3029","DOI":"10.1021\/acs.accounts.9b00354","volume":"52","author":"S-A Azizi","year":"2019","unstructured":"Azizi S-A, Kathayat RS, Dickinson BC (2019) Activity-based sensing of S-depalmitoylases: chemical technologies and biological discovery. Acc Chem Res 52:3029\u20133038. https:\/\/doi.org\/10.1021\/acs.accounts.9b00354","journal-title":"Acc Chem Res"},{"key":"4631_CR16","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2022261118","volume":"118","author":"W Yuan","year":"2021","unstructured":"Yuan W, Lu L, Rao M et al (2021) GFAP hyperpalmitoylation exacerbates astrogliosis and neurodegenerative pathology in PPT1-deficient mice. Proc Natl Acad Sci USA 118:e2022261118. https:\/\/doi.org\/10.1073\/pnas.2022261118","journal-title":"Proc Natl Acad Sci USA"},{"key":"4631_CR17","doi-asserted-by":"publisher","first-page":"1018","DOI":"10.3390\/ijms17071018","volume":"17","author":"AIM Salah Ud-Din","year":"2016","unstructured":"Salah Ud-Din AIM, Tikhomirova A, Roujeinikova A (2016) Structure and functional diversity of GCN5-related N-acetyltransferases (GNAT). Int J Mol Sci 17:1018. https:\/\/doi.org\/10.3390\/ijms17071018","journal-title":"Int J Mol Sci"},{"key":"4631_CR18","doi-asserted-by":"publisher","first-page":"132","DOI":"10.14336\/AD.2020.0329","volume":"12","author":"Y Li","year":"2021","unstructured":"Li Y, Huang H, Zhu M et al (2021) Roles of the MYST family in the pathogenesis of alzheimer\u2019s disease via histone or non-histone acetylation. Aging Dis 12:132\u2013142. https:\/\/doi.org\/10.14336\/AD.2020.0329","journal-title":"Aging Dis"},{"key":"4631_CR19","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.conb.2019.01.023","volume":"59","author":"M Lipinski","year":"2019","unstructured":"Lipinski M, del Blanco B, Barco A (2019) CBP\/p300 in brain development and plasticity: disentangling the KAT\u2019s cradle. Curr Opin Neurobiol 59:1\u20138. https:\/\/doi.org\/10.1016\/j.conb.2019.01.023","journal-title":"Curr Opin Neurobiol"},{"key":"4631_CR20","doi-asserted-by":"publisher","first-page":"377","DOI":"10.1016\/j.cmet.2024.11.005","volume":"37","author":"R Liu","year":"2025","unstructured":"Liu R, Ren X, Park YE et al (2025) Nuclear GTPSCS functions as a lactyl-CoA synthetase to promote histone lactylation and gliomagenesis. Cell Metab 37:377-394.e9. https:\/\/doi.org\/10.1016\/j.cmet.2024.11.005","journal-title":"Cell Metab"},{"key":"4631_CR21","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a018713","volume":"6","author":"E Seto","year":"2014","unstructured":"Seto E, Yoshida M (2014) Erasers of histone acetylation: the histone deacetylase enzymes. Cold Spring Harb Perspect Biol 6:a018713. https:\/\/doi.org\/10.1101\/cshperspect.a018713","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"4631_CR22","doi-asserted-by":"publisher","DOI":"10.1016\/j.biopha.2019.109166","volume":"117","author":"W-B Zhang","year":"2019","unstructured":"Zhang W-B, Yang F, Wang Y et al (2019) Inhibition of HDAC6 attenuates LPS-induced inflammation in macrophages by regulating oxidative stress and suppressing the TLR4-MAPK\/NF-\u03baB pathways. Biomed Pharmacother 117:109166. https:\/\/doi.org\/10.1016\/j.biopha.2019.109166","journal-title":"Biomed Pharmacother"},{"key":"4631_CR23","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1146\/annurev.pathol.4.110807.092250","volume":"5","author":"MC Haigis","year":"2010","unstructured":"Haigis MC, Sinclair DA (2010) Mammalian sirtuins: biological insights and disease relevance. Annu Rev Pathol 5:253\u2013295. https:\/\/doi.org\/10.1146\/annurev.pathol.4.110807.092250","journal-title":"Annu Rev Pathol"},{"key":"4631_CR24","doi-asserted-by":"publisher","first-page":"1801","DOI":"10.1016\/j.str.2015.08.004","volume":"23","author":"EM Flynn","year":"2015","unstructured":"Flynn EM, Huang OW, Poy F et al (2015) A subset of human bromodomains recognizes butyryllysine and crotonyllysine histone peptide modifications. Structure 23:1801\u20131814. https:\/\/doi.org\/10.1016\/j.str.2015.08.004","journal-title":"Structure"},{"key":"4631_CR25","doi-asserted-by":"publisher","first-page":"629","DOI":"10.1038\/cr.2016.49","volume":"26","author":"D Zhao","year":"2016","unstructured":"Zhao D, Guan H, Zhao S et al (2016) YEATS2 is a selective histone crotonylation reader. Cell Res 26:629\u2013632. https:\/\/doi.org\/10.1038\/cr.2016.49","journal-title":"Cell Res"},{"key":"4631_CR26","doi-asserted-by":"publisher","first-page":"558","DOI":"10.1016\/j.cell.2014.09.049","volume":"159","author":"Y