{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,28]],"date-time":"2026-07-28T01:01:21Z","timestamp":1785200481077,"version":"3.55.0"},"reference-count":210,"publisher":"Springer Science and Business Media LLC","issue":"12","license":[{"start":{"date-parts":[[2025,8,8]],"date-time":"2025-08-08T00:00:00Z","timestamp":1754611200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2025,8,8]],"date-time":"2025-08-08T00:00:00Z","timestamp":1754611200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Neurobiol"],"published-print":{"date-parts":[[2025,12]]},"DOI":"10.1007\/s12035-025-05264-y","type":"journal-article","created":{"date-parts":[[2025,8,8]],"date-time":"2025-08-08T18:52:47Z","timestamp":1754679167000},"page":"16489-16511","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Histone Deacetylase 2 in Alzheimer\u2019s Disease: A Comprehensive Molecular Blueprint for Therapeutic Targeting"],"prefix":"10.1007","volume":"62","author":[{"ORCID":"https:\/\/orcid.org\/0009-0006-2595-0098","authenticated-orcid":false,"given":"Kavuma","family":"Asadi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2014-7224","authenticated-orcid":false,"given":"Radha","family":"K.","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4213-2664","authenticated-orcid":false,"given":"Sairaj","family":"Satarker","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3458-9664","authenticated-orcid":false,"given":"Prasada Chowdari","family":"Gurram","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,8,8]]},"reference":[{"key":"5264_CR1","doi-asserted-by":"publisher","first-page":"104052","DOI":"10.1016\/j.drudis.2024.104052","volume":"29","author":"M Pereira","year":"2024","unstructured":"Pereira M, Cruz MT, Fortuna A, Bicker J (2024) Restoring the epigenome in Alzheimer\u2019s disease: advancing HDAC inhibitors as therapeutic agents. Drug Discov Today 29:104052. https:\/\/doi.org\/10.1016\/j.drudis.2024.104052","journal-title":"Drug Discov Today"},{"key":"5264_CR2","doi-asserted-by":"publisher","unstructured":"Gurram PC, Manandhar S, Satarker S et al (2022) Dopaminergic signaling as a plausible modulator of astrocytic toll-like receptor 4: a crosstalk between neuroinflammation and cognition. CNS Neurol Disord - Drug Targets 21. https:\/\/doi.org\/10.2174\/1871527321666220413090541","DOI":"10.2174\/1871527321666220413090541"},{"key":"5264_CR3","doi-asserted-by":"publisher","first-page":"150597","DOI":"10.1016\/j.bbrc.2024.150597","volume":"733","author":"P Chowdari Gurram","year":"2024","unstructured":"Chowdari Gurram P, Satarker S, Nampoothiri M (2024) Recent advances in the molecular signaling pathways of Substance P in Alzheimer\u2019s disease: link to neuroinflammation associated with toll-like receptors. Biochem Biophys Res Commun 733:150597. https:\/\/doi.org\/10.1016\/j.bbrc.2024.150597","journal-title":"Biochem Biophys Res Commun"},{"key":"5264_CR4","doi-asserted-by":"publisher","unstructured":"Nassar A, Nampoothiri M, Gurram PC et al (2023) Deciphering the molecular mechanism of REST regulation through DEGs and TFs in Alzheimer\u2019s disease. J Appl Pharm Sci 0:1\u201310. https:\/\/doi.org\/10.7324\/japs.2023.152245","DOI":"10.7324\/japs.2023.152245"},{"key":"5264_CR5","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41598-024-57188-7","volume":"14","author":"T Agarwal","year":"2024","unstructured":"Agarwal T, Manandhar S, Harish Kumar B et al (2024) Oxyresveratrol-\u03b2-cyclodextrin mitigates streptozotocin-induced Alzheimer\u2019s model cognitive impairment, histone deacetylase activity in rats: in silico & in vivo studies. Sci Rep 14:1\u201315. https:\/\/doi.org\/10.1038\/s41598-024-57188-7","journal-title":"Sci Rep"},{"key":"5264_CR6","doi-asserted-by":"publisher","first-page":"855","DOI":"10.1093\/jnen\/nly073","volume":"77","author":"M Ziemka-Nalecz","year":"2018","unstructured":"Ziemka-Nalecz M, Jaworska J, Sypecka J, Zalewska T (2018) Histone deacetylase inhibitors: a therapeutic key in neurological disorders? J Neuropathol Exp Neurol 77:855\u2013870. https:\/\/doi.org\/10.1093\/jnen\/nly073","journal-title":"J Neuropathol Exp Neurol"},{"key":"5264_CR7","doi-asserted-by":"publisher","first-page":"462398","DOI":"10.3389\/fphar.2020.00537","volume":"11","author":"S Shukla","year":"2020","unstructured":"Shukla S, Tekwani BL (2020) Histone deacetylases inhibitors in neurodegenerative diseases, neuroprotection and neuronal differentiation. Front Pharmacol 11:462398. https:\/\/doi.org\/10.3389\/fphar.2020.00537","journal-title":"Front Pharmacol"},{"key":"5264_CR8","doi-asserted-by":"publisher","first-page":"740","DOI":"10.2174\/1570159x18666200128125641","volume":"18","author":"VK Sharma","year":"2020","unstructured":"Sharma VK, Mehta V, Singh TG (2020) Alzheimer\u2019s disorder: epigenetic connection and associated risk factors. Curr Neuropharmacol 18:740\u2013753. https:\/\/doi.org\/10.2174\/1570159x18666200128125641","journal-title":"Curr Neuropharmacol"},{"key":"5264_CR9","doi-asserted-by":"publisher","first-page":"207","DOI":"10.1016\/B978-0-12-387665-2.00008-0","volume":"110","author":"EA Williamson","year":"2012","unstructured":"Williamson EA, Wray JW, Bansal P, Hromas R (2012) Overview for the histone codes for DNA repair. Prog Mol Biol Transl Sci 110:207\u2013227. https:\/\/doi.org\/10.1016\/B978-0-12-387665-2.00008-0","journal-title":"Prog Mol Biol Transl Sci"},{"key":"5264_CR10","doi-asserted-by":"publisher","first-page":"1563","DOI":"10.1016\/j.bcp.2006.06.016","volume":"72","author":"AS Quina","year":"2006","unstructured":"Quina AS, Buschbeck M, Di Croce L (2006) Chromatin structure and epigenetics. Biochem Pharmacol 72:1563\u20131569. https:\/\/doi.org\/10.1016\/j.bcp.2006.06.016","journal-title":"Biochem Pharmacol"},{"key":"5264_CR11","doi-asserted-by":"publisher","first-page":"4","DOI":"10.1038\/hdy.2010.54","volume":"105","author":"ER Gibney","year":"2010","unstructured":"Gibney ER, Nolan CM (2010) Epigenetics and gene expression. Heredity (Edinb) 105:4\u201313. https:\/\/doi.org\/10.1038\/hdy.2010.54","journal-title":"Heredity (Edinb)"},{"key":"5264_CR12","doi-asserted-by":"publisher","unstructured":"Kim E, H. Bisson W, V. L\u00f6hr C et al (2015) Histone and non-histone targets of dietary deacetylase inhibitors. Curr Top Med Chem 16:714\u2013731. https:\/\/doi.org\/10.2174\/1568026615666150825125857","DOI":"10.2174\/1568026615666150825125857"},{"key":"5264_CR13","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1080\/14728222.2021.1860016","volume":"25","author":"S Kumar","year":"2021","unstructured":"Kumar S, Attrish D, Srivastava A et al (2021) Non-histone substrates of histone deacetylases as potential therapeutic targets in epilepsy. Expert Opin Ther Targets 25:75\u201385. https:\/\/doi.org\/10.1080\/14728222.2021.1860016","journal-title":"Expert Opin Ther Targets"},{"key":"5264_CR14","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1016\/j.tins.2009.06.002","volume":"32","author":"DM Chuang","year":"2009","unstructured":"Chuang DM, Leng Y, Marinova Z et al (2009) Multiple roles of HDAC inhibition in neurodegenerative conditions. Trends Neurosci 32:591\u2013601. https:\/\/doi.org\/10.1016\/j.tins.2009.06.002","journal-title":"Trends Neurosci"},{"key":"5264_CR15","doi-asserted-by":"publisher","first-page":"620","DOI":"10.3390\/ph17050620","volume":"17","author":"A Curcio","year":"2024","unstructured":"Curcio A, Rocca R, Alcaro S, Artese A (2024) The histone deacetylase family: structural features and application of combined computational methods. Pharmaceuticals 17:620. https:\/\/doi.org\/10.3390\/ph17050620","journal-title":"Pharmaceuticals"},{"key":"5264_CR16","doi-asserted-by":"publisher","first-page":"107410","DOI":"10.1016\/j.phrs.2024.107410","volume":"208","author":"LY Zhang","year":"2024","unstructured":"Zhang LY, Zhang SY, Wen R et al (2024) Role of histone deacetylases and their inhibitors in neurological diseases. Pharmacol Res 208:107410. https:\/\/doi.org\/10.1016\/j.phrs.2024.107410","journal-title":"Pharmacol Res"},{"key":"5264_CR17","doi-asserted-by":"publisher","first-page":"158","DOI":"10.2174\/1570159x19666210609160017","volume":"20","author":"V Kumar","year":"2021","unstructured":"Kumar V, Kundu S, Singh A, Singh S (2021) Understanding the role of histone deacetylase and their inhibitors in neurodegenerative disorders: current targets and future perspective. Curr Neuropharmacol 20:158\u2013178. https:\/\/doi.org\/10.2174\/1570159x19666210609160017","journal-title":"Curr Neuropharmacol"},{"key":"5264_CR18","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s11696-022-02598-y","volume":"1","author":"PC Gurram","year":"2022","unstructured":"Gurram PC, Satarker S, Nassar A et al (2022) Virtual structure-based docking and molecular dynamics of FDA-approved drugs for the identification of potential IKKB inhibitors possessing dopaminergic activity in Alzheimer\u2019s disease. Chem Pap 1:1\u201318. https:\/\/doi.org\/10.1007\/s11696-022-02598-y","journal-title":"Chem Pap"},{"key":"5264_CR19","doi-asserted-by":"publisher","first-page":"312","DOI":"10.1016\/j.cell.2019.09.001","volume":"179","author":"JM Long","year":"2019","unstructured":"Long JM, Holtzman DM (2019) Alzheimer disease: an update on pathobiology and treatment strategies. Cell 179:312\u2013339. https:\/\/doi.org\/10.1016\/j.cell.2019.09.001","journal-title":"Cell"},{"key":"5264_CR20","doi-asserted-by":"publisher","first-page":"107","DOI":"10.3390\/ijms24010107","volume":"24","author":"AA Rostagno","year":"2023","unstructured":"Rostagno AA (2023) Pathogenesis of Alzheimer\u2019s disease. Int J Mol Sci 24:107. https:\/\/doi.org\/10.3390\/ijms24010107","journal-title":"Int J Mol Sci"},{"key":"5264_CR21","doi-asserted-by":"publisher","unstructured":"Breijyeh Z, Karaman R (2020) Comprehensive review on Alzheimer\u2019s disease: causes and treatment. Molecules 25. https:\/\/doi.org\/10.3390\/MOLECULES25245789","DOI":"10.3390\/MOLECULES25245789"},{"key":"5264_CR22","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s12035-023-03844-4","volume":"1","author":"S Satarker","year":"2023","unstructured":"Satarker S, Gurram PC, Nassar A et al (2023) Evaluating the role of N-acetyl-L-tryptophan in the A\u03b2 1\u201342-induced neuroinflammation and cognitive decline in Alzheimer\u2019s disease. Mol Neurobiol 1:1\u201320. https:\/\/doi.org\/10.1007\/s12035-023-03844-4","journal-title":"Mol Neurobiol"},{"key":"5264_CR23","doi-asserted-by":"publisher","first-page":"1816","DOI":"10.3390\/molecules27061816","volume":"27","author":"ZR Chen","year":"2022","unstructured":"Chen ZR, Huang JB, Yang SL, Hong FF (2022) Role of cholinergic signaling in Alzheimer\u2019s disease. Molecules 27:1816. https:\/\/doi.org\/10.3390\/molecules27061816","journal-title":"Molecules"},{"key":"5264_CR24","doi-asserted-by":"publisher","DOI":"10.1080\/07391102.2022.2156924","author":"P