{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,13]],"date-time":"2026-09-13T04:53:11Z","timestamp":1789275191977,"version":"build-2803163510"},"reference-count":160,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,7,15]],"date-time":"2025-07-15T00:00:00Z","timestamp":1752537600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["R01 NS123298"],"award-info":[{"award-number":["R01 NS123298"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["R61 NS122098"],"award-info":[{"award-number":["R61 NS122098"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","award":["R01 AG056259"],"award-info":[{"award-number":["R01 AG056259"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","award":["U01 AG088679"],"award-info":[{"award-number":["U01 AG088679"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","award":["R35 AG071734"],"award-info":[{"award-number":["R35 AG071734"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","award":["RF1 AG057409"],"award-info":[{"award-number":["RF1 AG057409"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","award":["R56 AG065372"],"award-info":[{"award-number":["R56 AG065372"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","award":["R01 AG078756"],"award-info":[{"award-number":["R01 AG078756"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000027","name":"National Institute on Alcohol Abuse and Alcoholism","doi-asserted-by":"publisher","award":["R01 DA048882"],"award-info":[{"award-number":["R01 DA048882"]}],"id":[{"id":"10.13039\/100000027","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000027","name":"National Institute on Alcohol Abuse and Alcoholism","doi-asserted-by":"publisher","award":["DP1 DA041722"],"award-info":[{"award-number":["DP1 DA041722"]}],"id":[{"id":"10.13039\/100000027","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000900","name":"California Institute for Regenerative Medicine","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000900","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007557","name":"California Institute of Regenerative Medicine","doi-asserted-by":"publisher","award":["ReMIND-L DISC4 16292"],"award-info":[{"award-number":["ReMIND-L DISC4 16292"]}],"id":[{"id":"10.13039\/100007557","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["neurotherapeuticsjournal.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Neurotherapeutics"],"published-print":{"date-parts":[[2025,10]]},"DOI":"10.1016\/j.neurot.2025.e00708","type":"journal-article","created":{"date-parts":[[2025,7,28]],"date-time":"2025-07-28T03:10:36Z","timestamp":1753672236000},"page":"e00708","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":4,"title":["Aberrant S-nitrosylation in the TCA cycle contributes to mitochondrial dysfunction, energy compromise, and synapse loss in neurodegenerative diseases"],"prefix":"10.1016","volume":"22","author":[{"given":"Tomohiro","family":"Nakamura","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anamika","family":"Sharma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stuart A.","family":"Lipton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.neurot.2025.e00708_bib1","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.3233\/JAD-160702","article-title":"Mitochondrial dysfunction and synaptic transmission failure in Alzheimer's disease","volume":"57","author":"Guo","year":"2017","journal-title":"J Alzheimers Dis"},{"key":"10.1016\/j.neurot.2025.e00708_bib2","doi-asserted-by":"crossref","DOI":"10.3390\/ijms23073627","article-title":"Synapses: the brain's energy-demanding sites","volume":"23","author":"Faria-Pereira","year":"2022","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.neurot.2025.e00708_bib3","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.conb.2019.02.001","article-title":"Powerhouse of the mind: mitochondrial plasticity at the synapse","volume":"57","author":"Rossi","year":"2019","journal-title":"Curr Opin Neurobiol"},{"key":"10.1016\/j.neurot.2025.e00708_bib4","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/S0074-7696(05)24002-0","article-title":"Apoptosis and necrosis in health and disease: role of mitochondria","volume":"224","author":"Nieminen","year":"2003","journal-title":"Int Rev Cytol"},{"key":"10.1016\/j.neurot.2025.e00708_bib5","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1002\/ana.410270502","article-title":"Synapse loss in frontal cortex biopsies in Alzheimer's disease: correlation with cognitive severity","volume":"27","author":"DeKosky","year":"1990","journal-title":"Ann Neurol"},{"key":"10.1016\/j.neurot.2025.e00708_bib6","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1177\/10738584221139761","article-title":"Mitochondria in aging and Alzheimer's disease: focus on mitophagy","volume":"30","author":"Pradeepkiran","year":"2024","journal-title":"Neuroscientist"},{"key":"10.1016\/j.neurot.2025.e00708_bib7","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1002\/ana.410300410","article-title":"Physical basis of cognitive alterations in Alzheimer's disease: synapse loss is the major correlate of cognitive impairment","volume":"30","author":"Terry","year":"1991","journal-title":"Ann Neurol"},{"key":"10.1016\/j.neurot.2025.e00708_bib8","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/j.cell.2022.12.032","article-title":"Hallmarks of neurodegenerative diseases","volume":"186","author":"Wilson","year":"2023","journal-title":"Cell"},{"key":"10.1016\/j.neurot.2025.e00708_bib9","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1016\/j.neuron.2013.05.005","article-title":"Aberrant protein S-nitrosylation in neurodegenerative diseases","volume":"78","author":"Nakamura","year":"2013","journal-title":"Neuron"},{"key":"10.1016\/j.neurot.2025.e00708_bib10","doi-asserted-by":"crossref","first-page":"3823","DOI":"10.1016\/j.neuron.2024.10.013","article-title":"Redox regulation, protein S-nitrosylation, and synapse loss in Alzheimer's and related dementias","volume":"112","author":"Oh","year":"2024","journal-title":"Neuron"},{"key":"10.1016\/j.neurot.2025.e00708_bib11","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1038\/nature05292","article-title":"Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases","volume":"443","author":"Lin","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.neurot.2025.e00708_bib12","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1016\/j.tem.2017.10.004","article-title":"'SNO'-Storms compromise protein activity and mitochondrial metabolism in neurodegenerative disorders","volume":"28","author":"Nakamura","year":"2017","journal-title":"Trends Endocrinol Metab"},{"key":"10.1016\/j.neurot.2025.e00708_bib13","doi-asserted-by":"crossref","DOI":"10.1126\/stke.2001.86.re1","article-title":"S-Nitrosylation