Li","year":"2014","unstructured":"Li Y, Wen H, Xi Y et al (2014) AF9 YEATS domain links histone acetylation to DOT1L-mediated H3K79 methylation. Cell 159:558\u2013571. https:\/\/doi.org\/10.1016\/j.cell.2014.09.049","journal-title":"Cell"},{"key":"4631_CR27","doi-asserted-by":"publisher","first-page":"2371","DOI":"10.3390\/biomedicines12102371","volume":"12","author":"L He","year":"2024","unstructured":"He L, Yin R, Hang W et al (2024) Oxygen glucose deprivation-induced lactylation of H3K9 contributes to M1 polarization and inflammation of microglia through TNF pathway. Biomedicines 12:2371. https:\/\/doi.org\/10.3390\/biomedicines12102371","journal-title":"Biomedicines"},{"key":"4631_CR28","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1038\/s41589-024-01680-8","volume":"21","author":"D Zhang","year":"2025","unstructured":"Zhang D, Gao J, Zhu Z et al (2025) Lysine L-lactylation is the dominant lactylation isomer induced by Glycolysis. Nat Chem Biol 21:91\u201399. https:\/\/doi.org\/10.1038\/s41589-024-01680-8","journal-title":"Nat Chem Biol"},{"key":"4631_CR29","doi-asserted-by":"publisher","first-page":"945485","DOI":"10.3389\/fimmu.2022.945485","volume":"13","author":"S Li","year":"2022","unstructured":"Li S, Wernersbach I, Harms GS, Sch\u00e4fer MKE (2022) Microglia subtypes show substrate- and time-dependent phagocytosis preferences and phenotype plasticity. Front Immunol 13:945485. https:\/\/doi.org\/10.3389\/fimmu.2022.945485","journal-title":"Front Immunol"},{"key":"4631_CR30","doi-asserted-by":"publisher","first-page":"151","DOI":"10.1038\/s41577-020-0406-2","volume":"21","author":"M Certo","year":"2021","unstructured":"Certo M, Tsai C-H, Pucino V et al (2021) Lactate modulation of immune responses in inflammatory versus tumour microenvironments. Nat Rev Immunol 21:151\u2013161. https:\/\/doi.org\/10.1038\/s41577-020-0406-2","journal-title":"Nat Rev Immunol"},{"key":"4631_CR31","doi-asserted-by":"publisher","DOI":"10.1002\/ctm2.1187","volume":"13","author":"C Wang","year":"2023","unstructured":"Wang C, Gao Y, Chen B, Jiang P (2023) Vitamin D receptor activation in microglia suppresses NOX2-mediated oxidative damage via PAT1 in vitro and in vivo. Clin Transl Med 13:e1187. https:\/\/doi.org\/10.1002\/ctm2.1187","journal-title":"Clin Transl Med"},{"key":"4631_CR32","doi-asserted-by":"publisher","first-page":"374","DOI":"10.1186\/s12964-024-01748-x","volume":"22","author":"X Jiang","year":"2024","unstructured":"Jiang X, Gao J, Fei X et al (2024) Global profiling of protein lactylation in microglia in experimental high-altitude cerebral edema. Cell Commun Signal 22:374. https:\/\/doi.org\/10.1186\/s12964-024-01748-x","journal-title":"Cell Commun Signal"},{"key":"4631_CR33","doi-asserted-by":"publisher","first-page":"757","DOI":"10.1016\/j.cmet.2018.03.008","volume":"27","author":"GA Brooks","year":"2018","unstructured":"Brooks GA (2018) The science and translation of lactate shuttle theory. Cell Metab 27:757\u2013785. https:\/\/doi.org\/10.1016\/j.cmet.2018.03.008","journal-title":"Cell Metab"},{"key":"4631_CR34","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1038\/s41422-023-00864-6","volume":"34","author":"Y Mao","year":"2024","unstructured":"Mao Y, Zhang J, Zhou Q et al (2024) Hypoxia induces mitochondrial protein lactylation to limit oxidative phosphorylation. Cell Res 34:13\u201330. https:\/\/doi.org\/10.1038\/s41422-023-00864-6","journal-title":"Cell Res"},{"key":"4631_CR35","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1038\/s41422-023-00872-6","volume":"34","author":"H Ren","year":"2024","unstructured":"Ren H, Zhang D (2024) Lactylation constrains OXPHOS under hypoxia. Cell Res 34:91\u201392. https:\/\/doi.org\/10.1038\/s41422-023-00872-6","journal-title":"Cell Res"},{"key":"4631_CR36","doi-asserted-by":"publisher","DOI":"10.1016\/j.arr.2019.100915","volume":"53","author":"L de Bari","year":"2019","unstructured":"de Bari L, Atlante A, Armeni T, Kalapos MP (2019) Synthesis and metabolism of methylglyoxal, S-D-lactoylglutathione and D-lactate in cancer and Alzheimer\u2019s disease. Exploring the crossroad of eternal youth and premature aging. Ageing Res Rev 53:100915. https:\/\/doi.org\/10.1016\/j.arr.2019.100915","journal-title":"Ageing Res Rev"},{"key":"4631_CR37","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2404899122","volume":"122","author":"J Gao","year":"2025","unstructured":"Gao J, Liu R, Huang K et al (2025) Dynamic investigation