Chowdari Gurram","year":"2022","unstructured":"Chowdari Gurram P, Satarker S, Kumar G et al (2022) Avanafil mediated dual inhibition of IKK\u03b2 and TNFR1 in an experimental paradigm of Alzheimer\u2019s disease: in silico and in vivo approach. J Biomol Struct Dyn. https:\/\/doi.org\/10.1080\/07391102.2022.2156924","journal-title":"J Biomol Struct Dyn"},{"key":"5264_CR25","doi-asserted-by":"publisher","first-page":"1577","DOI":"10.1016\/S0140-6736(20)32205-4","volume":"397","author":"P Scheltens","year":"2021","unstructured":"Scheltens P, De Strooper B, Kivipelto M et al (2021) Alzheimer\u2019s disease. Lancet 397:1577\u20131590. https:\/\/doi.org\/10.1016\/S0140-6736(20)32205-4","journal-title":"Lancet"},{"key":"5264_CR26","doi-asserted-by":"publisher","unstructured":"Nassar A, Satarker S, Gurram PC et al (2023) Repressor element-1 binding transcription factor (REST) as a possible epigenetic regulator of neurodegeneration and microRNA-based therapeutic strategies. Mol Neurobiol. https:\/\/doi.org\/10.1007\/s12035-023-03437-1","DOI":"10.1007\/s12035-023-03437-1"},{"key":"5264_CR27","doi-asserted-by":"publisher","unstructured":"Manandhar S, Gurram PC, Govindula A et al (2025) Voglibose attenuates amyloid beta\u2013induced memory deficits in a rodent model: a potential Alzheimer\u2019s therapy via Wnt signaling modulation. Mol Neurobiol. https:\/\/doi.org\/10.1007\/s12035-025-05047-5","DOI":"10.1007\/s12035-025-05047-5"},{"key":"5264_CR28","doi-asserted-by":"publisher","first-page":"663","DOI":"10.1016\/j.psc.2022.07.003","volume":"45","author":"BC Yarns","year":"2022","unstructured":"Yarns BC, Holiday KA, Carlson DM et al (2022) Pathophysiology of Alzheimer\u2019s disease. Psychiatr Clin North Am 45:663\u2013676. https:\/\/doi.org\/10.1016\/j.psc.2022.07.003","journal-title":"Psychiatr Clin North Am"},{"key":"5264_CR29","doi-asserted-by":"publisher","DOI":"10.1016\/J.EJPHAR.2020.173554","author":"M Vaz","year":"2020","unstructured":"Vaz M, Silvestre S (2020) Alzheimer\u2019s disease: recent treatment strategies. Eur J Pharmacol. https:\/\/doi.org\/10.1016\/J.EJPHAR.2020.173554","journal-title":"Eur J Pharmacol"},{"key":"5264_CR30","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.abq7105","author":"LT Zhou","year":"2023","unstructured":"Zhou LT, Liu D, Kang HC et al (2023) Tau pathology epigenetically remodels the neuron-glial cross-talk in Alzheimer\u2019s disease. Sci Adv. https:\/\/doi.org\/10.1126\/sciadv.abq7105","journal-title":"Sci Adv"},{"key":"5264_CR31","doi-asserted-by":"publisher","first-page":"2181","DOI":"10.7150\/ijbs.57078","volume":"17","author":"H Zhang","year":"2021","unstructured":"Zhang H, Wei W, Zhao M (2021) Review interaction between a\u03b2 and tau in the pathogenesis of Alzheimer\u2019s disease. Int J Biol Sci 17:2181\u20132192. https:\/\/doi.org\/10.7150\/ijbs.57078","journal-title":"Int J Biol Sci"},{"key":"5264_CR32","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1016\/j.conb.2021.03.003","volume":"69","author":"S Wegmann","year":"2021","unstructured":"Wegmann S, Biernat J, Mandelkow E (2021) A current view on Tau protein phosphorylation in Alzheimer\u2019s disease. Curr Opin Neurobiol 69:131\u2013138. https:\/\/doi.org\/10.1016\/j.conb.2021.03.003","journal-title":"Curr Opin Neurobiol"},{"key":"5264_CR33","doi-asserted-by":"publisher","first-page":"297","DOI":"10.3390\/antiox14030297","volume":"14","author":"DM Trofin","year":"2025","unstructured":"Trofin DM, Sardaru DP, Trofin D et al (2025) Oxidative stress in brain function. Antioxidants 14:297. https:\/\/doi.org\/10.3390\/antiox14030297","journal-title":"Antioxidants"},{"key":"5264_CR34","doi-asserted-by":"publisher","first-page":"490","DOI":"10.1016\/j.redox.2018.01.008","volume":"15","author":"JN Cobley","year":"2018","unstructured":"Cobley JN, Fiorello ML, Bailey DM (2018) 13 reasons why the brain is susceptible to oxidative stress. Redox Biol 15:490\u2013503. https:\/\/doi.org\/10.1016\/j.redox.2018.01.008","journal-title":"Redox Biol"},{"key":"5264_CR35","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s11011-024-01463-z","volume":"40","author":"PC Gurram","year":"2025","unstructured":"Gurram PC, Satarker S, Nassar A (2025) Dopamine agonist rotigotine mitigates lipopolysaccharide-induced neuroinflammation and memory impairment in mice. Metab Brain Dis 40:1\u201312. https:\/\/doi.org\/10.1007\/s11011-024-01463-z","journal-title":"Metab Brain Dis"},{"key":"5264_CR36","doi-asserted-by":"publisher","unstructured":"Nampoothiri M, Gurram PC, Bojja SL, Satarker S (2023) Phytochemical nanoformulations for neurological disorders. Adv Phytonanotechnology Treat Var Dis 179\u2013194. https:\/\/doi.org\/10.1201\/9781003231721-7","DOI":"10.1201\/9781003231721-7"},{"key":"5264_CR37","doi-asserted-by":"publisher","unstructured":"Nassar A, Kodi T, Satarker S, et al (2022) Astrocytic microRNAs and transcription factors in Alzheimer\u2019s disease and therapeutic interventions. Cells 11:. https:\/\/doi.org\/10.3390\/cells11244111","DOI":"10.3390\/cells11244111"},{"key":"5264_CR38","doi-asserted-by":"publisher","first-page":"539","DOI":"10.1038\/sj.cdd.4401769","volume":"13","author":"RN Saha","year":"2006","unstructured":"Saha RN, Pahan K (2006) HATs and HDACs in neurodegeneration: A tale of disconcerted acetylation homeostasis. Cell Death Differ 13:539\u2013550. https:\/\/doi.org\/10.1038\/sj.cdd.4401769","journal-title":"Cell Death Differ"},{"key":"5264_CR39","doi-asserted-by":"publisher","DOI":"10.15252\/emmm.201910622","author":"C Wu","year":"2020","unstructured":"Wu C, Jin L, Wang I et al (2020) HDAC1 dysregulation induces aberrant cell cycle and DNA damage in progress of TDP-43 proteinopathies. EMBO Mol Med. https:\/\/doi.org\/10.15252\/emmm.201910622","journal-title":"EMBO Mol Med"},{"key":"5264_CR40","doi-asserted-by":"publisher","first-page":"180","DOI":"10.1038\/nn.2471","volume":"13","author":"JY Kim","year":"2010","unstructured":"Kim JY, Shen S, Dietz K et al (2010) HDAC1 nuclear export induced by pathological conditions is essential for the onset of axonal damage. Nat Neurosci 13:180\u2013189. https:\/\/doi.org\/10.1038\/nn.2471","journal-title":"Nat Neurosci"},{"key":"5264_CR41","doi-asserted-by":"publisher","first-page":"35444","DOI":"10.1074\/jbc.M112.394544","volume":"287","author":"FH Bardai","year":"2012","unstructured":"Bardai FH, Price V, Zaayman M et al (2012) Histone deacetylase-1 (HDAC1) is a molecular switch between neuronal survival and death. J Biol Chem 287:35444\u201335453. https:\/\/doi.org\/10.1074\/jbc.M112.394544","journal-title":"J Biol Chem"},{"key":"5264_CR42","doi-asserted-by":"publisher","first-page":"4103","DOI":"10.2147\/JIR.S416239","volume":"16","author":"HK Wang","year":"2023","unstructured":"Wang HK, Su YT, Ho YC (2023) HDAC1 is involved in neuroinflammation and blood-brain barrier damage in stroke pathogenesis. J Inflamm Res 16:4103\u20134116. https:\/\/doi.org\/10.2147\/JIR.S416239","journal-title":"J Inflamm Res"},{"key":"5264_CR43","doi-asserted-by":"publisher","first-page":"2484","DOI":"10.1038\/s41467-020-16361-y","volume":"11","author":"PC Pao","year":"2020","unstructured":"Pao PC, Patnaik D, Watson LA et al (2020) HDAC1 modulates OGG1-initiated oxidative DNA damage repair in the aging brain and Alzheimer\u2019s disease. Nat Commun 11:2484. https:\/\/doi.org\/10.1038\/s41467-020-16361-y","journal-title":"Nat Commun"},{"key":"5264_CR44","doi-asserted-by":"publisher","first-page":"764","DOI":"10.1523\/JNEUROSCI.5052-10.2011","volume":"31","author":"SC McQuown","year":"2011","unstructured":"McQuown SC, Barrett RM, Matheos DP et al (2011) HDAC3 is a critical negative regulator of long-term memory formation. J Neurosci 31:764\u2013774. https:\/\/doi.org\/10.1523\/JNEUROSCI.5052-10.2011","journal-title":"J Neurosci"},{"key":"5264_CR45","doi-asserted-by":"publisher","unstructured":"Delcuve GP, Khan DH, Davie JR (2013) Roles of histone deacetylases in epigenetic regulation: emerging paradigms from studies with inhibitors. Epigenetics Pathol Explor Connect between Genet Mech Dis Expr 4:143\u2013171. https:\/\/doi.org\/10.1201\/b16304","DOI":"10.1201\/b16304"},{"key":"5264_CR46","doi-asserted-by":"publisher","first-page":"139","DOI":"10.2217\/epi.13.73","volume":"6","author":"Z Wang","year":"2014","unstructured":"Wang Z, Qin G, Zhao TC (2014) HDAC4: mechanism of regulation and biological functions. Epigenomics 6:139\u2013150. https:\/\/doi.org\/10.2217\/epi.13.73","journal-title":"Epigenomics"},{"key":"5264_CR47","doi-asserted-by":"publisher","first-page":"35","DOI":"10.3233\/JAD-2012-121009","volume":"33","author":"RC Agis-Balboa","year":"2013","unstructured":"Agis-Balboa RC, Pavelka Z, Kerimoglu C, Fischer A (2013) Loss of HDAC5 impairs memory function: implications for Alzheimer\u2019s disease. J Alzheimer\u2019s Dis 33:35\u201344. https:\/\/doi.org\/10.3233\/JAD-2012-121009","journal-title":"J Alzheimer\u2019s Dis"},{"key":"5264_CR48","doi-asserted-by":"publisher","unstructured":"Fukada M, Hanai A, Nakayama A et al (2012) Loss of deacetylation activity of Hdac6 affects emotional behavior in mice. PLoS One 7:. https:\/\/doi.org\/10.1371\/journal.pone.0030924","DOI":"10.1371\/journal.pone.0030924"},{"key":"5264_CR49","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1146\/annurev-neuro-061010-113613","volume":"34","author":"RJ O\u2019Brien","year":"2011","unstructured":"O\u2019Brien RJ, Wong PC (2011) Amyloid precursor protein processing and Alzheimer\u2019s disease. Annu Rev Neurosci 34:185\u2013204. https:\/\/doi.org\/10.1146\/annurev-neuro-061010-113613","journal-title":"Annu Rev Neurosci"},{"key":"5264_CR50","doi-asserted-by":"publisher","unstructured":"Choi H, Kim HJ, Kim J et al (2017) Increased acetylation of Peroxiredoxin1 by HDAC6 inhibition leads to recovery of A\u03b2-induced impaired axonal transport. Mol Neurodegener 12:23. https:\/\/doi.org\/10.1186\/S13024-017-0164-1\/FIGURES\/7","DOI":"10.1186\/S13024-017-0164-1\/FIGURES\/7"},{"key":"5264_CR51","doi-asserted-by":"publisher","first-page":"351ra106","DOI":"10.1126\/scitranslmed.aaf7551","volume":"8","author":"HY Wey","year":"2016","unstructured":"Wey HY, Gilbert TM, Z\u00fcrcher NR et al (2016) Insights into neuroepigenetics through human histone deacetylase PET imaging. Sci Transl Med 8:351ra106. https:\/\/doi.org\/10.1126\/scitranslmed.aaf7551","journal-title":"Sci Transl Med"},{"key":"5264_CR52","doi-asserted-by":"publisher","first-page":"214","DOI":"10.1111\/jnc.14144","volume":"143","author":"BS Durham","year":"2017","unstructured":"Durham BS, Grigg R, Wood IC (2017) Inhibition of histone deacetylase 1 or 2 reduces induced cytokine expression in microglia through a protein synthesis independent mechanism. J