{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,13]],"date-time":"2026-06-13T04:58:41Z","timestamp":1781326721599,"version":"3.54.1"},"reference-count":269,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,2,1]],"date-time":"2026-02-01T00:00:00Z","timestamp":1769904000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,2,1]],"date-time":"2026-02-01T00:00:00Z","timestamp":1769904000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,12,2]],"date-time":"2025-12-02T00:00:00Z","timestamp":1764633600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001871","name":"Foundation for Science and Technology","doi-asserted-by":"publisher","award":["LA\/P\/0058\/2020"],"award-info":[{"award-number":["LA\/P\/0058\/2020"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001871","name":"Foundation for Science and Technology","doi-asserted-by":"publisher","award":["UIDB\/04539\/2020"],"award-info":[{"award-number":["UIDB\/04539\/2020"]}],"id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001313","name":"Coventry University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001313","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100014013","name":"UK Research and Innovation","doi-asserted-by":"publisher","award":["MR\/W011840\/1"],"award-info":[{"award-number":["MR\/W011840\/1"]}],"id":[{"id":"10.13039\/100014013","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["European Journal of Medicinal Chemistry"],"published-print":{"date-parts":[[2026,2]]},"DOI":"10.1016\/j.ejmech.2025.118429","type":"journal-article","created":{"date-parts":[[2025,11,29]],"date-time":"2025-11-29T04:31:11Z","timestamp":1764390671000},"page":"118429","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"special_numbering":"C","title":["S-acylation and neuroinflammation: the therapeutic potential of zDHHC and deacylase modulation"],"prefix":"10.1016","volume":"303","author":[{"given":"Tiago A.","family":"Duarte","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Choa P.","family":"Ng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jorge A.R.","family":"Salvador","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ludovico","family":"Pipito","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jennifer","family":"Greaves","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6169-5035","authenticated-orcid":false,"given":"V\u00e2nia M.","family":"Moreira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib1","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1038\/s41392-023-01588-0","article-title":"Microglia in neurodegenerative diseases: mechanism and potential therapeutic targets","volume":"8","author":"Gao","year":"2023","journal-title":"Signal Transduct Target Ther"},{"issue":"9","key":"10.1016\/j.ejmech.2025.118429_bib2","doi-asserted-by":"crossref","first-page":"1198","DOI":"10.1038\/s41593-021-00904-7","article-title":"Revisiting the neurovascular unit","volume":"24","author":"Schaeffer","year":"2021","journal-title":"Nat. Neurosci."},{"issue":"6753","key":"10.1016\/j.ejmech.2025.118429_bib3","doi-asserted-by":"crossref","DOI":"10.1126\/science.adx0043","article-title":"Neuroinflammation across neurological diseases","volume":"388","author":"Shi","year":"2025","journal-title":"Science"},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib4","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1038\/s41392-023-01486-5","article-title":"Role of neuroinflammation in neurodegeneration development","volume":"8","author":"Zhang","year":"2023","journal-title":"Signal Transduct Target Ther"},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib5","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1038\/s41392-021-00687-0","article-title":"Pattern recognition receptors in health and diseases","volume":"6","author":"Li","year":"2021","journal-title":"Signal Transduct Target Ther"},{"key":"10.1016\/j.ejmech.2025.118429_bib6","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.pneurobio.2016.05.001","article-title":"Functions and mechanisms of microglia\/macrophages in neuroinflammation and neurogenesis after stroke","volume":"142","author":"Xiong","year":"2016","journal-title":"Prog Neurobiol"},{"key":"10.1016\/j.ejmech.2025.118429_bib7","doi-asserted-by":"crossref","DOI":"10.3389\/fneur.2023.1103416","article-title":"Microglia activation in central nervous system disorders: a review of recent mechanistic investigations and development efforts","volume":"14","author":"Qin","year":"2023","journal-title":"Front. Neurol."},{"key":"10.1016\/j.ejmech.2025.118429_bib8","doi-asserted-by":"crossref","first-page":"1416","DOI":"10.3389\/fimmu.2020.01416","article-title":"Crosstalk between astrocytes and Microglia: an overview","volume":"11","author":"Matejuk","year":"2020","journal-title":"Front. Immunol."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib9","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1186\/s40478-023-01526-9","article-title":"Roles of neuropathology-associated reactive astrocytes: a systematic review","volume":"11","author":"Lawrence","year":"2023","journal-title":"Acta Neuropathol Commun"},{"issue":"7638","key":"10.1016\/j.ejmech.2025.118429_bib10","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1038\/nature21029","article-title":"Neurotoxic reactive astrocytes are induced by activated microglia","volume":"541","author":"Liddelow","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.ejmech.2025.118429_bib11","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bbi.2016.03.010","article-title":"The blood-brain barrier in systemic inflammation","volume":"60","author":"Varatharaj","year":"2017","journal-title":"Brain Behav. Immun."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib12","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.tins.2014.09.003","article-title":"Autophagy in huntington disease and huntingtin in autophagy","volume":"38","author":"Martin","year":"2015","journal-title":"Trends Neurosci."},{"issue":"10","key":"10.1016\/j.ejmech.2025.118429_bib13","article-title":"Proteostasis disturbances and inflammation in neurodegenerative diseases","volume":"9","author":"Sonninen","year":"2020","journal-title":"CELLS-BASEL"},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib14","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1038\/nrm2084","article-title":"Palmitoylation: policing protein stability and traffic","volume":"8","author":"Linder","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118429_bib15","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1038\/s41580-024-00700-8","article-title":"Mechanisms and functions of protein S-acylation","volume":"25","author":"S Mesquita","year":"2024","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"39","key":"10.1016\/j.ejmech.2025.118429_bib16","doi-asserted-by":"crossref","first-page":"10436","DOI":"10.1021\/bi00090a020","article-title":"Binding of acylated peptides and fatty acids to phospholipid vesicles: pertinence to myristoylated proteins","volume":"32","author":"Peitzsch","year":"1993","journal-title":"Biochemistry"},{"issue":"11","key":"10.1016\/j.ejmech.2025.118429_bib17","doi-asserted-by":"crossref","first-page":"3813","DOI":"10.1021\/bi00011a039","article-title":"Doubly-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes","volume":"34","author":"Shahinian","year":"1995","journal-title":"Biochemistry"},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib18","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1016\/0092-8674(79)90321-0","article-title":"Fatty acid binding to vesicular stomatitis virus glycoprotein: a new type of post-translational modification of the viral glycoprotein","volume":"17","author":"Schmidt","year":"1979","journal-title":"Cell"},{"issue":"43","key":"10.1016\/j.ejmech.2025.118429_bib19","doi-asserted-by":"crossref","first-page":"41268","DOI":"10.1074\/jbc.M206573200","article-title":"Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae","volume":"277","author":"Lobo","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib20","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1083\/jcb.200206120","article-title":"The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase","volume":"159","author":"Roth","year":"2002","journal-title":"J. Cell Biol."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118429_bib21","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1016\/j.neuron.2004.12.005","article-title":"Identification of PSD-95 palmitoylating enzymes","volume":"44","author":"Fukata","year":"2004","journal-title":"Neuron"},{"key":"10.1016\/j.ejmech.2025.118429_bib22","doi-asserted-by":"crossref","first-page":"261","DOI":"10.12688\/f1000research.6464.1","article-title":"SwissPalm: protein Palmitoylation database","volume":"4","author":"Blanc","year":"2015","journal-title":"F1000Res"},{"key":"10.1016\/j.ejmech.2025.118429_bib23","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1007\/978-1-4939-9532-5_16","article-title":"SwissPalm 2: protein S-Palmitoylation database","volume":"2009","author":"Blanc","year":"2019","journal-title":"Methods Mol. Biol."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib24","doi-asserted-by":"crossref","DOI":"10.1042\/NS20210005","article-title":"A sticky situation: regulation and function of protein palmitoylation with a spotlight on the axon and axon initial segment","volume":"5","author":"Petropavlovskiy","year":"2021","journal-title":"Neuronal Signal"},{"issue":"8","key":"10.1016\/j.ejmech.2025.118429_bib25","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1004405","article-title":"Curation of the Mammalian palmitoylome indicates a pivotal role for palmitoylation in diseases and disorders of the nervous system and cancers","volume":"11","author":"Sanders","year":"2015","journal-title":"PLoS Comput. Biol."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib26","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1111\/nyas.13718","article-title":"Axon initial segments: structure, function, and disease","volume":"1420","author":"Huang","year":"2018","journal-title":"Ann. N. Y. Acad. Sci."},{"issue":"11","key":"10.1016\/j.ejmech.2025.118429_bib27","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1038\/sj.embor.7400277","article-title":"On the mechanism of protein palmitoylation","volume":"5","author":"Dietrich","year":"2004","journal-title":"EMBO Rep."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib28","doi-asserted-by":"crossref","DOI":"10.3390\/cells12030387","article-title":"S-Palmitoylation of synaptic proteins in neuronal plasticity in normal and pathological brains","volume":"12","author":"Buszka","year":"2023","journal-title":"Cells"},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib29","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1042\/BST20180429","article-title":"The molecular mechanism of DHHC protein acyltransferases","volume":"47","author":"Rana","year":"2019","journal-title":"Biochem. Soc. Trans."