Notable Publications:

• • 1. Li, Q, Jaroniec, CP & Surewicz, WK, Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers, BioRxiv. doi: 10.1101/2021.08.10.455830 2021

    2. Li, Q, Babinchak, WM. & Surewicz, WK, Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43. Nat Commun 12, 1620 (2021). https://doi.org/10.1038/s41467-021-21912-y

    3. Boyko, S., Surewicz, K & Surewicz, WK, Regulatory mechanisms of tau protein fibrillation under the conditions of liquid–liquid phase separation. Proc. Natl. Acad. Sci. 117, 31882 LP – 31890 (2020).

    4. Babinchak, WM, Dumm, B, Venus, S et al. Small molecules as potent biphasic modulators of protein liquid-liquid phase separation. Nat Commun 11, 5574 (2020). https://doi.org/10.1038/s41467-020-19211-z

    5. Boyko S, Qi X, Chen TH, Surewicz K, Surewicz WK, Liquid-liquid phase separation of tau protein: The crucial role of electrostatic interactions. J Biol Chem. 2019 Jul 19;294(29):11054-11059. doi: 10.1074/jbc.AC119.009198.

    6. Babinchak WM, Haider R, Dumm BK, Sarkar P, Surewicz K, Choi JK, Surewicz WK, The role of liquid-liquid phase separation in aggregation of the TDP-43 low-complexity domain. J Biol Chem. 2019 Apr 19;294(16):6306-6317. doi: 10.1074/jbc.RA118.007222.

    7. Li Q, Wang F, Xiao X, Kim C, Bohon J, Kiselar J, Safar JG, Ma J, Surewicz WK, Structural attributes of mammalian prion infectivity: Insights from studies with synthetic prions. J Biol Chem. 2018 Nov 30;293(48):18494-18503. doi: 10.1074/jbc.RA118.005622.

    8. Choi JK, Cali I, Surewicz K, Kong Q, Gambetti P, Surewicz WK, Amyloid Fibrils from the N-terminal Prion Protein Fragment are Infectious. Proc. Natl. Acad. Sci. U.S.A. 2016. 113 (48), 13851-13856.

    9. Scott-McKean JJ, K Surewicz, JK Choi, VA Ruffin, AI Salameh, K Nieznanski, AC Costa & Surewicz, WK, Soluble prion protein and its N-terminal fragment prevent impairment of synaptic plasticity by Abeta oligomers: Implications for novel therapeutic strategy in Alzheimer's disease. Neurobiol. Dis. 91:124-31, 2016.

    10. Safar JG, Xiao, X, Kabir, ME, Chen, S, Kim, C, Haldiman, S, Cohen, Y, Chen, W, Cohen, ML & Surewicz, WK, Structural determinants of phenotypic diversity and replication rate of human prions. PLoS Pathog. 11:e1004832, 2015.

    11. Kong Q, JL Mills, B Kundu, X Li, L Qing, K Surewicz, I Cali, S Huang, M Zheng, W Swietnicki, FD Sönnichsen, P Gambetti & WK Surewicz. Thermodynamic stabilization of the folded domain of prion protein inhibits prion infection in vivo. Cell Rep 4:248-54, 2013.

    12. Smirnovas V, GS Baron, DK Offerdahl, GJ Raymond, B Caughey & WK Surewicz. Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange. Nat. Struct. Mol. Biol. 18:504-6, 2011.

    13. Cobb NJ, FD Sönnichsen, H McHaourab & WK Surewicz. Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure. Proc. Natl. Acad. Sci. U.S.A. 104:18946-51, 2007.

    14. Lu, X, Wintrode, PL & Surewicz, WK, Beta-sheet core of human prion protein amyloid fibrils as determined by H/D exchange. Proc Natl Acad Sci USA 104, 1510-1515, 2007

    15. Jones EM & Surewicz, WK Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids. Cell 121:63-72, 2005.

    16. Vanik DL, Surewicz K & Surewicz WK, Molecular basis of barriers for interspecies transmissibility of mammalian prions, Mol Cell 14:139-145, 2004