{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,13]],"date-time":"2026-08-13T19:33:07Z","timestamp":1786649587093,"version":"build-2736575974"},"reference-count":320,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"10","license":[{"start":{"date-parts":[[2025,12,30]],"date-time":"2025-12-30T00:00:00Z","timestamp":1767052800000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0 http:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":["lww.com","ovid.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2026,10]]},"abstract":"<jats:p>\n                    The devastating neurodegenerative disorder of Alzheimer\u2019s disease hallmarks the presence of protein aggregates known as amyloid-\u03b2 plaques and neurofibrillary tangles, composed of amyloid-\u03b2 peptides and aberrantly phosphorylated Tau protein, respectively. The accumulation of these inclusions leads to significant alterations in neuronal homeostasis and overall brain function, resulting in a progressive and rapid cognitive decline. Autophagy, the molecular mechanism of cellular waste removal through the lysosomal pathway, accounts for the degradation of both amyloid-\u03b2 plaques and neurofibrillary tangles in the brain, conferring therefore protection against the pathology. In addition to general autophagy, several lines of evidence have reported the implication of selective autophagy receptors, including sequestosome 1\/p62, the neighbor of\n                    <jats:italic toggle=\"yes\">BRCA1<\/jats:italic>\n                    gene, the nuclear-dot protein 52, and optineurin, in mediating the autophagic clearance of amyloid-\u03b2, phosphorylated Tau, or both. Herein, we have highlighted autophagy and selective autophagy as pivotal mechanisms in Alzheimer\u2019s disease, underlining selective autophagy receptors as a potential target for treatments in the future.\n                  <\/jats:p>","DOI":"10.4103\/nrr.nrr-d-25-00976","type":"journal-article","created":{"date-parts":[[2025,12,30]],"date-time":"2025-12-30T11:00:11Z","timestamp":1767092411000},"page":"4785-4797","update-policy":"https:\/\/doi.org\/10.1097\/lww.0000000000001000","source":"Crossref","is-referenced-by-count":0,"title":["Autophagy and selective autophagy receptors: Key players against Alzheimer\u2019s disease"],"prefix":"10.4103","volume":"21","author":[{"given":"Krenare","family":"Bruqi","sequence":"first","affiliation":[{"name":"Univ Lyon, Univ Lyon 1, CNRS, INSERM, Physiopathologie et Ge\u0301ne\u0301tique du Neurone et du muscle, UMR5261, U1315, Institut Neuromyoge\u0300ne, Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0285-7449","authenticated-orcid":false,"given":"Flavie","family":"Strappazzon","sequence":"additional","affiliation":[{"name":"Univ Lyon, Univ Lyon 1, CNRS, INSERM, Physiopathologie et Ge\u0301ne\u0301tique du Neurone et du muscle, UMR5261, U1315, Institut Neuromyoge\u0300ne, Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"276","published-online":{"date-parts":[[2025,12,30]]},"reference":[{"key":"R1-20260803","doi-asserted-by":"crossref","first-page":"111480","DOI":"10.1016\/j.celrep.2022.111480","article-title":"Oligodendroglial macroautophagy is essential for myelin sheath turnover to prevent neurodegeneration and death","volume":"41","author":"Aber","year":"2022","journal-title":"Cell Rep"},{"key":"R2-20260803","doi-asserted-by":"crossref","first-page":"102726","DOI":"10.1016\/j.redox.2023.102726","article-title":"The KEAP1-NRF2 pathway: targets for 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