{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T07:17:14Z","timestamp":1793344634487,"version":"4.5.0"},"reference-count":135,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,9,1]],"date-time":"2025-09-01T00:00:00Z","timestamp":1756684800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,9,1]],"date-time":"2025-09-01T00:00:00Z","timestamp":1756684800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,6,25]],"date-time":"2025-06-25T00:00:00Z","timestamp":1750809600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003827","name":"Hungarian Scientific Research Fund","doi-asserted-by":"publisher","award":["K132695"],"award-info":[{"award-number":["K132695"]}],"id":[{"id":"10.13039\/501100003827","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003549","name":"Hungarian Scientific Research Fund","doi-asserted-by":"publisher","award":["FK134751"],"award-info":[{"award-number":["FK134751"]}],"id":[{"id":"10.13039\/501100003549","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003549","name":"Hungarian Scientific Research Fund","doi-asserted-by":"publisher","award":["143627"],"award-info":[{"award-number":["143627"]}],"id":[{"id":"10.13039\/501100003549","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100019771","name":"European Union's Research and Innovation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100019771","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002428","name":"Austrian Science Fund","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002428","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100015498","name":"Innov\u00e1ci\u00f3s \u00e9s Technol\u00f3giai Miniszt\u00e9rium","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100015498","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003825","name":"Magyar Tudom\u00e1nyos Akad\u00e9mia","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003825","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011903","name":"Richter Gedeon Talentum Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100011903","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002332","name":"Semmelweis Egyetem","doi-asserted-by":"publisher","award":["EFOP-3.6.3-VEKOP-16-2017-00009"],"award-info":[{"award-number":["EFOP-3.6.3-VEKOP-16-2017-00009"]}],"id":[{"id":"10.13039\/501100002332","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011019","name":"Nemzeti Kutat\u00e1si Fejleszt\u00e9si \u00e9s Innov\u00e1ci\u00f3s Hivatal","doi-asserted-by":"publisher","award":["RGH151414"],"award-info":[{"award-number":["RGH151414"]}],"id":[{"id":"10.13039\/501100011019","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011019","name":"Nemzeti Kutat\u00e1si Fejleszt\u00e9si \u00e9s Innov\u00e1ci\u00f3s Hivatal","doi-asserted-by":"publisher","award":["2022-1.1.1-KK-2022-00005"],"award-info":[{"award-number":["2022-1.1.1-KK-2022-00005"]}],"id":[{"id":"10.13039\/501100011019","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011019","name":"Nemzeti Kutat\u00e1si Fejleszt\u00e9si \u00e9s Innov\u00e1ci\u00f3s Hivatal","doi-asserted-by":"publisher","award":["VEKOP-2.3.3-15-2016-00006"],"award-info":[{"award-number":["VEKOP-2.3.3-15-2016-00006"]}],"id":[{"id":"10.13039\/501100011019","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100012550","name":"Nemzeti Kutat\u00e1si, Fejleszt\u00e9si \u00e9s Innovaci\u00f3s Alap","doi-asserted-by":"publisher","award":["TKP2021-EGA-25"],"award-info":[{"award-number":["TKP2021-EGA-25"]}],"id":[{"id":"10.13039\/501100012550","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100020916","name":"Hungarian Research Network","doi-asserted-by":"publisher","award":["1500207"],"award-info":[{"award-number":["1500207"]}],"id":[{"id":"10.13039\/100020916","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Redox Biology"],"published-print":{"date-parts":[[2025,9]]},"DOI":"10.1016\/j.redox.2025.103743","type":"journal-article","created":{"date-parts":[[2025,6,27]],"date-time":"2025-06-27T11:15:06Z","timestamp":1751022906000},"page":"103743","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":6,"special_numbering":"C","title":["Microgliosis, neuronal death, minor behavioral abnormalities and reduced endurance performance in alpha-ketoglutarate dehydrogenase complex deficient mice"],"prefix":"10.1016","volume":"85","author":[{"given":"M\u00e1rton","family":"Kokas","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andr\u00e1s","family":"Budai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"K\u00e1d\u00e1r","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Soroosh","family":"Mozaffaritabar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lei","family":"Zhou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"T\u00edmea","family":"T\u00e9gl\u00e1s","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rebeka S\u00e1ra","family":"Orova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D\u00e1niel","family":"G\u00e1sp\u00e1r","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Krist\u00f3f","family":"N\u00e9meth","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel Marton","family":"Toth","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nabil V.","family":"Sayour","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Csenger","family":"Kov\u00e1csh\u00e1zi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrea","family":"Xue","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R\u00e9ka Zsuzsanna","family":"Szatm\u00e1ri","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Be\u00e1ta","family":"T\u00f6r\u0151csik","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Domokos","family":"M\u00e1th\u00e9","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"No\u00e9mi","family":"Kov\u00e1cs","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kriszti\u00e1n","family":"Szigeti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P\u00e9ter","family":"Nagy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ildik\u00f3","family":"Szatm\u00e1ri","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Csaba","family":"Fekete","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tam\u00e1s","family":"Ar\u00e1nyi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zolt\u00e1n V.","family":"Varga","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P\u00e9ter","family":"Ferdinandy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zsolt","family":"Rad\u00e1k","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrey V.","family":"Kozlov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L\u00e1szl\u00f3","family":"Tretter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9876-1411","authenticated-orcid":false,"given":"T\u00edmea","family":"Koml\u00f3di","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Attila","family":"Ambrus","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"5","key":"10.1016\/j.redox.2025.103743_bib1","doi-asserted-by":"crossref","first-page":"1497","DOI":"10.1016\/S0021-9258(19)42910-4","article-title":"Regulation of mitochondrial alpha-ketoglutarate metabolism by product inhibition at alpha-ketoglutarate dehydrogenase","volume":"249","author":"Smith","year":"1974","journal-title":"J. Biol. Chem."