Role of post-translational modifications on the alpha-synuclein aggregation-related pathogenesis of Parkinson's disease
DC Field | Value | Language |
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dc.contributor.author | Yoo, Hajung | - |
dc.contributor.author | Lee, Jeongmin | - |
dc.contributor.author | Kim, Bokwang | - |
dc.contributor.author | Moon, Heechang | - |
dc.contributor.author | Jeong, Huisu | - |
dc.contributor.author | Lee, Kyungmi | - |
dc.contributor.author | Song, Woo Jeung | - |
dc.contributor.author | Hur, Junho K. | - |
dc.contributor.author | Oh, Yohan | - |
dc.date.accessioned | 2022-09-19T13:37:28Z | - |
dc.date.available | 2022-09-19T13:37:28Z | - |
dc.date.created | 2022-09-08 | - |
dc.date.issued | 2022-07 | - |
dc.identifier.issn | 1976-6696 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/171582 | - |
dc.description.abstract | Together with neuronal loss, the existence of insoluble inclusions of alpha-synuclein (alpha-syn) in the brain is widely accepted as a hallmark of synucleinopathies including Parkinson's disease (PD), multiple system atrophy, and dementia with Lewy body. Because the alpha-syn aggregates are deeply involved in the pathogenesis, there have been many attempts to demonstrate the mechanism of the aggregation and its potential causative factors including post-translational modifications (PTMs). Although no concrete conclusions have been made based on the previous study results, growing evidence suggests that modifications such as phosphorylation and ubiquitination can alter alpha-syn characteristics to have certain effects on the aggregation process in PD; either facilitating or inhibiting fibrillization. In the present work, we reviewed studies showing the significant impacts of PTMs on alpha-syn aggregation. Furthermore, the PTMs modulating alpha-syn aggregation-induced cell death have been discussed. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY | - |
dc.title | Role of post-translational modifications on the alpha-synuclein aggregation-related pathogenesis of Parkinson's disease | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Hur, Junho K. | - |
dc.contributor.affiliatedAuthor | Oh, Yohan | - |
dc.identifier.doi | 10.5483/BMBRep.2022.55.7.073 | - |
dc.identifier.scopusid | 2-s2.0-85135377212 | - |
dc.identifier.wosid | 000834791200003 | - |
dc.identifier.bibliographicCitation | BMB REPORTS, v.55, no.7, pp.323 - 335 | - |
dc.relation.isPartOf | BMB REPORTS | - |
dc.citation.title | BMB REPORTS | - |
dc.citation.volume | 55 | - |
dc.citation.number | 7 | - |
dc.citation.startPage | 323 | - |
dc.citation.endPage | 335 | - |
dc.type.rims | ART | - |
dc.type.docType | Review | - |
dc.identifier.kciid | ART002863038 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | Y | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.subject.keywordPlus | N-TERMINAL ACETYLATION | - |
dc.subject.keywordPlus | LEWY BODIES | - |
dc.subject.keywordPlus | IN-VITRO | - |
dc.subject.keywordPlus | REDUCES AGGREGATION | - |
dc.subject.keywordPlus | INCLUSION FORMATION | - |
dc.subject.keywordPlus | PATHOLOGICAL FORMS | - |
dc.subject.keywordPlus | O-GLCNACYLATION | - |
dc.subject.keywordPlus | RAT MODEL | - |
dc.subject.keywordPlus | PHOSPHORYLATION | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordAuthor | Alpha-synuclein | - |
dc.subject.keywordAuthor | Parkinson’s disease | - |
dc.subject.keywordAuthor | Post-translational modification | - |
dc.subject.keywordAuthor | Protein aggregation | - |
dc.identifier.url | https://www.bmbreports.org/journal/view.html?doi=10.5483/BMBRep.2022.55.7.073 | - |
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