Misfolded polyglutamine, polyalanine, and superoxide dismutase 1 aggregate via distinct pathways in the cell

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Polling, Saskia, Mok, Yee-Foong, Ramdzan, Yasmin M, Turner, Bradley J ORCID: 0000-0001-6580-7655, Yerbury, Justin J, Hill, Andrew F ORCID: 0000-0001-5581-2354 and Hatters, Danny M ORCID: 0000-0002-9965-2847 (2014) Misfolded polyglutamine, polyalanine, and superoxide dismutase 1 aggregate via distinct pathways in the cell. Journal of Biological Chemistry, 289 (10). pp. 6669-6680. ISSN 0021-9258

Abstract

Background: Protein aggregation is associated with neurodegenerative diseases. Results: We defined how the oligomeric state of disease-relevant mutant protein and homopolypeptides relate to clustering into inclusion subtypes IPOD and JUNQ. Conclusion: JUNQ protein and homopolypeptides relate to constitutively disrupted oligomeric states irrespective of inclusion formation. Significance: JUNQ inclusions may arise by cellular failure in degradation of abnormal oligomeric states.

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Item type Article
URI https://vuir.vu.edu.au/id/eprint/45725
DOI 10.1074/jbc.M113.520189
Official URL https://www.sciencedirect.com/science/article/pii/...
Subjects Current > FOR (2020) Classification > 3101 Biochemistry and cell biology
Current > Division/Research > Chancellery
Keywords misfolded proteins, cell biology, neurodegenerative disorders
Citations in Scopus 31 - View on Scopus
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