is emerging as a specific and fundamental posttranslational protein modification: head-to-head comparison with O-phosphorylation","volume":"2001","author":"Lane","year":"2001","journal-title":"Sci STKE"},{"key":"10.1016\/j.neurot.2025.e00708_bib14","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1038\/351714a0","article-title":"Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase","volume":"351","author":"Bredt","year":"1991","journal-title":"Nature"},{"key":"10.1016\/j.neurot.2025.e00708_bib15","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/j.molmed.2009.06.007","article-title":"Protein S-nitrosylation in health and disease: a current perspective","volume":"15","author":"Foster","year":"2009","journal-title":"Trends Mol Med"},{"key":"10.1016\/j.neurot.2025.e00708_bib16","doi-asserted-by":"crossref","first-page":"1849","DOI":"10.1016\/0006-2952(91)90581-O","article-title":"Isoforms of nitric oxide synthase. Characterization and purification from different cell types","volume":"42","author":"Forstermann","year":"1991","journal-title":"Biochem Pharmacol"},{"key":"10.1016\/j.neurot.2025.e00708_bib17","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/S0005-2728(99)00016-X","article-title":"Mammalian nitric oxide synthases","volume":"1411","author":"Stuehr","year":"1999","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.neurot.2025.e00708_bib18","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1038\/nrd2466","article-title":"The nitrate-nitrite-nitric oxide pathway in physiology and therapeutics","volume":"7","author":"Lundberg","year":"2008","journal-title":"Nat Rev Drug Discov"},{"key":"10.1016\/j.neurot.2025.e00708_bib19","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1038\/nchembio.260","article-title":"Nitrate and nitrite in biology, nutrition and therapeutics","volume":"5","author":"Lundberg","year":"2009","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib20","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2023.113514","article-title":"Astrocytes produce nitric oxide via nitrite reduction in mitochondria to regulate cerebral blood flow during brain hypoxia","volume":"42","author":"Christie","year":"2023","journal-title":"Cell Rep"},{"key":"10.1016\/j.neurot.2025.e00708_bib21","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1016\/0896-6273(92)90130-6","article-title":"Effect of nitric oxide production on the redox modulatory site of the NMDA receptor-channel complex","volume":"8","author":"Lei","year":"1992","journal-title":"Neuron"},{"key":"10.1016\/j.neurot.2025.e00708_bib22","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1073\/pnas.89.1.444","article-title":"S-nitrosylation of proteins with nitric oxide: synthesis and characterization of biologically active compounds","volume":"89","author":"Stamler","year":"1992","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.neurot.2025.e00708_bib23","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1038\/364626a0","article-title":"A redox-based mechanism for the neuroprotective and neurodestructive effects of nitric oxide and related nitroso-compounds","volume":"364","author":"Lipton","year":"1993","journal-title":"Nature"},{"key":"10.1016\/j.neurot.2025.e00708_bib24","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1016\/j.cbpa.2012.10.016","article-title":"Mechanisms of S-nitrosothiol formation and selectivity in nitric oxide signaling","volume":"16","author":"Smith","year":"2012","journal-title":"Curr Opin Chem Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib25","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/S0076-6879(05)96010-2","article-title":"S-Nitrosothiol formation","volume":"396","author":"Carver","year":"2005","journal-title":"Methods Enzymol"},{"key":"10.1016\/j.neurot.2025.e00708_bib26","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.neuron.2006.11.023","article-title":"Hypoxia enhances S-nitrosylation-mediated NMDA receptor inhibition via a thiol oxygen sensor motif","volume":"53","author":"Takahashi","year":"2007","journal-title":"Neuron"},{"key":"10.1016\/j.neurot.2025.e00708_bib27","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.nbd.2015.03.017","article-title":"Aberrant protein S-nitrosylation contributes to the pathophysiology of neurodegenerative diseases","volume":"84","author":"Nakamura","year":"2015","journal-title":"Neurobiol Dis"},{"key":"10.1016\/j.neurot.2025.e00708_bib28","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/j.molcel.2023.12.018","article-title":"Enzymatic and non-enzymatic transnitrosylation: \"SCAN\"ning the SNO-proteome","volume":"84","author":"Nakamura","year":"2024","journal-title":"Mol Cell"},{"key":"10.1016\/j.neurot.2025.e00708_bib29","doi-asserted-by":"crossref","first-page":"5812","DOI":"10.1016\/j.cell.2023.11.009","article-title":"An enzyme that selectively S-nitrosylates proteins to regulate insulin signaling","volume":"186","author":"Zhou","year":"2023","journal-title":"Cell"},{"key":"10.1016\/j.neurot.2025.e00708_bib30","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1016\/S0896-6273(00)80310-4","article-title":"(S)NO signals: translocation, regulation, and a consensus motif","volume":"18","author":"Stamler","year":"1997","journal-title":"Neuron"},{"key":"10.1016\/j.neurot.2025.e00708_bib31","doi-asserted-by":"crossref","first-page":"97","DOI":"10.2174\/156802607779318253","article-title":"Pharmacologic manipulation of nitric oxide signaling: targeting NOS dimerization and protein-protein interactions","volume":"7","author":"Paige","year":"2007","journal-title":"Curr Top Med Chem"},{"key":"10.1016\/j.neurot.2025.e00708_bib32","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1016\/j.jmb.2009.10.042","article-title":"Structural analysis of cysteine S-nitrosylation: a modified acid-based motif and the emerging role of trans-nitrosylation","volume":"395","author":"Marino","year":"2010","journal-title":"J Mol Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib33","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/j.abb.2016.10.015","article-title":"How are nitrosothiols formed de novo in vivo?","volume":"617","author":"Lancaster","year":"2017","journal-title":"Arch Biochem Biophys"},{"key":"10.1016\/j.neurot.2025.e00708_bib34","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1038\/nchembio720","article-title":"Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine","volume":"1","author":"Mitchell","year":"2005","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib35","doi-asserted-by":"crossref","DOI":"10.1126\/science.aaw0843","article-title":"Noncanonical transnitrosylation network contributes to synapse loss in Alzheimer's