Neurochem 143:214\u2013224. https:\/\/doi.org\/10.1111\/jnc.14144","journal-title":"J Neurochem"},{"key":"5264_CR53","doi-asserted-by":"publisher","first-page":"55","DOI":"10.1038\/nature07925","volume":"459","author":"JS Guan","year":"2009","unstructured":"Guan JS, Haggarty SJ, Giacometti E et al (2009) HDAC2 negatively regulates memory formation and synaptic plasticity. Nature 459:55\u201360. https:\/\/doi.org\/10.1038\/nature07925","journal-title":"Nature"},{"key":"5264_CR54","doi-asserted-by":"publisher","first-page":"556","DOI":"10.3390\/genes11050556","volume":"11","author":"G Milazzo","year":"2020","unstructured":"Milazzo G, Mercatelli D, Di Muzio G et al (2020) Histone deacetylases (HDACs): evolution, specificity, role in transcriptional complexes, and pharmacological actionability. Genes (Basel) 11:556. https:\/\/doi.org\/10.3390\/genes11050556","journal-title":"Genes (Basel)"},{"key":"5264_CR55","doi-asserted-by":"publisher","first-page":"1319","DOI":"10.1016\/j.celrep.2017.07.044","volume":"20","author":"H Yamakawa","year":"2017","unstructured":"Yamakawa H, Cheng J, Penney J et al (2017) The transcription factor Sp3 cooperates with HDAC2 to regulate synaptic function and plasticity in neurons. Cell Rep 20:1319\u20131334. https:\/\/doi.org\/10.1016\/j.celrep.2017.07.044","journal-title":"Cell Rep"},{"key":"5264_CR56","doi-asserted-by":"publisher","first-page":"86","DOI":"10.1016\/j.arr.2014.09.004","volume":"18","author":"A Savioz","year":"2014","unstructured":"Savioz A, Leuba G, Vallet PG (2014) A framework to understand the variations of PSD-95 expression in brain aging and in Alzheimer\u2019s disease. Ageing Res Rev 18:86\u201394. https:\/\/doi.org\/10.1016\/j.arr.2014.09.004","journal-title":"Ageing Res Rev"},{"key":"5264_CR57","doi-asserted-by":"publisher","unstructured":"Atluri VSR, Tiwari S, Rodriguez M et al (2020) Inhibition of amyloid-beta production, associated neuroinflammation, and histone deacetylase 2-mediated epigenetic modifications prevent neuropathology in Alzheimer\u2019s disease in vitro model. Front Aging Neurosci 11:. https:\/\/doi.org\/10.3389\/fnagi.2019.00342","DOI":"10.3389\/fnagi.2019.00342"},{"key":"5264_CR58","doi-asserted-by":"publisher","first-page":"817","DOI":"10.1016\/0896-6273(93)90111-4","volume":"11","author":"DJ Perkel","year":"1993","unstructured":"Perkel DJ, Petrozzino JJ, Nicoll RA, Connor JA (1993) The role of Ca2+ entry via synaptically activated NMDA receptors in the induction of long-term potentiation. Neuron 11:817\u2013823. https:\/\/doi.org\/10.1016\/0896-6273(93)90111-4","journal-title":"Neuron"},{"key":"5264_CR59","doi-asserted-by":"publisher","first-page":"994","DOI":"10.1134\/S0006297920090023","volume":"85","author":"AA Borodinova","year":"2020","unstructured":"Borodinova AA, Balaban PM (2020) Epigenetic regulation as a basis for long-term changes in the nervous system: in search of specificity mechanisms. Biochemistry (Moscow) 85:994\u20131010. https:\/\/doi.org\/10.1134\/S0006297920090023","journal-title":"Biochemistry (Moscow)"},{"key":"5264_CR60","doi-asserted-by":"publisher","first-page":"2432","DOI":"10.1007\/s12035-017-0490-x","volume":"55","author":"P Singh","year":"2018","unstructured":"Singh P, Thakur MK (2018) Histone deacetylase 2 inhibition attenuates downregulation of hippocampal plasticity gene expression during aging. Mol Neurobiol 55:2432\u20132442. https:\/\/doi.org\/10.1007\/s12035-017-0490-x","journal-title":"Mol Neurobiol"},{"key":"5264_CR61","doi-asserted-by":"publisher","unstructured":"Yan X, Liu J, Ye Z et al (2016) CaMKII-mediated CREB phosphorylation is involved in Ca2+-induced BDNF mRNA transcription and neurite outgrowth promoted by electrical stimulation. PLoS One 11:. https:\/\/doi.org\/10.1371\/journal.pone.0162784","DOI":"10.1371\/journal.pone.0162784"},{"key":"5264_CR62","doi-asserted-by":"publisher","first-page":"425433","DOI":"10.3389\/fnins.2019.00043","volume":"13","author":"J Liu","year":"2019","unstructured":"Liu J, Chang L, Song Y (2019) The role of NMDA receptors in Alzheimer\u2019s disease. Front Neurosci 13:425433. https:\/\/doi.org\/10.3389\/fnins.2019.00043","journal-title":"Front Neurosci"},{"key":"5264_CR63","doi-asserted-by":"publisher","first-page":"322","DOI":"10.1016\/S0962-8924(00)01800-6","volume":"10","author":"D Chin","year":"2000","unstructured":"Chin D, Means AR (2000) Calmodulin: a prototypical calcium sensor. Trends Cell Biol 10:322\u2013328. https:\/\/doi.org\/10.1016\/S0962-8924(00)01800-6","journal-title":"Trends Cell Biol"},{"key":"5264_CR64","doi-asserted-by":"publisher","unstructured":"Penney J, Tsai LH (2014) Histone deacetylases in memory and cognition. Sci Signal 7:. https:\/\/doi.org\/10.1126\/scisignal.aaa0069","DOI":"10.1126\/scisignal.aaa0069"},{"key":"5264_CR65","doi-asserted-by":"publisher","first-page":"5979","DOI":"10.1128\/mcb.21.17.5979-5991.2001","volume":"21","author":"Y-L Yao","year":"2001","unstructured":"Yao Y-L, Yang W-M, Seto E (2001) Regulation of transcription factor YY1 by acetylation and deacetylation. Mol Cell Biol 21:5979\u20135991. https:\/\/doi.org\/10.1128\/mcb.21.17.5979-5991.2001","journal-title":"Mol Cell Biol"},{"key":"5264_CR66","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1016\/j.celrep.2017.09.045","volume":"21","author":"E Fern\u00e1ndez","year":"2017","unstructured":"Fern\u00e1ndez E, Collins MO, Frank RAW et al (2017) Arc requires PSD95 for assembly into postsynaptic complexes involved with neural dysfunction and intelligence. Cell Rep 21:679\u2013691. https:\/\/doi.org\/10.1016\/j.celrep.2017.09.045","journal-title":"Cell Rep"},{"key":"5264_CR67","doi-asserted-by":"publisher","unstructured":"Verheul TCJ, van Hijfte L, Perenthaler E, Barakat TS (2020) The why of YY1: mechanisms of transcriptional regulation by Yin Yang 1. Front Cell Dev Biol. https:\/\/doi.org\/10.3389\/fcell.2020.592164","DOI":"10.3389\/fcell.2020.592164"},{"key":"5264_CR68","doi-asserted-by":"publisher","first-page":"147898","DOI":"10.1016\/j.gene.2023.147898","volume":"892","author":"A Nassar","year":"2024","unstructured":"Nassar A, Kodi T, Satarker S et al (2024) Astrocytic transcription factors REST, YY1, and putative microRNAs in Parkinson\u2019s disease and advanced therapeutic strategies. Gene 892:147898. https:\/\/doi.org\/10.1016\/j.gene.2023.147898","journal-title":"Gene"},{"key":"5264_CR69","doi-asserted-by":"publisher","first-page":"1506","DOI":"10.1038\/nn.4395","volume":"19","author":"M Mahgoub","year":"2016","unstructured":"Mahgoub M, Adachi M, Suzuki K et al (2016) MeCP2 and histone deacetylases 1 and 2 in dorsal striatum collectively suppress repetitive behaviors. Nat Neurosci 19:1506\u20131512. https:\/\/doi.org\/10.1038\/nn.4395","journal-title":"Nat Neurosci"},{"key":"5264_CR70","doi-asserted-by":"publisher","first-page":"4218","DOI":"10.3390\/ijms24044218","volume":"24","author":"YM Vuu","year":"2023","unstructured":"Vuu YM, Roberts CT, Rastegar M (2023) MeCP2 is an epigenetic factor that links DNA methylation with brain metabolism. Int J Mol Sci 24:4218. https:\/\/doi.org\/10.3390\/ijms24044218","journal-title":"Int J Mol Sci"},{"key":"5264_CR71","doi-asserted-by":"publisher","unstructured":"Ausi\u00f3 J, de Paz AM, Esteller M (2014) MeCP2: the long trip from a chromatin protein to neurological disorders. Trends Mol Med 20:487\u2013498. https:\/\/doi.org\/10.1016\/j.molmed.2014.03.004","DOI":"10.1016\/j.molmed.2014.03.004"},{"key":"5264_CR72","doi-asserted-by":"publisher","unstructured":"Singh D (2022) Astrocytic and microglial cells as the modulators of neuroinflammation in Alzheimer\u2019s disease. J Neuroinflammation 19:. https:\/\/doi.org\/10.1186\/s12974-022-02565-0","DOI":"10.1186\/s12974-022-02565-0"},{"key":"5264_CR73","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s12974-019-1640-z","volume":"16","author":"XY Sun","year":"2019","unstructured":"Sun XY, Zheng T, Yang X (2019) HDAC2 hyperexpression alters hippocampal neuronal transcription and microglial activity in neuroinflammation-induced cognitive dysfunction. J Neuroinflammation 16:1\u201317. https:\/\/doi.org\/10.1186\/s12974-019-1640-z","journal-title":"J Neuroinflammation"},{"key":"5264_CR74","doi-asserted-by":"publisher","first-page":"752","DOI":"10.1016\/j.ymthe.2017.01.018","volume":"25","author":"D Liu","year":"2017","unstructured":"Liu D, Tang H, Li XY et al (2017) Targeting the HDAC2\/HNF-4A\/miR-101b\/AMPK pathway rescues tauopathy and dendritic abnormalities in Alzheimer\u2019s disease. Mol Ther 25:752\u2013764. https:\/\/doi.org\/10.1016\/j.ymthe.2017.01.018","journal-title":"Mol Ther"},{"key":"5264_CR75","doi-asserted-by":"publisher","first-page":"302","DOI":"10.1016\/j.mcn.2008.07.010","volume":"39","author":"K Kanninen","year":"2008","unstructured":"Kanninen K, Malm TM, Jyrkk\u00e4nen HK et al (2008) Nuclear factor erythroid 2-related factor 2 protects against beta amyloid. Mol Cell Neurosci 39:302\u2013313. https:\/\/doi.org\/10.1016\/j.mcn.2008.07.010","journal-title":"Mol Cell Neurosci"},{"key":"5264_CR76","doi-asserted-by":"publisher","first-page":"392","DOI":"10.1016\/j.it.2009.07.001","volume":"30","author":"BJ Baker","year":"2009","unstructured":"Baker BJ, Akhtar LN, Benveniste EN (2009) SOCS1 and SOCS3 in the control of CNS immunity. Trends Immunol 30:392\u2013400. https:\/\/doi.org\/10.1016\/j.it.2009.07.001","journal-title":"Trends Immunol"},{"key":"5264_CR77","doi-asserted-by":"publisher","first-page":"1371","DOI":"10.3390\/antiox12071371","volume":"12","author":"M Hammad","year":"2023","unstructured":"Hammad M, Raftari M, Ces\u00e1rio R et al (2023) Roles of oxidative stress and Nrf2 signaling in pathogenic and non-pathogenic cells: a possible general mechanism of resistance to therapy. Antioxidants 12:1371. https:\/\/doi.org\/10.3390\/antiox12071371","journal-title":"Antioxidants"},{"key":"5264_CR78","doi-asserted-by":"publisher","first-page":"110373","DOI":"10.1016\/j.biopha.2020.110373","volume":"129","author":"V Sharma","year":"2020","unstructured":"Sharma V, Kaur A, Singh TG (2020) Counteracting role of nuclear factor erythroid 2-related factor 2 pathway in Alzheimer\u2019s disease. Biomed Pharmacother 129:110373. https:\/\/doi.org\/10.1016\/j.biopha.2020.110373","journal-title":"Biomed Pharmacother"},{"key":"5264_CR79","doi-asserted-by":"publisher","first-page":"401","DOI":"10.1146\/annurev-pharmtox-011112-140320","volume":"53","author":"Q Ma","year":"2013","unstructured":"Ma Q (2013) Role of Nrf2 in oxidative stress and toxicity. Annu Rev Pharmacol Toxicol 53:401\u2013426. https:\/\/doi.org\/10.1146\/annurev-pharmtox-011112-140320","journal-title":"Annu Rev Pharmacol Toxicol"},{"key":"5264_CR80","doi-asserted-by":"publisher","first-page":"5718","DOI":"10.1093\/nar\/gkq212","volume":"38","author":"D