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib30","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1080\/10409238.2017.1409191","article-title":"Protein depalmitoylases","volume":"53","author":"Won","year":"2018","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118429_bib31","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1152\/physrev.00032.2014","article-title":"The physiology of protein S-acylation","volume":"95","author":"Chamberlain","year":"2015","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.ejmech.2025.118429_bib32","article-title":"Regulation of dynamic protein S-Acylation","volume":"8","author":"Chen","year":"2021","journal-title":"Front. Mol. Biosci."},{"issue":"18","key":"10.1016\/j.ejmech.2025.118429_bib33","doi-asserted-by":"crossref","first-page":"4983","DOI":"10.1016\/j.jmb.2020.05.023","article-title":"Structure and mechanism of DHHC protein acyltransferases","volume":"432","author":"Stix","year":"2020","journal-title":"J. Mol. Biol."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib34","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1016\/j.coph.2012.02.003","article-title":"Ras family of small GTPases in immunity and inflammation","volume":"12","author":"Johnson","year":"2012","journal-title":"Curr. Opin. Pharmacol."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118429_bib35","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1016\/j.cell.2006.03.042","article-title":"Global analysis of protein palmitoylation in yeast","volume":"125","author":"Roth","year":"2006","journal-title":"Cell"},{"issue":"6","key":"10.1016\/j.ejmech.2025.118429_bib36","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1016\/j.neuron.2004.11.027","article-title":"Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins","volume":"44","author":"Huang","year":"2004","journal-title":"Neuron"},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib37","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1016\/j.bbalip.2006.03.010","article-title":"Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins","volume":"1761","author":"Ohno","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"issue":"12","key":"10.1016\/j.ejmech.2025.118429_bib38","doi-asserted-by":"crossref","first-page":"2766","DOI":"10.1111\/febs.12263","article-title":"What does S-palmitoylation do to membrane proteins?","volume":"280","author":"Blaskovic","year":"2013","journal-title":"FEBS J."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118429_bib39","doi-asserted-by":"crossref","first-page":"1118","DOI":"10.1194\/jlr.R600007-JLR200","article-title":"Protein palmitoylation by a family of DHHC protein S-acyltransferases","volume":"47","author":"Mitchell","year":"2006","journal-title":"J. Lipid Res."},{"issue":"24","key":"10.1016\/j.ejmech.2025.118429_bib40","doi-asserted-by":"crossref","first-page":"6431","DOI":"10.1523\/JNEUROSCI.0419-16.2016","article-title":"Identification of PSD-95 depalmitoylating enzymes","volume":"36","author":"Yokoi","year":"2016","journal-title":"J. Neurosci."},{"key":"10.1016\/j.ejmech.2025.118429_bib41","doi-asserted-by":"crossref","DOI":"10.1038\/npjbcancer.2016.28","article-title":"Palmitoylation: a protein S-acylation with implications for breast cancer","volume":"2","author":"Anderson","year":"2016","journal-title":"npj Breast Cancer"},{"issue":"14","key":"10.1016\/j.ejmech.2025.118429_bib42","doi-asserted-by":"crossref","first-page":"9759","DOI":"10.1021\/acs.jmedchem.1c00624","article-title":"\u03b1\/\u03b2-Hydrolase Domain (ABHD) inhibitors as new potential therapeutic options against lipid-related diseases","volume":"64","author":"Bononi","year":"2021","journal-title":"J. Med. Chem."},{"issue":"10","key":"10.1016\/j.ejmech.2025.118429_bib43","doi-asserted-by":"crossref","first-page":"6153","DOI":"10.1021\/acscatal.5b01539","article-title":"How the same core catalytic machinery catalyzes 17 different reactions: the serine-histidine-aspartate catalytic triad of \u03b1\/\u03b2-Hydrolase fold enzymes","volume":"5","author":"Rauwerdink","year":"2015","journal-title":"ACS Catal."},{"issue":"8","key":"10.1016\/j.ejmech.2025.118429_bib44","first-page":"2981","article-title":"Ankyrin-bound fatty acid turns over rapidly at the erythrocyte plasma membrane","volume":"7","author":"Staufenbiel","year":"1987","journal-title":"Mol. Cell Biol."},{"issue":"30","key":"10.1016\/j.ejmech.2025.118429_bib45","doi-asserted-by":"crossref","first-page":"22566","DOI":"10.1016\/S0021-9258(18)41567-0","article-title":"Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras","volume":"268","author":"Camp","year":"1993","journal-title":"J. Biol. Chem."},{"issue":"37","key":"10.1016\/j.ejmech.2025.118429_bib46","doi-asserted-by":"crossref","first-page":"23212","DOI":"10.1016\/S0021-9258(17)31641-1","article-title":"Molecular cloning and expression of palmitoyl-protein thioesterase","volume":"269","author":"Camp","year":"1994","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib47","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/S0021-9258(17)42360-X","article-title":"Reengineering the specificity of a serine active-site enzyme. Two active-site mutations convert a hydrolase to a transferase","volume":"269","author":"Witkowski","year":"1994","journal-title":"J. Biol. Chem."},{"issue":"26","key":"10.1016\/j.ejmech.2025.118429_bib48","doi-asserted-by":"crossref","first-page":"15831","DOI":"10.1074\/jbc.271.26.15831","article-title":"Lysosomal targeting of palmitoyl-protein thioesterase","volume":"271","author":"Verkruyse","year":"1996","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib49","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.tins.2021.12.004","article-title":"Lysosomal dysfunction in neurodegeneration: emerging concepts and methods","volume":"45","author":"Udayar","year":"2022","journal-title":"Trends Neurosci."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib50","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1038\/s41556-024-01608-3","article-title":"Lysosome repair fails in ageing and Alzheimer's disease","volume":"27","author":"Vrancx","year":"2025","journal-title":"Nat. Cell Biol."},{"issue":"11","key":"10.1016\/j.ejmech.2025.118429_bib51","doi-asserted-by":"crossref","first-page":"2399","DOI":"10.3390\/cells9112399","article-title":"The emerging role of the lysosome in parkinson's disease","volume":"9","author":"Navarro-Romero","year":"2020","journal-title":"CELLS-BASEL"},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib52","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1186\/s13024-018-0300-6","article-title":"Emerging new roles of the lysosome and neuronal ceroid lipofuscinoses","volume":"14","author":"Mukherjee","year":"2019","journal-title":"Mol. Neurodegener."},{"issue":"7","key":"10.1016\/j.ejmech.2025.118429_bib53","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1016\/0092-8674(94)90445-6","article-title":"Activation and depalmitoylation of Gs alpha","volume":"77","author":"Wedegaertner","year":"1994","journal-title":"Cell"},{"issue":"9","key":"10.1016\/j.ejmech.2025.118429_bib54","first-page":"1901","article-title":"Novel determinants of H-Ras plasma membrane localization and transformation","volume":"13","author":"Willumsen","year":"1996","journal-title":"Oncogene"},{"issue":"25","key":"10.1016\/j.ejmech.2025.118429_bib55","doi-asserted-by":"crossref","first-page":"15830","DOI":"10.1074\/jbc.273.25.15830","article-title":"A cytoplasmic acyl-protein thioesterase that removes palmitate from G protein alpha subunits and p21(RAS)","volume":"273","author":"Duncan","year":"1998","journal-title":"J. Biol. Chem."},{"issue":"11","key":"10.1016\/j.ejmech.2025.118429_bib56","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1016\/S0969-2126(00)00529-3","article-title":"Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A","volume":"8","author":"Devedjiev","year":"2000","journal-title":"Structure"},{"issue":"11","key":"10.1016\/j.ejmech.2025.118429_bib57","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0015045","article-title":"Acyl-protein thioesterase 2 catalyzes the deacylation of peripheral membrane-associated GAP-43","volume":"5","author":"Tomatis","year":"2010","journal-title":"PLoS One"},{"issue":"Pt 23","key":"10.1016\/j.ejmech.2025.118429_bib58","doi-asserted-by":"crossref","first-page":"4007","DOI":"10.1242\/jcs.059287","article-title":"Palmitoylation and depalmitoylation dynamics at a glance","volume":"123","author":"Conibear","year":"2010","journal-title":"J. Cell Sci."},{"issue":"23","key":"10.1016\/j.ejmech.2025.118429_bib59","doi-asserted-by":"crossref","DOI":"10.1172\/JCI177924","article-title":"Palmitoylation acts as a checkpoint for MAVS aggregation to promote antiviral innate immune responses","volume":"134","author":"Wang","year":"2024","journal-title":"J. Clin. Investig."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib60","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202405042","article-title":"An S-acylated N-terminus and a conserved loop regulate the activity of the ABHD17 deacylase","volume":"224","author":"Holme","year":"2025","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.ejmech.2025.118429_bib61","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.11306","article-title":"ABHD17 proteins are novel protein depalmitoylases that regulate N-Ras palmitate turnover and subcellular localization","volume":"4","author":"Lin","year":"2015","journal-title":"eLife"},{"issue":"8","key":"10.1016\/j.ejmech.2025.118429_bib62","doi-asserted-by":"crossref","DOI":"10.3390\/ijms23084390","article-title":"Neurodevelopmental disorders associated with PSD-95 and its interaction partners","volume":"23","author":"Levy","year":"2022","journal-title":"Int. J. Mol. Sci."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib63","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.cell.2017.06.009","article-title":"RAS proteins and their regulators in human disease","volume":"170","author":"Simanshu","year":"2017","journal-title":"Cell"},{"issue":"6372","key":"10.1016\/j.ejmech.2025.118429_bib64","doi-asserted-by":"crossref","DOI":"10.1126\/science.aao6326","article-title":"Fatty acyl recognition and transfer by an integral membrane","volume":"359","author":"Rana","year":"2018","journal-title":"Science."},{"issue":"10","key":"10.1016\/j.ejmech.2025.118429_bib65","doi-asserted-by":"crossref","first-page":"7236","DOI":"10.1074\/jbc.M111.337246","article-title":"DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities","volume":"287","author":"Jennings","year":"2012","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib66","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1042\/BST20160304","article-title":"Structure and function of DHHC protein S-acyltransferases","volume":"45","author":"Gottlieb","year":"2017","journal-title":"Biochem. Soc. Trans."},{"issue":"8","key":"10.1016\/j.ejmech.2025.118429_bib67","doi-asserted-by":"crossref","first-page":"E1365","DOI":"10.1073\/pnas.1612254114","article-title":"Molecular basis of fatty acid selectivity in the zDHHC family of S-acyltransferases revealed by click chemistry","volume":"114","author":"Greaves","year":"2017","journal-title":"Proc Natl Acad Sci U S A."