disease","volume":"371","author":"Nakamura","year":"2021","journal-title":"Science"},{"key":"10.1016\/j.neurot.2025.e00708_bib36","doi-asserted-by":"crossref","first-page":"14330","DOI":"10.1073\/pnas.1105172108","article-title":"S-Nitrosylation activates Cdk5 and contributes to synaptic spine loss induced by beta-amyloid peptide","volume":"108","author":"Qu","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.neurot.2025.e00708_bib37","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1126\/science.1171091","article-title":"S-Nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury","volume":"324","author":"Cho","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.neurot.2025.e00708_bib38","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1038\/71090","article-title":"Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation","volume":"3","author":"Choi","year":"2000","journal-title":"Nat Neurosci"},{"key":"10.1016\/j.neurot.2025.e00708_bib39","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.1126\/science.1073634","article-title":"S-Nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death","volume":"297","author":"Gu","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.neurot.2025.e00708_bib40","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1016\/j.molcel.2017.12.019","article-title":"Evidence against stable protein S-nitrosylation as a widespread mechanism of post-translational regulation","volume":"69","author":"Wolhuter","year":"2018","journal-title":"Mol Cell"},{"key":"10.1016\/j.neurot.2025.e00708_bib41","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/nrm3391","article-title":"H(2)S signalling through protein sulfhydration and beyond","volume":"13","author":"Paul","year":"2012","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib42","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.neuron.2011.05.033","article-title":"S-Nitrosylation and S-palmitoylation reciprocally regulate synaptic targeting of PSD-95","volume":"71","author":"Ho","year":"2011","journal-title":"Neuron"},{"key":"10.1016\/j.neurot.2025.e00708_bib43","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1016\/S1074-5521(96)90133-7","article-title":"Generation of nitric oxide from S-nitrosothiols using protein-bound Cu2+ sources","volume":"3","author":"Dicks","year":"1996","journal-title":"Chem Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib44","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1093\/oxfordjournals.jbchem.a021883","article-title":"Ascorbic acid and reducing agents regulate the fates and functions of S-nitrosothiols","volume":"122","author":"Kashiba-Iwatsuki","year":"1997","journal-title":"J Biochem"},{"key":"10.1016\/j.neurot.2025.e00708_bib45","doi-asserted-by":"crossref","first-page":"1331","DOI":"10.1089\/ars.2017.7403","article-title":"Protein S-nitrosylation: determinants of specificity and enzymatic regulation of S-Nitrosothiol-Based signaling","volume":"30","author":"Stomberski","year":"2019","journal-title":"Antioxid Redox Signal"},{"key":"10.1016\/j.neurot.2025.e00708_bib46","doi-asserted-by":"crossref","first-page":"1050","DOI":"10.1126\/science.1158265","article-title":"Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins","volume":"320","author":"Benhar","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.neurot.2025.e00708_bib47","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1038\/nrm2764","article-title":"Protein denitrosylation: enzymatic mechanisms and cellular functions","volume":"10","author":"Benhar","year":"2009","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib48","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1038\/35055104","article-title":"Protein S-nitrosylation: a physiological signal for neuronal nitric oxide","volume":"3","author":"Jaffrey","year":"2001","journal-title":"Nat Cell Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib49","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1073\/pnas.0508412103","article-title":"SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures","volume":"103","author":"Hao","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.neurot.2025.e00708_bib50","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1016\/j.freeradbiomed.2010.05.001","article-title":"Detection of protein S-nitrosation using irreversible biotinylation procedures (IBP)","volume":"49","author":"Huang","year":"2010","journal-title":"Free Radic Biol Med"},{"key":"10.1016\/j.neurot.2025.e00708_bib51","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1038\/nbt.1545","article-title":"Proteomic analysis of S-nitrosylation and denitrosylation by resin-assisted capture","volume":"27","author":"Forrester","year":"2009","journal-title":"Nat Biotechnol"},{"key":"10.1016\/j.neurot.2025.e00708_bib52","doi-asserted-by":"crossref","first-page":"2195","DOI":"10.1038\/s41467-019-10182-4","article-title":"Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique","volume":"10","author":"Mnatsakanyan","year":"2019","journal-title":"Nat Commun"},{"key":"10.1016\/j.neurot.2025.e00708_bib53","doi-asserted-by":"crossref","first-page":"16958","DOI":"10.1073\/pnas.1008036107","article-title":"Structural profiling of endogenous S-nitrosocysteine residues reveals unique features that accommodate diverse mechanisms for protein S-nitrosylation","volume":"107","author":"Doulias","year":"2010","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.neurot.2025.e00708_bib54","doi-asserted-by":"crossref","first-page":"7693","DOI":"10.1021\/ja401565w","article-title":"Mechanism-based triarylphosphine-ester probes for capture of endogenous RSNOs","volume":"135","author":"Seneviratne","year":"2013","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.neurot.2025.e00708_bib55","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.ade0764","article-title":"Mechanistic insight into female predominance in Alzheimer's disease based on aberrant protein S-nitrosylation of C3","volume":"8","author":"Yang","year":"2022","journal-title":"Sci Adv"},{"key":"10.1016\/j.neurot.2025.e00708_bib56","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1016\/j.chembiol.2023.06.018","article-title":"S-Nitrosylation-mediated dysfunction of TCA cycle enzymes in synucleinopathy studied in postmortem human brains and hiPSC-derived neurons","volume":"30","author":"Doulias","year":"2023","journal-title":"Cell Chem Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib57","article-title":"Metabolic bypass rescues aberrant S-nitrosylation-Induced TCA cycle inhibition and synapse loss in Alzheimer's disease human neurons","volume":"11","author":"Andreyev","year":"2024","journal-title":"Adv Sci (Weinh)"},{"key":"10.1016\/j.neurot.2025.e00708_bib58","doi-asserted-by":"crossref","first-page":"4152","DOI":"10.1073\/pnas.1521318113","article-title":"S-Nitrosation