},{"issue":"12","key":"10.1016\/j.redox.2025.103743_bib2","doi-asserted-by":"crossref","first-page":"3836","DOI":"10.1016\/S0021-9258(19)42550-7","article-title":"Properties and subunit composition of the pig heart 2-oxoglutarate dehydrogenase","volume":"249","author":"Koike","year":"1974","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2025.103743_bib3","first-page":"187","article-title":"Structure, assembly and function of mammalian alpha-keto acid dehydrogenase complexes","author":"Koike","year":"1976","journal-title":"Adv. Biophys."},{"key":"10.1016\/j.redox.2025.103743_bib4","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1111\/j.1749-6632.1999.tb07818.x","article-title":"The alpha-ketoglutarate dehydrogenase complex","volume":"893","author":"Sheu","year":"1999","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.redox.2025.103743_bib5","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1007\/978-3-031-58843-3_13","article-title":"Mitochondrial alpha-keto acid dehydrogenase complexes: recent developments on structure and function in health and disease","volume":"104","author":"Szabo","year":"2024","journal-title":"Subcell. Biochem."},{"issue":"12","key":"10.1016\/j.redox.2025.103743_bib7","doi-asserted-by":"crossref","first-page":"1897","DOI":"10.1002\/jnr.22659","article-title":"The \"B space\" of mitochondrial phosphorylation","volume":"89","author":"Chinopoulos","year":"2011","journal-title":"J. Neurosci. Res."},{"issue":"6","key":"10.1016\/j.redox.2025.103743_bib8","doi-asserted-by":"crossref","first-page":"2392","DOI":"10.1096\/fj.12-220202","article-title":"The negative impact of alpha-ketoglutarate dehydrogenase complex deficiency on matrix substrate-level phosphorylation","volume":"27","author":"Kiss","year":"2013","journal-title":"FASEB J."},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib9","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.tcb.2020.09.010","article-title":"Metabolic coordination of cell fate by alpha-ketoglutarate-dependent dioxygenases","volume":"31","author":"Baksh","year":"2021","journal-title":"Trends Cell Biol."},{"issue":"7539","key":"10.1016\/j.redox.2025.103743_bib10","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1038\/nature13981","article-title":"Intracellular alpha-ketoglutarate maintains the pluripotency of embryonic stem cells","volume":"518","author":"Carey","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.redox.2025.103743_bib11","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1146\/annurev-biochem-061516-044724","article-title":"2-Oxoglutarate-dependent oxygenases","volume":"87","author":"Islam","year":"2018","journal-title":"Annu. Rev. Biochem."},{"issue":"12","key":"10.1016\/j.redox.2025.103743_bib12","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1038\/s41568-020-00303-3","article-title":"2-Oxoglutarate-dependent dioxygenases in cancer","volume":"20","author":"Losman","year":"2020","journal-title":"Nat. Rev. Cancer"},{"issue":"7775","key":"10.1016\/j.redox.2025.103743_bib13","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1038\/s41586-019-1577-5","article-title":"Alpha-ketoglutarate links p53 to cell fate during tumour suppression","volume":"573","author":"Morris","year":"2019","journal-title":"Nature"},{"issue":"7680","key":"10.1016\/j.redox.2025.103743_bib14","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1038\/nature24294","article-title":"BCAT1 restricts alphaKG levels in AML stem cells leading to IDHmut-like DNA hypermethylation","volume":"551","author":"Raffel","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.redox.2025.103743_bib15","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1016\/j.freeradbiomed.2015.10.001","article-title":"Formation of reactive oxygen species by human and bacterial pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components","volume":"89","author":"Ambrus","year":"2015","journal-title":"Free Radic. Biol. Med."},{"issue":"20","key":"10.1016\/j.redox.2025.103743_bib16","doi-asserted-by":"crossref","first-page":"5004","DOI":"10.1046\/j.1432-1033.2002.03204.x","article-title":"Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species","volume":"269","author":"Bunik","year":"2002","journal-title":"Eur. J. Biochem."},{"issue":"36","key":"10.1016\/j.redox.2025.103743_bib17","doi-asserted-by":"crossref","first-page":"7779","DOI":"10.1523\/JNEUROSCI.1899-04.2004","article-title":"Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species","volume":"24","author":"Starkov","year":"2004","journal-title":"J. Neurosci."},{"issue":"36","key":"10.1016\/j.redox.2025.103743_bib18","doi-asserted-by":"crossref","first-page":"7771","DOI":"10.1523\/JNEUROSCI.1842-04.2004","article-title":"Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase","volume":"24","author":"Tretter","year":"2004","journal-title":"J. Neurosci."},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib19","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1046\/j.1471-4159.1999.0730220.x","article-title":"Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals: inhibition of alpha-ketoglutarate dehydrogenase","volume":"73","author":"Chinopoulos","year":"1999","journal-title":"J. Neurochem."},{"issue":"24","key":"10.1016\/j.redox.2025.103743_bib20","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."},{"issue":"1464","key":"10.1016\/j.redox.2025.103743_bib21","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."