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- Publisher Website: 10.3390/ijms21186910
- Scopus: eid_2-s2.0-85091505292
- PMID: 32967102
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Article: Implications of the Orb2 amyloid structure in huntington’s disease
Title | Implications of the Orb2 amyloid structure in huntington’s disease |
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Authors | |
Keywords | Huntington’s disease Polyglutamine Cryo-EM Huntingtin Functional amyloids CPEB Orb2 |
Issue Date | 2020 |
Citation | International Journal of Molecular Sciences, 2020, v. 21, n. 18, article no. 6910 How to Cite? |
Abstract | Huntington’s disease is a progressive, autosomal dominant, neurodegenerative disorder caused by an expanded CAG repeat in the huntingtin gene. As a result, the translated protein, huntingtin, contains an abnormally long polyglutamine stretch that makes it prone to misfold and aggregating. Aggregation of huntingtin is believed to be the cause of Huntington’s disease. However, understanding on how, and why, huntingtin aggregates are deleterious has been hampered by lack of enough relevant structural data. In this review, we discuss our recent findings on a glutamine-based functional amyloid isolated from Drosophila brain and how this information provides plausible structural insight on the structure of huntingtin deposits in the brain. |
Persistent Identifier | http://hdl.handle.net/10722/299467 |
ISSN | 2023 Impact Factor: 4.9 2023 SCImago Journal Rankings: 1.179 |
PubMed Central ID | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Hervás, Rubén | - |
dc.contributor.author | Murzin, Alexey G. | - |
dc.contributor.author | Si, Kausik | - |
dc.date.accessioned | 2021-05-21T03:34:28Z | - |
dc.date.available | 2021-05-21T03:34:28Z | - |
dc.date.issued | 2020 | - |
dc.identifier.citation | International Journal of Molecular Sciences, 2020, v. 21, n. 18, article no. 6910 | - |
dc.identifier.issn | 1661-6596 | - |
dc.identifier.uri | http://hdl.handle.net/10722/299467 | - |
dc.description.abstract | Huntington’s disease is a progressive, autosomal dominant, neurodegenerative disorder caused by an expanded CAG repeat in the huntingtin gene. As a result, the translated protein, huntingtin, contains an abnormally long polyglutamine stretch that makes it prone to misfold and aggregating. Aggregation of huntingtin is believed to be the cause of Huntington’s disease. However, understanding on how, and why, huntingtin aggregates are deleterious has been hampered by lack of enough relevant structural data. In this review, we discuss our recent findings on a glutamine-based functional amyloid isolated from Drosophila brain and how this information provides plausible structural insight on the structure of huntingtin deposits in the brain. | - |
dc.language | eng | - |
dc.relation.ispartof | International Journal of Molecular Sciences | - |
dc.rights | This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. | - |
dc.subject | Huntington’s disease | - |
dc.subject | Polyglutamine | - |
dc.subject | Cryo-EM | - |
dc.subject | Huntingtin | - |
dc.subject | Functional amyloids | - |
dc.subject | CPEB | - |
dc.subject | Orb2 | - |
dc.title | Implications of the Orb2 amyloid structure in huntington’s disease | - |
dc.type | Article | - |
dc.description.nature | published_or_final_version | - |
dc.identifier.doi | 10.3390/ijms21186910 | - |
dc.identifier.pmid | 32967102 | - |
dc.identifier.pmcid | PMC7555547 | - |
dc.identifier.scopus | eid_2-s2.0-85091505292 | - |
dc.identifier.volume | 21 | - |
dc.identifier.issue | 18 | - |
dc.identifier.spage | article no. 6910 | - |
dc.identifier.epage | article no. 6910 | - |
dc.identifier.eissn | 1422-0067 | - |
dc.identifier.isi | WOS:000580903400001 | - |