of proteins relevant to Alzheimer's disease during early stages of neurodegeneration","volume":"113","author":"Seneviratne","year":"2016","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.neurot.2025.e00708_bib59","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1007\/s13365-021-00970-4","article-title":"TCA cycle metabolic compromise due to an aberrant S-nitrosoproteome in HIV-associated neurocognitive disorder with methamphetamine use","volume":"27","author":"Doulias","year":"2021","journal-title":"J Neurovirol"},{"key":"10.1016\/j.neurot.2025.e00708_bib60","doi-asserted-by":"crossref","DOI":"10.1126\/scisignal.2003252","article-title":"Nitric oxide regulates mitochondrial fatty acid metabolism through reversible protein S-nitrosylation","volume":"6","author":"Doulias","year":"2013","journal-title":"Sci Signal"},{"key":"10.1016\/j.neurot.2025.e00708_bib61","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1007\/s00018-023-04814-8","article-title":"Mitochondria as central hubs in synaptic modulation","volume":"80","author":"Duarte","year":"2023","journal-title":"Cell Mol Life Sci"},{"key":"10.1016\/j.neurot.2025.e00708_bib62","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1016\/j.neuron.2015.03.035","article-title":"A cellular perspective on brain energy metabolism and functional imaging","volume":"86","author":"Magistretti","year":"2015","journal-title":"Neuron"},{"key":"10.1016\/j.neurot.2025.e00708_bib63","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/j.cmet.2017.06.021","article-title":"Neuronal stimulation triggers neuronal glycolysis and not lactate uptake","volume":"26","author":"Diaz-Garcia","year":"2017","journal-title":"Cell Metab"},{"key":"10.1016\/j.neurot.2025.e00708_bib64","doi-asserted-by":"crossref","DOI":"10.3390\/antiox12101816","article-title":"Effects of redox homeostasis and mitochondrial damage on Alzheimer's disease","volume":"12","author":"Wu","year":"2023","journal-title":"Antioxidants"},{"key":"10.1016\/j.neurot.2025.e00708_bib65","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1016\/j.bbadis.2009.08.010","article-title":"Cause and consequence: mitochondrial dysfunction initiates and propagates neuronal dysfunction, neuronal death and behavioral abnormalities in age-associated neurodegenerative diseases","volume":"1802","author":"Gibson","year":"2010","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.neurot.2025.e00708_bib66","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1002\/ana.20474","article-title":"Mitochondrial abnormalities in Alzheimer brain: mechanistic implications","volume":"57","author":"Bubber","year":"2005","journal-title":"Ann Neurol"},{"key":"10.1016\/j.neurot.2025.e00708_bib67","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0197-0186(02)00225-5","article-title":"Deficits in a tricarboxylic acid cycle enzyme in brains from patients with Parkinson's disease","volume":"43","author":"Gibson","year":"2003","journal-title":"Neurochem Int"},{"key":"10.1016\/j.neurot.2025.e00708_bib68","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbagen.2021.129889","article-title":"Structure of the dihydrolipoamide succinyltransferase (E2) component of the human alpha-ketoglutarate dehydrogenase complex (hKGDHc) revealed by cryo-EM and cross-linking mass spectrometry: implications for the overall hKGDHc structure","volume":"1865","author":"Nagy","year":"2021","journal-title":"Biochim Biophys Acta Gen Subj"},{"key":"10.1016\/j.neurot.2025.e00708_bib69","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1042\/BJ20131664","article-title":"Studies on the regulation of the human E1 subunit of the 2-oxoglutarate dehydrogenase complex, including the identification of a novel calcium-binding site","volume":"459","author":"Armstrong","year":"2014","journal-title":"Biochem J"},{"key":"10.1016\/j.neurot.2025.e00708_bib70","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.niox.2019.04.005","article-title":"The effect of nitric oxide on mitochondrial respiration","volume":"88","author":"Poderoso","year":"2019","journal-title":"Nitric Oxide"},{"key":"10.1016\/j.neurot.2025.e00708_bib71","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1042\/BJ20100633","article-title":"Identification of S-nitrosated mitochondrial proteins by S-nitrosothiol difference in gel electrophoresis (SNO-DIGE): implications for the regulation of mitochondrial function by reversible S-nitrosation","volume":"430","author":"Chouchani","year":"2010","journal-title":"Biochem J"},{"key":"10.1016\/j.neurot.2025.e00708_bib72","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1161\/CIRCRESAHA.107.155879","article-title":"Preconditioning results in S-nitrosylation of proteins involved in regulation of mitochondrial energetics and calcium transport","volume":"101","author":"Sun","year":"2007","journal-title":"Circ Res"},{"key":"10.1016\/j.neurot.2025.e00708_bib73","doi-asserted-by":"crossref","DOI":"10.3390\/ijms232012403","article-title":"The alpha-ketoglutarate dehydrogenase complex as a hub of plasticity in neurodegeneration and regeneration","volume":"23","author":"Hansen","year":"2022","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.neurot.2025.e00708_bib74","doi-asserted-by":"crossref","first-page":"8972","DOI":"10.1523\/JNEUROSCI.20-24-08972.2000","article-title":"Inhibition of Krebs cycle enzymes by hydrogen peroxide: a key role of [alpha]-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress","volume":"20","author":"Tretter","year":"2000","journal-title":"J Neurosci"},{"key":"10.1016\/j.neurot.2025.e00708_bib75","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1385\/MN:31:1-3:043","article-title":"The alpha-ketoglutarate-dehydrogenase complex: a mediator between mitochondria and oxidative stress in neurodegeneration","volume":"31","author":"Gibson","year":"2005","journal-title":"Mol Neurobiol"},{"key":"10.1016\/j.neurot.2025.e00708_bib76","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.mcn.2012.07.005","article-title":"An update on the role of mitochondrial alpha-ketoglutarate dehydrogenase in oxidative stress","volume":"55","author":"Starkov","year":"2013","journal-title":"Mol Cell Neurosci"},{"key":"10.1016\/j.neurot.2025.e00708_bib77","doi-asserted-by":"crossref","first-page":"2335","DOI":"10.1098\/rstb.2005.1764","article-title":"Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress","volume":"360","author":"Tretter","year":"2005","journal-title":"Philos Trans R Soc Lond B Biol Sci"},{"key":"10.1016\/j.neurot.2025.e00708_bib78","doi-asserted-by":"crossref","first-page":"17640","DOI":"10.1074\/jbc.M110.203018","article-title":"Inactivation and reactivation of the mitochondrial