of hypoxia-induced L-lactylation. Proc Natl Acad Sci USA 122:e2404899122. https:\/\/doi.org\/10.1073\/pnas.2404899122","journal-title":"Proc Natl Acad Sci USA"},{"key":"4631_CR38","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1038\/s41422-024-01060-w","volume":"35","author":"Q Zhao","year":"2025","unstructured":"Zhao Q, Wang Q, Yao Q et al (2025) Nonenzymatic lysine D-lactylation induced by glyoxalase II substrate SLG dampens inflammatory immune responses. Cell Res 35:97\u2013116. https:\/\/doi.org\/10.1038\/s41422-024-01060-w","journal-title":"Cell Res"},{"key":"4631_CR39","doi-asserted-by":"publisher","first-page":"786666","DOI":"10.3389\/fimmu.2021.786666","volume":"12","author":"X Chu","year":"2021","unstructured":"Chu X, Di C, Chang P et al (2021) Lactylated histone H3K18 as a potential biomarker for the diagnosis and predicting the severity of septic shock. Front Immunol 12:786666. https:\/\/doi.org\/10.3389\/fimmu.2021.786666","journal-title":"Front Immunol"},{"key":"4631_CR40","doi-asserted-by":"publisher","DOI":"10.1186\/s12974-023-02879-7","volume":"20","author":"L Wei","year":"2023","unstructured":"Wei L, Yang X, Wang J et al (2023) H3K18 lactylation of senescent microglia potentiates brain aging and Alzheimer\u2019s disease through the NF\u03baB signaling pathway. J Neuroinflammation 20:208. https:\/\/doi.org\/10.1186\/s12974-023-02879-7","journal-title":"J Neuroinflammation"},{"key":"4631_CR41","doi-asserted-by":"publisher","first-page":"58","DOI":"10.1038\/nchembio.495","volume":"7","author":"Z Zhang","year":"2011","unstructured":"Zhang Z, Tan M, Xie Z et al (2011) Identification of lysine succinylation as a new post-translational modification. Nat Chem Biol 7:58\u201363. https:\/\/doi.org\/10.1038\/nchembio.495","journal-title":"Nat Chem Biol"},{"key":"4631_CR42","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2410628121","volume":"121","author":"J Zhang","year":"2024","unstructured":"Zhang J, Wei Y, Yue Y et al (2024) RIPK4 promotes oxidative stress and ferroptotic death through the downregulation of ACSM1. Proc Natl Acad Sci USA 121:e2410628121. https:\/\/doi.org\/10.1073\/pnas.2410628121","journal-title":"Proc Natl Acad Sci USA"},{"key":"4631_CR43","doi-asserted-by":"publisher","DOI":"10.1002\/advs.202402030","volume":"11","author":"P Deng","year":"2024","unstructured":"Deng P, Fan T, Gao P et al (2024) SIRT5-mediated desuccinylation of RAB7A protects against cadmium-induced Alzheimer\u2019s disease-like pathology by restoring autophagic flux. Adv Sci 11:e2402030. https:\/\/doi.org\/10.1002\/advs.202402030","journal-title":"Adv Sci"},{"key":"4631_CR44","doi-asserted-by":"publisher","first-page":"85","DOI":"10.1038\/s41421-023-00573-9","volume":"9","author":"J Li","year":"2023","unstructured":"Li J, Lu L, Liu L et al (2023) HDAC1\/2\/3 are major histone desuccinylases critical for promoter desuccinylation. Cell Discov 9:85. https:\/\/doi.org\/10.1038\/s41421-023-00573-9","journal-title":"Cell Discov"},{"key":"4631_CR45","doi-asserted-by":"publisher","first-page":"885685","DOI":"10.3389\/fimmu.2022.885685","volume":"13","author":"Y Zou","year":"2022","unstructured":"Zou Y, Bai X-H, Kong L-C et al (2022) Involvement of histone lysine crotonylation in the regulation of nerve-injury-induced neuropathic pain. Front Immunol 13:885685. https:\/\/doi.org\/10.3389\/fimmu.2022.885685","journal-title":"Front Immunol"},{"key":"4631_CR46","doi-asserted-by":"publisher","first-page":"1475","DOI":"10.1038\/s41593-021-00905-6","volume":"24","author":"P Hasel","year":"2021","unstructured":"Hasel P, Rose IVL, Sadick JS et al (2021) Neuroinflammatory astrocyte subtypes in the mouse brain. Nat Neurosci 24:1475\u20131487. https:\/\/doi.org\/10.1038\/s41593-021-00905-6","journal-title":"Nat Neurosci"},{"key":"4631_CR47","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2024.114529","volume":"43","author":"H Li","year":"2024","unstructured":"Li H, Liuha X, Chen R et al (2024) Pyruvate dehydrogenase complex E1 subunit \u03b1 crotonylation modulates cocaine-associated memory through hippocampal neuron activation. Cell Rep 43:114529. https:\/\/doi.org\/10.1016\/j.celrep.2024.114529","journal-title":"Cell Rep"},{"key":"4631_CR48","doi-asserted-by":"publisher","first-page":"1401","DOI":"10.1042\/BCJ20190042","volume":"476","author":"JS Rane","year":"2019","unstructured":"Rane JS, Kumari A, Panda D (2019) An acetylation mimicking mutation, K274Q, in Tau imparts neurotoxicity by enhancing Tau aggregation