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib68","doi-asserted-by":"crossref","DOI":"10.1098\/rsob.210026","article-title":"Substrate recruitment by zDHHC protein acyltransferases","volume":"11","author":"Malgapo","year":"2021","journal-title":"Open Biol."},{"issue":"43","key":"10.1016\/j.ejmech.2025.118429_bib69","doi-asserted-by":"crossref","first-page":"14640","DOI":"10.1074\/jbc.REV120.014717","article-title":"Regulatory effects of post-translational modifications on zDHHC","volume":"295","author":"Zmuda","year":"2020","journal-title":"J. Biol. Chem."},{"issue":"36","key":"10.1016\/j.ejmech.2025.118429_bib70","doi-asserted-by":"crossref","first-page":"21939","DOI":"10.1074\/jbc.M115.657668","article-title":"Identification of a novel sequence motif recognized by the ankyrin repeat domain of zDHHC17\/13 S-Acyltransferases","volume":"290","author":"Lemonidis","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2025.118429_bib71","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.56058","article-title":"The palmitoyl acyltransferase ZDHHC14 controls Kv1-family potassium channel clustering at the axon initial segment","volume":"9","author":"Sanders","year":"2020","journal-title":"eLife"},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib72","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1016\/j.neuron.2011.11.021","article-title":"Palmitoylation by DHHC5\/8 targets GRIP1 to dendritic endosomes to regulate AMPA-R trafficking","volume":"73","author":"Thomas","year":"2012","journal-title":"Neuron"},{"issue":"39","key":"10.1016\/j.ejmech.2025.118429_bib73","doi-asserted-by":"crossref","first-page":"15401","DOI":"10.1523\/JNEUROSCI.1283-13.2013","article-title":"DHHC8-dependent PICK1 palmitoylation is required for induction of cerebellar long-term synaptic depression","volume":"33","author":"Thomas","year":"2013","journal-title":"J. Neurosci."},{"issue":"9","key":"10.1016\/j.ejmech.2025.118429_bib74","doi-asserted-by":"crossref","first-page":"4573","DOI":"10.1073\/pnas.080508097","article-title":"The crystal structure of palmitoyl protein thioesterase 1 and the molecular basis of infantile neuronal ceroid lipofuscinosis","volume":"97","author":"Bellizzi","year":"2000","journal-title":"Proc Natl Acad Sci U S A."},{"issue":"39","key":"10.1016\/j.ejmech.2025.118429_bib75","doi-asserted-by":"crossref","first-page":"37957","DOI":"10.1074\/jbc.M301225200","article-title":"The crystal structure of palmitoyl protein thioesterase-2 (PPT2) reveals the basis for divergent substrate specificities of the two lysosomal thioesterases, PPT1 and PPT2","volume":"278","author":"Calero","year":"2003","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib76","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1016\/j.bbalip.2013.01.002","article-title":"Mammalian alpha beta hydrolase domain (ABHD) proteins: lipid metabolizing enzymes at the interface of cell signaling and energy metabolism","volume":"1831","author":"Lord","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"issue":"12","key":"10.1016\/j.ejmech.2025.118429_bib77","doi-asserted-by":"crossref","first-page":"3374","DOI":"10.1021\/acschembio.6b00720","article-title":"Molecular mechanism for isoform-selective inhibition of acyl protein thioesterases 1 and 2 (APT1 and APT2)","volume":"11","author":"Won","year":"2016","journal-title":"ACS Chem. Biol."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib78","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1093\/protein\/5.3.197","article-title":"The alpha\/beta hydrolase fold","volume":"5","author":"Ollis","year":"1992","journal-title":"Protein Eng."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118429_bib79","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1111\/febs.15071","article-title":"The modular structure of \u03b1\/\u03b2-hydrolases","volume":"287","author":"Bauer","year":"2020","journal-title":"FEBS J."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118429_bib80","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1002\/prot.26661","article-title":"A conserved but structurally divergent loop in acyl protein thioesterase 1 regulates its catalytic activity, ligand binding, and folded stability","volume":"92","author":"Harris","year":"2024","journal-title":"Proteins"},{"issue":"18","key":"10.1016\/j.ejmech.2025.118429_bib81","doi-asserted-by":"crossref","first-page":"14718","DOI":"10.1074\/jbc.M111.335547","article-title":"Distinct acyl protein transferases and thioesterases control surface expression of calcium-activated potassium channels","volume":"287","author":"Tian","year":"2012","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib82","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1194\/jlr.M019851","article-title":"Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity despite close relationship to acyl protein thioesterases","volume":"53","author":"B\u00fcrger","year":"2012","journal-title":"J. Lipid Res."},{"issue":"19","key":"10.1016\/j.ejmech.2025.118429_bib83","doi-asserted-by":"crossref","DOI":"10.1016\/j.molcel.2023.09.007","article-title":"Targeting LYPLAL1-mediated cGAS depalmitoylation enhances the response to anti-tumor immunotherapy","volume":"83","author":"Fan","year":"2023","journal-title":"Mol Cell"},{"issue":"12","key":"10.1016\/j.ejmech.2025.118429_bib84","doi-asserted-by":"crossref","first-page":"1232","DOI":"10.1038\/s41589-019-0399-y","article-title":"ABHD10 is an S-depalmitoylase affecting redox homeostasis through peroxiredoxin-5","volume":"15","author":"Cao","year":"2019","journal-title":"Nat. Chem. Biol."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib85","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1038\/s41589-021-00753-2","article-title":"Palmitoylated acyl protein thioesterase APT2 deforms membranes to extract substrate acyl chains","volume":"17","author":"Abrami","year":"2021","journal-title":"Nat. Chem. Biol."},{"issue":"13","key":"10.1016\/j.ejmech.2025.118429_bib86","doi-asserted-by":"crossref","first-page":"9112","DOI":"10.1074\/jbc.M112.421073","article-title":"Dynamic palmitoylation links cytosol-membrane shuttling of acyl-protein thioesterase-1 and acyl-protein thioesterase-2 with that of proto-oncogene H-ras product and growth-associated protein-43","volume":"288","author":"Kong","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2025.118429_bib87","doi-asserted-by":"crossref","DOI":"10.1016\/j.plipres.2025.101354","article-title":"Different chains for different gains: how acyl chain diversity shapes S-acylated protein function","volume":"100","author":"Busquets Hern\u00e1ndez","year":"2025","journal-title":"Prog. Lipid Res."},{"key":"10.1016\/j.ejmech.2025.118429_bib88","doi-asserted-by":"crossref","DOI":"10.1016\/j.plefa.2020.102175","article-title":"Acyl-CoA synthetases as regulators of brain phospholipid acyl-chain diversity","volume":"161","author":"Fernandez","year":"2020","journal-title":"Prostaglandins Leukot. Essent. Fatty Acids"},{"issue":"7","key":"10.1016\/j.ejmech.2025.118429_bib89","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1038\/nrm2417","article-title":"Mechanisms of membrane fusion: disparate players and common principles","volume":"9","author":"Martens","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib90","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1038\/s42004-021-00603-1","article-title":"Acyl-chain saturation regulates the order of phosphatidylinositol 4,5-bisphosphate nanodomains","volume":"4","author":"Borges-Ara\u00fajo","year":"2021","journal-title":"Commun. Chem."},{"key":"10.1016\/j.ejmech.2025.118429_bib91","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.34394","article-title":"Acyl chain asymmetry and polyunsaturation of brain phospholipids facilitate membrane vesiculation without leakage","volume":"7","author":"Manni","year":"2018","journal-title":"eLife"},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib92","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1091\/mbc.e07-07-0719","article-title":"Polyunsaturated fatty acids influence synaptojanin localization to regulate synaptic vesicle recycling","volume":"19","author":"Marza","year":"2008","journal-title":"Mol. Biol. Cell"},{"issue":"10","key":"10.1016\/j.ejmech.2025.118429_bib93","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2023.113195","article-title":"Very-long-chain fatty acids are crucial to neuronal polarity by providing sphingolipids to lipid rafts","volume":"42","author":"Honda","year":"2023","journal-title":"Cell Rep."},{"issue":"8","key":"10.1016\/j.ejmech.2025.118429_bib94","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1038\/nchembio.405","article-title":"Palmitoylome profiling reveals S-palmitoylation-dependent antiviral activity of IFITM3","volume":"6","author":"Yount","year":"2010","journal-title":"Nat. Chem. Biol."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib95","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003124","article-title":"IFITM proteins restrict viral membrane hemifusion","volume":"9","author":"Li","year":"2013","journal-title":"PLoS Pathog."},{"issue":"16","key":"10.1016\/j.ejmech.2025.118429_bib96","doi-asserted-by":"crossref","first-page":"4302","DOI":"10.1073\/pnas.1602244113","article-title":"Mass-tag labeling reveals site-specific and endogenous levels of protein S-fatty acylation","volume":"113","author":"Percher","year":"2016","journal-title":"Proc Natl Acad Sci U S A."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib97","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2020.108572","article-title":"ApoE4 impairs Neuron-astrocyte coupling of fatty acid metabolism","volume":"34","author":"Qi","year":"2021","journal-title":"Cell Rep."},{"issue":"36","key":"10.1016\/j.ejmech.2025.118429_bib98","doi-asserted-by":"crossref","first-page":"33032","DOI":"10.1074\/jbc.M204607200","article-title":"Mass spectrometric analysis of GAP-43\/neuromodulin reveals the presence of a variety of fatty acylated species","volume":"277","author":"Liang","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118429_bib99","doi-asserted-by":"crossref","first-page":"1420","DOI":"10.1111\/febs.16344","article-title":"Lipid metabolism and Alzheimer's disease: clinical evidence, mechanistic link and therapeutic promise","volume":"290","author":"Yin","year":"2023","journal-title":"FEBS J."