alpha-ketoglutarate dehydrogenase complex","volume":"286","author":"Shi","year":"2011","journal-title":"J Biol Chem"},{"key":"10.1016\/j.neurot.2025.e00708_bib79","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/j.freeradbiomed.2024.09.024","article-title":"Mapping of oxidative modifications on the alpha-keto glutarate dehydrogenase complex induced by singlet oxygen: effects on structure and activity","volume":"224","author":"Gao","year":"2024","journal-title":"Free Radic Biol Med"},{"key":"10.1016\/j.neurot.2025.e00708_bib80","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.bbrc.2022.02.093","article-title":"Structural basis for the activity and regulation of human alpha-ketoglutarate dehydrogenase revealed by Cryo-EM","volume":"602","author":"Zhong","year":"2022","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.neurot.2025.e00708_bib81","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1107\/S205225252000696X","article-title":"Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolism","volume":"7","author":"Bezerra","year":"2020","journal-title":"IUCrJ"},{"key":"10.1016\/j.neurot.2025.e00708_bib82","doi-asserted-by":"crossref","DOI":"10.3390\/life11050407","article-title":"Toward an understanding of the structural and mechanistic aspects of protein-protein interactions in 2-oxoacid dehydrogenase complexes","volume":"11","author":"Nemeria","year":"2021","journal-title":"Life"},{"key":"10.1016\/j.neurot.2025.e00708_bib83","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1021\/bi7017464","article-title":"Reversible inhibition of alpha-ketoglutarate dehydrogenase by hydrogen peroxide: glutathionylation and protection of lipoic acid","volume":"47","author":"Applegate","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.neurot.2025.e00708_bib84","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1038\/s41589-022-01153-w","article-title":"Nitric oxide-driven modifications of lipoic arm inhibit alpha-ketoacid dehydrogenases","volume":"19","author":"Seim","year":"2023","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib85","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1002\/jnr.23827","article-title":"Sex and the development of Alzheimer's disease","volume":"95","author":"Pike","year":"2017","journal-title":"J Neurosci Res"},{"key":"10.1016\/j.neurot.2025.e00708_bib86","doi-asserted-by":"crossref","first-page":"25891","DOI":"10.1074\/jbc.M313853200","article-title":"New insights into protein S-nitrosylation. Mitochondria as a model system","volume":"279","author":"Foster","year":"2004","journal-title":"J Biol Chem"},{"key":"10.1016\/j.neurot.2025.e00708_bib87","doi-asserted-by":"crossref","first-page":"123","DOI":"10.3109\/10715762.2012.752078","article-title":"Reversible inactivation of dihydrolipoamide dehydrogenase by mitochondrial hydrogen peroxide","volume":"47","author":"Yan","year":"2013","journal-title":"Free Radic Res"},{"key":"10.1016\/j.neurot.2025.e00708_bib88","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.taap.2008.12.010","article-title":"Impaired mitochondrial respiration and protein nitration in the rat hippocampus after acute inhalation of combustion smoke","volume":"235","author":"Lee","year":"2009","journal-title":"Toxicol Appl Pharmacol"},{"key":"10.1016\/j.neurot.2025.e00708_bib89","doi-asserted-by":"crossref","first-page":"L996","DOI":"10.1152\/ajplung.00337.2005","article-title":"Modifications of proteins by 4-hydroxy-2-nonenal in the ventilatory muscles of rats","volume":"290","author":"Hussain","year":"2006","journal-title":"Am J Physiol Lung Cell Mol Physiol"},{"key":"10.1016\/j.neurot.2025.e00708_bib90","doi-asserted-by":"crossref","first-page":"5114","DOI":"10.1038\/s41467-023-40738-4","article-title":"Pyruvate dehydrogenase operates as an intramolecular nitroxyl generator during macrophage metabolic reprogramming","volume":"14","author":"Palmieri","year":"2023","journal-title":"Nat Commun"},{"key":"10.1016\/j.neurot.2025.e00708_bib91","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.abb.2016.08.014","article-title":"The chemical biology of HNO signaling","volume":"617","author":"Bianco","year":"2017","journal-title":"Arch Biochem Biophys"},{"key":"10.1016\/j.neurot.2025.e00708_bib92","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1016\/S0896-6273(00)80859-4","article-title":"Attenuation of NMDA receptor activity and neurotoxicity by nitroxyl anion, NO","volume":"24","author":"Kim","year":"1999","journal-title":"Neuron"},{"key":"10.1016\/j.neurot.2025.e00708_bib93","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1038\/s41467-020-14433-7","article-title":"Nitric oxide orchestrates metabolic rewiring in M1 macrophages by targeting aconitase 2 and pyruvate dehydrogenase","volume":"11","author":"Palmieri","year":"2020","journal-title":"Nat Commun"},{"key":"10.1016\/j.neurot.2025.e00708_bib94","doi-asserted-by":"crossref","DOI":"10.3390\/ijms25189950","article-title":"Mitochondrial aconitase and its contribution to the pathogenesis of neurodegenerative diseases","volume":"25","author":"Padalko","year":"2024","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.neurot.2025.e00708_bib95","doi-asserted-by":"crossref","first-page":"11986","DOI":"10.1021\/bi0509393","article-title":"Sites and mechanisms of aconitase inactivation by peroxynitrite: modulation by citrate and glutathione","volume":"44","author":"Han","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.neurot.2025.e00708_bib96","doi-asserted-by":"crossref","first-page":"14846","DOI":"10.1021\/bi0353979","article-title":"Redox-dependent modulation of aconitase activity in intact mitochondria","volume":"42","author":"Bulteau","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.neurot.2025.e00708_bib97","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1016\/j.freeradbiomed.2007.01.007","article-title":"Mitochondrial aconitase reaction with nitric oxide, S-nitrosoglutathione, and peroxynitrite: mechanisms and relative contributions to aconitase inactivation","volume":"42","author":"Tortora","year":"2007","journal-title":"Free Radic Biol Med"},{"key":"10.1016\/j.neurot.2025.e00708_bib98","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1016\/j.celrep.2013.02.013","article-title":"Inhibition of mitochondrial aconitase by succination in fumarate hydratase deficiency","volume":"3","author":"Ternette","year":"2013","journal-title":"Cell Rep"},{"key":"10.1016\/j.neurot.2025.e00708_bib99","doi-asserted-by":"crossref","first-page":"1144","DOI":"10.1016\/j.bbapap.2013.03.005","article-title":"Carbonylation of mitochondrial aconitase with 4-hydroxy-2-(E)-nonenal: localization and relative reactivity of addition