and inhibiting tubulin polymerization. Biochem J 476:1401\u20131417. https:\/\/doi.org\/10.1042\/BCJ20190042","journal-title":"Biochem J"},{"key":"4631_CR49","doi-asserted-by":"publisher","first-page":"600368","DOI":"10.3389\/fcell.2020.600368","volume":"8","author":"X Yang","year":"2020","unstructured":"Yang X, Chatterjee V, Ma Y et al (2020) Protein palmitoylation in leukocyte signaling and function. Front Cell Dev Biol 8:600368. https:\/\/doi.org\/10.3389\/fcell.2020.600368","journal-title":"Front Cell Dev Biol"},{"key":"4631_CR50","doi-asserted-by":"publisher","first-page":"3336","DOI":"10.1016\/j.molcel.2024.08.001","volume":"84","author":"L Nie","year":"2024","unstructured":"Nie L, Fei C, Fan Y et al (2024) Consecutive palmitoylation and phosphorylation orchestrates NLRP3 membrane trafficking and inflammasome activation. Mol Cell 84:3336-3353.e7. https:\/\/doi.org\/10.1016\/j.molcel.2024.08.001","journal-title":"Mol Cell"},{"key":"4631_CR51","doi-asserted-by":"publisher","first-page":"354","DOI":"10.1038\/nature16959","volume":"530","author":"Y He","year":"2016","unstructured":"He Y, Zeng MY, Yang D et al (2016) NEK7 is an essential mediator of NLRP3 activation downstream of potassium efflux. Nature 530:354\u2013357. https:\/\/doi.org\/10.1038\/nature16959","journal-title":"Nature"},{"key":"4631_CR52","doi-asserted-by":"publisher","first-page":"250","DOI":"10.1038\/ni.3333","volume":"17","author":"H Shi","year":"2016","unstructured":"Shi H, Wang Y, Li X et al (2016) NLRP3 activation and mitosis are mutually exclusive events coordinated by NEK7, a new inflammasome component. Nat Immunol 17:250\u2013258. https:\/\/doi.org\/10.1038\/ni.3333","journal-title":"Nat Immunol"},{"key":"4631_CR53","doi-asserted-by":"publisher","first-page":"4570","DOI":"10.1016\/j.molcel.2023.11.015","volume":"83","author":"S Zheng","year":"2023","unstructured":"Zheng S, Que X, Wang S et al (2023) ZDHHC5-mediated NLRP3 palmitoylation promotes NLRP3-NEK7 interaction and inflammasome activation. Mol Cell 83:4570-4585.e7. https:\/\/doi.org\/10.1016\/j.molcel.2023.11.015","journal-title":"Mol Cell"},{"key":"4631_CR54","doi-asserted-by":"publisher","first-page":"281","DOI":"10.1016\/j.molcel.2022.12.002","volume":"83","author":"L Wang","year":"2023","unstructured":"Wang L, Cai J, Zhao X et al (2023) Palmitoylation prevents sustained inflammation by limiting NLRP3 inflammasome activation through chaperone-mediated autophagy. Mol Cell 83:281-297.e10. https:\/\/doi.org\/10.1016\/j.molcel.2022.12.002","journal-title":"Mol Cell"},{"key":"4631_CR55","doi-asserted-by":"publisher","first-page":"1541","DOI":"10.1038\/s41418-022-00942-z","volume":"29","author":"L Zhou","year":"2022","unstructured":"Zhou L, He X, Wang L et al (2022) Palmitoylation restricts SQSTM1\/p62-mediated autophagic degradation of NOD2 to modulate inflammation. Cell Death Differ 29:1541\u20131551. https:\/\/doi.org\/10.1038\/s41418-022-00942-z","journal-title":"Cell Death Differ"},{"key":"4631_CR56","doi-asserted-by":"publisher","first-page":"588","DOI":"10.1038\/nrd.2018.97","volume":"17","author":"MSJ Mangan","year":"2018","unstructured":"Mangan MSJ, Olhava EJ, Roush WR et al (2018) Targeting the NLRP3 inflammasome in inflammatory diseases. Nat Rev Drug Discov 17:588\u2013606. https:\/\/doi.org\/10.1038\/nrd.2018.97","journal-title":"Nat Rev Drug Discov"},{"key":"4631_CR57","doi-asserted-by":"publisher","first-page":"981285","DOI":"10.3389\/fimmu.2022.981285","volume":"13","author":"T Zhou","year":"2022","unstructured":"Zhou T, Cheng X, He Y et al (2022) Function and mechanism of histone \u03b2-hydroxybutyrylation in health and disease. Front Immunol 13:981285. https:\/\/doi.org\/10.3389\/fimmu.2022.981285","journal-title":"Front Immunol"},{"key":"4631_CR58","doi-asserted-by":"publisher","DOI":"10.1111\/acel.14368","volume":"24","author":"W Han","year":"2025","unstructured":"Han W, Zhang B, Zhao W et al (2025) Ketogenic \u03b2-hydroxybutyrate regulates \u03b2-hydroxybutyrylation of TCA cycle-associated enzymes and attenuates disease-associated pathologies in alzheimer\u2019s mice. Aging Cell 24:e14368. https:\/\/doi.org\/10.1111\/acel.14368","journal-title":"Aging Cell"},{"key":"4631_CR59","doi-asserted-by":"publisher","DOI":"10.1126\/scitranslmed.aay8329","volume":"12","author":"J-P Song","year":"2020","unstructured":"Song J-P, Chen L, Chen X et al (2020) Elevated plasma \u03b2-hydroxybutyrate predicts adverse outcomes and disease progression in patients with