},{"issue":"11","key":"10.1016\/j.ejmech.2025.118429_bib100","doi-asserted-by":"crossref","DOI":"10.3390\/biom14111362","article-title":"Exploring the dynamic changes of brain lipids, lipid rafts, and lipid droplets in aging and Alzheimer's disease","volume":"14","author":"Cerasuolo","year":"2024","journal-title":"Biomolecules"},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib101","doi-asserted-by":"crossref","first-page":"691","DOI":"10.3233\/JAD-2012-110629","article-title":"Plasma and brain fatty acid profiles in mild cognitive impairment and Alzheimer's disease","volume":"29","author":"Cunnane","year":"2012","journal-title":"J Alzheimers Dis"},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib102","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pmed.1002266","article-title":"Association between fatty acid metabolism in the brain and Alzheimer disease neuropathology and cognitive performance: a nontargeted metabolomic study","volume":"14","author":"Snowden","year":"2017","journal-title":"PLoS Med."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib103","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1038\/s41580-018-0085-z","article-title":"Dynamics and functions of lipid droplets","volume":"20","author":"Olzmann","year":"2019","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib104","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1186\/s12964-025-02398-3","article-title":"Lipid overload meets S-palmitoylation: a metabolic signalling nexus driving cardiovascular and heart disease","volume":"23","author":"Zhang","year":"2025","journal-title":"Cell Commun. Signal."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib105","doi-asserted-by":"crossref","first-page":"139","DOI":"10.3892\/ijmm.2025.5580","article-title":"Lipid metabolism in microglia: emerging mechanisms and therapeutic opportunities for neurodegenerative diseases","volume":"56","author":"Sun","year":"2025","journal-title":"Int. J. Mol. Med."},{"key":"10.1016\/j.ejmech.2025.118429_bib106","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.75804","article-title":"Exploring the expression patterns of palmitoylating and de-palmitoylating enzymes in the mouse brain using the curated RNA-seq database BrainPalmSeq","volume":"11","author":"Wild","year":"2022","journal-title":"eLife"},{"key":"10.1016\/j.ejmech.2025.118429_bib107","doi-asserted-by":"crossref","first-page":"8","DOI":"10.3389\/fnmol.2019.00008","article-title":"Role of palmitoylation of postsynaptic proteins in promoting synaptic plasticity","volume":"12","author":"Matt","year":"2019","journal-title":"Front. Mol. Neurosci."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib108","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1186\/s13041-020-00717-y","article-title":"Roles of palmitoylation in structural long-term synaptic plasticity","volume":"14","author":"Ji","year":"2021","journal-title":"Mol. Brain"},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib109","doi-asserted-by":"crossref","first-page":"1500","DOI":"10.1073\/pnas.1217121110","article-title":"ABHD12 controls brain lysophosphatidylserine pathways that are deregulated in a murine model of the neurodegenerative disease PHARC","volume":"110","author":"Blankman","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"24","key":"10.1016\/j.ejmech.2025.118429_bib110","doi-asserted-by":"crossref","first-page":"7043","DOI":"10.1111\/febs.15728","article-title":"Protein cysteine palmitoylation in immunity and inflammation","volume":"288","author":"Lin","year":"2021","journal-title":"FEBS J."},{"issue":"24","key":"10.1016\/j.ejmech.2025.118429_bib111","doi-asserted-by":"crossref","DOI":"10.1016\/j.molcel.2023.11.015","article-title":"ZDHHC5-mediated NLRP3 palmitoylation promotes NLRP3-NEK7 interaction and inflammasome activation","volume":"83","author":"Zheng","year":"2023","journal-title":"Mol Cell"},{"issue":"13","key":"10.1016\/j.ejmech.2025.118429_bib112","doi-asserted-by":"crossref","DOI":"10.3390\/ijms20133328","article-title":"The NLRP3 inflammasome: an overview of mechanisms of activation and regulation","volume":"20","author":"Kelley","year":"2019","journal-title":"Int. J. Mol. Sci."},{"issue":"9","key":"10.1016\/j.ejmech.2025.118429_bib113","doi-asserted-by":"crossref","first-page":"2114","DOI":"10.1038\/s41423-021-00740-6","article-title":"NLRP3 inflammasome activation and cell death","volume":"18","author":"Huang","year":"2021","journal-title":"Cell. Mol. Immunol."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib114","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1038\/s41423-025-01275-w","article-title":"NLRP3 inflammasome in neuroinflammation and central nervous system diseases","volume":"22","author":"Xu","year":"2025","journal-title":"Cell. Mol. Immunol."},{"issue":"7","key":"10.1016\/j.ejmech.2025.118429_bib115","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1038\/s41582-023-00822-1","article-title":"Functional roles of reactive astrocytes in neuroinflammation and neurodegeneration","volume":"19","author":"Patani","year":"2023","journal-title":"Nat. Rev. Neurol."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib116","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1186\/s11658-024-00625-2","article-title":"Palmitoylation of synaptic proteins: roles in functional regulation and pathogenesis of neurodegenerative diseases","volume":"29","author":"Peng","year":"2024","journal-title":"Cell. Mol. Biol. Lett."},{"issue":"30","key":"10.1016\/j.ejmech.2025.118429_bib117","doi-asserted-by":"crossref","first-page":"21313","DOI":"10.1074\/jbc.274.30.21313","article-title":"SNAP-25 is targeted to the plasma membrane through a novel membrane-binding domain","volume":"274","author":"Gonzalo","year":"1999","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib118","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1083\/jcb.201302071","article-title":"Local palmitoylation cycles define activity-regulated postsynaptic subdomains","volume":"202","author":"Fukata","year":"2013","journal-title":"J. Cell Biol."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib119","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1042\/BCJ20210719","article-title":"SNARE proteins: zip codes in vesicle targeting?","volume":"479","author":"Koike","year":"2022","journal-title":"Biochem. J."},{"issue":"Pt 1","key":"10.1016\/j.ejmech.2025.118429_bib120","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1042\/BST0380163","article-title":"Regulation of SNAP-25 trafficking and function by palmitoylation","volume":"38","author":"Greaves","year":"2010","journal-title":"Biochem. Soc. Trans."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib121","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1111\/j.1471-4159.2009.06205.x","article-title":"Palmitoylation of the synaptic vesicle fusion machinery","volume":"110","author":"Prescott","year":"2009","journal-title":"J. Neurochem."},{"key":"10.1016\/j.ejmech.2025.118429_bib122","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.78182","article-title":"Syntaxin-1A modulates vesicle fusion in mammalian neurons via juxtamembrane domain dependent palmitoylation of its transmembrane domain","volume":"11","author":"Vardar","year":"2022","journal-title":"eLife"},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib123","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1038\/nrn2788","article-title":"Protein palmitoylation in neuronal development and synaptic plasticity","volume":"11","author":"Fukata","year":"2010","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.ejmech.2025.118429_bib124","article-title":"Function of protein S-Palmitoylation in immunity and immune-related diseases","volume":"12","author":"Zhang","year":"2021","journal-title":"Front. Immunol."},{"key":"10.1016\/j.ejmech.2025.118429_bib125","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2024.103064","article-title":"SELENOK-dependent CD36 palmitoylation regulates microglial functions and A\u03b2 phagocytosis","volume":"70","author":"Ouyang","year":"2024","journal-title":"Redox Biol."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib126","doi-asserted-by":"crossref","DOI":"10.1016\/j.neurot.2024.e00482","article-title":"From defense to disease: IFITM3 in immunity and Alzheimer's disease","volume":"22","author":"Kehs","year":"2025","journal-title":"Neurotherapeutics"},{"issue":"S1","key":"10.1016\/j.ejmech.2025.118429_bib127","doi-asserted-by":"crossref","DOI":"10.1096\/fasebj.2019.33.1_supplement.654.9","article-title":"H\u2010Ras signaling mediates microglia proliferation contributing to neuropathology in INCL mice","volume":"33","author":"Sadhukhan","year":"2019","journal-title":"FASEB J."},{"key":"10.1016\/j.ejmech.2025.118429_bib128","doi-asserted-by":"crossref","DOI":"10.3389\/fimmu.2022.812774","article-title":"Toll-Like receptor signaling and its role in cell-mediated immunity","volume":"13","author":"Duan","year":"2022","journal-title":"Front. Immunol."},{"key":"10.1016\/j.ejmech.2025.118429_bib129","article-title":"NF-\u03baB signaling in inflammation","volume":"2","author":"Liu","year":"2017","journal-title":"Signal Transduct Target Ther"},{"issue":"Suppl 1","key":"10.1016\/j.ejmech.2025.118429_bib130","doi-asserted-by":"crossref","first-page":"S17","DOI":"10.1016\/S1353-8020(11)70008-6","article-title":"Misfolded \u03b1-synuclein and toll-like receptors: therapeutic targets for Parkinson's disease","volume":"18","author":"B\u00e9raud","year":"2012","journal-title":"Parkinsonism Relat Disord"},{"issue":"16","key":"10.1016\/j.ejmech.2025.118429_bib131","doi-asserted-by":"crossref","DOI":"10.3390\/ijms23168885","article-title":"Increased expression of interferon-induced transmembrane 3 (IFITM3) in stroke and other inflammatory conditions in the brain","volume":"23","author":"Harmon","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ejmech.2025.118429_bib132","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1016\/j.ejphar.2014.08.034","article-title":"Induction of interferon-induced transmembrane protein 3 gene expression by lipopolysaccharide in astrocytes","volume":"745","author":"Nakajima","year":"2014","journal-title":"Eur. J. Pharmacol."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib133","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1186\/s13195-022-01002-x","article-title":"Increased levels of the synaptic proteins PSD-95, SNAP-25, and neurogranin in the cerebrospinal fluid of patients with Alzheimer's disease","volume":"14","author":"Kivis\u00e4kk","year":"2022","journal-title":"Alzheimers Res. Ther."},{"issue":"32","key":"10.1016\/j.ejmech.2025.118429_bib134","doi-asserted-by":"crossref","first-page":"24629","DOI":"10.1074\/jbc.M110.119289","article-title":"Palmitoylation of the SNAP25 protein family: specificity and regulation by DHHC palmitoyl transferases","volume":"285","author":"Greaves","year":"2010","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib135","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1186\/s40001-023-01360-8","article-title":"SNAP25 is a potential target for early stage Alzheimer's disease and Parkinson's disease","volume":"28","author":"Wang","year":"2023","journal-title":"Eur. J. Med. Res."},{"issue":"52","key":"10.1016\/j.ejmech.2025.118429_bib136","doi-asserted-by":"crossref","first-page":"21517","DOI":"10.1074\/jbc.M117.800482","article-title":"The palmitoyltransferase ZDHHC20 enhances interferon-induced transmembrane protein 3 (IFITM3) palmitoylation and antiviral activity","volume":"292","author":"McMichael","year":"2017","journal-title":"J. Biol. Chem."