sites","volume":"1834","author":"Liu","year":"2013","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.neurot.2025.e00708_bib100","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbcan.2024.189102","article-title":"Molecular biology and novel therapeutics for IDH mutant gliomas: the new era of IDH inhibitors","volume":"1879","author":"Kitagawa","year":"2024","journal-title":"Biochim Biophys Acta Rev Cancer"},{"key":"10.1016\/j.neurot.2025.e00708_bib101","doi-asserted-by":"crossref","first-page":"2123","DOI":"10.1038\/s41467-023-37744-x","article-title":"IDH3gamma functions as a redox switch regulating mitochondrial energy metabolism and contractility in the heart","volume":"14","author":"Nanadikar","year":"2023","journal-title":"Nat Commun"},{"key":"10.1016\/j.neurot.2025.e00708_bib102","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1016\/S0891-5849(02)00981-4","article-title":"Inactivation of NADP(+)-dependent isocitrate dehydrogenase by nitric oxide","volume":"33","author":"Yang","year":"2002","journal-title":"Free Radic Biol Med"},{"key":"10.1016\/j.neurot.2025.e00708_bib103","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1038\/s41556-018-0124-1","article-title":"The multifaceted contributions of mitochondria to cellular metabolism","volume":"20","author":"Spinelli","year":"2018","journal-title":"Nat Cell Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib104","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1126\/science.6823561","article-title":"Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis","volume":"219","author":"Langston","year":"1983","journal-title":"Science"},{"key":"10.1016\/j.neurot.2025.e00708_bib105","doi-asserted-by":"crossref","first-page":"1351","DOI":"10.1016\/j.cell.2013.11.009","article-title":"Isogenic human iPSC Parkinson's model shows nitrosative stress-induced dysfunction in MEF2-PGC1alpha transcription","volume":"155","author":"Ryan","year":"2013","journal-title":"Cell"},{"key":"10.1016\/j.neurot.2025.e00708_bib106","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1016\/j.bbabio.2017.02.009","article-title":"NO control of mitochondrial function in normal and transformed cells","volume":"1858","author":"Tengan","year":"2017","journal-title":"Biochim Biophys Acta Bioenerg"},{"key":"10.1016\/j.neurot.2025.e00708_bib107","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1038\/nm.3212","article-title":"Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I","volume":"19","author":"Chouchani","year":"2013","journal-title":"Nat Med"},{"key":"10.1016\/j.neurot.2025.e00708_bib108","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1016\/j.chembiol.2021.10.010","article-title":"ND3 Cys39 in complex I is exposed during mitochondrial respiration","volume":"29","author":"Burger","year":"2022","journal-title":"Cell Chem Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib109","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1111\/jnc.14870","article-title":"Quantitative proteomics of synaptosome S-nitrosylation in Alzheimer's disease","volume":"152","author":"Wijasa","year":"2020","journal-title":"J Neurochem"},{"key":"10.1016\/j.neurot.2025.e00708_bib110","doi-asserted-by":"crossref","first-page":"4170","DOI":"10.1158\/0008-5472.CAN-15-2637","article-title":"S-Nitrosylation of the mitochondrial chaperone TRAP1 sensitizes hepatocellular carcinoma cells to inhibitors of succinate dehydrogenase","volume":"76","author":"Rizza","year":"2016","journal-title":"Cancer Res"},{"key":"10.1016\/j.neurot.2025.e00708_bib111","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1161\/CIRCRESAHA.110.232173","article-title":"Simultaneous measurement of protein oxidation and S-nitrosylation during preconditioning and ischemia\/reperfusion injury with resin-assisted capture","volume":"108","author":"Kohr","year":"2011","journal-title":"Circ Res"},{"key":"10.1016\/j.neurot.2025.e00708_bib112","doi-asserted-by":"crossref","first-page":"C840","DOI":"10.1152\/ajpcell.00325.2004","article-title":"Nitric oxide-induced persistent inhibition and nitrosylation of active site cysteine residues of mitochondrial cytochrome-c oxidase in lung endothelial cells","volume":"288","author":"Zhang","year":"2005","journal-title":"Am J Physiol Cell Physiol"},{"key":"10.1016\/j.neurot.2025.e00708_bib113","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/0014-5793(94)01290-3","article-title":"Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase","volume":"356","author":"Brown","year":"1994","journal-title":"FEBS Lett"},{"key":"10.1016\/j.neurot.2025.e00708_bib114","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1161\/ATVBAHA.108.181628","article-title":"Nitric oxide, cytochrome C oxidase, and the cellular response to hypoxia","volume":"30","author":"Taylor","year":"2010","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib115","doi-asserted-by":"crossref","DOI":"10.3390\/brainsci11060677","article-title":"Systems biology reveals S-Nitrosylation-Dependent regulation of mitochondrial functions in mice with Shank3 mutation associated with autism spectrum disorder","volume":"11","author":"Kartawy","year":"2021","journal-title":"Brain Sci"},{"key":"10.1016\/j.neurot.2025.e00708_bib116","doi-asserted-by":"crossref","first-page":"3900","DOI":"10.1038\/sj.emboj.7601253","article-title":"Nitric oxide-induced mitochondrial fission is regulated by dynamin-related GTPases in neurons","volume":"25","author":"Barsoum","year":"2006","journal-title":"EMBO J"},{"key":"10.1016\/j.neurot.2025.e00708_bib117","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.neures.2011.02.005","article-title":"Regulation of axonal mitochondrial transport and its impact on synaptic transmission","volume":"70","author":"Cai","year":"2011","journal-title":"Neurosci Res"},{"key":"10.1016\/j.neurot.2025.e00708_bib118","doi-asserted-by":"crossref","first-page":"9090","DOI":"10.1523\/JNEUROSCI.1357-09.2009","article-title":"Impaired balance of mitochondrial fission and fusion in Alzheimer's disease","volume":"29","author":"Wang","year":"2009","journal-title":"J Neurosci"},{"key":"10.1016\/j.neurot.2025.e00708_bib119","doi-asserted-by":"crossref","first-page":"2495","DOI":"10.1093\/hmg\/ddr139","article-title":"Impaired mitochondrial dynamics and abnormal interaction of amyloid beta with mitochondrial protein Drp1 in neurons from patients with Alzheimer's disease: implications for neuronal damage","volume":"20","author":"Manczak","year":"2011","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.neurot.2025.e00708_bib120","doi-asserted-by":"crossref","first-page":"2538","DOI":"10.1093\/hmg\/dds072","article-title":"Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer's disease neurons: implications for mitochondrial dysfunction and neuronal