arrhythmogenic cardiomyopathy. Sci Transl Med 12:eaay8329. https:\/\/doi.org\/10.1126\/scitranslmed.aay8329","journal-title":"Sci Transl Med"},{"key":"4631_CR60","doi-asserted-by":"publisher","first-page":"1505","DOI":"10.1038\/s42255-024-01093-w","volume":"6","author":"J Qin","year":"2024","unstructured":"Qin J, Huang X, Gou S et al (2024) Ketogenic diet reshapes cancer metabolism through lysine \u03b2-hydroxybutyrylation. Nat Metab 6:1505\u20131528. https:\/\/doi.org\/10.1038\/s42255-024-01093-w","journal-title":"Nat Metab"},{"key":"4631_CR61","doi-asserted-by":"publisher","first-page":"194","DOI":"10.1016\/j.molcel.2016.03.036","volume":"62","author":"Z Xie","year":"2016","unstructured":"Xie Z, Zhang D, Chung D et al (2016) Metabolic regulation of gene expression by histone lysine \u03b2-hydroxybutyrylation. Mol Cell 62:194\u2013206. https:\/\/doi.org\/10.1016\/j.molcel.2016.03.036","journal-title":"Mol Cell"},{"key":"4631_CR62","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2025.139597","volume":"300","author":"C Yang","year":"2025","unstructured":"Yang C, Wu X, Jiang Z et al (2025) Evodiamine rescues lipopolysaccharide-induced cognitive impairment via C\/EBP-\u03b2-COX2 axis-regulated neuroinflammation. Int J Biol Macromol 300:139597. https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.139597","journal-title":"Int J Biol Macromol"},{"key":"4631_CR63","doi-asserted-by":"publisher","first-page":"102","DOI":"10.1016\/j.metabol.2015.10.001","volume":"65","author":"EC Graff","year":"2016","unstructured":"Graff EC, Fang H, Wanders D, Judd RL (2016) Anti-inflammatory effects of the hydroxycarboxylic acid receptor 2. Metabolism 65:102\u2013113. https:\/\/doi.org\/10.1016\/j.metabol.2015.10.001","journal-title":"Metabolism"},{"key":"4631_CR64","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1038\/nm.3804","volume":"21","author":"Y-H Youm","year":"2015","unstructured":"Youm Y-H, Nguyen KY, Grant RW et al (2015) The ketone metabolite \u03b2-hydroxybutyrate blocks NLRP3 inflammasome-mediated inflammatory disease. Nat Med 21:263\u2013269. https:\/\/doi.org\/10.1038\/nm.3804","journal-title":"Nat Med"},{"key":"4631_CR65","doi-asserted-by":"publisher","first-page":"63","DOI":"10.1038\/nrn.2017.156","volume":"19","author":"MP Mattson","year":"2018","unstructured":"Mattson MP, Moehl K, Ghena N et al (2018) Intermittent metabolic switching, neuroplasticity and brain health. Nat Rev Neurosci 19:63\u201380. https:\/\/doi.org\/10.1038\/nrn.2017.156","journal-title":"Nat Rev Neurosci"},{"key":"4631_CR66","doi-asserted-by":"publisher","first-page":"854","DOI":"10.1038\/s41592-022-01523-1","volume":"19","author":"N Wan","year":"2022","unstructured":"Wan N, Wang N, Yu S et al (2022) Cyclic immonium ion of lactyllysine reveals widespread lactylation in the human proteome. Nat Methods 19:854\u2013864. https:\/\/doi.org\/10.1038\/s41592-022-01523-1","journal-title":"Nat Methods"},{"key":"4631_CR67","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1186\/s12974-020-01740-5","volume":"17","author":"X-T He","year":"2020","unstructured":"He X-T, Hu X-F, Zhu C et al (2020) Suppression of histone deacetylases by SAHA relieves bone cancer pain in rats via inhibiting activation of glial cells in spinal dorsal horn and dorsal root ganglia. J Neuroinflammation 17:125. https:\/\/doi.org\/10.1186\/s12974-020-01740-5","journal-title":"J Neuroinflammation"},{"key":"4631_CR68","doi-asserted-by":"publisher","DOI":"10.1016\/j.redox.2024.103064","volume":"70","author":"P Ouyang","year":"2024","unstructured":"Ouyang P, Cai Z, Peng J et al (2024) SELENOK-dependent CD36 palmitoylation regulates microglial functions and a\u03b2 phagocytosis. Redox Biol 70:103064. https:\/\/doi.org\/10.1016\/j.redox.2024.103064","journal-title":"Redox Biol"},{"key":"4631_CR69","doi-asserted-by":"publisher","first-page":"757","DOI":"10.1038\/s41556-024-01397-9","volume":"26","author":"N Zhang","year":"2024","unstructured":"Zhang N, Zhang J, Yang Y et al (2024) A palmitoylation-depalmitoylation relay spatiotemporally controls GSDMD activation in pyroptosis. Nat Cell Biol 26:757\u2013769. https:\/\/doi.org\/10.1038\/s41556-024-01397-9","journal-title":"Nat Cell Biol"},{"key":"4631_CR70","doi-asserted-by":"publisher","DOI":"10.1126\/sciimmunol.adn1452","volume":"9","author":"A Balasubramanian","year":"2024","unstructured":"Balasubramanian A, Hsu AY, Ghimire L et al (2024) The palmitoylation of gasdermin D directs its membrane translocation and pore