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118429_bib137","doi-asserted-by":"crossref","DOI":"10.1128\/mbio.02289-22","article-title":"ABHD16A negatively regulates the palmitoylation and antiviral function of IFITM proteins","volume":"13","author":"Shi","year":"2022","journal-title":"mBio"},{"issue":"7831","key":"10.1016\/j.ejmech.2025.118429_bib138","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1038\/s41586-020-2681-2","article-title":"The innate immunity protein IFITM3 modulates \u03b3-secretase in Alzheimer's disease","volume":"586","author":"Hur","year":"2020","journal-title":"Nature"},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib139","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/j.molcel.2016.04.003","article-title":"Inhibition of DHHC20-Mediated EGFR palmitoylation creates a dependence on EGFR signaling","volume":"62","author":"Runkle","year":"2016","journal-title":"Mol Cell"},{"key":"10.1016\/j.ejmech.2025.118429_bib140","doi-asserted-by":"crossref","DOI":"10.1016\/j.arr.2022.101791","article-title":"Implicative role of epidermal growth factor receptor and its associated signaling partners in the pathogenesis of Alzheimer's disease","volume":"83","author":"Jayaswamy","year":"2023","journal-title":"Ageing Res. Rev."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib141","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2024.114070","article-title":"NLRP3 Cys126 palmitoylation by ZDHHC7 promotes inflammasome activation","volume":"43","author":"Yu","year":"2024","journal-title":"Cell Rep."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118429_bib142","doi-asserted-by":"crossref","DOI":"10.1016\/j.molcel.2022.12.002","article-title":"Palmitoylation prevents sustained inflammation by limiting NLRP3 inflammasome activation through chaperone-mediated autophagy","volume":"83","author":"Wang","year":"2023","journal-title":"Mol Cell"},{"key":"10.1016\/j.ejmech.2025.118429_bib143","article-title":"The role of NLRP3 inflammasome in Alzheimer's Disease and potential therapeutic targets","volume":"13","author":"Liang","year":"2022","journal-title":"Front. Pharmacol."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib144","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1038\/s41392-024-01971-5","article-title":"Palmitoylation regulates myelination by modulating the ZDHHC3-Cadm4 axis in the central nervous system","volume":"9","author":"Chang","year":"2024","journal-title":"Signal Transduct Target Ther"},{"issue":"6","key":"10.1016\/j.ejmech.2025.118429_bib145","doi-asserted-by":"crossref","first-page":"3793","DOI":"10.1074\/jbc.M808920200","article-title":"Alzheimer disease Abeta production in the absence of S-palmitoylation-dependent targeting of BACE1 to lipid rafts","volume":"284","author":"Vetrivel","year":"2009","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib146","article-title":"Synaptic proteins in CSF relate to Parkinson's disease stage markers","volume":"3","author":"Bereczki","year":"2017","journal-title":"npj Parkinson's Dis."},{"key":"10.1016\/j.ejmech.2025.118429_bib147","doi-asserted-by":"crossref","DOI":"10.3389\/fnagi.2025.1566465","article-title":"Calcineurin-mediated regulation of growth-associated protein 43 is essential for neurite and synapse formation and protects against \u03b1-synuclein-induced degeneration","volume":"17","author":"Grebenik","year":"2025","journal-title":"Front. Aging Neurosci."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118429_bib148","doi-asserted-by":"crossref","first-page":"2707","DOI":"10.1021\/acschemneuro.8b00558","article-title":"Palmitoylation by multiple DHHC enzymes enhances dopamine transporter function and stability","volume":"10","author":"Bolland","year":"2019","journal-title":"ACS Chem. Neurosci."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib149","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1038\/s41531-021-00161-2","article-title":"Dynamic control of the dopamine transporter in neurotransmission and homeostasis","volume":"7","author":"Bu","year":"2021","journal-title":"npj Parkinson's Dis."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118429_bib150","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1038\/s41418-018-0124-5","article-title":"MPTP-driven NLRP3 inflammasome activation in microglia plays a central role in dopaminergic neurodegeneration","volume":"26","author":"Lee","year":"2019","journal-title":"Cell Death Differ."},{"issue":"36","key":"10.1016\/j.ejmech.2025.118429_bib151","doi-asserted-by":"crossref","first-page":"8897","DOI":"10.1523\/JNEUROSCI.2171-08.2008","article-title":"Fibroblast growth factor-regulated palmitoylation of the neural cell adhesion molecule determines neuronal morphogenesis","volume":"28","author":"Ponimaskin","year":"2008","journal-title":"J. Neurosci."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118429_bib152","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1111\/jnc.12236","article-title":"Progression in multiple sclerosis is associated with low endogenous NCAM","volume":"125","author":"Gnanapavan","year":"2013","journal-title":"J. Neurochem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib153","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-023-43650-z","article-title":"Cyclical palmitoylation regulates TLR9 signalling and systemic autoimmunity in mice","volume":"15","author":"Ni","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.ejmech.2025.118429_bib154","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1186\/s12915-014-0091-3","article-title":"Chemoproteomics reveals toll-like receptor fatty acylation","volume":"12","author":"Chesarino","year":"2014","journal-title":"BMC Biol."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib155","first-page":"75","article-title":"Role of toll-like receptors in multiple sclerosis","volume":"2","author":"Miranda-Hernandez","year":"2013","journal-title":"Am J Clin Exp Immunol"},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib156","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-022-16840-w","article-title":"Expression of antioxidant enzymes in lesions of multiple sclerosis and its models","volume":"12","author":"Moezzi","year":"2022","journal-title":"Sci. Rep."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib157","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-017-16457-4","article-title":"DHHC5-mediated palmitoylation of S1P receptor subtype 1 determines G-protein coupling","volume":"7","author":"Badawy","year":"2017","journal-title":"Sci. Rep."},{"issue":"10306","key":"10.1016\/j.ejmech.2025.118429_bib158","doi-asserted-by":"crossref","first-page":"1184","DOI":"10.1016\/S0140-6736(21)00244-0","article-title":"Sphingosine 1-phosphate receptor modulators in multiple sclerosis and other conditions","volume":"398","author":"McGinley","year":"2021","journal-title":"Lancet"},{"issue":"2","key":"10.1016\/j.ejmech.2025.118429_bib159","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1002\/glia.24113","article-title":"DHHC5 facilitates oligodendrocyte development by palmitoylating and activating STAT3","volume":"70","author":"Ma","year":"2022","journal-title":"Glia"},{"issue":"7829","key":"10.1016\/j.ejmech.2025.118429_bib160","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1038\/s41586-020-2799-2","article-title":"A STAT3 palmitoylation cycle promotes T H 17 differentiation and colitis","volume":"586","author":"Zhang","year":"2020","journal-title":"Nature"},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib161","doi-asserted-by":"crossref","DOI":"10.1172\/jci.insight.142376","article-title":"A STAT3 inhibitor ameliorates CNS autoimmunity by restoring teff:treg balance","volume":"6","author":"Aqel","year":"2021","journal-title":"JCI Insight"},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib162","doi-asserted-by":"crossref","first-page":"6370","DOI":"10.1038\/s41467-023-42170-0","article-title":"Palmitoylation-driven PHF2 ubiquitination remodels lipid metabolism through the SREBP1c axis in hepatocellular carcinoma","volume":"14","author":"Jeong","year":"2023","journal-title":"Nat. Commun."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118429_bib163","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1038\/nn1702","article-title":"Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function","volume":"9","author":"Yanai","year":"2006","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.ejmech.2025.118429_bib164","doi-asserted-by":"crossref","DOI":"10.1016\/j.nbd.2021.105479","article-title":"Rescue of aberrant huntingtin palmitoylation ameliorates mutant huntingtin-induced toxicity","volume":"158","author":"Lemari\u00e9","year":"2021","journal-title":"Neurobiol. Dis."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib165","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1111\/j.1471-4159.2007.04703.x","article-title":"Loss of SNAP-25 and rabphilin 3a in sensory-motor cortex in Huntington's disease","volume":"103","author":"Smith","year":"2007","journal-title":"J. Neurochem."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118429_bib166","doi-asserted-by":"crossref","first-page":"3518","DOI":"10.1074\/jbc.M113.513945","article-title":"Bidirectional control of postsynaptic density-95 (PSD-95) clustering by Huntingtin","volume":"289","author":"Parsons","year":"2014","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib167","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0146466","article-title":"Reversible cysteine acylation regulates the activity of Human palmitoyl-protein thioesterase 1 (PPT1)","volume":"11","author":"Segal-Salto","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.ejmech.2025.118429_bib168","doi-asserted-by":"crossref","first-page":"25","DOI":"10.3389\/fnsyn.2019.00025","article-title":"Depalmitoylation by palmitoyl-protein thioesterase 1 in neuronal health and degeneration","volume":"11","author":"Koster","year":"2019","journal-title":"Front. Synaptic Neurosci."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib169","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.3001590","article-title":"Identification of substrates of palmitoyl protein thioesterase 1 highlights roles of depalmitoylation in disulfide bond formation and synaptic function","volume":"20","author":"Gorenberg","year":"2022","journal-title":"PLoS Biol."},{"key":"10.1016\/j.ejmech.2025.118429_bib170","doi-asserted-by":"crossref","DOI":"10.3389\/fphys.2023.1166125","article-title":"Lost in traffic: consequences of altered palmitoylation in neurodegeneration","volume":"14","author":"Ramzan","year":"2023","journal-title":"Front. Physiol."