Malhotra","year":"2010","unstructured":"Malhotra D, Portales-Casamar E, Singh A et al (2010) Global mapping of binding sites for Nrf2 identifies novel targets in cell survival response through chip-seq profiling and network analysis. Nucleic Acids Res 38:5718\u20135734. https:\/\/doi.org\/10.1093\/nar\/gkq212","journal-title":"Nucleic Acids Res"},{"key":"5264_CR81","doi-asserted-by":"publisher","first-page":"575","DOI":"10.1016\/j.trci.2018.06.014","volume":"4","author":"JW Kinney","year":"2018","unstructured":"Kinney JW, Bemiller SM, Murtishaw AS et al (2018) Inflammation as a central mechanism in Alzheimer\u2019s disease. Alzheimer\u2019s Dement Transl Res Clin Interv 4:575\u2013590. https:\/\/doi.org\/10.1016\/j.trci.2018.06.014","journal-title":"Alzheimer\u2019s Dement Transl Res Clin Interv"},{"key":"5264_CR82","doi-asserted-by":"publisher","first-page":"1884","DOI":"10.3390\/cells10081884","volume":"10","author":"DA Davies","year":"2021","unstructured":"Davies DA, Adlimoghaddam A, Albensi BC (2021) Role of nrf2 in synaptic plasticity and memory in Alzheimer\u2019s disease. Cells 10:1884. https:\/\/doi.org\/10.3390\/cells10081884","journal-title":"Cells"},{"key":"5264_CR83","doi-asserted-by":"publisher","first-page":"110988","DOI":"10.1016\/j.brainresbull.2024.110988","volume":"213","author":"M Yan","year":"2024","unstructured":"Yan M, Sun Z, Zhang S et al (2024) SOCS modulates JAK-STAT pathway as a novel target to mediate the occurrence of neuroinflammation: molecular details and treatment options. Brain Res Bull 213:110988. https:\/\/doi.org\/10.1016\/j.brainresbull.2024.110988","journal-title":"Brain Res Bull"},{"key":"5264_CR84","doi-asserted-by":"publisher","first-page":"5474","DOI":"10.3390\/molecules25225474","volume":"25","author":"S Saha","year":"2020","unstructured":"Saha S, Buttari B, Panieri E et al (2020) An overview of Nrf2 signaling pathway and its role in inflammation. Molecules 25:5474. https:\/\/doi.org\/10.3390\/molecules25225474","journal-title":"Molecules"},{"key":"5264_CR85","doi-asserted-by":"publisher","first-page":"17089","DOI":"10.1073\/pnas.0508517102","volume":"102","author":"A Kimura","year":"2005","unstructured":"Kimura A, Naka T, Muta T et al (2005) Suppressor of cytokine signaling-1 selectively inhibits LPS-induced IL-6 production by regulating JAK-STAT. Proc Natl Acad Sci U S A 102:17089\u201317094. https:\/\/doi.org\/10.1073\/pnas.0508517102","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5264_CR86","doi-asserted-by":"publisher","first-page":"223","DOI":"10.1186\/s12974-022-02584-x","volume":"19","author":"RJ Boyd","year":"2022","unstructured":"Boyd RJ, Avramopoulos D, Jantzie LL, McCallion AS (2022) Neuroinflammation represents a common theme amongst genetic and environmental risk factors for Alzheimer and Parkinson diseases. J Neuroinflammation 19:223. https:\/\/doi.org\/10.1186\/s12974-022-02584-x","journal-title":"J Neuroinflammation"},{"key":"5264_CR87","doi-asserted-by":"publisher","first-page":"826","DOI":"10.1093\/brain\/aww330","volume":"140","author":"S Alves","year":"2017","unstructured":"Alves S, Churlaud G, Audrain M (2017) Interleukin-2 improves amyloid pathology, synaptic failure and memory in Alzheimer\u2019s disease mice. Brain 140:826\u2013842. https:\/\/doi.org\/10.1093\/brain\/aww330","journal-title":"Brain"},{"key":"5264_CR88","doi-asserted-by":"publisher","first-page":"460","DOI":"10.1016\/j.molmed.2007.09.002","volume":"13","author":"T Kawai","year":"2007","unstructured":"Kawai T, Akira S (2007) Signaling to NF-\u03baB by toll-like receptors. Trends Mol Med 13:460\u2013469. https:\/\/doi.org\/10.1016\/j.molmed.2007.09.002","journal-title":"Trends Mol Med"},{"key":"5264_CR89","doi-asserted-by":"publisher","first-page":"7123","DOI":"10.18632\/oncotarget.3344","volume":"6","author":"T Wagner","year":"2015","unstructured":"Wagner T, Kiweler N, Wolff K et al (2015) Sumoylation of HDAC2 promotes NF-\u03baB-dependent gene expression. Oncotarget 6:7123\u20137135. https:\/\/doi.org\/10.18632\/oncotarget.3344","journal-title":"Oncotarget"},{"key":"5264_CR90","doi-asserted-by":"publisher","first-page":"7065","DOI":"10.1128\/mcb.21.20.7065-7077.2001","volume":"21","author":"BP Ashburner","year":"2001","unstructured":"Ashburner BP, Westerheide SD, Baldwin AS (2001) The p65 (RelA) subunit of NF-\u03baB interacts with the histone deacetylase (HDAC) corepressors HDAC1 and HDAC2 to negatively regulate gene expression. Mol Cell Biol 21:7065\u20137077. https:\/\/doi.org\/10.1128\/mcb.21.20.7065-7077.2001","journal-title":"Mol Cell Biol"},{"key":"5264_CR91","doi-asserted-by":"publisher","first-page":"a000034","DOI":"10.1101\/cshperspect.a000034","volume":"1","author":"A Oeckinghaus","year":"2009","unstructured":"Oeckinghaus A, Ghosh S (2009) The NF-kappaB family of transcription factors and its regulation. Cold Spring Harb Perspect Biol 1:a000034. https:\/\/doi.org\/10.1101\/cshperspect.a000034","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"5264_CR92","doi-asserted-by":"publisher","first-page":"2587","DOI":"10.3390\/biomedicines11092587","volume":"11","author":"BS Sivamaruthi","year":"2023","unstructured":"Sivamaruthi BS, Raghani N, Chorawala M et al (2023) NF-\u03baB pathway and its inhibitors: a promising frontier in the management of Alzheimer\u2019s disease. Biomedicines 11:2587. https:\/\/doi.org\/10.3390\/biomedicines11092587","journal-title":"Biomedicines"},{"key":"5264_CR93","doi-asserted-by":"publisher","first-page":"1717","DOI":"10.3390\/cells9071717","volume":"9","author":"JA Rodr\u00edguez-G\u00f3mez","year":"2020","unstructured":"Rodr\u00edguez-G\u00f3mez JA, Kavanagh E, Engskog-Vlachos P et al (2020) Microglia: agents of the CNS pro-inflammatory response. Cells 9:1717. https:\/\/doi.org\/10.3390\/cells9071717","journal-title":"Cells"},{"key":"5264_CR94","doi-asserted-by":"publisher","unstructured":"Hu X, li J, Fu M et al (2021) The JAK\/STAT signaling pathway: from bench to clinic. Signal Transduct Target Ther 6:1\u201333. https:\/\/doi.org\/10.1038\/s41392-021-00791-1","DOI":"10.1038\/s41392-021-00791-1"},{"key":"5264_CR95","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3390\/ijms21176070","volume":"21","author":"TM Sim","year":"2020","unstructured":"Sim TM, Tarini D, Dheen ST et al (2020) Nanoparticle-based technology approaches to the management of neurological disorders. Int J Mol Sci 21:1\u201332. https:\/\/doi.org\/10.3390\/ijms21176070","journal-title":"Int J Mol Sci"},{"key":"5264_CR96","doi-asserted-by":"publisher","first-page":"79","DOI":"10.3390\/cells13010079","volume":"13","author":"Y Ma","year":"2024","unstructured":"Ma Y, Wang W, Liu S (2024) Epigenetic regulation of neuroinflammation in Alzheimer\u2019s disease. Cells 13:79. https:\/\/doi.org\/10.3390\/cells13010079","journal-title":"Cells"},{"key":"5264_CR97","doi-asserted-by":"publisher","first-page":"590","DOI":"10.3390\/brainsci14060590","volume":"14","author":"Y Yang","year":"2024","unstructured":"Yang Y, Qiu L (2024) Research progress on the pathogenesis, diagnosis, and drug therapy of Alzheimer\u2019s disease. Brain Sci 14:590. https:\/\/doi.org\/10.3390\/brainsci14060590","journal-title":"Brain Sci"},{"key":"5264_CR98","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1017\/S1461145711000149","volume":"15","author":"CH Chen","year":"2012","unstructured":"Chen CH, Zhou W, Liu S et al (2012) Increased NF-\u03baB signalling up-regulates BACE1 expression and its therapeutic potential in Alzheimer\u2019s disease. Int J Neuropsychopharmacol 15:77\u201390. https:\/\/doi.org\/10.1017\/S1461145711000149","journal-title":"Int J Neuropsychopharmacol"},{"key":"5264_CR99","doi-asserted-by":"publisher","DOI":"10.1186\/1750-1326-1-4","author":"KS Vetrivel","year":"2006","unstructured":"Vetrivel KS, Zhang YW, Xu H, Thinakaran G (2006) Pathological and physiological functions of presenilins. Mol Neurodegener. https:\/\/doi.org\/10.1186\/1750-1326-1-4","journal-title":"Mol Neurodegener"},{"key":"5264_CR100","doi-asserted-by":"publisher","first-page":"98","DOI":"10.3389\/fnagi.2013.00098","volume":"5","author":"MOW Grimm","year":"2013","unstructured":"Grimm MOW, Mett J, Stahlmann CP et al (2013) Neprilysin and A\u03b2 clearance: impact of the APP intracellular domain in NEP regulation and implications in Alzheimer\u2019s disease. Front Aging Neurosci 5:98. https:\/\/doi.org\/10.3389\/fnagi.2013.00098","journal-title":"Front Aging Neurosci"},{"key":"5264_CR101","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1111\/jnc.12680","volume":"130","author":"C Kerridge","year":"2014","unstructured":"Kerridge C, Belyaev ND, Nalivaeva NN, Turner AJ (2014) The A\u03b2-clearance protein transthyretin, like neprilysin, is epigenetically regulated by the amyloid precursor protein intracellular domain. J Neurochem 130:419\u2013431. https:\/\/doi.org\/10.1111\/jnc.12680","journal-title":"J Neurochem"},{"key":"5264_CR102","doi-asserted-by":"publisher","first-page":"e40756","DOI":"10.1016\/j.heliyon.2024.e40756","volume":"10","author":"ZF Vahid","year":"2024","unstructured":"Vahid ZF, Eskandani M, Dadashi H et al (2024) Recent advances in potential enzymes and their therapeutic inhibitors for the treatment of Alzheimer\u2019s disease. Heliyon 10:e40756. https:\/\/doi.org\/10.1016\/j.heliyon.2024.e40756","journal-title":"Heliyon"},{"key":"5264_CR103","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3389\/fnagi.2014.00235","volume":"6","author":"NN Nalivaeva","year":"2014","unstructured":"Nalivaeva NN, Belyaev ND, Kerridge C, Turner AJ (2014) Amyloid-clearing proteins and their epigenetic regulation as a therapeutic target in Alzheimer\u00e2\u20ac\u2122s disease. Front Aging Neurosci 6:1\u201333. https:\/\/doi.org\/10.3389\/fnagi.2014.00235","journal-title":"Front Aging Neurosci"},{"key":"5264_CR104","doi-asserted-by":"publisher","unstructured":"Behl M, Zhang Y, Zheng W (2009) Involvement of insulin-degrading enzyme in the clearance of beta-amyloid at the blood-CSF barrier: consequences of lead exposure. Cerebrospinal Fluid Res 6. https:\/\/doi.org\/10.1186\/1743-8454-6-11","DOI":"10.1186\/1743-8454-6-11"},{"key":"5264_CR105","doi-asserted-by":"publisher","unstructured":"Yang S shuang, Zhang R, Wang G, Zhang Y fang (2017) The development prospection of HDAC inhibitors as a potential therapeutic direction in Alzheimer\u2019s disease. Transl Neurodegener 6:1\u20136. https:\/\/doi.org\/10.1186\/s40035-017-0089-1","DOI":"10.1186\/s40035-017-0089-1"},{"key":"5264_CR106","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1016\/j.nbd.2016.07.007","volume":"107","author":"E Zenaro","year":"2017","unstructured":"Zenaro E, Piacentino G, Constantin G (2017) The blood-brain barrier in Alzheimer\u2019s disease. Neurobiol Dis 107:41\u201356. https:\/\/doi.org\/10.1016\/j.nbd.2016.07.007","journal-title":"Neurobiol