},{"issue":"9","key":"10.1016\/j.redox.2025.103743_bib22","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1038\/s44161-024-00531-y","article-title":"Alpha-ketoglutarate promotes cardiomyocyte proliferation and heart regeneration after myocardial infarction","volume":"3","author":"Shi","year":"2024","journal-title":"Nat Cardiovasc Res"},{"issue":"4","key":"10.1016\/j.redox.2025.103743_bib23","first-page":"1436","article-title":"Targeting 2-oxoglutarate dehydrogenase for cancer treatment","volume":"12","author":"Chang","year":"2022","journal-title":"Am. J. Cancer Res."},{"issue":"8","key":"10.1016\/j.redox.2025.103743_bib24","doi-asserted-by":"crossref","first-page":"1030","DOI":"10.1002\/jnr.23196","article-title":"Which way does the citric acid cycle turn during hypoxia? The critical role of alpha-ketoglutarate dehydrogenase complex","volume":"91","author":"Chinopoulos","year":"2013","journal-title":"J. Neurosci. Res."},{"issue":"2","key":"10.1016\/j.redox.2025.103743_bib25","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/S0197-0186(99)00114-X","article-title":"The alpha-ketoglutarate dehydrogenase complex in neurodegeneration","volume":"36","author":"Gibson","year":"2000","journal-title":"Neurochem. Int."},{"issue":"20","key":"10.1016\/j.redox.2025.103743_bib26","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."},{"issue":"4","key":"10.1016\/j.redox.2025.103743_bib27","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1016\/j.ajhg.2019.02.017","article-title":"Recurrent germline DLST mutations in individuals with multiple pheochromocytomas and paragangliomas","volume":"104","author":"Remacha","year":"2019","journal-title":"Am. J. Hum. Genet."},{"issue":"1\u20132","key":"10.1016\/j.redox.2025.103743_bib28","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1007\/s42977-023-00155-6","article-title":"Lipoamide dehydrogenase (LADH) deficiency: medical perspectives of the structural and functional characterization of LADH and its pathogenic variants","volume":"74","author":"Szabo","year":"2023","journal-title":"Biol Futur"},{"key":"10.1016\/j.redox.2025.103743_bib29","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/s40170-017-0165-0","article-title":"The alpha-ketoglutarate dehydrogenase complex in cancer metabolic plasticity","volume":"5","author":"Vatrinet","year":"2017","journal-title":"Cancer Metabol."},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib30","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/S0022-3476(84)80591-0","article-title":"Lipoamide dehydrogenase deficiency with primary lactic acidosis: favorable response to treatment with oral lipoic acid","volume":"104","author":"Matalon","year":"1984","journal-title":"J. Pediatr."},{"key":"10.1016\/j.redox.2025.103743_bib31","series-title":"GeneReviews((R))","article-title":"Dihydrolipoamide dehydrogenase deficiency","author":"Quinonez","year":"1993"},{"key":"10.1016\/j.redox.2025.103743_bib32","doi-asserted-by":"crossref","unstructured":"A. Shaag, A. Saada, I. Berger, H. Mandel, A. Joseph, A. Feigenbaum, O.N. Elpeleg, Molecular basis of lipoamide dehydrogenase deficiency in Ashkenazi jews, Am. J. Med. Genet. 82 (2) (1999) 177\u2013182, doi:10.1002\/(sici)1096-8628(19990115)82:2<177::aid-ajmg15>3.3.co;2-0.","DOI":"10.1002\/(SICI)1096-8628(19990115)82:2<177::AID-AJMG15>3.0.CO;2-9"},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib33","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1006\/bbrc.1999.1133","article-title":"Lipoamide dehydrogenase deficiency due to a novel mutation in the interface domain","volume":"262","author":"Shany","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.redox.2025.103743_bib34","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.neuint.2017.05.018","article-title":"Human dihydrolipoamide dehydrogenase (E3) deficiency: novel insights into the structural basis and molecular pathomechanism","volume":"117","author":"Ambrus","year":"2018","journal-title":"Neurochem. Int."},{"issue":"4","key":"10.1016\/j.redox.2025.103743_bib35","first-page":"3135","article-title":"Association of OGG1 and DLST promoter methylation with alzheimer's disease in Xinjiang population","volume":"16","author":"Chen","year":"2018","journal-title":"Exp. Ther. Med."},{"issue":"4","key":"10.1016\/j.redox.2025.103743_bib36","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1002\/ana.410440414","article-title":"Alpha-ketoglutarate dehydrogenase in alzheimer brains bearing the APP670\/671 mutation","volume":"44","author":"Gibson","year":"1998","journal-title":"Ann. Neurol."},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib37","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1002\/ana.410430121","article-title":"Association between the gene encoding the E2 subunit of the alpha-ketoglutarate dehydrogenase complex and parkinson's disease","volume":"43","author":"Kobayashi","year":"1998","journal-title":"Ann. Neurol."},{"issue":"9088","key":"10.1016\/j.redox.2025.103743_bib38","doi-asserted-by":"crossref","first-page":"1367","DOI":"10.1016\/S0140-6736(05)65139-2","article-title":"Alzheimer's disease and DLST genotype","volume":"350","author":"Nakano","year":"1997","journal-title":"Lancet"},{"key":"10.1016\/j.redox.2025.103743_bib39","doi-asserted-by":"crossref","unstructured":"K.F. Sheu, A.M. Brown, V. Haroutunian, B.S. Kristal, H. Thaler, M. Lesser, R.N. Kalaria, N.R. Relkin, R.C. Mohs, L. Lilius, L. Lannfelt, J.P. Blass, Modulation by DLST of the genetic risk of alzheimer\u2019s disease in a very elderly population, Ann. Neurol. 45 (1) (1999) 48\u201353, doi:10.1002\/1531-8249(199901)45:1<48::AID-ART9>3.0.CO;2-V.","DOI":"10.1002\/1531-8249(199901)45:1<48::AID-ART9>3.0.CO;2-V"},{"issue":"7","key":"10.1016\/j.redox.2025.103743_bib40","doi-asserted-by":"crossref","first-page":"1505","DOI":"10.1212\/WNL.52.7.1505","article-title":"A DLST genotype associated with reduced risk for Alzheimer\u2019s disease","volume":"52","author":"Sheu","year":"1999","journal-title":"Neurology"},{"issue":"12","key":"10.1016\/j.redox.2025.103743_bib41","doi-asserted-by":"crossref","first-page":"2913","DOI":"10.1093\/emboj\/cdg299","article-title":"Truncated product of the bifunctional DLST gene involved in biogenesis of the respiratory chain","volume":"22","author":"Kanamori","year":"2003","journal-title":"EMBO J."