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118429_bib171","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1093\/procel\/pwae026","article-title":"Alzheimer's disease: insights into pathology, molecular mechanisms, and therapy","volume":"16","author":"Zheng","year":"2025","journal-title":"Protein Cell"},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib172","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1159\/000369101","article-title":"Amyloid-beta: a crucial factor in Alzheimer's disease","volume":"24","author":"Sadigh-Eteghad","year":"2015","journal-title":"Med. Princ. Pract."},{"issue":"40","key":"10.1016\/j.ejmech.2025.118429_bib173","doi-asserted-by":"crossref","DOI":"10.1523\/JNEUROSCI.1225-24.2024","article-title":"Altered protein palmitoylation as disease mechanism in neurodegenerative disorders","volume":"44","author":"Wlodarczyk","year":"2024","journal-title":"J. Neurosci."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118429_bib174","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/j.pneurobio.2011.11.002","article-title":"Putting proteins in their place: palmitoylation in Huntington disease and other neuropsychiatric diseases","volume":"97","author":"Young","year":"2012","journal-title":"Prog Neurobiol"},{"key":"10.1016\/j.ejmech.2025.118429_bib175","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.phrs.2016.06.008","article-title":"Palmitoylation in Alzheimer's disease and other neurodegenerative diseases","volume":"111","author":"Cho","year":"2016","journal-title":"Pharmacol. Res."},{"issue":"27","key":"10.1016\/j.ejmech.2025.118429_bib176","doi-asserted-by":"crossref","first-page":"11169","DOI":"10.1523\/JNEUROSCI.4704-12.2013","article-title":"Palmitoylation of amyloid precursor protein regulates amyloidogenic processing in lipid rafts","volume":"33","author":"Bhattacharyya","year":"2013","journal-title":"J. Neurosci."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib177","doi-asserted-by":"crossref","DOI":"10.1085\/jgp.202112888","article-title":"Neuronal KCNQ2\/3 channels are recruited to lipid raft microdomains by palmitoylation of BACE1","volume":"154","author":"Dai","year":"2022","journal-title":"J. Gen. Physiol."},{"issue":"5495","key":"10.1016\/j.ejmech.2025.118429_bib178","doi-asserted-by":"crossref","first-page":"1364","DOI":"10.1126\/science.290.5495.1364","article-title":"PSD-95 involvement in maturation of excitatory synapses","volume":"290","author":"El-Husseini","year":"2000","journal-title":"Science"},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib179","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1083\/jcb.200903101","article-title":"Mobile DHHC palmitoylating enzyme mediates activity-sensitive synaptic targeting of PSD-95","volume":"186","author":"Noritake","year":"2009","journal-title":"J. Cell Biol."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118429_bib180","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1016\/S0002-9440(10)63436-0","article-title":"Synaptic changes in Alzheimer's disease: increased amyloid-beta and gliosis in surviving terminals is accompanied by decreased PSD-95 fluorescence","volume":"165","author":"Gylys","year":"2004","journal-title":"Am. J. Pathol."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib181","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1007\/s00401-011-0843-x","article-title":"Postsynaptic degeneration as revealed by PSD-95 reduction occurs after advanced A\u03b2 and tau pathology in transgenic mouse models of Alzheimer's disease","volume":"122","author":"Shao","year":"2011","journal-title":"Acta Neuropathol."},{"issue":"9","key":"10.1016\/j.ejmech.2025.118429_bib182","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2021.109194","article-title":"PSD-95 protects synapses from \u03b2-amyloid","volume":"35","author":"Dore","year":"2021","journal-title":"Cell Rep."},{"issue":"13","key":"10.1016\/j.ejmech.2025.118429_bib183","doi-asserted-by":"crossref","DOI":"10.1242\/jcs.230052","article-title":"Regulation of dendrite morphology and excitatory synapse formation by zDHHC15","volume":"132","author":"Shah","year":"2019","journal-title":"J. Cell Sci."},{"issue":"21","key":"10.1016\/j.ejmech.2025.118429_bib184","doi-asserted-by":"crossref","first-page":"7501","DOI":"10.1074\/jbc.RA120.012726","article-title":"The linker domain of the SNARE protein SNAP25 acts as a flexible molecular spacer that ensures efficient S-acylation","volume":"295","author":"Salaun","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2025.118429_bib185","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1186\/1750-1326-9-53","article-title":"SNAP-25 is a promising novel cerebrospinal fluid biomarker for synapse degeneration in Alzheimer's disease","volume":"9","author":"Brinkmalm","year":"2014","journal-title":"Mol. Neurodegener."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118429_bib186","doi-asserted-by":"crossref","first-page":"1864","DOI":"10.1046\/j.1471-4159.1997.69051864.x","article-title":"Characterization of the palmitoylation domain of SNAP-25","volume":"69","author":"Lane","year":"1997","journal-title":"J. Neurochem."},{"issue":"8","key":"10.1016\/j.ejmech.2025.118429_bib187","doi-asserted-by":"crossref","first-page":"1244","DOI":"10.1016\/j.celrep.2015.07.044","article-title":"Amyloid-\u03b2 oligomers May impair SNARE-Mediated exocytosis by direct binding to Syntaxin 1a","volume":"12","author":"Yang","year":"2015","journal-title":"Cell Rep."},{"issue":"22","key":"10.1016\/j.ejmech.2025.118429_bib188","doi-asserted-by":"crossref","DOI":"10.3390\/ijms232214018","article-title":"Altered cortical palmitoylation induces widespread molecular disturbances in Parkinson's Disease","volume":"23","author":"Cervilla-Mart\u00ednez","year":"2022","journal-title":"Int. J. Mol. Sci."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib189","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/S0896-6273(00)80705-9","article-title":"Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs","volume":"22","author":"Craven","year":"1999","journal-title":"Neuron"},{"key":"10.1016\/j.ejmech.2025.118429_bib190","doi-asserted-by":"crossref","first-page":"4","DOI":"10.3389\/neuro.02.004.2008","article-title":"Excitation control: balancing PSD-95 function at the synapse","volume":"1","author":"Keith","year":"2008","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.ejmech.2025.118429_bib191","doi-asserted-by":"crossref","DOI":"10.1016\/j.chemosphere.2019.124378","article-title":"Synaptic dopamine release is positively regulated by SNAP-25 that involves in benzo[a]pyrene-induced neurotoxicity","volume":"237","author":"Yang","year":"2019","journal-title":"Chemosphere"},{"issue":"7","key":"10.1016\/j.ejmech.2025.118429_bib192","doi-asserted-by":"crossref","first-page":"5175","DOI":"10.1074\/jbc.M110.187872","article-title":"Palmitoylation controls dopamine transporter kinetics, degradation, and protein kinase C-dependent regulation","volume":"286","author":"Foster","year":"2011","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib193","doi-asserted-by":"crossref","first-page":"200","DOI":"10.3934\/Neuroscience.2023017","article-title":"Depletion of dopamine in Parkinson's disease and relevant therapeutic options: a review of the literature","volume":"10","author":"Ramesh","year":"2023","journal-title":"AIMS Neurosci"},{"issue":"48","key":"10.1016\/j.ejmech.2025.118429_bib194","doi-asserted-by":"crossref","first-page":"29095","DOI":"10.1074\/jbc.M115.667055","article-title":"Reciprocal phosphorylation and palmitoylation Control dopamine transporter kinetics","volume":"290","author":"Moritz","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2025.118429_bib195","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.neuroscience.2024.12.029","article-title":"A review on multiple sclerosis: unravelling the complexities of pathogenesis, progression, mechanisms and therapeutic innovations","volume":"567","author":"Rida","year":"2025","journal-title":"Neuroscience"},{"key":"10.1016\/j.ejmech.2025.118429_bib196","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2021.653101","article-title":"Neuron-Oligodendrocyte interactions in the structure and integrity of axons","volume":"9","author":"Duncan","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.ejmech.2025.118429_bib197","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1016\/j.nbd.2016.03.023","article-title":"Activation of oligodendroglial Stat3 is required for efficient remyelination","volume":"91","author":"Steelman","year":"2016","journal-title":"Neurobiol. Dis."},{"issue":"888","key":"10.1016\/j.ejmech.2025.118429_bib198","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.adr2008","article-title":"SMAD2 S-palmitoylation promotes its linker region phosphorylation and T H 17 cell differentiation in a mouse model of multiple sclerosis","volume":"18","author":"Zhang","year":"2025","journal-title":"Sci. Signal."},{"issue":"8","key":"10.1016\/j.ejmech.2025.118429_bib199","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1111\/j.1365-2443.2009.01319.x","article-title":"Palmitoylation of the sphingosine 1-phosphate receptor S1P is involved in its signaling functions and internalization","volume":"14","author":"Ohno","year":"2009","journal-title":"Genes Cells"},{"key":"10.1016\/j.ejmech.2025.118429_bib200","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.97151","article-title":"Micro-scale control of oligodendrocyte morphology and myelination by the intellectual disability-linked protein acyltransferase ZDHHC9","volume":"13","author":"Jeong","year":"2025","journal-title":"eLife"},{"issue":"7","key":"10.1016\/j.ejmech.2025.118429_bib201","doi-asserted-by":"crossref","first-page":"1452","DOI":"10.1002\/glia.70016","article-title":"The X-Linked intellectual disability gene, ZDHHC9 , is important for oligodendrocyte subtype determination and myelination","volume":"73","author":"White","year":"2025","journal-title":"Glia"},{"key":"10.1016\/j.ejmech.2025.118429_bib202","article-title":"Huntington disease: advances in the understanding of its mechanisms","volume":"3","author":"Gatto","year":"2020","journal-title":"Clin Park Relat Disord"},{"issue":"7","key":"10.1016\/j.ejmech.2025.118429_bib203","doi-asserted-by":"crossref","DOI":"10.3390\/ijms25073845","article-title":"Huntington's disease: complex pathogenesis and therapeutic strategies","volume":"25","author":"Tong","year":"2024","journal-title":"Int. J. Mol. Sci."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib204","doi-asserted-by":"crossref","first-page":"1385","DOI":"10.1042\/BST20231290","article-title":"Let's get fat: emergence of S-acylation as a therapeutic target in Huntington disease","volume":"52","author":"Martin","year":"2024","journal-title":"Biochem. Soc. Trans."},{"issue":"20","key":"10.1016\/j.ejmech.2025.118429_bib205","doi-asserted-by":"crossref","first-page":"3899","DOI":"10.1093\/hmg\/ddr308","article-title":"Altered palmitoylation and neuropathological deficits in mice lacking HIP14","volume":"20","author":"Singaraja","year":"2011","journal-title":"Hum. Mol. Genet."