Dis"},{"key":"5264_CR107","doi-asserted-by":"publisher","first-page":"948","DOI":"10.3390\/pharmaceutics16070948","volume":"16","author":"S Petralla","year":"2024","unstructured":"Petralla S, Panayotova M, Franchina E et al (2024) Low-density lipoprotein receptor-related protein 1 as a potential therapeutic target in Alzheimer\u2019s disease. Pharmaceutics 16:948. https:\/\/doi.org\/10.3390\/pharmaceutics16070948","journal-title":"Pharmaceutics"},{"key":"5264_CR108","doi-asserted-by":"publisher","first-page":"524","DOI":"10.3390\/biomedicines9050524","volume":"9","author":"IG Onyango","year":"2021","unstructured":"Onyango IG, Jauregui GV, \u010carn\u00e1 M et al (2021) Neuroinflammation in Alzheimer\u2019s disease. Biomedicines 9:524. https:\/\/doi.org\/10.3390\/biomedicines9050524","journal-title":"Biomedicines"},{"key":"5264_CR109","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/1750-1326-1-4","volume":"1","author":"KS Vetrivel","year":"2006","unstructured":"Vetrivel KS, Zhang YW, Xu H, Thinakaran G (2006) Pathological and physiological functions of presenilins. Mol Neurodegener 1:1\u201312. https:\/\/doi.org\/10.1186\/1750-1326-1-4","journal-title":"Mol Neurodegener"},{"key":"5264_CR110","doi-asserted-by":"publisher","first-page":"71","DOI":"10.3233\/JAD-2008-13108","volume":"13","author":"B Brock","year":"2008","unstructured":"Brock B, Basha R, DiPalma K et al (2008) Co-localization and distribution of cerebral APP and SP1 and its relationship to amyloidogenesis. J Alzheimer\u2019s Dis 13:71\u201380. https:\/\/doi.org\/10.3233\/JAD-2008-13108","journal-title":"J Alzheimer\u2019s Dis"},{"key":"5264_CR111","doi-asserted-by":"publisher","first-page":"1093","DOI":"10.1016\/j.omtn.2021.01.017","volume":"23","author":"L Xie","year":"2021","unstructured":"Xie L, Zhou Q, Chen X et al (2021) Elucidation of the Hdac2\/Sp1\/miR-204-5p\/Bcl-2 axis as a modulator of cochlear apoptosis via in vivo\/in vitro models of acute hearing loss. Mol Ther Nucleic Acids 23:1093\u20131109. https:\/\/doi.org\/10.1016\/j.omtn.2021.01.017","journal-title":"Mol Ther Nucleic Acids"},{"key":"5264_CR112","doi-asserted-by":"publisher","first-page":"32","DOI":"10.2174\/1567205012666141218140953","volume":"12","author":"R Baranello","year":"2015","unstructured":"Baranello R, Bharani K, Padmaraju V et al (2015) Amyloid-beta protein clearance and degradation (ABCD) pathways and their role in Alzheimer\u2019s disease. Curr Alzheimer Res 12:32\u201346. https:\/\/doi.org\/10.2174\/1567205012666141218140953","journal-title":"Curr Alzheimer Res"},{"key":"5264_CR113","doi-asserted-by":"publisher","first-page":"388","DOI":"10.1016\/S1474-4422(15)70016-5","volume":"14","author":"MT Heneka","year":"2015","unstructured":"Heneka MT, Carson MJ, El KJ et al (2015) Neuroinflammation in Alzheimer\u2019s disease. Lancet Neurol 14:388\u2013405. https:\/\/doi.org\/10.1016\/S1474-4422(15)70016-5","journal-title":"Lancet Neurol"},{"key":"5264_CR114","doi-asserted-by":"publisher","first-page":"1105","DOI":"10.3233\/JAD-161088","volume":"57","author":"E T\u00f6nnies","year":"2017","unstructured":"T\u00f6nnies E, Trushina E (2017) Oxidative stress, synaptic dysfunction, and Alzheimer\u2019s disease. J Alzheimer\u2019s Dis 57:1105\u20131121. https:\/\/doi.org\/10.3233\/JAD-161088","journal-title":"J Alzheimer\u2019s Dis"},{"key":"5264_CR115","doi-asserted-by":"publisher","first-page":"1250","DOI":"10.1523\/JNEUROSCI.2444-14.2015","volume":"35","author":"S Peng","year":"2015","unstructured":"Peng S, Zhao S, Yan F et al (2015) HDAC2 selectively regulates FOXO3a-mediated gene transcription during oxidative stress-induced neuronal cell death. J Neurosci 35:1250\u20131259. https:\/\/doi.org\/10.1523\/JNEUROSCI.2444-14.2015","journal-title":"J Neurosci"},{"key":"5264_CR116","doi-asserted-by":"publisher","first-page":"759","DOI":"10.1016\/j.chembiol.2016.06.011","volume":"23","author":"AR Maolanon","year":"2016","unstructured":"Maolanon AR, Madsen AS, Olsen CA (2016) Innovative strategies for selective inhibition of histone deacetylases. Cell Chem Biol 23:759\u2013768. https:\/\/doi.org\/10.1016\/j.chembiol.2016.06.011","journal-title":"Cell Chem Biol"},{"key":"5264_CR117","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1196\/ANNALS.1427.024","volume":"1147","author":"W Qin","year":"2008","unstructured":"Qin W, Zhao W, Ho L et al (2008) Regulation of forkhead transcription factor FoxO3a contributes to calorie restriction-induced prevention of Alzheimer\u2019s disease-type amyloid neuropathology and spatial memory deterioration. Ann N Y Acad Sci 1147:335. https:\/\/doi.org\/10.1196\/ANNALS.1427.024","journal-title":"Ann N Y Acad Sci"},{"key":"5264_CR118","doi-asserted-by":"publisher","first-page":"1978","DOI":"10.1016\/j.bbamcr.2011.03.010","volume":"1813","author":"X Zhang","year":"2011","unstructured":"Zhang X, Tang N, Hadden TJ, Rishi AK (2011) Akt, foxo and regulation of apoptosis. Biochimica et Biophysica Acta (BBA) 1813:1978\u20131986. https:\/\/doi.org\/10.1016\/j.bbamcr.2011.03.010","journal-title":"Biochimica et Biophysica Acta (BBA)"},{"key":"5264_CR119","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1016\/j.freeradbiomed.2021.12.001","volume":"179","author":"QM Chen","year":"2022","unstructured":"Chen QM (2022) Nrf2 for protection against oxidant generation and mitochondrial damage in cardiac injury. Free Radic Biol Med 179:133\u2013143. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2021.12.001","journal-title":"Free Radic Biol Med"},{"issue":"13","key":"5264_CR120","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3390\/ijms21134777","volume":"21","author":"F He","year":"2020","unstructured":"He F, Ru X, Wen T (2020) NRF2, a transcription factor for stress response and beyond. Int J Mol Sci 21(13):1\u201323. https:\/\/doi.org\/10.3390\/ijms21134777","journal-title":"Int J Mol Sci"},{"issue":"5","key":"5264_CR121","doi-asserted-by":"publisher","first-page":"1075","DOI":"10.3390\/antiox12051075","volume":"12","author":"O Abu Shelbayeh","year":"2023","unstructured":"Abu Shelbayeh O, Arroum T, Morris S, Busch KB (2023) PGC-1\u03b1 is a master regulator of mitochondrial lifecycle and ROS stress response. Antioxidants 12(5):1075. https:\/\/doi.org\/10.3390\/antiox12051075","journal-title":"Antioxidants"},{"key":"5264_CR122","doi-asserted-by":"publisher","first-page":"3438","DOI":"10.1021\/acschemneuro.2c00440","volume":"13","author":"J Miao","year":"2022","unstructured":"Miao J, Chen Z, Wu Y et al (2022) Sp1 inhibits PGC-1\u03b1 via HDAC2-catalyzed histone deacetylation in chronic constriction injury-induced neuropathic pain. ACS Chem Neurosci 13:3438\u20133452. https:\/\/doi.org\/10.1021\/acschemneuro.2c00440","journal-title":"ACS Chem Neurosci"},{"key":"5264_CR123","doi-asserted-by":"publisher","first-page":"647054","DOI":"10.3389\/fnmol.2021.647054","volume":"14","author":"RL Mueller","year":"2021","unstructured":"Mueller RL, Combs B, Alhadidy MM et al (2021) Tau: a signaling hub protein. Front Mol Neurosci 14:647054. https:\/\/doi.org\/10.3389\/fnmol.2021.647054","journal-title":"Front Mol Neurosci"},{"key":"5264_CR124","doi-asserted-by":"publisher","first-page":"12841","DOI":"10.3390\/ijms232112841","volume":"23","author":"P Rawat","year":"2022","unstructured":"Rawat P, Sehar U, Bisht J et al (2022) Phosphorylated tau in Alzheimer\u2019s disease and other tauopathies. Int J Mol Sci 23:12841. https:\/\/doi.org\/10.3390\/ijms232112841","journal-title":"Int J Mol Sci"},{"key":"5264_CR125","doi-asserted-by":"publisher","first-page":"9987","DOI":"10.3390\/ijms22189987","volume":"22","author":"A S\u0229dzikowska","year":"2021","unstructured":"S\u0229dzikowska A, Szablewski L (2021) Insulin and insulin resistance in Alzheimer\u2019s disease. Int J Mol Sci 22:9987. https:\/\/doi.org\/10.3390\/ijms22189987","journal-title":"Int J Mol Sci"},{"key":"5264_CR126","doi-asserted-by":"publisher","unstructured":"Hernandez F, Lucas JJ, Avila J (2013) GSK3 and tau: two convergence points in Alzheimer\u2019s disease. J Alzheimer\u2019s Dis 33:. https:\/\/doi.org\/10.3233\/JAD-2012-129025","DOI":"10.3233\/JAD-2012-129025"},{"key":"5264_CR127","doi-asserted-by":"publisher","first-page":"396","DOI":"10.1016\/j.bbadis.2009.12.009","volume":"1802","author":"EK Kim","year":"2010","unstructured":"Kim EK, Choi EJ (2010) Pathological roles of MAPK signaling pathways in human diseases. Biochim Biophys Acta - Mol Basis Dis 1802:396\u2013405. https:\/\/doi.org\/10.1016\/j.bbadis.2009.12.009","journal-title":"Biochim Biophys Acta - Mol Basis Dis"},{"key":"5264_CR128","doi-asserted-by":"publisher","first-page":"561","DOI":"10.1016\/j.neuropharm.2009.11.010","volume":"58","author":"L Munoz","year":"2010","unstructured":"Munoz L, Ammit AJ (2010) Targeting p38 MAPK pathway for the treatment of Alzheimer\u2019s disease. Neuropharmacology 58:561\u2013568. https:\/\/doi.org\/10.1016\/j.neuropharm.2009.11.010","journal-title":"Neuropharmacology"},{"key":"5264_CR129","doi-asserted-by":"publisher","first-page":"851","DOI":"10.3390\/cells11050851","volume":"11","author":"Y Li","year":"2022","unstructured":"Li Y, Li S, Wu H (2022) Ubiquitination-proteasome system (UPS) and autophagy two main protein degradation machineries in response to cell stress. Cells 11:851. https:\/\/doi.org\/10.3390\/cells11050851","journal-title":"Cells"},{"key":"5264_CR130","doi-asserted-by":"publisher","first-page":"1430","DOI":"10.1038\/s41418-023-01154-9","volume":"30","author":"YS Yu","year":"2023","unstructured":"Yu YS, Kim H, Il KK, Baek SH (2023) Epigenetic regulation of autophagy by histone-modifying enzymes under nutrient stress. Cell Death Differ 30:1430\u20131436. https:\/\/doi.org\/10.1038\/s41418-023-01154-9","journal-title":"Cell Death Differ"},{"key":"5264_CR131","doi-asserted-by":"publisher","first-page":"309","DOI":"10.2217\/14796708.3.3.309","volume":"3","author":"SJ Cherra","year":"2008","unstructured":"Cherra SJ, Chu CT (2008) Autophagy in neuroprotection and neurodegeneration: a question of balance. Future Neurol 3:309\u2013323. https:\/\/doi.org\/10.2217\/14796708.3.3.309","journal-title":"Future Neurol"},{"key":"5264_CR132","doi-asserted-by":"publisher","DOI":"10.1016\/j.pharmthera.2022.108171","author":"M Eshraghi","year":"2022","unstructured":"Eshraghi M, Ahmadi M, Afshar S et al (2022) Enhancing autophagy in Alzheimer\u2019s disease through drug repositioning. Pharmacol Ther. https:\/\/doi.org\/10.1016\/j.pharmthera.2022.108171","journal-title":"Pharmacol Ther"},{"key":"5264_CR133","doi-asserted-by":"publisher","first-page":"655","DOI":"10.1016\/j.arcmed.2012.10.015","volume":"43","author":"V Shukla","year":"2012","unstructured":"Shukla V, Skuntz S, Pant HC (2012) Deregulated Cdk5 activity is involved in inducing