},{"issue":"8","key":"10.1016\/j.redox.2025.103743_bib42","doi-asserted-by":"crossref","DOI":"10.3390\/antiox11081487","article-title":"Reverse and forward electron flow-induced H2O2 formation is decreased in alpha-ketoglutarate dehydrogenase (alpha-KGDH) subunit (E2 or E3) heterozygote knock out animals","volume":"11","author":"Horvath","year":"2022","journal-title":"Antioxidants"},{"issue":"3","key":"10.1016\/j.redox.2025.103743_bib43","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1006\/geno.1997.4670","article-title":"Characterization of the mouse dihydrolipoamide dehydrogenase (dld) gene: genomic structure, promoter sequence, and chromosomal localization","volume":"41","author":"Johnson","year":"1997","journal-title":"Genomics"},{"issue":"26","key":"10.1016\/j.redox.2025.103743_bib44","doi-asserted-by":"crossref","first-page":"14512","DOI":"10.1073\/pnas.94.26.14512","article-title":"Targeted disruption of the murine dihydrolipoamide dehydrogenase gene (dld) results in perigastrulation lethality","volume":"94","author":"Johnson","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"2","key":"10.1016\/j.redox.2025.103743_bib45","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1016\/j.nbd.2009.07.023","article-title":"Mice deficient in dihydrolipoyl succinyl transferase show increased vulnerability to mitochondrial toxins","volume":"36","author":"Yang","year":"2009","journal-title":"Neurobiol. Dis."},{"issue":"7527","key":"10.1016\/j.redox.2025.103743_bib46","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"},{"issue":"9","key":"10.1016\/j.redox.2025.103743_bib47","doi-asserted-by":"crossref","first-page":"2617","DOI":"10.1016\/j.celrep.2018.04.104","article-title":"Accumulation of succinate in cardiac ischemia primarily occurs via canonical Krebs cycle activity","volume":"23","author":"Zhang","year":"2018","journal-title":"Cell Rep."},{"issue":"1\u20132","key":"10.1016\/j.redox.2025.103743_bib48","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1093\/ilar\/ilab016","article-title":"Mouse anesthesia: the art and science","volume":"62","author":"Navarro","year":"2021","journal-title":"ILAR J."},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib49","doi-asserted-by":"crossref","DOI":"10.2144\/00291bm09","article-title":"Preparation of PCR-Quality mouse genomic DNA with hot sodium hydroxide and tris (HotSHOT)","volume":"29","author":"Truett","year":"2000","journal-title":"Biotechniques"},{"issue":"5","key":"10.1016\/j.redox.2025.103743_bib50","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1007\/s10863-018-9766-8","article-title":"Membrane potential and delta pH dependency of reverse electron transport-associated hydrogen peroxide production in brain and heart mitochondria","volume":"50","author":"Komlodi","year":"2018","journal-title":"J. Bioenerg. Biomembr."},{"issue":"6","key":"10.1016\/j.redox.2025.103743_bib51","doi-asserted-by":"crossref","first-page":"752","DOI":"10.1038\/jcbfm.1987.130","article-title":"Cerebral ischemia and reperfusion: prevention of brain mitochondrial injury by lidoflazine","volume":"7","author":"Rosenthal","year":"1987","journal-title":"J. Cerebr. Blood Flow Metabol."},{"issue":"2","key":"10.1016\/j.redox.2025.103743_bib52","doi-asserted-by":"crossref","DOI":"10.3390\/antiox10020305","article-title":"Methylene blue bridges the inhibition and produces unusual respiratory changes in complex III-inhibited mitochondria. Studies on rats, mice and Guinea pigs","volume":"10","author":"Svab","year":"2021","journal-title":"Antioxidants"},{"issue":"3","key":"10.1016\/j.redox.2025.103743_bib53","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/j.mito.2009.12.148","article-title":"Isolation of mitochondria for biogenetical studies: an update","volume":"10","author":"Fernandez-Vizarra","year":"2010","journal-title":"Mitochondrion"},{"issue":"2","key":"10.1016\/j.redox.2025.103743_bib54","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1016\/S0021-9258(18)57021-6","article-title":"Determination of serum proteins by means of the biuret reaction","volume":"177","author":"Gornall","year":"1949","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2025.103743_bib55","series-title":"Basic Exercises in Immunochemistry: a Laboratory Manual","first-page":"168","article-title":"Protein determination by the biuret method","author":"Nowotny","year":"1979"},{"key":"10.1016\/j.redox.2025.103743_bib56","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1007\/978-1-4939-7831-1_3","article-title":"High-resolution FluoRespirometry and OXPHOS protocols for human cells, permeabilized fibers from small biopsies of muscle, and isolated mitochondria","volume":"1782","author":"Doerrier","year":"2018","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.redox.2025.103743_bib57","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/j.neuropharm.2017.05.009","article-title":"Methylene blue stimulates substrate-level phosphorylation catalysed by succinyl-CoA ligase in the citric acid cycle","volume":"123","author":"Komlodi","year":"2017","journal-title":"Neuropharmacology"},{"key":"10.1016\/j.redox.2025.103743_bib58","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1016\/0076-6879(79)55025-3","article-title":"Assay of citric acid cycle intermediates and related compounds--update with tissue metabolite levels and intracellular distribution","volume":"55","author":"Williamson","year":"1979","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.redox.2025.103743_bib59","article-title":"Facts and artefacts on the oxygen dependence of hydrogen peroxide production using Amplex UltraRed","author":"Komlodi","year":"2021","journal-title":"Bioenerg Commun"},{"key":"10.1016\/j.redox.2025.103743_bib60","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/B978-0-12-801415-8.00012-6","article-title":"Measurement of ROS homeostasis in isolated mitochondria","volume":"547","author":"Tretter","year":"2014","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.redox.2025.103743_bib61","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.freeradbiomed.2015.11.011","article-title":"Carboxylesterase converts Amplex Red to resorufin: implications for mitochondrial H2O2 release assays","volume":"90","author":"Miwa","year":"2016","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.redox.2025.103743_bib62","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1007\/978-1-4939-7831-1_8","article-title":"Comparison of mitochondrial incubation media for measurement of respiration and hydrogen peroxide production","volume":"1782","author":"Komlodi","year":"2018","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.redox.2025.103743_bib63","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1007\/978-1-4939-2257-4_22","article-title":"Simultaneous high-resolution measurement of mitochondrial respiration and hydrogen peroxide production","volume":"1264","author":"Krumschnabel","year":"2015","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.redox.2025.103743_bib64","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0076-6879(96)69007-7","article-title":"Measuring nitric oxide and superoxide: rate constants for aconitase reactivity","volume":"269","author":"Hausladen","year":"1996","journal-title":"Methods Enzymol."