Witold K. Surewicz
Affiliations: | Case Western Reserve University School of Medicine, Cleveland, OH, United States |
Area:
General Biophysics, BiochemistryGoogle:
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Publications
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| Li Q, Jaroniec CP, Surewicz WK. (2022) Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers. Nature Structural & Molecular Biology |
| Qi Z, Surewicz K, Surewicz WK, et al. (2022) Influence of the Dynamically Disordered N-Terminal Tail Domain on the Amyloid Core Structure of Human Y145Stop Prion Protein Fibrils. Frontiers in Molecular Biosciences. 9: 841790 |
| Li Q, Babinchak WM, Surewicz WK. (2021) Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43. Nature Communications. 12: 1620 |
| Dao HH, Hlaing MZ, Ma Y, et al. (2020) C and N chemical shift assignments of A117V and M129V human Y145Stop prion protein amyloid fibrils. Biomolecular Nmr Assignments |
| Nemani SK, Xiao X, Cali I, et al. (2020) A novel mechanism of phenotypic heterogeneity in Creutzfeldt-Jakob disease. Acta Neuropathologica Communications. 8: 85 |
| Singh V, Xu L, Boyko S, et al. (2020) Zinc promotes liquid-liquid phase separation of tau protein. The Journal of Biological Chemistry |
| Babinchak WM, Surewicz WK. (2020) Liquid-Liquid Phase Separation and Its Mechanistic Role in Pathological Protein Aggregation. Journal of Molecular Biology. 432: 1910-1925 |
| Cracco L, Xiao X, Nemani SK, et al. (2019) Gerstmann-Sträussler-Scheinker disease revisited: accumulation of covalently-linked multimers of internal prion protein fragments. Acta Neuropathologica Communications. 7: 1 |
| Boyko S, Qi X, Chen TH, et al. (2019) Liquid-liquid phase separation of tau protein: The crucial role of electrostatic interactions. The Journal of Biological Chemistry |
| Babinchak WM, Haider R, Dumm BK, et al. (2019) The role of liquid-liquid phase separation in aggregation of the TDP-43 low complexity domain. The Journal of Biological Chemistry |