Alzheimer\u2019s disease. Arch Med Res 43:655\u2013662. https:\/\/doi.org\/10.1016\/j.arcmed.2012.10.015","journal-title":"Arch Med Res"},{"key":"5264_CR134","doi-asserted-by":"publisher","first-page":"102548","DOI":"10.3389\/fnmol.2014.00065","volume":"7","author":"T Kimura","year":"2014","unstructured":"Kimura T, Ishiguro K, Hisanaga SI (2014) Physiological and pathological phosphorylation of tau by Cdk5. Front Mol Neurosci 7:102548. https:\/\/doi.org\/10.3389\/fnmol.2014.00065","journal-title":"Front Mol Neurosci"},{"key":"5264_CR135","doi-asserted-by":"publisher","DOI":"10.1186\/s13024-017-0191-y","author":"E Patrick","year":"2017","unstructured":"Patrick E, Rajagopal S, Wong HKA et al (2017) Dissecting the role of non-coding RNAs in the accumulation of amyloid and tau neuropathologies in Alzheimer\u2019s disease. Mol Neurodegener. https:\/\/doi.org\/10.1186\/s13024-017-0191-y","journal-title":"Mol Neurodegener"},{"key":"5264_CR136","doi-asserted-by":"publisher","first-page":"524976","DOI":"10.3389\/fneur.2020.00288","volume":"11","author":"X Kou","year":"2020","unstructured":"Kou X, Chen D, Chen N (2020) The regulation of microRNAs in Alzheimer\u2019s disease. Front Neurol 11:524976. https:\/\/doi.org\/10.3389\/fneur.2020.00288","journal-title":"Front Neurol"},{"key":"5264_CR137","doi-asserted-by":"publisher","first-page":"463","DOI":"10.1002\/ibra.12121","volume":"9","author":"HY Qin","year":"2023","unstructured":"Qin HY, Liu JY, Fang CL et al (2023) DNA methylation: the epigenetic mechanism of Alzheimer\u2019s disease. Ibrain 9:463\u2013472. https:\/\/doi.org\/10.1002\/ibra.12121","journal-title":"Ibrain"},{"key":"5264_CR138","doi-asserted-by":"publisher","first-page":"102556","DOI":"10.1016\/j.arr.2024.102556","volume":"102","author":"T Behl","year":"2024","unstructured":"Behl T, Kyada A, Roopashree R et al (2024) Epigenetic biomarkers in Alzheimer\u2019s disease: diagnostic and prognostic relevance. Ageing Res Rev 102:102556. https:\/\/doi.org\/10.1016\/j.arr.2024.102556","journal-title":"Ageing Res Rev"},{"key":"5264_CR139","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41467-022-33394-7","volume":"13","author":"G Shireby","year":"2022","unstructured":"Shireby G, Dempster EL, Policicchio S (2022) DNA methylation signatures of Alzheimer\u2019s disease neuropathology in the cortex are primarily driven by variation in non-neuronal cell-types. Nat Commun 13:1\u201314. https:\/\/doi.org\/10.1038\/s41467-022-33394-7","journal-title":"Nat Commun"},{"key":"5264_CR140","doi-asserted-by":"publisher","first-page":"985023","DOI":"10.3389\/fnmol.2022.985023","volume":"15","author":"M Shirinian","year":"2022","unstructured":"Shirinian M, Chen C, Uchida S, Jadavji NM (2022) Editorial: the role of epigenetics in neuropsychiatric disorders. Front Mol Neurosci 15:985023. https:\/\/doi.org\/10.3389\/fnmol.2022.985023","journal-title":"Front Mol Neurosci"},{"key":"5264_CR141","doi-asserted-by":"publisher","first-page":"140759","DOI":"10.1016\/j.bbapap.2022.140759","volume":"1870","author":"Z Soloviev","year":"2022","unstructured":"Soloviev Z, Bullock JMA, James JMB et al (2022) Structural mass spectrometry decodes domain interaction and dynamics of the full-length human histone deacetylase 2. Biochim Biophys Acta - Proteins Proteomics 1870:140759. https:\/\/doi.org\/10.1016\/j.bbapap.2022.140759","journal-title":"Biochim Biophys Acta - Proteins Proteomics"},{"key":"5264_CR142","doi-asserted-by":"publisher","first-page":"804","DOI":"10.1039\/c4sc02130d","volume":"6","author":"FF Wagner","year":"2015","unstructured":"Wagner FF, Zhang YL, Fass DM et al (2015) Kinetically selective inhibitors of histone deacetylase 2 (HDAC2) as cognition enhancers. Chem Sci 6:804\u2013815. https:\/\/doi.org\/10.1039\/c4sc02130d","journal-title":"Chem Sci"},{"key":"5264_CR143","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s00894-022-05103-0","volume":"28","author":"P Pai","year":"2022","unstructured":"Pai P, Kumar A, Shetty MG et al (2022) Identification of potent HDAC 2 inhibitors using E-pharmacophore modelling, structure-based virtual screening and molecular dynamic simulation. J Mol Model 28:1\u201314. https:\/\/doi.org\/10.1007\/s00894-022-05103-0","journal-title":"J Mol Model"},{"key":"5264_CR144","doi-asserted-by":"publisher","first-page":"96","DOI":"10.1111\/jnc.14309","volume":"145","author":"EA Thomas","year":"2018","unstructured":"Thomas EA, D\u2019Mello SR (2018) Complex neuroprotective and neurotoxic effects of histone deacetylases. J Neurochem 145:96\u2013110. https:\/\/doi.org\/10.1111\/jnc.14309","journal-title":"J Neurochem"},{"key":"5264_CR145","doi-asserted-by":"publisher","first-page":"806","DOI":"10.4161\/epi.20922","volume":"7","author":"RS Lahue","year":"2012","unstructured":"Lahue RS, Frizzell A (2012) Histone deacetylase complexes as caretakers of genome stability. Epigenetics 7:806\u2013810. https:\/\/doi.org\/10.4161\/epi.20922","journal-title":"Epigenetics"},{"key":"5264_CR146","doi-asserted-by":"publisher","unstructured":"Zhu Y, Huang Y, Tang T, Xie Y (2024) HDAC1 and HDAC2 orchestrate Wnt signaling to regulate neural progenitor transition during brain development. iScience 27:110600. https:\/\/doi.org\/10.1016\/j.isci.2024.110600","DOI":"10.1016\/j.isci.2024.110600"},{"key":"5264_CR147","doi-asserted-by":"publisher","first-page":"171","DOI":"10.1387\/ijdb.150071tz","volume":"59","author":"J Jaworska","year":"2015","unstructured":"Jaworska J, Ziemka-Nalecz M, Zalewska T (2015) Histone deacetylases 1 and 2 are required for brain development. Int J Dev Biol 59:171\u2013177. https:\/\/doi.org\/10.1387\/ijdb.150071tz","journal-title":"Int J Dev Biol"},{"key":"5264_CR148","doi-asserted-by":"publisher","first-page":"8242","DOI":"10.1073\/pnas.1000478107","volume":"107","author":"OM Dovey","year":"2010","unstructured":"Dovey OM, Foster CT, Cowley SM (2010) Histone deacetylase 1 (HDAC1), but not HDAC2, controls embryonic stem cell differentiation. Proc Natl Acad Sci U S A 107:8242\u20138247. https:\/\/doi.org\/10.1073\/pnas.1000478107","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5264_CR149","doi-asserted-by":"publisher","first-page":"34901","DOI":"10.1074\/jbc.M109.038356","volume":"284","author":"Y Luo","year":"2009","unstructured":"Luo Y, Jian W, Stavreva D et al (2009) Trans-regulation of histone deacetylase activities through acetylation. J Biol Chem 284:34901\u201334910. https:\/\/doi.org\/10.1074\/jbc.M109.038356","journal-title":"J Biol Chem"},{"key":"5264_CR150","doi-asserted-by":"publisher","first-page":"17576","DOI":"10.1039\/d1cp02264d","volume":"23","author":"Y Yang","year":"2021","unstructured":"Yang Y, Hu B, Yang Y et al (2021) Rational design of selective HDAC2 inhibitors for liver cancer treatment: computational insights into the selectivity mechanism through molecular dynamics simulations and QM\/MM calculations. Phys Chem Chem Phys 23:17576\u201317590. https:\/\/doi.org\/10.1039\/d1cp02264d","journal-title":"Phys Chem Chem Phys"},{"key":"5264_CR151","doi-asserted-by":"publisher","first-page":"16354","DOI":"10.1038\/s41598-021-95837-3","volume":"11","author":"JS Chen","year":"2021","unstructured":"Chen JS, Wang HK, Hsu CY et al (2021) HDAC1 deregulation promotes neuronal loss and deficit of motor function in stroke pathogenesis. Sci Rep 11:16354. https:\/\/doi.org\/10.1038\/s41598-021-95837-3","journal-title":"Sci Rep"},{"key":"5264_CR152","doi-asserted-by":"publisher","first-page":"2173","DOI":"10.1007\/s00018-012-0921-9","volume":"69","author":"N Reichert","year":"2012","unstructured":"Reichert N, Choukrallah MA, Matthias P (2012) Multiple roles of class I HDACs in proliferation, differentiation, and development. Cell Mol Life Sci 69:2173\u20132187. https:\/\/doi.org\/10.1007\/s00018-012-0921-9","journal-title":"Cell Mol Life Sci"},{"key":"5264_CR153","doi-asserted-by":"publisher","first-page":"13712","DOI":"10.1038\/s41598-018-32009-w","volume":"8","author":"CAS Banks","year":"2018","unstructured":"Banks CAS, Miah S, Adams MK et al (2018) Differential HDAC1\/2 network analysis reveals a role for prefoldin\/CCT in HDAC1\/2 complex assembly. Sci Rep 8:13712. https:\/\/doi.org\/10.1038\/s41598-018-32009-w","journal-title":"Sci Rep"},{"key":"5264_CR154","doi-asserted-by":"publisher","first-page":"690848","DOI":"10.1155\/2011\/690848","volume":"2011","author":"S Chiocca","year":"2011","unstructured":"Chiocca S, Segr\u00e9 CV (2011) Regulating the regulators: the post-translational code of class i HDAC1 and HDAC2. J Biomed Biotechnol 2011:690848. https:\/\/doi.org\/10.1155\/2011\/690848","journal-title":"J Biomed Biotechnol"},{"key":"5264_CR155","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3390\/ijms22052526","volume":"22","author":"H Frankowski","year":"2021","unstructured":"Frankowski H, Yeboah F, Berry BJ et al (2021) Knock-down of HDAC2 in human induced pluripotent stem cell derived neurons improves neuronal mitochondrial dynamics, neuronal maturation and reduces amyloid beta peptides. Int J Mol Sci 22:1\u201319. https:\/\/doi.org\/10.3390\/ijms22052526","journal-title":"Int J Mol Sci"},{"key":"5264_CR156","doi-asserted-by":"publisher","DOI":"10.1096\/fj.202301762RR","author":"N Davis","year":"2024","unstructured":"Davis N, Taylor B, Abelleira-Hervas L et al (2024) Histone deacetylase-3 regulates the expression of the amyloid precursor protein and its inhibition promotes neuroregenerative pathways in Alzheimer\u2019s disease models. FASEB J. https:\/\/doi.org\/10.1096\/fj.202301762RR","journal-title":"FASEB J"},{"key":"5264_CR157","doi-asserted-by":"publisher","unstructured":"Li Y, Izhar T, Kanekiyo T (2025) HDAC3 as an emerging therapeutic target for Alzheimer\u2019s disease and other neurological disorders. Mol Neurobiol. https:\/\/doi.org\/10.1007\/s12035-025-04866-w","DOI":"10.1007\/s12035-025-04866-w"},{"key":"5264_CR158","doi-asserted-by":"publisher","first-page":"734","DOI":"10.1038\/s41419-021-04019-6","volume":"12","author":"L Ning","year":"2021","unstructured":"Ning L, Rui X, Bo W, Qing G (2021) The critical roles of histone deacetylase 3 in the pathogenesis of solid organ injury. Cell Death Dis 12:734. https:\/\/doi.org\/10.1038\/s41419-021-04019-6","journal-title":"Cell Death Dis"},{"key":"5264_CR159","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1016\/S1097-2765(01)00429-4","volume":"9","author":"W Fischle","year":"2002","unstructured":"Fischle W, Dequiedt F, Hendzel MJ et al (2002) Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT\/N-CoR. Mol Cell 9:45\u201357. https:\/\/doi.org\/10.1016\/S1097-2765(01)00429-4","journal-title":"Mol Cell"},{"key":"5264_CR160","doi-asserted-by":"publisher","first-page":"1419685","DOI":"10.3389\/fimmu.2024.1419685","volume":"15","author":"N Watson","year":"2024","unstructured":"Watson N, Kuppuswamy