},{"issue":"5","key":"10.1016\/j.redox.2025.103743_bib65","doi-asserted-by":"crossref","first-page":"1376","DOI":"10.1111\/j.1471-4159.1986.tb00768.x","article-title":"Brain alpha-ketoglutarate dehydrogenase complex: kinetic properties, regional distribution, and effects of inhibitors","volume":"47","author":"Lai","year":"1986","journal-title":"J. Neurochem."},{"key":"10.1016\/j.redox.2025.103743_bib66","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1007\/978-1-59745-528-2_20","article-title":"BiSearch: ePCR tool for native or bisulfite-treated genomic template","volume":"402","author":"Aranyi","year":"2007","journal-title":"Methods Mol. Biol."},{"issue":"8","key":"10.1016\/j.redox.2025.103743_bib67","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2022.104693","article-title":"The metabolic stress response: adaptation to acute-, repeated- and chronic challenges in mice","volume":"25","author":"Kuti","year":"2022","journal-title":"iScience"},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib68","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/S0091-3057(96)00479-0","article-title":"Chronic ethanol ingestion-induced changes in open-field behavior and oxidative stress in the rat","volume":"58","author":"Harkany","year":"1997","journal-title":"Pharmacol. Biochem. Behav."},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib69","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0166-4328(05)80315-8","article-title":"A new one-trial test for neurobiological studies of memory in rats. III. Spatial vs. non-spatial working memory","volume":"51","author":"Ennaceur","year":"1992","journal-title":"Behav. Brain Res."},{"issue":"2","key":"10.1016\/j.redox.2025.103743_bib70","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1111\/j.1755-5949.2009.00078.x","article-title":"Neuroprotective effects of vinpocetine and its major metabolite cis-apovincaminic acid on NMDA-Induced neurotoxicity in a rat entorhinal cortex lesion model","volume":"15","author":"Nyakas","year":"2009","journal-title":"CNS Neurosci. Ther."},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib71","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/0165-0270(84)90007-4","article-title":"Developments of a water-maze procedure for studying spatial learning in the rat","volume":"11","author":"Morris","year":"1984","journal-title":"J. Neurosci. Methods"},{"key":"10.1016\/j.redox.2025.103743_bib72","article-title":"The treadmill fatigue test: a simple, high-throughput assay of fatigue-like behavior for the mouse","volume":"111","author":"Dougherty","year":"2016","journal-title":"J. Vis. Exp."},{"issue":"11","key":"10.1016\/j.redox.2025.103743_bib73","doi-asserted-by":"crossref","first-page":"1797","DOI":"10.1373\/clinchem.2003.022178","article-title":"Use of tandem mass spectrometry for multianalyte screening of dried blood specimens from newborns","volume":"49","author":"Chace","year":"2003","journal-title":"Clin. Chem."},{"key":"10.1016\/j.redox.2025.103743_bib74","article-title":"Comparison of mouse models of heart failure with reduced ejection fraction","author":"Sayour","year":"2024","journal-title":"ESC Heart Fail"},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib75","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1093\/cvr\/cvaa110","article-title":"Towards standardization of echocardiography for the evaluation of left ventricular function in adult rodents: a position paper of the ESC working group on myocardial function","volume":"117","author":"Zacchigna","year":"2021","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/j.redox.2025.103743_bib76","series-title":"An introduction to OXPHOS analysis","article-title":"Mitochondrial pathways and respiratory control","author":"Gnaiger","year":"2020"},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib77","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/0005-2728(69)90091-7","article-title":"Inhibitory action of oxaloacetate on succinate oxidation in rat-liver mitochondria and the mechanism of its reversal","volume":"172","author":"Wojtczak","year":"1969","journal-title":"Biochim. Biophys. Acta"},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib78","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/0005-2744(69)90310-6","article-title":"The inhibition of succinate dehydrogenase by oxalacetate","volume":"191","author":"Wojtczak","year":"1969","journal-title":"Biochim. Biophys. Acta"},{"issue":"6","key":"10.1016\/j.redox.2025.103743_bib79","doi-asserted-by":"crossref","first-page":"1352","DOI":"10.1046\/j.1471-4159.2003.02263.x","article-title":"Mice deficient in dihydrolipoamide dehydrogenase show increased vulnerability to MPTP, malonate and 3-nitropropionic acid neurotoxicity","volume":"88","author":"Klivenyi","year":"2004","journal-title":"J. Neurochem."},{"issue":"2","key":"10.1016\/j.redox.2025.103743_bib80","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1006\/bbrc.2000.2310","article-title":"ATP synthesis in lipoamide dehydrogenase deficiency","volume":"269","author":"Saada","year":"2000","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"5","key":"10.1016\/j.redox.2025.103743_bib81","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1134\/S0006297915050028","article-title":"Mitochondrial ROS metabolism: 10 years later","volume":"80","author":"Andreyev","year":"2015","journal-title":"Biochemistry (Mosc)"},{"issue":"7","key":"10.1016\/j.redox.2025.103743_bib82","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/s41580-022-00456-z","article-title":"Defining roles of specific reactive oxygen species (ROS) in cell biology and physiology","volume":"23","author":"Sies","year":"2022","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"2","key":"10.1016\/j.redox.2025.103743_bib83","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1017\/S0033583500005795","article-title":"Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants","volume":"29","author":"Skulachev","year":"1996","journal-title":"Q. Rev. Biophys."