damage","volume":"21","author":"Manczak","year":"2012","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.neurot.2025.e00708_bib121","doi-asserted-by":"crossref","DOI":"10.3390\/cells8090961","article-title":"Dynamics of dynamin-related protein 1 in Alzheimer's disease and other neurodegenerative diseases","volume":"8","author":"Oliver","year":"2019","journal-title":"Cells"},{"key":"10.1016\/j.neurot.2025.e00708_bib122","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1186\/s12933-024-02254-7","article-title":"MAP4K4 exacerbates cardiac microvascular injury in diabetes by facilitating S-nitrosylation modification of Drp1","volume":"23","author":"Chen","year":"2024","journal-title":"Cardiovasc Diabetol"},{"key":"10.1016\/j.neurot.2025.e00708_bib123","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms10242","article-title":"Elevated glucose and oligomeric beta-amyloid disrupt synapses via a common pathway of aberrant protein S-nitrosylation","volume":"7","author":"Akhtar","year":"2016","journal-title":"Nat Commun"},{"key":"10.1016\/j.neurot.2025.e00708_bib124","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1038\/45159","article-title":"Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration","volume":"402","author":"Patrick","year":"1999","journal-title":"Nature"},{"key":"10.1016\/j.neurot.2025.e00708_bib125","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1016\/j.molmed.2004.07.001","article-title":"Cdk5 deregulation in the pathogenesis of Alzheimer's disease","volume":"10","author":"Cruz","year":"2004","journal-title":"Trends Mol Med"},{"key":"10.1016\/j.neurot.2025.e00708_bib126","doi-asserted-by":"crossref","first-page":"14366","DOI":"10.1523\/JNEUROSCI.3899-10.2010","article-title":"S-Nitrosylation of cyclin-dependent kinase 5 (cdk5) regulates its kinase activity and dendrite growth during neuronal development","volume":"30","author":"Zhang","year":"2010","journal-title":"J Neurosci"},{"key":"10.1016\/j.neurot.2025.e00708_bib127","doi-asserted-by":"crossref","first-page":"391","DOI":"10.3233\/JAD-2006-10407","article-title":"Redox proteomics identification of oxidatively modified brain proteins in inherited Alzheimer's disease: an initial assessment","volume":"10","author":"Butterfield","year":"2006","journal-title":"J Alzheimers Dis"},{"key":"10.1016\/j.neurot.2025.e00708_bib128","doi-asserted-by":"crossref","first-page":"13256","DOI":"10.1074\/jbc.M314124200","article-title":"Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases","volume":"279","author":"Choi","year":"2004","journal-title":"J Biol Chem"},{"key":"10.1016\/j.neurot.2025.e00708_bib129","article-title":"S-Nitrosylation of UCHL1 induces its structural instability and promotes alpha-synuclein aggregation","volume":"7","author":"Kumar","year":"2017","journal-title":"Sci Rep"},{"key":"10.1016\/j.neurot.2025.e00708_bib130","doi-asserted-by":"crossref","DOI":"10.1016\/j.biopha.2022.112918","article-title":"Are mitophagy enhancers therapeutic targets for Alzheimer's disease?","volume":"149","author":"Pradeepkiran","year":"2022","journal-title":"Biomed Pharmacother"},{"key":"10.1016\/j.neurot.2025.e00708_bib131","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.molmed.2019.07.002","article-title":"Mitophagy and neuroprotection","volume":"26","author":"Lou","year":"2020","journal-title":"Trends Mol Med"},{"key":"10.1016\/j.neurot.2025.e00708_bib132","doi-asserted-by":"crossref","first-page":"2171","DOI":"10.1016\/j.celrep.2017.10.068","article-title":"S-nitrosylation of PINK1 attenuates PINK1\/parkin-dependent mitophagy in hiPSC-based Parkinson's disease models","volume":"21","author":"Oh","year":"2017","journal-title":"Cell Rep"},{"key":"10.1016\/j.neurot.2025.e00708_bib133","doi-asserted-by":"crossref","first-page":"10810","DOI":"10.1073\/pnas.0404161101","article-title":"Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity","volume":"101","author":"Yao","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.neurot.2025.e00708_bib134","doi-asserted-by":"crossref","first-page":"2202","DOI":"10.1038\/srep02202","article-title":"S-Nitrosylation regulates mitochondrial quality control via activation of parkin","volume":"3","author":"Ozawa","year":"2013","journal-title":"Sci Rep"},{"key":"10.1016\/j.neurot.2025.e00708_bib135","doi-asserted-by":"crossref","first-page":"1328","DOI":"10.1126\/science.1093891","article-title":"S-Nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function","volume":"304","author":"Chung","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.neurot.2025.e00708_bib136","doi-asserted-by":"crossref","first-page":"3476","DOI":"10.1093\/hmg\/ddw189","article-title":"The PINK1, synphilin-1 and SIAH-1 complex constitutes a novel mitophagy pathway","volume":"25","author":"Szargel","year":"2016","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.neurot.2025.e00708_bib137","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1038\/s41556-018-0176-2","article-title":"Mechanisms of mitophagy in cellular homeostasis, physiology and pathology","volume":"20","author":"Palikaras","year":"2018","journal-title":"Nat Cell Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib138","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.molcel.2011.04.029","article-title":"Complex inhibitory effects of nitric oxide on autophagy","volume":"43","author":"Sarkar","year":"2011","journal-title":"Mol Cell"},{"key":"10.1016\/j.neurot.2025.e00708_bib139","doi-asserted-by":"crossref","first-page":"3011","DOI":"10.1523\/JNEUROSCI.1508-21.2022","article-title":"S-nitrosylation of p62 inhibits autophagic flux to promote alpha-synuclein secretion and spread in Parkinson's disease and Lewy body dementia","volume":"42","author":"Oh","year":"2022","journal-title":"J Neurosci"},{"key":"10.1016\/j.neurot.2025.e00708_bib140","doi-asserted-by":"crossref","first-page":"2137","DOI":"10.1038\/s41418-022-01004-0","article-title":"S-Nitrosylation of cathepsin B affects autophagic flux and accumulation of protein aggregates in neurodegenerative disorders","volume":"29","author":"Kim","year":"2022","journal-title":"Cell Death Differ"},{"key":"10.1016\/j.neurot.2025.e00708_bib141","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1038\/s41573-020-0072-x","article-title":"Brain energy rescue: an emerging therapeutic concept for neurodegenerative disorders of ageing","volume":"19","author":"Cunnane","year":"2020","journal-title":"Nat Rev Drug Discov"},{"key":"10.1016\/j.neurot.2025.e00708_bib142","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.ccr.2004.11.022","article-title":"Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase","volume":"7","author":"Selak","year":"2005","journal-title":"Cancer