S, Ledford WL, Sukumari-Ramesh S (2024) The role of HDAC3 in inflammation: mechanisms and therapeutic implications. Front Immunol 15:1419685. https:\/\/doi.org\/10.3389\/fimmu.2024.1419685","journal-title":"Front Immunol"},{"key":"5264_CR161","doi-asserted-by":"publisher","unstructured":"Abdallah DI, de Araujo ED, Patel NH et al (2023) Medicinal chemistry advances in targeting class I histone deacetylases. Explor Target Anti-tumor Ther 4:757\u2013779. https:\/\/doi.org\/10.37349\/etat.2023.00166","DOI":"10.37349\/etat.2023.00166"},{"issue":"27","key":"5264_CR162","doi-asserted-by":"publisher","first-page":"3062","DOI":"10.1038\/onc.2011.32","volume":"30","author":"J Duque-Afonso","year":"2011","unstructured":"Duque-Afonso J, Yalcin A, Berg T et al (2011) The HDAC class I-specific inhibitor entinostat (MS-275) effectively relieves epigenetic silencing of the LAT2 gene mediated by AML1\/ETO. Oncogene 30(27):3062\u20133072. https:\/\/doi.org\/10.1038\/onc.2011.32","journal-title":"Oncogene"},{"key":"5264_CR163","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s10020-021-00375-3","volume":"27","author":"P Liu","year":"2021","unstructured":"Liu P, Xiao J, Wang Y (2021) Posttranslational modification and beyond: interplay between histone deacetylase 6 and heat-shock protein 90. Mol Med 27:1\u201312. https:\/\/doi.org\/10.1186\/s10020-021-00375-3","journal-title":"Mol Med"},{"key":"5264_CR164","doi-asserted-by":"publisher","first-page":"2099","DOI":"10.1021\/acschemneuro.4c00061","volume":"15","author":"A Santini","year":"2024","unstructured":"Santini A, Tassinari E, Poeta E et al (2024) First in class dual non-ATP-competitive glycogen synthase kinase 3\u03b2\/histone deacetylase inhibitors as a potential therapeutic to treat Alzheimer\u2019s disease. ACS Chem Neurosci 15:2099\u20132111. https:\/\/doi.org\/10.1021\/acschemneuro.4c00061","journal-title":"ACS Chem Neurosci"},{"issue":"2","key":"5264_CR165","doi-asserted-by":"publisher","first-page":"151202","DOI":"10.1016\/j.ejcb.2022.151202","volume":"101","author":"AA Balmik","year":"2022","unstructured":"Balmik AA, Chinnathambi S (2022) Inter-relationship of histone deacetylase-6 with Tau-cytoskeletal organization and remodeling. Eur J Cell Biol 101(2):151202. https:\/\/doi.org\/10.1016\/j.ejcb.2022.151202","journal-title":"Eur J Cell Biol"},{"key":"5264_CR166","doi-asserted-by":"publisher","first-page":"1274","DOI":"10.3390\/ijms26031274","volume":"26","author":"L Asaad","year":"2025","unstructured":"Asaad L, Pepperrell B, McErlean E, Furlong F (2025) Regulation of HDAC6 catalytic activity in cancer: the role of post-translational modifications and protein\u2013protein interactions. Int J Mol Sci 26:1274. https:\/\/doi.org\/10.3390\/ijms26031274","journal-title":"Int J Mol Sci"},{"key":"5264_CR167","doi-asserted-by":"publisher","first-page":"2401","DOI":"10.1074\/jbc.C500241200","volume":"281","author":"Y Zhang","year":"2006","unstructured":"Zhang Y, Gilquin B, Khochbin S, Matthias P (2006) Two catalytic domains are required for protein deacetylation. J Biol Chem 281:2401\u20132404. https:\/\/doi.org\/10.1074\/jbc.C500241200","journal-title":"J Biol Chem"},{"key":"5264_CR168","doi-asserted-by":"publisher","first-page":"4679","DOI":"10.1080\/07391102.2023.2222177","volume":"42","author":"A Anand","year":"2024","unstructured":"Anand A, Ghosh P, Singh R et al (2024) Identification of potent histone deacetylase 2 (HDAC2) inhibitors through combined structure and ligand-based designs and molecular modelling approach. J Biomol Struct Dyn 42:4679\u20134698. https:\/\/doi.org\/10.1080\/07391102.2023.2222177","journal-title":"J Biomol Struct Dyn"},{"key":"5264_CR169","doi-asserted-by":"publisher","first-page":"4577","DOI":"10.1111\/bcp.14889","volume":"87","author":"AD Bondarev","year":"2021","unstructured":"Bondarev AD, Attwood MM, Jonsson J et al (2021) Recent developments of HDAC inhibitors: emerging indications and novel molecules. Br J Clin Pharmacol 87:4577\u20134597. https:\/\/doi.org\/10.1111\/bcp.14889","journal-title":"Br J Clin Pharmacol"},{"key":"5264_CR170","doi-asserted-by":"publisher","first-page":"20","DOI":"10.1016\/j.nepig.2014.10.002","volume":"1","author":"CH Volmar","year":"2015","unstructured":"Volmar CH, Wahlestedt C (2015) Histone deacetylases (HDACs) and brain function. Neuroepigenetics 1:20\u201327. https:\/\/doi.org\/10.1016\/j.nepig.2014.10.002","journal-title":"Neuroepigenetics"},{"key":"5264_CR171","doi-asserted-by":"publisher","first-page":"1964","DOI":"10.3390\/cells13231964","volume":"13","author":"AFMT Rahman","year":"2024","unstructured":"Rahman AFMT, Bulbule S, Belayet J B (2024) JRM-28, a novel HDAC2 inhibitor, upregulates plasticity-associated proteins in hippocampal neurons and enhances morphological plasticity via activation of CREB: implications for Alzheimer\u2019s disease. Cells 13:1964. https:\/\/doi.org\/10.3390\/cells13231964","journal-title":"Cells"},{"key":"5264_CR172","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1186\/s13195-024-01384-0","volume":"16","author":"M Zhang","year":"2024","unstructured":"Zhang M, Wang W, Ye Q et al (2024) Histone deacetylase inhibitors VPA and WT161 ameliorate the pathological features and cognitive impairments of the APP\/PS1 Alzheimer\u2019s disease mouse model by regulating the expression of APP secretases. Alzheimer\u2019s Res Ther 16:15. https:\/\/doi.org\/10.1186\/s13195-024-01384-0","journal-title":"Alzheimer\u2019s Res Ther"},{"key":"5264_CR173","doi-asserted-by":"publisher","first-page":"630","DOI":"10.1248\/cpb.c23-00027","volume":"72","author":"Y Yamashita","year":"2024","unstructured":"Yamashita Y, Itoh Y, Takada Y, Suzuki T (2024) Epigenetic inhibitors as Alzheimer\u2019s disease therapeutic agents. Chem Pharm Bull 72:630\u2013637. https:\/\/doi.org\/10.1248\/cpb.c23-00027","journal-title":"Chem Pharm Bull"},{"key":"5264_CR174","doi-asserted-by":"publisher","first-page":"e12487","DOI":"10.1002\/trc2.12487","volume":"10","author":"SE Arnold","year":"2024","unstructured":"Arnold SE, Hendrix S, Nicodemus-Johnson J et al (2024) Biological effects of sodium phenylbutyrate and taurursodiol in Alzheimer\u2019s disease. Alzheimer\u2019s Dement Transl Res Clin Interv 10:e12487. https:\/\/doi.org\/10.1002\/trc2.12487","journal-title":"Alzheimer\u2019s Dement Transl Res Clin Interv"},{"key":"5264_CR175","unstructured":"Diseases GC for N (2019) Clinical trial to determine tolerable doses of vorinostat in patients with mild Alzheimer disease (VostatAD01). In: Clinicaltrials.gov. https:\/\/clinicaltrials.gov\/ct2\/show\/NCT03056495. Accessed 30 May 2025"},{"key":"5264_CR176","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1186\/s40035-017-0089-1","volume":"6","author":"S Yang","year":"2017","unstructured":"Yang S, Zhang R, Wang G, Zhang Y (2017) The development prospection of HDAC inhibitors as a potential therapeutic direction in Alzheimer\u2019s disease. Transl Neurodegener 6:19. https:\/\/doi.org\/10.1186\/s40035-017-0089-1","journal-title":"Transl Neurodegener"},{"key":"5264_CR177","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1016\/j.mcn.2016.09.003","volume":"77","author":"S Shukla","year":"2016","unstructured":"Shukla S, Shariat-Madar Z, Walker LA, Tekwani BL (2016) Mechanism for neurotropic action of vorinostat, a pan histone deacetylase inhibitor. Mol Cell Neurosci 77:11\u201320. https:\/\/doi.org\/10.1016\/j.mcn.2016.09.003","journal-title":"Mol Cell Neurosci"},{"key":"5264_CR178","doi-asserted-by":"publisher","first-page":"494","DOI":"10.1111\/j.1476-5381.2011.01575.x","volume":"165","author":"SH Chen","year":"2012","unstructured":"Chen SH, Wu HM, Ossola B et al (2012) Suberoylanilide hydroxamic acid, a histone deacetylase inhibitor, protects dopaminergic neurons from neurotoxin-induced damage. Br J Pharmacol 165:494\u2013505. https:\/\/doi.org\/10.1111\/j.1476-5381.2011.01575.x","journal-title":"Br J Pharmacol"},{"key":"5264_CR179","doi-asserted-by":"publisher","first-page":"110","DOI":"10.1016\/j.ydbio.2022.07.002","volume":"490","author":"TA Khan","year":"2022","unstructured":"Khan TA, Guo A, Martin J et al (2022) Directed mechanisms for apical dendrite development during neuronal polarization. Dev Biol 490:110\u2013116. https:\/\/doi.org\/10.1016\/j.ydbio.2022.07.002","journal-title":"Dev Biol"},{"key":"5264_CR180","doi-asserted-by":"publisher","first-page":"117","DOI":"10.3389\/fnmol.2018.00117","volume":"11","author":"X Chen","year":"2018","unstructured":"Chen X, Wang H, Zhou M et al (2018) Valproic acid attenuates traumatic brain injury-induced inflammation in vivo: involvement of autophagy and the Nrf2\/ARE signaling pathway. Front Mol Neurosci 11:117. https:\/\/doi.org\/10.3389\/fnmol.2018.00117","journal-title":"Front Mol Neurosci"},{"key":"5264_CR181","doi-asserted-by":"publisher","first-page":"1621","DOI":"10.1007\/s11064-014-1241-2","volume":"39","author":"S Chen","year":"2014","unstructured":"Chen S, Wu H, Klebe D et al (2014) Valproic acid: a new candidate of therapeutic application for the acute central nervous system injuries. Neurochem Res 39:1621\u20131633. https:\/\/doi.org\/10.1007\/s11064-014-1241-2","journal-title":"Neurochem Res"},{"key":"5264_CR182","doi-asserted-by":"publisher","unstructured":"Dai C, Liu B, Peng B et al (2021) Entinostat improves motor function and neuronal damage via downregulating NLRP3 inflammasome activation after spinal cord injury. Front Pharmacol 12:. https:\/\/doi.org\/10.3389\/fphar.2021.774539","DOI":"10.3389\/fphar.2021.774539"},{"key":"5264_CR183","doi-asserted-by":"publisher","unstructured":"Liang T, Zhang Y, Wu S et al (2022) The role of NLRP3 inflammasome in Alzheimer\u2019s disease and potential therapeutic targets. Front Pharmacol. https:\/\/doi.org\/10.3389\/fphar.2022.845185","DOI":"10.3389\/fphar.2022.845185"},{"key":"5264_CR184","doi-asserted-by":"publisher","first-page":"884","DOI":"10.1021\/acsmedchemlett.8b00099","volume":"9","author":"S Hiranaka","year":"2018","unstructured":"Hiranaka S, Tega Y, Higuchi K et al (2018) Design, synthesis, and blood-brain barrier transport study of pyrilamine derivatives as histone deacetylase inhibitors. ACS Med Chem Lett 9:884\u2013888. https:\/\/doi.org\/10.1021\/acsmedchemlett.8b00099","journal-title":"ACS Med Chem Lett"},{"key":"5264_CR185","doi-asserted-by":"publisher","unstructured":"Shen Y, Zhao J, Yang R et al (2024) Panobinostat attenuates experimental autoimmune encephalomyelitis in mice via suppressing oxidative stress-related neuroinflammation and mitochondrial dysfunction. Int J Mol Sci 25:. https:\/\/doi.org\/10.3390\/ijms252212035","DOI":"10.3390\/ijms252212035"},{"key":"5264_CR186","doi-asserted-by":"publisher","unstructured":"Sun J, Wang F, Li H et al (2015) Neuroprotective effect of sodium butyrate against cerebral