},{"issue":"22","key":"10.1016\/j.redox.2025.103743_bib84","doi-asserted-by":"crossref","first-page":"5169","DOI":"10.1016\/S0021-9258(18)99410-X","article-title":"Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome beta region of the respiratory chain of beef heart submitochondrial particles","volume":"242","author":"Hinkle","year":"1967","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.redox.2025.103743_bib85","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1007\/s10541-005-0102-7","article-title":"Mitochondrial metabolism of reactive oxygen species","volume":"70","author":"Andreyev","year":"2005","journal-title":"Biochemistry (Mosc)"},{"issue":"2","key":"10.1016\/j.redox.2025.103743_bib86","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1016\/0003-9861(85)90293-0","article-title":"Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria","volume":"237","author":"Turrens","year":"1985","journal-title":"Arch. Biochem. Biophys."},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib87","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/S0014-5793(97)01159-9","article-title":"High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria","volume":"416","author":"Korshunov","year":"1997","journal-title":"FEBS Lett."},{"issue":"4","key":"10.1016\/j.redox.2025.103743_bib88","doi-asserted-by":"crossref","DOI":"10.15252\/embr.202255548","article-title":"Reverse electron transfer is activated during aging and contributes to aging and age-related disease","volume":"24","author":"Rimal","year":"2023","journal-title":"EMBO Rep."},{"issue":"5","key":"10.1016\/j.redox.2025.103743_bib89","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1046\/j.0022-3042.2002.00744.x","article-title":"Generation of reactive oxygen species by the mitochondrial electron transport chain","volume":"80","author":"Liu","year":"2002","journal-title":"J. Neurochem."},{"issue":"2","key":"10.1016\/j.redox.2025.103743_bib90","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-9861(77)90035-2","article-title":"Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria","volume":"180","author":"Cadenas","year":"1977","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.redox.2025.103743_bib91","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2024.103047","article-title":"Reactive oxygen species generation by reverse electron transfer at mitochondrial complex I under simulated early reperfusion conditions","volume":"70","author":"Tabata Fukushima","year":"2024","journal-title":"Redox Biol."},{"issue":"5","key":"10.1016\/j.redox.2025.103743_bib92","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1016\/j.molcel.2016.01.028","article-title":"The mitochondrial basis of aging","volume":"61","author":"Sun","year":"2016","journal-title":"Mol. Cell"},{"issue":"9","key":"10.1016\/j.redox.2025.103743_bib93","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0007095","article-title":"Oxidative inactivation of mitochondrial aconitase results in iron and H2O2-mediated neurotoxicity in rat primary mesencephalic cultures","volume":"4","author":"Cantu","year":"2009","journal-title":"PLoS One"},{"issue":"5","key":"10.1016\/j.redox.2025.103743_bib94","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."},{"issue":"4","key":"10.1016\/j.redox.2025.103743_bib95","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1016\/j.neuroscience.2008.02.071","article-title":"Influence of mitochondrial enzyme deficiency on adult neurogenesis in mouse models of neurodegenerative diseases","volume":"153","author":"Calingasan","year":"2008","journal-title":"Neuroscience"},{"issue":"13","key":"10.1016\/j.redox.2025.103743_bib96","doi-asserted-by":"crossref","first-page":"9661","DOI":"10.1016\/S0021-9258(18)98400-0","article-title":"Macrosialin, a mouse macrophage-restricted glycoprotein, is a member of the lamp\/lgp family","volume":"268","author":"Holness","year":"1993","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.redox.2025.103743_bib97","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1084\/jem.174.4.827","article-title":"Macrosialin, a macrophage-restricted membrane sialoprotein differentially glycosylated in response to inflammatory stimuli","volume":"174","author":"Rabinowitz","year":"1991","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.redox.2025.103743_bib98","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/j.bbi.2016.07.158","article-title":"NOX2 drives M1-like microglial\/macrophage activation and neurodegeneration following experimental traumatic brain injury","volume":"58","author":"Kumar","year":"2016","journal-title":"Brain Behav. Immun."},{"issue":"6","key":"10.1016\/j.redox.2025.103743_bib99","doi-asserted-by":"crossref","first-page":"2468","DOI":"10.1046\/j.1471-4159.1996.66062468.x","article-title":"Amyloid beta protein primes cultured rat microglial cells for an enhanced phorbol 12-myristate 13-acetate-induced respiratory burst activity","volume":"66","author":"Van Muiswinkel","year":"1996","journal-title":"J. Neurochem."},{"key":"10.1016\/j.redox.2025.103743_bib100","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/j.jocn.2021.05.038","article-title":"Neuroinflammation preceding primary central nervous system lymphoma (PCNSL) - case reports and literature review","volume":"89","author":"Norrington","year":"2021","journal-title":"J. Clin. Neurosci."},{"issue":"7","key":"10.1016\/j.redox.2025.103743_bib101","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1093\/gerona\/glx177","article-title":"Nrf2 deficiency exacerbates obesity-induced oxidative stress, neurovascular dysfunction, blood-brain barrier disruption, neuroinflammation, amyloidogenic gene expression, and cognitive decline in mice, mimicking the aging phenotype","volume":"73","author":"Tarantini","year":"2018","journal-title":"J Gerontol A Biol Sci Med Sci"},{"issue":"3","key":"10.1016\/j.redox.2025.103743_bib102","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1083\/jcb.119.3.493","article-title":"Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation","volume":"119","author":"Gavrieli","year":"1992","journal-title":"J. Cell Biol."