formation during pyroptosis. Sci Immunol 9:eadn1452. https:\/\/doi.org\/10.1126\/sciimmunol.adn1452","journal-title":"Sci Immunol"},{"key":"4631_CR71","doi-asserted-by":"publisher","first-page":"500","DOI":"10.1016\/j.tcb.2024.10.005","volume":"35","author":"N Zhang","year":"2025","unstructured":"Zhang N, Yang Y, Xu D (2025) Emerging roles of palmitoylation in pyroptosis. Trends Cell Biol 35:500\u2013514. https:\/\/doi.org\/10.1016\/j.tcb.2024.10.005","journal-title":"Trends Cell Biol"},{"key":"4631_CR72","doi-asserted-by":"publisher","first-page":"e0275428","DOI":"10.1371\/journal.pone.0275428","volume":"17","author":"Z-B Dong","year":"2022","unstructured":"Dong Z-B, Wang Y-J, Cheng M-L et al (2022) 2-bromopalmitate decreases spinal inflammation and attenuates oxaliplatin-induced neuropathic pain via reducing Drp1-mediated mitochondrial dysfunction. PLoS ONE 17:e0275428. https:\/\/doi.org\/10.1371\/journal.pone.0275428","journal-title":"PLoS ONE"},{"key":"4631_CR73","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2024.114609","volume":"43","author":"J Xu","year":"2024","unstructured":"Xu J, Pickard JM, N\u00fa\u00f1ez G (2024) FDA-approved disulfiram inhibits the NLRP3 inflammasome by regulating NLRP3 palmitoylation. Cell Rep 43:114609. https:\/\/doi.org\/10.1016\/j.celrep.2024.114609","journal-title":"Cell Rep"},{"key":"4631_CR74","doi-asserted-by":"publisher","first-page":"867","DOI":"10.1038\/s41467-025-56344-5","volume":"16","author":"B Huang","year":"2025","unstructured":"Huang B, Wang H, Liu S et al (2025) Palmitoylation-dependent regulation of GPX4 suppresses ferroptosis. Nat Commun 16:867. https:\/\/doi.org\/10.1038\/s41467-025-56344-5","journal-title":"Nat Commun"},{"key":"4631_CR75","doi-asserted-by":"publisher","first-page":"2871","DOI":"10.1007\/s10571-023-01325-9","volume":"43","author":"J Sun","year":"2023","unstructured":"Sun J, Pu C, Yang E et al (2023) Macrophage\/microglia Sirt3 contributes to the anti-inflammatory effects of Resveratrol against experimental intracerebral hemorrhage in mice. Cell Mol Neurobiol 43:2871\u20132882. https:\/\/doi.org\/10.1007\/s10571-023-01325-9","journal-title":"Cell Mol Neurobiol"},{"key":"4631_CR76","doi-asserted-by":"publisher","first-page":"126","DOI":"10.2174\/1570159X15666170703113212","volume":"16","author":"F Sarubbo","year":"2018","unstructured":"Sarubbo F, Esteban S, Miralles A, Moranta D (2018) Effects of Resveratrol and other polyphenols on Sirt1: relevance to brain function during aging. Curr Neuropharmacol 16:126\u2013136. https:\/\/doi.org\/10.2174\/1570159X15666170703113212","journal-title":"Curr Neuropharmacol"},{"key":"4631_CR77","doi-asserted-by":"publisher","first-page":"2016","DOI":"10.1007\/s12640-022-00624-1","volume":"40","author":"J Guo","year":"2022","unstructured":"Guo J, Xue H, Zhong H et al (2022) Involvement of LARP7 in activation of SIRT1 to inhibit NF-\u03baB signaling protects microglia from acrylamide-induced neuroinflammation. Neurotox Res 40:2016\u20132026. https:\/\/doi.org\/10.1007\/s12640-022-00624-1","journal-title":"Neurotox Res"},{"key":"4631_CR78","doi-asserted-by":"publisher","DOI":"10.1002\/advs.202402710","volume":"11","author":"Q Yu","year":"2024","unstructured":"Yu Q, Zhang J, Li J et al (2024) Sirtuin 5-mediated desuccinylation of ALDH2 alleviates mitochondrial oxidative stress following acetaminophen-induced acute liver injury. Adv Sci 11:e2402710. https:\/\/doi.org\/10.1002\/advs.202402710","journal-title":"Adv Sci"},{"key":"4631_CR79","doi-asserted-by":"publisher","first-page":"12460","DOI":"10.1021\/acs.jmedchem.0c00830","volume":"63","author":"TCS Ho","year":"2020","unstructured":"Ho TCS, Chan AHY, Ganesan A (2020) Thirty years of HDAC inhibitors: 2020 insight and hindsight. J Med Chem 63:12460\u201312484. https:\/\/doi.org\/10.1021\/acs.jmedchem.0c00830","journal-title":"J Med Chem"},{"key":"4631_CR80","doi-asserted-by":"publisher","DOI":"10.1016\/j.biopha.2024.117295","volume":"179","author":"S-Y Zhang","year":"2024","unstructured":"Zhang S-Y, Zhang L-Y, Wen R et al (2024) Histone deacetylases and their inhibitors in inflammatory diseases. Biomed Pharmacother 179:117295. https:\/\/doi.org\/10.1016\/j.biopha.2024.117295","journal-title":"Biomed Pharmacother"},{"key":"4631_CR81","doi-asserted-by":"publisher","first-page":"e85570","DOI":"10.1371\/journal.pone.0085570","volume":"9","author":"J Meng","year":"2014","unstructured":"Meng J, Li Y, Camarillo C et al (2014) The anti-tumor histone deacetylase