Cell"},{"key":"10.1016\/j.neurot.2025.e00708_bib143","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms12317","article-title":"Cell-permeable succinate prodrugs bypass mitochondrial complex I deficiency","volume":"7","author":"Ehinger","year":"2016","journal-title":"Nat Commun"},{"key":"10.1016\/j.neurot.2025.e00708_bib144","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1038\/nature13909","article-title":"Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS","volume":"515","author":"Chouchani","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.neurot.2025.e00708_bib145","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.freeradbiomed.2013.04.010","article-title":"Antioxidants as therapies: can we improve on nature?","volume":"66","author":"Murphy","year":"2014","journal-title":"Free Radic Biol Med"},{"key":"10.1016\/j.neurot.2025.e00708_bib146","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1038\/s41467-023-36232-6","article-title":"Pivotal role for S-nitrosylation of DNA methyltransferase 3B in epigenetic regulation of tumorigenesis","volume":"14","author":"Okuda","year":"2023","journal-title":"Nat Commun"},{"key":"10.1016\/j.neurot.2025.e00708_bib147","doi-asserted-by":"crossref","first-page":"2429","DOI":"10.1021\/acschembio.4c00403","article-title":"Discovery of a compound that inhibits IRE1alpha S-Nitrosylation and preserves the endoplasmic reticulum stress response under nitrosative stress","volume":"19","author":"Kurogi","year":"2024","journal-title":"ACS Chem Biol"},{"key":"10.1016\/j.neurot.2025.e00708_bib148","doi-asserted-by":"crossref","DOI":"10.1038\/srep14812","article-title":"Regulation of the unfolded protein response via S-nitrosylation of sensors of endoplasmic reticulum stress","volume":"5","author":"Nakato","year":"2015","journal-title":"Sci Rep"},{"key":"10.1016\/j.neurot.2025.e00708_bib149","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1126\/science.aaa0079","article-title":"METABOLISM. S-Nitrosylation links obesity-associated inflammation to endoplasmic reticulum dysfunction","volume":"349","author":"Yang","year":"2015","journal-title":"Science"},{"key":"10.1016\/j.neurot.2025.e00708_bib150","doi-asserted-by":"crossref","DOI":"10.1038\/srep14781","article-title":"Pharmacologically targeted NMDA receptor antagonism by NitroMemantine for cerebrovascular disease","volume":"5","author":"Takahashi","year":"2015","journal-title":"Sci Rep"},{"key":"10.1016\/j.neurot.2025.e00708_bib151","doi-asserted-by":"crossref","first-page":"E2518","DOI":"10.1073\/pnas.1306832110","article-title":"Abeta induces astrocytic glutamate release, extrasynaptic NMDA receptor activation, and synaptic loss","volume":"110","author":"Talantova","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.neurot.2025.e00708_bib152","doi-asserted-by":"crossref","first-page":"5751","DOI":"10.1038\/s41380-020-0776-7","article-title":"NitroSynapsin ameliorates hypersynchronous neural network activity in Alzheimer hiPSC models","volume":"26","author":"Ghatak","year":"2021","journal-title":"Mol Psychiatr"},{"key":"10.1016\/j.neurot.2025.e00708_bib153","doi-asserted-by":"crossref","first-page":"1488","DOI":"10.1038\/s41467-017-01563-8","article-title":"NitroSynapsin therapy for a mouse MEF2C haploinsufficiency model of human autism","volume":"8","author":"Tu","year":"2017","journal-title":"Nat Commun"},{"key":"10.1016\/j.neurot.2025.e00708_bib154","doi-asserted-by":"crossref","DOI":"10.1016\/j.coph.2022.102267","article-title":"Towards development of disease-modifying therapy for Alzheimer's disease using redox chemical biology pathways","volume":"66","author":"Lipton","year":"2022","journal-title":"Curr Opin Pharmacol"},{"key":"10.1016\/j.neurot.2025.e00708_bib155","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.tips.2015.10.002","article-title":"Protein S-nitrosylation as a therapeutic target for neurodegenerative diseases","volume":"37","author":"Nakamura","year":"2016","journal-title":"Trends Pharmacol Sci"},{"key":"10.1016\/j.neurot.2025.e00708_bib156","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1038\/nrd1958","article-title":"Paradigm shift in neuroprotection by NMDA receptor blockade: memantine and beyond","volume":"5","author":"Lipton","year":"2006","journal-title":"Nat Rev Drug Discov"},{"key":"10.1016\/j.neurot.2025.e00708_bib157","doi-asserted-by":"crossref","DOI":"10.3389\/fnins.2023.1206688","article-title":"Systemic alterations of tricarboxylic acid cycle enzymes in Alzheimer's disease","volume":"17","author":"Jia","year":"2023","journal-title":"Front Neurosci"},{"key":"10.1016\/j.neurot.2025.e00708_bib158","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1038\/s41467-019-13668-3","article-title":"Mitochondrial TCA cycle metabolites control physiology and disease","volume":"11","author":"Martinez-Reyes","year":"2020","journal-title":"Nat Commun"},{"key":"10.1016\/j.neurot.2025.e00708_bib159","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1038\/nature25986","article-title":"Itaconate is an anti-inflammatory metabolite that activates Nrf2 via alkylation of KEAP1","volume":"556","author":"Mills","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.neurot.2025.e00708_bib160","doi-asserted-by":"crossref","first-page":"2844","DOI":"10.1016\/j.molcel.2022.05.009","article-title":"Itaconate is a lysosomal inducer that promotes antibacterial innate immunity","volume":"82","author":"Zhang","year":"2022","journal-title":"Mol Cell"}],"container-title":["Neurotherapeutics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1878747925001862?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1878747925001862?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,20]],"date-time":"2025-11-20T11:36:58Z","timestamp":1763638618000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1878747925001862"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,10]]},"references-count":160,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2025,10]]}},"alternative-id":["S1878747925001862"],"URL":"https:\/\/doi.org\/10.1016\/j.neurot.2025.e00708","relation":{},"ISSN":["1878-7479"],"issn-type":[{"value":"1878-7479","type":"print"}],"subject":[],"published":{"date-parts":[[2025,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Aberrant S-nitrosylation in the TCA cycle contributes to mitochondrial dysfunction, energy compromise, and synapse loss in neurodegenerative diseases","name":"articletitle","label":"Article Title"},{"value":"Neurotherapeutics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.neurot.2025.e00708","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Author(s). Published by Elsevier Inc. on behalf of American Society for Experimental NeuroTherapeutics.","name":"copyright","label":"Copyright"}],"article-number":"e00708"}}