Abstract
Background: How misfolded proteins such as mutant huntingtin aggregate in the cell remains enigmatic. Results:Webuilt a platform to view how aggregation proceeds and assessed the impact of quality control chaperones hsp40 and hsp70. Conclusion: hsp70 enhanced survival of cells with aggregates; hsp40 suppressed aggregation. Significance: We developed a new toolkit to illustrate the impact of protein aggregation on cell biology. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Ormsby, A. R., Ramdzan, Y. M., Mok, Y. F., Jovanoski, K. D., & Hatters, D. M. (2013). A platform to view huntingtin exon 1 aggregation flux in the cell reveals divergent influences from chaperones hsp40 and hsp70. Journal of Biological Chemistry, 288(52), 37192–37203. https://doi.org/10.1074/jbc.M113.486944
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