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118429_bib206","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0036315","article-title":"Low levels of human HIP14 are sufficient to rescue neuropathological, behavioural, and enzymatic defects due to loss of murine HIP14 in Hip14-\/- mice","volume":"7","author":"Young","year":"2012","journal-title":"PLoS One"},{"issue":"14","key":"10.1016\/j.ejmech.2025.118429_bib207","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abb0799","article-title":"Increasing brain palmitoylation rescues behavior and neuropathology in Huntington disease mice","volume":"7","author":"Virlogeux","year":"2021","journal-title":"Sci. Adv."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib208","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1111\/cns.12804","article-title":"Potassium channel dysfunction in neurons and astrocytes in Huntington's disease","volume":"24","author":"Zhang","year":"2018","journal-title":"CNS Neurosci. Ther."},{"issue":"S1","key":"10.1016\/j.ejmech.2025.118429_bib209","doi-asserted-by":"crossref","DOI":"10.1096\/fasebj.28.1_supplement.466.1","article-title":"Molecular basis of infantile Batten disease: impact of disordered palmitoylated protein degradation on the nervous system (466.1)","volume":"28","author":"Hofmann","year":"2014","journal-title":"FASEB J."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118429_bib210","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1093\/hmg\/ddi451","article-title":"Palmitoyl-protein thioesterase-1 deficiency mediates the activation of the unfolded protein response and neuronal apoptosis in INCL","volume":"15","author":"Zhang","year":"2006","journal-title":"Hum. Mol. Genet."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib211","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1093\/hmg\/10.1.69","article-title":"Palmitoyl protein thioesterase (PPT) localizes into synaptosomes and synaptic vesicles in neurons: implications for infantile neuronal ceroid lipofuscinosis (INCL)","volume":"10","author":"Lehtovirta","year":"2001","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.ejmech.2025.118429_bib212","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.40316","article-title":"Developmental NMDA receptor dysregulation in the infantile neuronal ceroid lipofuscinosis mouse model","volume":"8","author":"Koster","year":"2019","journal-title":"eLife"},{"key":"10.1016\/j.ejmech.2025.118429_bib213","doi-asserted-by":"crossref","first-page":"92","DOI":"10.3389\/fncel.2019.00092","article-title":"The interactome of palmitoyl-protein thioesterase 1 (PPT1) affects neuronal morphology and function","volume":"13","author":"Sapir","year":"2019","journal-title":"Front. Cell. Neurosci."},{"key":"10.1016\/j.ejmech.2025.118429_bib214","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.cbpa.2021.07.002","article-title":"Inhibitors of DHHC family proteins","volume":"65","author":"Lan","year":"2021","journal-title":"Curr. Opin. Chem. Biol."},{"issue":"10","key":"10.1016\/j.ejmech.2025.118429_bib215","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0075232","article-title":"2-Bromopalmitate reduces protein deacylation by inhibition of acyl-protein thioesterase enzymatic activities","volume":"8","author":"Pedro","year":"2013","journal-title":"PLoS One"},{"issue":"2","key":"10.1016\/j.ejmech.2025.118429_bib216","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1194\/jlr.M800270-JLR200","article-title":"2-Bromopalmitate and 2-(2-hydroxy-5-nitro-benzylidene)-benzo[b]thiophen-3-one inhibit DHHC-mediated palmitoylation in vitro","volume":"50","author":"Jennings","year":"2009","journal-title":"J. Lipid Res."},{"issue":"9","key":"10.1016\/j.ejmech.2025.118429_bib217","doi-asserted-by":"crossref","first-page":"1912","DOI":"10.1021\/cb400380s","article-title":"Profiling targets of the irreversible palmitoylation inhibitor 2-bromopalmitate","volume":"8","author":"Davda","year":"2013","journal-title":"ACS Chem. Biol."},{"issue":"8","key":"10.1016\/j.ejmech.2025.118429_bib218","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1021\/acschembio.1c00405","article-title":"Development of an acrylamide-based inhibitor of protein S-Acylation","volume":"16","author":"Azizi","year":"2021","journal-title":"ACS Chem. Biol."},{"issue":"4","key":"10.1016\/j.ejmech.2025.118429_bib219","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1083\/jcb.124.4.521","article-title":"Novel inhibitory action of tunicamycin homologues suggests a role for dynamic protein fatty acylation in growth cone-mediated neurite extension","volume":"124","author":"Patterson","year":"1994","journal-title":"J. Cell Biol."},{"issue":"24","key":"10.1016\/j.ejmech.2025.118429_bib220","doi-asserted-by":"crossref","first-page":"4932","DOI":"10.1021\/jm980591s","article-title":"Structure-activity studies of cerulenin analogues as protein palmitoylation inhibitors","volume":"42","author":"Lawrence","year":"1999","journal-title":"J. Med. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib221","doi-asserted-by":"crossref","first-page":"3632","DOI":"10.1038\/s41598-019-39968-8","article-title":"Identification of novel inhibitors of DLK palmitoylation and signaling by high content screening","volume":"9","author":"Martin","year":"2019","journal-title":"Sci. Rep."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib222","doi-asserted-by":"crossref","DOI":"10.1016\/j.chembiol.2021.07.012","article-title":"Artemisinin inhibits NRas palmitoylation by targeting the protein acyltransferase ZDHHC6","volume":"29","author":"Qiu","year":"2022","journal-title":"Cell Chem. Biol."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118429_bib223","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0125399","article-title":"Curcumin prevents palmitoylation of Integrin \u03b24 in breast cancer cells","volume":"10","author":"Coleman","year":"2015","journal-title":"PLoS One"},{"issue":"10","key":"10.1016\/j.ejmech.2025.118429_bib224","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.102469","article-title":"Development of a novel high-throughput screen for the identification of new inhibitors of protein S-acylation","volume":"298","author":"Salaun","year":"2022","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2025.118429_bib225","article-title":"A selective S-acyltransferase inhibitor suppresses tumor growth","author":"Lee","year":"2024","journal-title":"bioRxiv [Preprint]"},{"issue":"10","key":"10.1016\/j.ejmech.2025.118429_bib226","doi-asserted-by":"crossref","first-page":"11870","DOI":"10.1021\/acsomega.3c09607","article-title":"Identification of new modulators and inhibitors of palmitoyl-protein thioesterase 1 for CLN1 batten disease and cancer","volume":"9","author":"Puhl","year":"2024","journal-title":"ACS Omega"},{"issue":"11","key":"10.1016\/j.ejmech.2025.118429_bib227","doi-asserted-by":"crossref","first-page":"2413","DOI":"10.1194\/jlr.M030411","article-title":"Biochemical and pharmacological characterization of human \u03b1\/\u03b2-hydrolase domain containing 6 (ABHD6) and 12 (ABHD12)","volume":"53","author":"Navia-Paldanius","year":"2012","journal-title":"J. Lipid Res."},{"issue":"42","key":"10.1016\/j.ejmech.2025.118429_bib228","doi-asserted-by":"crossref","first-page":"9832","DOI":"10.1002\/anie.201102965","article-title":"Development of highly potent inhibitors of the ras-targeting human acyl protein thioesterases based on substrate similarity design","volume":"50","author":"Hedberg","year":"2011","journal-title":"Angew Chem. Int. Ed. Engl."},{"issue":"42","key":"10.1016\/j.ejmech.2025.118429_bib229","doi-asserted-by":"crossref","first-page":"9838","DOI":"10.1002\/anie.201102967","article-title":"Identification of acyl protein thioesterases 1 and 2 as the cellular targets of the ras-signaling modulators palmostatin B and M","volume":"50","author":"Rusch","year":"2011","journal-title":"Angew Chem Int Ed Engl."},{"key":"10.1016\/j.ejmech.2025.118429_bib230","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmcl.2021.128414","article-title":"Chemical proteomic analysis of palmostatin beta-lactone analogs that affect N-Ras palmitoylation","volume":"53","author":"Suciu","year":"2021","journal-title":"Bioorg Med Chem Lett"},{"issue":"21","key":"10.1016\/j.ejmech.2025.118429_bib231","doi-asserted-by":"crossref","first-page":"8253","DOI":"10.1073\/pnas.1118193109","article-title":"Autophagy inhibitor Lys05 has single-agent antitumor activity and reproduces the phenotype of a genetic autophagy deficiency","volume":"109","author":"McAfee","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"11","key":"10.1016\/j.ejmech.2025.118429_bib232","doi-asserted-by":"crossref","first-page":"1266","DOI":"10.1158\/2159-8290.CD-17-0741","article-title":"A unified approach to targeting the lysosome's degradative and growth signaling roles","volume":"7","author":"Rebecca","year":"2017","journal-title":"Cancer Discov."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118429_bib233","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1158\/2159-8290.CD-18-0706","article-title":"PPT1 promotes tumor growth and is the molecular target of chloroquine derivatives in cancer","volume":"9","author":"Rebecca","year":"2019","journal-title":"Cancer Discov."},{"issue":"7","key":"10.1016\/j.ejmech.2025.118429_bib234","doi-asserted-by":"crossref","first-page":"928","DOI":"10.1016\/j.chembiol.2015.05.018","article-title":"Selective N-Hydroxyhydantoin carbamate inhibitors of Mammalian serine hydrolases","volume":"22","author":"Cognetta","year":"2015","journal-title":"Chem Biol"},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib235","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1159\/000522418","article-title":"First-In-Human effects of PPT1 inhibition using the oral treatment with GNS561\/Ezurpimtrostat in patients with primary and secondary liver cancers","volume":"11","author":"Harding","year":"2022","journal-title":"Liver Cancer"},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib236","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1080\/15548627.2021.1988357","article-title":"GNS561, a clinical-stage PPT1 inhibitor, is efficient against hepatocellular carcinoma","volume":"18","author":"Brun","year":"2022","journal-title":"Autophagy"},{"issue":"6","key":"10.1016\/j.ejmech.2025.118429_bib237","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1007\/s10637-019-00741-3","article-title":"GNS561, a new lysosomotropic small molecule, for the treatment of intrahepatic cholangiocarcinoma","volume":"37","author":"Brun","year":"2019","journal-title":"Invest New Drugs"},{"issue":"31","key":"10.1016\/j.ejmech.2025.118429_bib238","doi-asserted-by":"crossref","first-page":"4975","DOI":"10.1002\/anie.200462625","article-title":"Development and biological evaluation of acyl protein thioesterase 1 (APT1) inhibitors","volume":"44","author":"Deck","year":"2005","journal-title":"Angew Chem. Int. Ed. Engl."