{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,6]],"date-time":"2026-09-06T04:59:03Z","timestamp":1788670743227,"version":"build-2803163510"},"reference-count":124,"publisher":"Oxford University Press (OUP)","issue":"5","license":[{"start":{"date-parts":[[2023,12,26]],"date-time":"2023-12-26T00:00:00Z","timestamp":1703548800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/pages\/standard-publication-reuse-rights"}],"funder":[{"DOI":"10.13039\/100000049","name":"National Institute on Aging","doi-asserted-by":"publisher","award":["R37AG037319"],"award-info":[{"award-number":["R37AG037319"]}],"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":["R01AG069426"],"award-info":[{"award-number":["R01AG069426"]}],"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":["1RF1AG077848"],"award-info":[{"award-number":["1RF1AG077848"]}],"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":["P30AG035982"],"award-info":[{"award-number":["P30AG035982"]}],"id":[{"id":"10.13039\/100000049","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2024,5,3]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Mitochondrial dysfunction is an early pathological feature of Alzheimer disease and plays a crucial role in the development and progression of Alzheimer\u2019s disease. Strategies to rescue mitochondrial function and cognition remain to be explored. Cyclophilin D (CypD), the peptidylprolyl isomerase F (PPIase), is a key component in opening the mitochondrial membrane permeability transition pore, leading to mitochondrial dysfunction and cell death. Blocking membrane permeability transition pore opening by inhibiting CypD activity is a promising therapeutic approach for Alzheimer\u2019s disease. However, there is currently no effective CypD inhibitor for Alzheimer\u2019s disease, with previous candidates demonstrating high toxicity, poor ability to cross the blood\u2013brain barrier, compromised biocompatibility and low selectivity. Here, we report a new class of non-toxic and biocompatible CypD inhibitor, ebselen, using a conventional PPIase assay to screen a library of \u223c2000 FDA-approved drugs with crystallographic analysis of the CypD-ebselen crystal structure (PDB code: 8EJX). More importantly, we assessed the effects of genetic and pharmacological blockade of CypD on Alzheimer\u2019s disease mitochondrial and glycolytic bioenergetics in Alzheimer\u2019s disease-derived mitochondrial cybrid cells, an ex vivo human sporadic Alzheimer\u2019s disease mitochondrial model, and on synaptic function, inflammatory response and learning and memory in Alzheimer\u2019s disease mouse models.<\/jats:p>\n               <jats:p>Inhibition of CypD by ebselen protects against sporadic Alzheimer\u2019s disease- and amyloid-\u03b2-induced mitochondrial and glycolytic perturbation, synaptic and cognitive dysfunction, together with suppressing neuroinflammation in the brain of Alzheimer\u2019s disease mouse models, which is linked to CypD-related membrane permeability transition pore formation.<\/jats:p>\n               <jats:p>Thus, CypD inhibitors have the potential to slow the progression of neurodegenerative diseases, including Alzheimer\u2019s disease, by boosting mitochondrial bioenergetics and improving synaptic and cognitive function.<\/jats:p>","DOI":"10.1093\/brain\/awad432","type":"journal-article","created":{"date-parts":[[2023,12,26]],"date-time":"2023-12-26T09:52:31Z","timestamp":1703584351000},"page":"1710-1725","source":"Crossref","is-referenced-by-count":62,"title":["New cyclophilin D inhibitor rescues mitochondrial and cognitive function in Alzheimer\u2019s disease"],"prefix":"10.1093","volume":"147","author":[{"given":"Sourav","family":"Samanta","sequence":"first","affiliation":[{"name":"Division of Surgical Science of Department of Surgery, Columbia University in New York , New York, NY 10032 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Firoz","family":"Akhter","sequence":"additional","affiliation":[{"name":"Division of Surgical Science of Department of Surgery, Columbia University in New York , New York, NY 10032 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anuradha","family":"Roy","sequence":"additional","affiliation":[{"name":"High Throughput Screening Laboratory, Del M. Shankel Structural Biology Center , University of Kansas, Lawrence, KS 66047 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Doris","family":"Chen","sequence":"additional","affiliation":[{"name":"Higuchi Bioscience Center, School of Pharmacy, University of Kansas , Lawrence, KS 66047 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Benjamin","family":"Turner","sequence":"additional","affiliation":[{"name":"High Throughput Screening Laboratory, Del M. Shankel Structural Biology Center , University of Kansas, Lawrence, KS 66047 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yongfu","family":"Wang","sequence":"additional","affiliation":[{"name":"Higuchi Bioscience Center, School of Pharmacy, University of Kansas , Lawrence, KS 66047 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicolina","family":"Clemente","sequence":"additional","affiliation":[{"name":"Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute , New York, NY 12180-3590 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chunyu","family":"Wang","sequence":"additional","affiliation":[{"name":"Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute , New York, NY 12180-3590 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Russell Howard","family":"Swerdlow","sequence":"additional","affiliation":[{"name":"Department of Neurology, University of Kansas Medical Center , Kansas City, KS 66160 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kevin P","family":"Battaile","sequence":"additional","affiliation":[{"name":"New York Structural Biology Center, NSLS-II , Upton, NY 11973 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Scott","family":"Lovell","sequence":"additional","affiliation":[{"name":"Protein Structure and X-Ray Crystallography Laboratory , The University of Kansas, Lawrence, KS 66047 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2597-8967","authenticated-orcid":false,"given":"Shi Fang","family":"Yan","sequence":"additional","affiliation":[{"name":"Division of Surgical Science of Department of Surgery, Columbia University in New York , New York, NY 10032 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