ischemia\/reperfusion injury in mice. Biomed Res Int 2015:. https:\/\/doi.org\/10.1155\/2015\/395895","DOI":"10.1155\/2015\/395895"},{"key":"5264_CR187","doi-asserted-by":"publisher","first-page":"2348","DOI":"10.1007\/s11064-021-03369-z","volume":"46","author":"AB Bayazid","year":"2021","unstructured":"Bayazid AB, Jang YA, Kim YM et al (2021) Neuroprotective effects of sodium butyrate through suppressing neuroinflammation and modulating antioxidant enzymes. Neurochem Res 46:2348\u20132358. https:\/\/doi.org\/10.1007\/s11064-021-03369-z","journal-title":"Neurochem Res"},{"key":"5264_CR188","doi-asserted-by":"publisher","unstructured":"Bayazid AB, Kim JG, Azam S et al (2022) Sodium butyrate ameliorates neurotoxicity and exerts anti-inflammatory effects in high fat diet-fed mice. Food Chem Toxicol. https:\/\/doi.org\/10.1016\/j.fct.2021.112743","DOI":"10.1016\/j.fct.2021.112743"},{"key":"5264_CR189","doi-asserted-by":"publisher","unstructured":"Lumpkin CJ, Harris AW, Connell AJ et al (2023) Evaluation of the orally bioavailable 4-phenylbutyrate-tethered trichostatin A analogue AR42 in models of spinal muscular atrophy. Sci Rep 13:. https:\/\/doi.org\/10.1038\/s41598-023-37496-0","DOI":"10.1038\/s41598-023-37496-0"},{"key":"5264_CR190","doi-asserted-by":"publisher","unstructured":"Yadav A, Huang TC, Chen SH et al (2021) Sodium phenylbutyrate inhibits Schwann cell inflammation via HDAC and NF\u03baB to promote axonal regeneration and remyelination. J Neuroinflammation. https:\/\/doi.org\/10.1186\/s12974-021-02273-1","DOI":"10.1186\/s12974-021-02273-1"},{"key":"5264_CR191","doi-asserted-by":"publisher","first-page":"1123","DOI":"10.1017\/S1461145708009024","volume":"11","author":"X Wu","year":"2008","unstructured":"Wu X, Chen PS, Dallas S et al (2008) Histone deacetylase inhibitors up-regulate astrocyte GDNF and BDNF gene transcription and protect dopaminergic neurons. Int J Neuropsychopharmacol 11:1123\u20131134. https:\/\/doi.org\/10.1017\/S1461145708009024","journal-title":"Int J Neuropsychopharmacol"},{"key":"5264_CR192","doi-asserted-by":"publisher","first-page":"308","DOI":"10.1111\/cns.12217","volume":"20","author":"M Zhu","year":"2014","unstructured":"Zhu M, Li WW, Lu CZ (2014) Histone decacetylase inhibitors prevent mitochondrial fragmentation and elicit early neuroprotection against MPP+. CNS Neurosci Ther 20:308\u2013316. https:\/\/doi.org\/10.1111\/cns.12217","journal-title":"CNS Neurosci Ther"},{"key":"5264_CR193","doi-asserted-by":"publisher","unstructured":"Zeng H, Xu L, Zou Y, Wang S (2021) Romidepsin and metformin nanomaterials delivery on streptozocin for the treatment of Alzheimer\u2019s disease in animal model. Biomed Pharmacother 141:. https:\/\/doi.org\/10.1016\/j.biopha.2021.111864","DOI":"10.1016\/j.biopha.2021.111864"},{"key":"5264_CR194","doi-asserted-by":"publisher","first-page":"304","DOI":"10.1093\/hmg\/ddn357","volume":"18","author":"J Hauke","year":"2009","unstructured":"Hauke J, Riessland M, Lunke S et al (2009) Survival motor neuron gene 2 silencing by DNA methylation correlates with spinal muscular atrophy disease severity and can be bypassed by histone deacetylase inhibition. Hum Mol Genet 18:304\u2013317. https:\/\/doi.org\/10.1093\/hmg\/ddn357","journal-title":"Hum Mol Genet"},{"key":"5264_CR195","doi-asserted-by":"publisher","unstructured":"Cleophas MCP, Cri\u015fan TO, Kl\u00fcck V et al (2019) Romidepsin suppresses monosodium urate crystal-induced cytokine production through upregulation of suppressor of cytokine signaling 1 expression. Arthritis Res Ther. https:\/\/doi.org\/10.1186\/s13075-019-1834-x","DOI":"10.1186\/s13075-019-1834-x"},{"key":"5264_CR196","doi-asserted-by":"publisher","unstructured":"Dennison J, Mendez A, Szeto A et al (2023) Low-dose chidamide treatment displays sex-specific differences in the 3xTg-AD mouse. Biomolecules. https:\/\/doi.org\/10.3390\/biom13091324","DOI":"10.3390\/biom13091324"},{"key":"5264_CR197","doi-asserted-by":"publisher","first-page":"174","DOI":"10.1107\/S2053230X17003740","volume":"73","author":"C V\u00e9nien-Bryan","year":"2017","unstructured":"V\u00e9nien-Bryan C, Li Z, Vuillard L, Boutin JA (2017) Cryo-electron microscopy and X-ray crystallography: complementary approaches to structural biology and drug discovery. Acta Crystallogr Sect Struct Biol Commun 73:174\u2013183. https:\/\/doi.org\/10.1107\/S2053230X17003740","journal-title":"Acta Crystallogr Sect Struct Biol Commun"},{"issue":"1","key":"5264_CR198","doi-asserted-by":"publisher","first-page":"4851","DOI":"10.1038\/s41467-023-40253-6","volume":"14","author":"L Yang","year":"2023","unstructured":"Yang L, Wagner T, Mechaly A et al (2023) High resolution cryo-EM and crystallographic snapshots of the actinobacterial two-in-one 2-oxoglutarate dehydrogenase. Nat Commun 14(1):4851. https:\/\/doi.org\/10.1038\/s41467-023-40253-6","journal-title":"Nat Commun"},{"key":"5264_CR199","doi-asserted-by":"publisher","unstructured":"Firdaus Z, Li X (2024) Epigenetic explorations of neurological disorders, the identification methods, and therapeutic avenues. Int J Mol Sci 25:. https:\/\/doi.org\/10.3390\/ijms252111658","DOI":"10.3390\/ijms252111658"},{"key":"5264_CR200","doi-asserted-by":"publisher","unstructured":"Cornu M, Lemaitre T, Kieffer C, Voisin-Chiret AS (2025) PROTAC 2.0: expanding the frontiers of targeted protein degradation. Drug Discov Today 30:104376. https:\/\/doi.org\/10.1016\/j.drudis.2025.104376","DOI":"10.1016\/j.drudis.2025.104376"},{"key":"5264_CR201","doi-asserted-by":"publisher","first-page":"901","DOI":"10.1016\/j.ijbiomac.2022.03.203","volume":"208","author":"S Arora","year":"2022","unstructured":"Arora S, Kanekiyo T, Singh J (2022) Functionalized nanoparticles for brain targeted BDNF gene therapy to rescue Alzheimer\u2019s disease pathology in transgenic mouse model. Int J Biol Macromol 208:901\u2013911. https:\/\/doi.org\/10.1016\/j.ijbiomac.2022.03.203","journal-title":"Int J Biol Macromol"},{"key":"5264_CR202","doi-asserted-by":"publisher","DOI":"10.3390\/ijms24065851","author":"M Ren","year":"2023","unstructured":"Ren M, Zhou Y, Tu T et al (2023) RVG peptide-functionalized favipiravir nanoparticle delivery system facilitates antiviral therapy of neurotropic virus infection in a mouse model. Int J Mol Sci. https:\/\/doi.org\/10.3390\/ijms24065851","journal-title":"Int J Mol Sci"},{"key":"5264_CR203","doi-asserted-by":"publisher","unstructured":"Nederveen JP, Warnier G, Di Carlo A et al (2021) Extracellular vesicles and exosomes: insights from exercise science. Front Physiol 11:. https:\/\/doi.org\/10.3389\/fphys.2020.604274","DOI":"10.3389\/fphys.2020.604274"},{"key":"5264_CR204","doi-asserted-by":"publisher","unstructured":"Dalvi A, Ravi PR, Uppuluri CT (2021) Rufinamide-loaded chitosan nanoparticles in xyloglucan-based thermoresponsive in situ gel for direct nose to brain delivery. Front Pharmacol. https:\/\/doi.org\/10.3389\/fphar.2021.691936","DOI":"10.3389\/fphar.2021.691936"},{"key":"5264_CR205","doi-asserted-by":"publisher","first-page":"2183","DOI":"10.1016\/j.molcel.2021.04.015","volume":"81","author":"SJ Hogg","year":"2021","unstructured":"Hogg SJ, Motorna O, Cluse LA (2021) Targeting histone acetylation dynamics and oncogenic transcription by catalytic P300\/CBP inhibition. Mol Cell 81:2183\u20132200. https:\/\/doi.org\/10.1016\/j.molcel.2021.04.015","journal-title":"Mol Cell"},{"key":"5264_CR206","doi-asserted-by":"publisher","first-page":"630600","DOI":"10.3389\/fgeed.2021.630600","volume":"3","author":"A McTague","year":"2021","unstructured":"McTague A, Rossignoli G, Ferrini A et al (2021) Genome editing in iPSC-based neural systems: from disease models to future therapeutic strategies. Front Genome Ed 3:630600. https:\/\/doi.org\/10.3389\/fgeed.2021.630600","journal-title":"Front Genome Ed"},{"key":"5264_CR207","doi-asserted-by":"publisher","first-page":"1235","DOI":"10.1016\/j.neuron.2024.01.013","volume":"112","author":"A Ramakrishnan","year":"2024","unstructured":"Ramakrishnan A, Piehl N, Simonton B (2024) Epigenetic dysregulation in Alzheimer\u2019s disease peripheral immunity. Neuron 112:1235\u20131248. https:\/\/doi.org\/10.1016\/j.neuron.2024.01.013","journal-title":"Neuron"},{"key":"5264_CR208","doi-asserted-by":"publisher","first-page":"496","DOI":"10.1038\/s41573-023-00688-4","volume":"22","author":"B Van de Sande","year":"2023","unstructured":"Van de Sande B, Lee JS, Mutasa-Gottgens E et al (2023) Applications of single-cell RNA sequencing in drug discovery and development. Nat Rev Drug Discov 22:496\u2013520. https:\/\/doi.org\/10.1038\/s41573-023-00688-4","journal-title":"Nat Rev Drug Discov"},{"key":"5264_CR209","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3390\/jpm10030061","volume":"10","author":"C Villa","year":"2020","unstructured":"Villa C, Lavitrano M, Salvatore E, Combi R (2020) Molecular and imaging biomarkers in Alzheimer\u2019s disease: a focus on recent insights. J Pers Med 10:1\u201332. https:\/\/doi.org\/10.3390\/jpm10030061","journal-title":"J Pers Med"},{"key":"5264_CR210","doi-asserted-by":"publisher","first-page":"875","DOI":"10.3233\/JAD-180539","volume":"67","author":"JT Wiedrick","year":"2019","unstructured":"Wiedrick JT, Phillips JI, Lusardi TA et al (2019) Validation of microRNA biomarkers for Alzheimer\u2019s disease in human cerebrospinal fluid. J Alzheimer\u2019s Dis 67:875\u2013891. https:\/\/doi.org\/10.3233\/JAD-180539","journal-title":"J Alzheimer\u2019s Dis"}],"container-title":["Molecular Neurobiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12035-025-05264-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s12035-025-05264-y\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12035-025-05264-y.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T13:12:24Z","timestamp":1761570744000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s12035-025-05264-y"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,8,8]]},"references-count":210,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2025,12]]}},"alternative-id":["5264"],"URL":"https:\/\/doi.org\/10.1007\/s12035-025-05264-y","relation":{},"ISSN":["0893-7648","1559-1182"],"issn-type":[{"value":"0893-7648","type":"print"},{"value":"1559-1182","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,8,8]]},"assertion":[{"value":"15 April 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"23 July 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"8 August 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Not applicable.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent to Participate"}},{"value":"Not applicable.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent to Publication"}},{"value":"The authors declare no competing interests.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}