},{"issue":"8","key":"10.1016\/j.redox.2025.103743_bib103","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1101\/lm.2135211","article-title":"Associative retrieval processes in the human medial temporal lobe: hippocampal retrieval success and CA1 mismatch detection","volume":"18","author":"Chen","year":"2011","journal-title":"Learn. Mem."},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib104","doi-asserted-by":"crossref","first-page":"1","DOI":"10.5607\/en.2017.26.1.1","article-title":"Segregated cell populations enable distinct parallel encoding within the radial axis of the CA1 pyramidal layer","volume":"26","author":"Geiller","year":"2017","journal-title":"Exp Neurobiol"},{"issue":"4","key":"10.1016\/j.redox.2025.103743_bib105","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1007\/BF00308809","article-title":"Neuropathological stageing of Alzheimer-related changes","volume":"82","author":"Braak","year":"1991","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.redox.2025.103743_bib106","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.neuroscience.2015.08.033","article-title":"Structural imaging of hippocampal subfields in healthy aging and Alzheimer\u2019s disease","volume":"309","author":"de Flores","year":"2015","journal-title":"Neuroscience"},{"key":"10.1016\/j.redox.2025.103743_bib107","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.neuroscience.2012.04.050","article-title":"Age-dependent neuroinflammatory responses and deficits in long-term potentiation in the hippocampus during systemic inflammation","volume":"216","author":"Liu","year":"2012","journal-title":"Neuroscience"},{"issue":"12","key":"10.1016\/j.redox.2025.103743_bib108","doi-asserted-by":"crossref","first-page":"10888","DOI":"10.1074\/jbc.M409064200","article-title":"Reduction in the E2k subunit of the alpha-ketoglutarate dehydrogenase complex has effects independent of complex activity","volume":"280","author":"Shi","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2025.103743_bib109","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.neuint.2016.02.011","article-title":"Mild mitochondrial metabolic deficits by alpha-ketoglutarate dehydrogenase inhibition cause prominent changes in intracellular autophagic signaling: potential role in the pathobiology of Alzheimer\u2019s disease","volume":"96","author":"Banerjee","year":"2016","journal-title":"Neurochem. Int."},{"issue":"20","key":"10.1016\/j.redox.2025.103743_bib110","doi-asserted-by":"crossref","first-page":"3919","DOI":"10.1093\/hmg\/ddq306","article-title":"Mitochondrial loss, dysfunction and altered dynamics in Huntington\u2019s disease","volume":"19","author":"Kim","year":"2010","journal-title":"Hum. Mol. Genet."},{"issue":"13","key":"10.1016\/j.redox.2025.103743_bib111","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\u2019s disease: implications for neuronal damage","volume":"20","author":"Manczak","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.redox.2025.103743_bib112","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.freeradbiomed.2013.03.018","article-title":"Mitochondrial diseases of the brain","volume":"63","author":"Chaturvedi","year":"2013","journal-title":"Free Radic. Biol. Med."},{"issue":"1\u20132","key":"10.1016\/j.redox.2025.103743_bib113","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.mito.2006.11.017","article-title":"Mitochondrial transcription factor A (TFAM): roles in maintenance of mtDNA and cellular functions","volume":"7","author":"Kang","year":"2007","journal-title":"Mitochondrion"},{"issue":"12","key":"10.1016\/j.redox.2025.103743_bib114","doi-asserted-by":"crossref","first-page":"2297","DOI":"10.1016\/j.bbamcr.2012.08.007","article-title":"Mitophagy is triggered by mild oxidative stress in a mitochondrial fission dependent manner","volume":"1823","author":"Frank","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"issue":"6","key":"10.1016\/j.redox.2025.103743_bib115","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1016\/j.tips.2013.04.005","article-title":"Toward clinical application of the Keap1-Nrf2 pathway","volume":"34","author":"Suzuki","year":"2013","journal-title":"Trends Pharmacol. Sci."},{"issue":"4","key":"10.1016\/j.redox.2025.103743_bib116","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1089\/ars.2012.4615","article-title":"p53 orchestrates the PGC-1alpha-mediated antioxidant response upon mild redox and metabolic imbalance","volume":"18","author":"Aquilano","year":"2013","journal-title":"Antioxidants Redox Signal."},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib117","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1002\/bjs.10978","article-title":"Mitochondrial function after associating liver partition and portal vein ligation for staged hepatectomy in an experimental model","volume":"106","author":"Budai","year":"2019","journal-title":"Br. J. Surg."},{"issue":"7","key":"10.1016\/j.redox.2025.103743_bib118","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0271606","article-title":"The effect of cyclophilin D depletion on liver regeneration following associating liver partition and portal vein ligation for staged hepatectomy","volume":"17","author":"Daradics","year":"2022","journal-title":"PLoS One"},{"issue":"8","key":"10.1016\/j.redox.2025.103743_bib119","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1002\/jhbp.945","article-title":"The effects of physical prehabilitation: improved liver regeneration and mitochondrial function after ALPPS operation in a rodent model","volume":"28","author":"Fard-Aghaie","year":"2021","journal-title":"J Hepatobiliary Pancreat Sci"},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib120","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1038\/s41420-024-01953-0","article-title":"PGC-1a mediated mitochondrial biogenesis promotes recovery and survival of neuronal cells from cellular degeneration","volume":"10","author":"You","year":"2024","journal-title":"Cell Death Discov."