Full metadata record
DC Field | Value | Language |
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dc.contributor.author | Jo, Myungjin | - |
dc.contributor.author | Lee, Shinrye | - |
dc.contributor.author | Jeon, Yu-Mi | - |
dc.contributor.author | Kim, Seyeon | - |
dc.contributor.author | Kwon, Younghwi | - |
dc.contributor.author | Kim, Hyung-Jun | - |
dc.date.accessioned | 2021-01-22T07:33:52Z | - |
dc.date.available | 2021-01-22T07:33:52Z | - |
dc.date.created | 2020-10-26 | - |
dc.date.issued | 2020-10 | - |
dc.identifier.issn | 1226-3613 | - |
dc.identifier.uri | http://hdl.handle.net/20.500.11750/12795 | - |
dc.description.abstract | TAR DNA-binding protein 43 (TDP-43) is a highly conserved nuclear RNA/DNA-binding protein involved in the regulation of RNA processing. The accumulation of TDP-43 aggregates in the central nervous system is a common feature of many neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), Alzheimer’s disease (AD), and limbic predominant age-related TDP-43 encephalopathy (LATE). Accumulating evidence suggests that prion-like spreading of aberrant protein aggregates composed of tau, amyloid-β, and α-synuclein is involved in the progression of neurodegenerative diseases such as AD and PD. Similar to those of prion-like proteins, pathological aggregates of TDP-43 can be transferred from cell-to-cell in a seed-dependent and self-templating manner. Here, we review clinical and experimental studies supporting the prion-like spreading of misfolded TDP-43 and discuss the molecular mechanisms underlying the propagation of these pathological aggregated proteins. The idea that misfolded TDP-43 spreads in a prion-like manner between cells may guide novel therapeutic strategies for TDP-43-associated neurodegenerative diseases. © 2020, The Author(s). | - |
dc.language | English | - |
dc.publisher | Springer Nature | - |
dc.title | The role of TDP-43 propagation in neurodegenerative diseases: integrating insights from clinical and experimental studies | - |
dc.type | Article | - |
dc.identifier.doi | 10.1038/s12276-020-00513-7 | - |
dc.identifier.wosid | 000578224900001 | - |
dc.identifier.scopusid | 2-s2.0-85092365632 | - |
dc.identifier.bibliographicCitation | Experimental and Molecular Medicine, v.52, no.10, pp.1652 - 1662 | - |
dc.identifier.kciid | ART002636434 | - |
dc.description.isOpenAccess | TRUE | - |
dc.subject.keywordPlus | MUTATIONS | - |
dc.subject.keywordPlus | PRIONS | - |
dc.subject.keywordPlus | PTDP-43 PATHOLOGY | - |
dc.subject.keywordPlus | NUCLEAR IMPORT | - |
dc.subject.keywordPlus | FRONTOTEMPORAL LOBAR DEGENERATION | - |
dc.subject.keywordPlus | AMYOTROPHIC-LATERAL-SCLEROSIS | - |
dc.subject.keywordPlus | TAR-DNA-BINDING | - |
dc.subject.keywordPlus | ALZHEIMERS-DISEASE | - |
dc.subject.keywordPlus | ALPHA-SYNUCLEIN | - |
dc.subject.keywordPlus | AGGREGATION | - |
dc.citation.endPage | 1662 | - |
dc.citation.number | 10 | - |
dc.citation.startPage | 1652 | - |
dc.citation.title | Experimental and Molecular Medicine | - |
dc.citation.volume | 52 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology; Research & Experimental Medicine | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology; Medicine, Research & Experimental | - |
dc.type.docType | Review | - |