inhibitor SAHA and the natural flavonoid Curcumin exhibit synergistic neuroprotection against amyloid-beta toxicity. PLoS One 9:e85570. https:\/\/doi.org\/10.1371\/journal.pone.0085570","journal-title":"PLoS One"},{"key":"4631_CR82","doi-asserted-by":"publisher","first-page":"12262","DOI":"10.1038\/s41598-025-96241-x","volume":"15","author":"S Mancino","year":"2025","unstructured":"Mancino S, Boraso M, Galmozzi A et al (2025) Dose-dependent dual effects of HDAC inhibitors on glial inflammatory response. Sci Rep 15:12262. https:\/\/doi.org\/10.1038\/s41598-025-96241-x","journal-title":"Sci Rep"},{"key":"4631_CR83","doi-asserted-by":"publisher","first-page":"3664","DOI":"10.1021\/acs.jproteome.7b00380","volume":"16","author":"Q Wu","year":"2017","unstructured":"Wu Q, Li W, Wang C et al (2017) Ultradeep lysine crotonylome reveals the crotonylation enhancement on both histones and nonhistone proteins by SAHA treatment. J Proteome Res 16:3664\u20133671. https:\/\/doi.org\/10.1021\/acs.jproteome.7b00380","journal-title":"J Proteome Res"},{"key":"4631_CR84","doi-asserted-by":"publisher","first-page":"306","DOI":"10.1038\/s41551-019-0375-6","volume":"3","author":"H Yao","year":"2019","unstructured":"Yao H, Lan J, Li C et al (2019) Inhibiting PD-L1 palmitoylation enhances T-cell immune responses against tumours. Nat Biomed Eng 3:306\u2013317. https:\/\/doi.org\/10.1038\/s41551-019-0375-6","journal-title":"Nat Biomed Eng"},{"key":"4631_CR85","doi-asserted-by":"publisher","first-page":"2821","DOI":"10.1080\/15548627.2023.2187957","volume":"19","author":"L Wang","year":"2023","unstructured":"Wang L, Cui J (2023) Palmitoylation promotes chaperone-mediated autophagic degradation of NLRP3 to modulate inflammation. Autophagy 19:2821\u20132823. https:\/\/doi.org\/10.1080\/15548627.2023.2187957","journal-title":"Autophagy"},{"key":"4631_CR86","doi-asserted-by":"publisher","first-page":"338","DOI":"10.1080\/15548627.2024.2395158","volume":"21","author":"S Yang","year":"2025","unstructured":"Yang S, Li M, Lian G et al (2025) ABHD8 antagonizes inflammation by facilitating chaperone-mediated autophagy-mediated degradation of NLRP3. Autophagy 21:338\u2013351. https:\/\/doi.org\/10.1080\/15548627.2024.2395158","journal-title":"Autophagy"},{"key":"4631_CR87","doi-asserted-by":"publisher","first-page":"379","DOI":"10.1038\/s41420-022-01167-2","volume":"8","author":"L Zhuang","year":"2022","unstructured":"Zhuang L, Luo X, Wu S et al (2022) Disulfiram alleviates pristane-induced lupus via inhibiting GSDMD-mediated pyroptosis. Cell Death Discov 8:379. https:\/\/doi.org\/10.1038\/s41420-022-01167-2","journal-title":"Cell Death Discov"},{"key":"4631_CR88","doi-asserted-by":"publisher","first-page":"736","DOI":"10.1038\/s41590-020-0669-6","volume":"21","author":"JJ Hu","year":"2020","unstructured":"Hu JJ, Liu X, Xia S et al (2020) FDA-approved disulfiram inhibits pyroptosis by blocking gasdermin D pore formation. Nat Immunol 21:736\u2013745. https:\/\/doi.org\/10.1038\/s41590-020-0669-6","journal-title":"Nat Immunol"},{"key":"4631_CR89","doi-asserted-by":"publisher","DOI":"10.1016\/j.intimp.2022.108545","volume":"105","author":"S Wei","year":"2022","unstructured":"Wei S, Xiao Z, Huang J et al (2022) Disulfiram inhibits oxidative stress and NLRP3 inflammasome activation to prevent LPS-induced cardiac injury. Int Immunopharmacol 105:108545. https:\/\/doi.org\/10.1016\/j.intimp.2022.108545","journal-title":"Int Immunopharmacol"},{"key":"4631_CR90","doi-asserted-by":"publisher","first-page":"874","DOI":"10.1038\/s41419-024-07268-3","volume":"15","author":"Y-P Bai","year":"2024","unstructured":"Bai Y-P, Xing Y-J, Ma T et al (2024) \u03b2-hydroxybutyrate suppresses M1 macrophage polarization through \u03b2-hydroxybutyrylation of the STAT1 protein. Cell Death Dis 15:874. https:\/\/doi.org\/10.1038\/s41419-024-07268-3","journal-title":"Cell Death Dis"},{"key":"4631_CR91","doi-asserted-by":"publisher","first-page":"326","DOI":"10.1016\/j.immuni.2025.01.007","volume":"58","author":"RM McManus","year":"2025","unstructured":"McManus RM, Komes MP, Griep A et al (2025) NLRP3-mediated glutaminolysis controls microglial phagocytosis to promote Alzheimer\u2019s disease progression. Immunity 58:326-343e11. https:\/\/doi.org\/10.1016\/j.immuni.2025.01.007","journal-title":"Immunity"},{"key":"4631_CR92","doi-asserted-by":"publisher","DOI":"10.1002\/advs.202300738","volume":"10","author":"Y Zhao","year":"2023","unstructured":"Zhao Y, Zhang J, Cheng X et