},{"issue":"8","key":"10.1016\/j.redox.2025.103743_bib121","doi-asserted-by":"crossref","DOI":"10.1111\/jcmm.18051","article-title":"PGC-1alpha regulates the interplay between oxidative stress, senescence and autophagy in the ageing retina important in age-related macular degeneration","volume":"28","author":"Gurubaran","year":"2024","journal-title":"J. Cell Mol. Med."},{"issue":"7","key":"10.1016\/j.redox.2025.103743_bib122","article-title":"Oxidative stress and mitochondrial damage in dry age-related macular degeneration like NFE2L2\/PGC-1alpha (-\/-) mouse model evoke complement component C5a independent of C3","volume":"10","author":"Gurubaran","year":"2021","journal-title":"Biology"},{"key":"10.1016\/j.redox.2025.103743_bib123","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/j.redox.2017.07.006","article-title":"NRF2 deficiency replicates transcriptomic changes in Alzheimer's patients and worsens APP and TAU pathology","volume":"13","author":"Rojo","year":"2017","journal-title":"Redox Biol."},{"key":"10.1016\/j.redox.2025.103743_bib124","doi-asserted-by":"crossref","DOI":"10.1016\/j.exger.2020.110882","article-title":"Impairment of PGC-1alpha-mediated mitochondrial biogenesis precedes mitochondrial dysfunction and Alzheimer\u2019s pathology in the 3xTg mouse model of Alzheimer\u2019s disease","volume":"133","author":"Singulani","year":"2020","journal-title":"Exp. Gerontol."},{"issue":"18","key":"10.1016\/j.redox.2025.103743_bib125","doi-asserted-by":"crossref","DOI":"10.3390\/cells11182849","article-title":"A role for PGC-1a in the control of abnormal mitochondrial dynamics in Alzheimer\u2019s disease","volume":"11","author":"Wang","year":"2022","journal-title":"Cells"},{"issue":"8","key":"10.1016\/j.redox.2025.103743_bib126","doi-asserted-by":"crossref","first-page":"4137","DOI":"10.1016\/j.bbagen.2013.04.006","article-title":"Punctum on two different transcription factors regulated by PGC-1alpha: nuclear factor erythroid-derived 2-like 2 and nuclear respiratory factor 2","volume":"1830","author":"Baldelli","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.redox.2025.103743_bib127","doi-asserted-by":"crossref","DOI":"10.1016\/j.arr.2024.102353","article-title":"Unraveling the NRF2 confusion: distinguishing nuclear respiratory factor 2 from nuclear erythroid factor 2","volume":"98","author":"George","year":"2024","journal-title":"Ageing Res. Rev."},{"issue":"3","key":"10.1016\/j.redox.2025.103743_bib128","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1111\/j.1471-4159.1993.tb03635.x","article-title":"Cerebral vulnerability is associated with selective increase in extracellular glutamate concentration in experimental thiamine deficiency","volume":"61","author":"Hazell","year":"1993","journal-title":"J. Neurochem."},{"key":"10.1016\/j.redox.2025.103743_bib129","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2023.102669","article-title":"Oxoglutarate dehydrogenase complex controls glutamate-mediated neuronal death","volume":"62","author":"Weidinger","year":"2023","journal-title":"Redox Biol."},{"key":"10.1016\/j.redox.2025.103743_bib130","doi-asserted-by":"crossref","DOI":"10.1177\/1756286418774254","article-title":"Danger signals in stroke and their role on microglia activation after ischemia","volume":"11","author":"Gulke","year":"2018","journal-title":"Ther Adv Neurol Disord"},{"issue":"7","key":"10.1016\/j.redox.2025.103743_bib131","doi-asserted-by":"crossref","first-page":"796","DOI":"10.1038\/nm.2399","article-title":"The immunology of stroke: from mechanisms to translation","volume":"17","author":"Iadecola","year":"2011","journal-title":"Nat. Med."},{"issue":"6","key":"10.1016\/j.redox.2025.103743_bib132","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1007\/s11307-018-1201-3","article-title":"Evaluation of brain nuclear medicine imaging tracers in a murine model of sepsis-associated encephalopathy","volume":"20","author":"Szollosi","year":"2018","journal-title":"Mol. Imag. Biol."},{"issue":"5","key":"10.1016\/j.redox.2025.103743_bib133","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1136\/jnnp.2003.028175","article-title":"Applications of positron emission tomography (PET) in neurology","volume":"75","author":"Tai","year":"2004","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"key":"10.1016\/j.redox.2025.103743_bib134","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.neuroimage.2015.12.044","article-title":"Glucose consumption of inflammatory cells masks metabolic deficits in the brain","volume":"128","author":"Backes","year":"2016","journal-title":"Neuroimage"},{"issue":"615","key":"10.1016\/j.redox.2025.103743_bib135","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.abe5640","article-title":"Microglial activation states drive glucose uptake and FDG-PET alterations in neurodegenerative diseases","volume":"13","author":"Xiang","year":"2021","journal-title":"Sci. Transl. Med."},{"issue":"1","key":"10.1016\/j.redox.2025.103743_bib136","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.biocel.2012.07.002","article-title":"Up-regulation of 2-oxoglutarate dehydrogenase as a stress response","volume":"45","author":"Graf","year":"2013","journal-title":"Int. J. Biochem. Cell Biol."}],"container-title":["Redox Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2213231725002563?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2213231725002563?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,22]],"date-time":"2026-05-22T10:53:55Z","timestamp":1779447235000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2213231725002563"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,9]]},"references-count":135,"alternative-id":["S2213231725002563"],"URL":"https:\/\/doi.org\/10.1016\/j.redox.2025.103743","relation":{},"ISSN":["2213-2317"],"issn-type":[{"value":"2213-2317","type":"print"}],"subject":[],"published":{"date-parts":[[2025,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Microgliosis, neuronal death, minor behavioral abnormalities and reduced endurance performance in alpha-ketoglutarate dehydrogenase complex deficient mice","name":"articletitle","label":"Article Title"},{"value":"Redox Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.redox.2025.103743","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 B.V.","name":"copyright","label":"Copyright"}],"article-number":"103743"}}