},{"issue":"15","key":"10.1016\/j.ejmech.2025.118429_bib239","doi-asserted-by":"crossref","first-page":"4121","DOI":"10.1002\/chem.200501128","article-title":"Synthesis and evaluation of acyl protein thioesterase 1 (APT1) inhibitors","volume":"12","author":"Biel","year":"2006","journal-title":"Chemistry"},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib240","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1002\/cbic.201200571","article-title":"Boron-based inhibitors of acyl protein thioesterases 1 and 2","volume":"14","author":"Zimmermann","year":"2013","journal-title":"Chembiochem"},{"key":"10.1016\/j.ejmech.2025.118429_bib241","series-title":"Probe Reports from the NIH Molecular Libraries Program","article-title":"An in Vivo Active Carbamate-based Dual Inhibitor of Lysophospholipase 1 (LYPLA1) and Lysophospholipase 2 (LYPLA2)","author":"Hulce","year":"2014"},{"key":"10.1016\/j.ejmech.2025.118429_bib242","series-title":"Probe Reports from the NIH Molecular Libraries Program","article-title":"Optimization and characterization of a triazole urea dual inhibitor for lysophospholipase 1 (LYPLA1) and lysophospholipase 2 (LYPLA2)","author":"Adibekian","year":"2011"},{"issue":"8","key":"10.1016\/j.ejmech.2025.118429_bib243","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1038\/s41589-021-00785-8","article-title":"ABHD17 regulation of plasma membrane palmitoylation and N-Ras-dependent cancer growth","volume":"17","author":"Remsberg","year":"2021","journal-title":"Nat. Chem. Biol."},{"issue":"9","key":"10.1016\/j.ejmech.2025.118429_bib244","doi-asserted-by":"crossref","first-page":"2529","DOI":"10.1021\/acschembio.6b00266","article-title":"Discovery of a selective covalent inhibitor of lysophospholipase-like 1 (LYPLAL1) as a tool to evaluate the role of this serine hydrolase in metabolism","volume":"11","author":"Ahn","year":"2016","journal-title":"ACS Chem. Biol."},{"issue":"9","key":"10.1016\/j.ejmech.2025.118429_bib245","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1038\/s41589-020-0555-4","article-title":"Discovery of small-molecule enzyme activators by activity-based protein profiling","volume":"16","author":"Kok","year":"2020","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.ejmech.2025.118429_bib246","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2020.112353","article-title":"Therapeutic potential of targeting \u03b1\/\u03b2-Hydrolase domain-containing 6 (ABHD6)","volume":"198","author":"Deng","year":"2020","journal-title":"Eur. J. Med. Chem."},{"issue":"15","key":"10.1016\/j.ejmech.2025.118429_bib247","doi-asserted-by":"crossref","first-page":"6610","DOI":"10.1021\/jm500681z","article-title":"Discovery of glycine sulfonamides as dual inhibitors of sn-1-diacylglycerol lipase \u03b1 and \u03b1\/\u03b2-hydrolase domain 6","volume":"57","author":"Janssen","year":"2014","journal-title":"J. Med. Chem."},{"issue":"20","key":"10.1016\/j.ejmech.2025.118429_bib248","doi-asserted-by":"crossref","first-page":"9062","DOI":"10.1021\/acs.jmedchem.8b00951","article-title":"Identification of ABX-1431, a selective inhibitor of Monoacylglycerol lipase and clinical candidate for treatment of neurological disorders","volume":"61","author":"Cisar","year":"2018","journal-title":"J. Med. Chem."},{"issue":"33","key":"10.1016\/j.ejmech.2025.118429_bib249","doi-asserted-by":"crossref","first-page":"28723","DOI":"10.1074\/jbc.M110.202853","article-title":"Dual inhibition of alpha\/beta-hydrolase domain 6 and fatty acid amide hydrolase increases endocannabinoid levels in neurons","volume":"286","author":"Marrs","year":"2011","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.ejmech.2025.118429_bib250","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1073\/pnas.1522364112","article-title":"Rapid and profound rewiring of brain lipid signaling networks by acute diacylglycerol lipase inhibition","volume":"113","author":"Ogasawara","year":"2016","journal-title":"Proc Natl Acad Sci U S A."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118429_bib251","doi-asserted-by":"crossref","first-page":"982","DOI":"10.1039\/C7MD00029D","article-title":"Chiral disubstituted piperidinyl ureas: a class of dual diacylglycerol lipase-\u03b1 and ABHD6 inhibitors","volume":"8","author":"Deng","year":"2017","journal-title":"Medchemcomm"},{"issue":"31","key":"10.1016\/j.ejmech.2025.118429_bib252","doi-asserted-by":"crossref","first-page":"9594","DOI":"10.1021\/ja073650c","article-title":"A functional proteomic strategy to discover inhibitors for uncharacterized hydrolases","volume":"129","author":"Li","year":"2007","journal-title":"J. Am. Chem. Soc."},{"issue":"49","key":"10.1016\/j.ejmech.2025.118429_bib253","doi-asserted-by":"crossref","first-page":"20941","DOI":"10.1073\/pnas.1011663107","article-title":"Superfamily-wide portrait of serine hydrolase inhibition achieved by library-versus-library screening","volume":"107","author":"Bachovchin","year":"2010","journal-title":"Proc Natl Acad Sci U S A."},{"issue":"2","key":"10.1016\/j.ejmech.2025.118429_bib254","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1002\/cmdc.201402453","article-title":"Optimization of 1,2,5-thiadiazole carbamates as potent and selective ABHD6 inhibitors","volume":"10","author":"Patel","year":"2015","journal-title":"ChemMedChem"},{"issue":"21","key":"10.1016\/j.ejmech.2025.118429_bib255","doi-asserted-by":"crossref","DOI":"10.1002\/cmdc.202100406","article-title":"Design and synthesis of highly potent and specific ABHD6 inhibitors","volume":"18","author":"Malamas","year":"2023","journal-title":"ChemMedChem"},{"issue":"21","key":"10.1016\/j.ejmech.2025.118429_bib256","doi-asserted-by":"crossref","first-page":"8270","DOI":"10.1021\/jm400899c","article-title":"Discovery and optimization of piperidyl-1,2,3-triazole ureas as potent, selective, and in vivo-active inhibitors of \u03b1\/\u03b2-hydrolase domain containing 6 (ABHD6)","volume":"56","author":"Hsu","year":"2013","journal-title":"J. Med. Chem."},{"issue":"11","key":"10.1016\/j.ejmech.2025.118429_bib257","doi-asserted-by":"crossref","first-page":"5068","DOI":"10.1021\/ja300799t","article-title":"Competitive activity-based protein profiling identifies aza-\u03b2-lactams as a versatile chemotype for serine hydrolase inhibition","volume":"134","author":"Zuhl","year":"2012","journal-title":"J. Am. Chem. Soc."},{"issue":"6","key":"10.1016\/j.ejmech.2025.118429_bib258","doi-asserted-by":"crossref","first-page":"2659","DOI":"10.1021\/ja412431g","article-title":"Remodeling natural products: chemistry and serine hydrolase activity of a rocaglate-derived \u03b2-lactone","volume":"136","author":"Lajkiewicz","year":"2014","journal-title":"J. Am. Chem. Soc."},{"issue":"17","key":"10.1016\/j.ejmech.2025.118429_bib259","doi-asserted-by":"crossref","first-page":"3608","DOI":"10.1039\/C4CC09107H","article-title":"Facile synthesis of borofragments and their evaluation in activity-based protein profiling","volume":"51","author":"Adachi","year":"2015","journal-title":"Chem. Commun."},{"issue":"5","key":"10.1016\/j.ejmech.2025.118429_bib260","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0098286","article-title":"Discovery of triterpenoids as reversible inhibitors of \u03b1\/\u03b2-hydrolase domain containing 12 (ABHD12)","volume":"9","author":"Parkkari","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.ejmech.2025.118429_bib261","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/j.fitote.2018.02.027","article-title":"New cycloartane-type ester triterpenes from Euphorbia pterococca and biological evaluation","volume":"127","author":"Benabdelaziz","year":"2018","journal-title":"Fitoterapia"},{"issue":"12","key":"10.1016\/j.ejmech.2025.118429_bib262","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1038\/s41589-018-0155-8","article-title":"Selective blockade of the lyso-PS lipase ABHD12 stimulates immune responses in vivo","volume":"14","author":"Ogasawara","year":"2018","journal-title":"Nat. Chem. Biol."},{"issue":"3","key":"10.1016\/j.ejmech.2025.118429_bib263","doi-asserted-by":"crossref","first-page":"1643","DOI":"10.1021\/acs.jmedchem.8b01958","article-title":"Discovery and optimization of selective and in vivo active inhibitors of the Lysophosphatidylserine Lipase \u03b1\/\u03b2-Hydrolase domain-containing 12 (ABHD12)","volume":"62","author":"Ogasawara","year":"2019","journal-title":"J. Med. Chem."},{"issue":"10","key":"10.1016\/j.ejmech.2025.118429_bib264","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0109869","article-title":"Biochemical and pharmacological characterization of the human lymphocyte antigen B-associated transcript 5 (BAT5\/ABHD16A)","volume":"9","author":"Savinainen","year":"2014","journal-title":"PLoS One"},{"issue":"2","key":"10.1016\/j.ejmech.2025.118429_bib265","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1038\/nchembio.1721","article-title":"Immunomodulatory lysophosphatidylserines are regulated by ABHD16A and ABHD12 interplay","volume":"11","author":"Kamat","year":"2015","journal-title":"Nat. Chem. Biol."},{"issue":"12","key":"10.1016\/j.ejmech.2025.118429_bib266","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1021\/acsmedchemlett.8b00442","article-title":"Discovery of 12-Thiazole abietanes as selective inhibitors of the Human Metabolic Serine hydrolase hABHD16A","volume":"9","author":"Ahonen","year":"2018","journal-title":"ACS Med. Chem. Lett."},{"issue":"22","key":"10.1016\/j.ejmech.2025.118429_bib267","doi-asserted-by":"crossref","first-page":"5838","DOI":"10.1016\/j.bmcl.2008.06.091","article-title":"Selectivity of inhibitors of endocannabinoid biosynthesis evaluated by activity-based protein profiling","volume":"18","author":"Hoover","year":"2008","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.ejmech.2025.118429_bib268","series-title":"inventorABHD12 Inhibitors and Methods of Making and Using Same","author":"Grice","year":"2020"},{"issue":"10","key":"10.1016\/j.ejmech.2025.118429_bib269","doi-asserted-by":"crossref","first-page":"1404","DOI":"10.1021\/acsmedchemlett.3c00313","article-title":"Probing the interactions of thiazole abietane inhibitors with the human serine hydrolases ABHD16A and ABHD12","volume":"14","author":"Ahonen","year":"2023","journal-title":"ACS Med. Chem. Lett."}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523425011948?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523425011948?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,6,13]],"date-time":"2026-06-13T04:50:52Z","timestamp":1781326252000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523425011948"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,2]]},"references-count":269,"alternative-id":["S0223523425011948"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2025.118429","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2026,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"S-acylation and neuroinflammation: the therapeutic potential of zDHHC and deacylase modulation","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2025.118429","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Authors. Published by Elsevier Masson SAS.","name":"copyright","label":"Copyright"}],"article-number":"118429"}}