Ronald B. Wetzel
Affiliations: | The University of Tennessee, Knoxville, TN, United States |
Area:
Neuroscience Biology, Cell Biology, Molecular BiologyGoogle:
"Ronald Wetzel"Mean distance: 53433
Cross-listing: Chemistry Tree
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Publications
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| Wetzel R. (2020) Exploding the Repeat Length Paradigm while Exploring Amyloid Toxicity in Huntington's Disease. Accounts of Chemical Research. 53: 2347-2357 |
| Drombosky KW, Rode S, Kodali R, et al. (2018) Mutational analysis implicates the amyloid fibril as the toxic entity in Huntington's disease. Neurobiology of Disease |
| Wetzel R, Chemuru S, Misra P, et al. (2018) An Aggregate Weight-Normalized Thioflavin-T Measurement Scale for Characterizing Polymorphic Amyloids and Assembly Intermediates. Methods in Molecular Biology (Clifton, N.J.). 1777: 121-144 |
| Lin HK, Boatz JC, Krabbendam IE, et al. (2017) Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core. Nature Communications. 8: 15462 |
| Kar K, Baker MA, Lengyel GA, et al. (2016) Backbone engineering within a latent β-hairpin structure to design inhibitors of polyglutamine amyloid formation. Journal of Molecular Biology |
| Misra P, Kodali R, Chemuru S, et al. (2016) Rapid α-oligomer formation mediated by the Aβ C terminus initiates an amyloid assembly pathway. Nature Communications. 7: 12419 |
| Sahoo B, Arduini I, Drombosky KW, et al. (2016) Folding Landscape of Mutant Huntingtin Exon1: Diffusible Multimers, Oligomers and Fibrils, and No Detectable Monomer. Plos One. 11: e0155747 |
| Hoop CL, Lin HK, Kar K, et al. (2016) Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core. Proceedings of the National Academy of Sciences of the United States of America |
| Sahoo B, Drombosky KW, Wetzel R. (2016) Fluorescence Correlation Spectroscopy: A Tool to Study Protein Oligomerization and Aggregation In Vitro and In Vivo. Methods in Molecular Biology (Clifton, N.J.). 1345: 67-87 |
| Chemuru S, Kodali R, Wetzel R. (2016) C-Terminal Threonine Reduces Aβ43 Amyloidogenicity Compared with Aβ42. Journal of Molecular Biology. 428: 274-291 |