al (2023) Targeting L-selectin lymphocytes to deliver immunosuppressive drug in lymph nodes for durable multiple sclerosis treatment. Adv Sci 10:e2300738. https:\/\/doi.org\/10.1002\/advs.202300738","journal-title":"Adv Sci"},{"key":"4631_CR93","doi-asserted-by":"publisher","first-page":"1413","DOI":"10.1038\/s41423-023-01089-8","volume":"20","author":"J Cao","year":"2023","unstructured":"Cao J, Ji L, Zhan Y et al (2023) MST4 kinase regulates immune thrombocytopenia by phosphorylating STAT1-mediated M1 polarization of macrophages. Cell Mol Immunol 20:1413\u20131427. https:\/\/doi.org\/10.1038\/s41423-023-01089-8","journal-title":"Cell Mol Immunol"},{"key":"4631_CR94","doi-asserted-by":"publisher","first-page":"280","DOI":"10.1186\/s12974-020-01948-5","volume":"17","author":"DC Shippy","year":"2020","unstructured":"Shippy DC, Wilhelm C, Viharkumar PA et al (2020) \u03b2-hydroxybutyrate inhibits inflammasome activation to attenuate Alzheimer\u2019s disease pathology. J Neuroinflammation 17:280. https:\/\/doi.org\/10.1186\/s12974-020-01948-5","journal-title":"J Neuroinflammation"},{"key":"4631_CR95","doi-asserted-by":"publisher","first-page":"805881","DOI":"10.3389\/fimmu.2022.805881","volume":"13","author":"J Qi","year":"2022","unstructured":"Qi J, Gan L, Fang J et al (2022) Beta-hydroxybutyrate: a dual function molecular and immunological barrier function regulator. Front Immunol 13:805881. https:\/\/doi.org\/10.3389\/fimmu.2022.805881","journal-title":"Front Immunol"},{"key":"4631_CR96","doi-asserted-by":"publisher","first-page":"1660","DOI":"10.1016\/j.jacc.2020.12.065","volume":"77","author":"SR Yurista","year":"2021","unstructured":"Yurista SR, Chong C-R, Badimon JJ et al (2021) Therapeutic potential of ketone bodies for patients with cardiovascular disease: JACC state-of-the-art review. J Am Coll Cardiol 77:1660\u20131669. https:\/\/doi.org\/10.1016\/j.jacc.2020.12.065","journal-title":"J Am Coll Cardiol"},{"key":"4631_CR97","doi-asserted-by":"publisher","first-page":"54","DOI":"10.14283\/jpad.2022.3","volume":"9","author":"KI Avgerinos","year":"2022","unstructured":"Avgerinos KI, Mullins RJ, Egan JM, Kapogiannis D (2022) Ketone ester effects on biomarkers of brain metabolism and cognitive performance in cognitively intact adults\u2009\u2265\u200955 years old. A study protocol for a double-blinded randomized controlled clinical trial. J Prev Alzheimers Dis 9:54\u201366. https:\/\/doi.org\/10.14283\/jpad.2022.3","journal-title":"J Prev Alzheimers Dis"},{"key":"4631_CR98","doi-asserted-by":"publisher","first-page":"510","DOI":"10.1038\/nbt.3199","volume":"33","author":"IB Hilton","year":"2015","unstructured":"Hilton IB, D\u2019Ippolito AM, Vockley CM et al (2015) Epigenome editing by a CRISPR-Cas9-based acetyltransferase activates genes from promoters and enhancers. Nat Biotechnol 33:510\u2013517. https:\/\/doi.org\/10.1038\/nbt.3199","journal-title":"Nat Biotechnol"},{"key":"4631_CR99","doi-asserted-by":"publisher","DOI":"10.1002\/advs.202302130","volume":"10","author":"M Xu","year":"2023","unstructured":"Xu M, Tan J, Zhu L et al (2023) Palmitoyltransferase ZDHHC3 aggravates nonalcoholic steatohepatitis by targeting S-palmitoylated IRHOM2. Adv Sci 10:e2302130. https:\/\/doi.org\/10.1002\/advs.202302130","journal-title":"Adv Sci"}],"container-title":["Neurochemical Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11064-025-04631-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11064-025-04631-4","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11064-025-04631-4.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,3,4]],"date-time":"2026-03-04T10:11:51Z","timestamp":1772619111000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s11064-025-04631-4"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12,29]]},"references-count":99,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2026,2]]}},"alternative-id":["4631"],"URL":"https:\/\/doi.org\/10.1007\/s11064-025-04631-4","relation":{},"ISSN":["0364-3190","1573-6903"],"issn-type":[{"value":"0364-3190","type":"print"},{"value":"1573-6903","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,12,29]]},"assertion":[{"value":"9 September 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"1 December 2025","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"9 December 2025","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"29 December 2025","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing Interests"}}],"article-number":"22"}}