{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T00:05:04Z","timestamp":1790553904223,"version":"4.1.0"},"reference-count":213,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2021,10,22]],"date-time":"2021-10-22T00:00:00Z","timestamp":1634860800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Life"],"abstract":"<jats:p>\u03b1-synuclein is considered the main pathological protein in a variety of neurodegenerative disorders, such as Parkinson\u2019s disease, multiple system atrophy, and dementia with Lewy bodies. As of now, numerous studies have been aimed at examining the post-translational modifications of \u03b1-synuclein to determine their effects on \u03b1-synuclein aggregation, propagation, and oligomerization, as well as the potential cellular pathway dysfunctions caused by \u03b1-synuclein, to determine the role of the protein in disease progression. Furthermore, \u03b1-synuclein also appears to contribute to the fibrilization of tau and amyloid beta, which are crucial proteins in Alzheimer\u2019s disease, advocating for \u03b1-synuclein\u2019s preeminent role in neurodegeneration. Due to this, investigating the mechanisms of toxicity of \u03b1-synuclein in neurodegeneration may lead to a more proficient understanding of the timeline progression in neurodegenerative synucleinopathies and could thereby lead to the development of potent targeted therapies.<\/jats:p>","DOI":"10.3390\/life11111126","type":"journal-article","created":{"date-parts":[[2021,10,24]],"date-time":"2021-10-24T22:07:11Z","timestamp":1635113231000},"page":"1126","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Examining the Toxicity of \u03b1-Synuclein in Neurodegenerative Disorders"],"prefix":"10.3390","volume":"11","author":[{"given":"Frank Y.","family":"Shan","sequence":"first","affiliation":[{"name":"Department of Anatomic Pathology, Baylor Scott & White Medical Center, College of Medicine, Texas A&M University, Temple, TX 76508, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kar-Ming","family":"Fung","sequence":"additional","affiliation":[{"name":"Department of Pathology, University of Oklahoma Medical Center, University of Oklahoma, Norman, OK 73019, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tarek","family":"Zieneldien","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences, Taneja College of Pharmacy, University of South Florida, Tampa, FL 33620, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Janice","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences, Taneja College of Pharmacy, University of South Florida, Tampa, FL 33620, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chuanhai","family":"Cao","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences, Taneja College of Pharmacy, University of South Florida, Tampa, FL 33620, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4426-0168","authenticated-orcid":false,"given":"Jason H.","family":"Huang","sequence":"additional","affiliation":[{"name":"Department of Neurosurgery, Baylor Scott & White Medical Center, College of Medicine, Texas A&M University, Temple, TX 76508, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,10,22]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1242\/dmm.030205","article-title":"Neurodegenerative disease: Models, mechanisms, and a new hope","volume":"10","author":"Gitler","year":"2017","journal-title":"Dis. 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