{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T19:23:04Z","timestamp":1792264984955,"version":"4.4.0"},"reference-count":238,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2020,5,10]],"date-time":"2020-05-10T00:00:00Z","timestamp":1589068800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Cells have developed elaborate quality-control mechanisms for proteins and organelles to maintain cellular homeostasis. Such quality-control mechanisms are maintained by conformational folding via molecular chaperones and by degradation through the ubiquitin-proteasome or autophagy-lysosome system. Accumulating evidence suggests that impaired autophagy contributes to the accumulation of intracellular inclusion bodies consisting of misfolded proteins, which is a hallmark of most neurodegenerative diseases. In addition, genetic mutations in core autophagy-related genes have been reported to be linked to neurodegenerative diseases, such as Alzheimer\u2019s disease, Parkinson\u2019s disease, and Huntington\u2019s disease. Conversely, the pathogenic proteins, such as amyloid \u03b2 and \u03b1-synuclein, are detrimental to the autophagy pathway. Here, we review the recent advances in understanding the relationship between autophagic defects and the pathogenesis of neurodegenerative diseases and suggest autophagy induction as a promising strategy for the treatment of these conditions.<\/jats:p>","DOI":"10.3390\/ijms21093369","type":"journal-article","created":{"date-parts":[[2020,5,11]],"date-time":"2020-05-11T10:01:18Z","timestamp":1589191278000},"page":"3369","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":190,"title":["Autophagy in Neurodegenerative Diseases: A Hunter for Aggregates"],"prefix":"10.3390","volume":"21","author":[{"given":"Hyungsun","family":"Park","sequence":"first","affiliation":[{"name":"Department of Anatomy, College of Medicine, Inha University, Incheon 22212, Korea"},{"name":"Hypoxia-related Disease Research Center, College of Medicine, Inha University, Incheon 22212, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5235-8993","authenticated-orcid":false,"given":"Ju-Hee","family":"Kang","sequence":"additional","affiliation":[{"name":"Hypoxia-related Disease Research Center, College of Medicine, Inha University, Incheon 22212, Korea"},{"name":"Department of Pharmacology, College of Medicine, Inha University, Incheon 22212, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seongju","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Anatomy, College of Medicine, Inha University, Incheon 22212, Korea"},{"name":"Hypoxia-related Disease Research Center, College of Medicine, Inha University, Incheon 22212, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,5,10]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"3865","DOI":"10.1093\/hmg\/ddu101","article-title":"Neuronal Tsc1\/2 complex controls autophagy through AMPK-dependent regulation of ULK1","volume":"23","author":"Wertz","year":"2014","journal-title":"Hum. 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