Publications

Found 31 results
Filters: Author is Eisenberg, David S  [Clear All Filters]
2019
Seidler, P. Matthew, Boyer, D. R., Murray, K. A., Yang, T. P., Bentzel, M., Sawaya, M. R., Rosenberg, G., Cascio, D., Williams, C. Kazu, Newell, K. L., Ghetti, B., DeTure, M. A., Dickson, D. W., Vinters, H. V., and Eisenberg, D. S. (2019) Structure-based inhibitors halt prion-like seeding by Alzheimer's disease-and tauopathy-derived brain tissue samples. J Biol Chem. 294, 16451-16464
2020
Lu, J., Cao, Q., Hughes, M. P., Sawaya, M. R., Boyer, D. R., Cascio, D., and Eisenberg, D. S. (2020) CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid. Nat Commun. 11, 4090
Abskharon, R., Seidler, P. Matthew, Sawaya, M. R., Cascio, D., Yang, T. P., Philipp, S., Williams, C. Kazu, Newell, K. L., Ghetti, B., DeTure, M. A., Dickson, D. W., Vinters, H. V., Felgner, P. L., Nakajima, R., Glabe, C. G., and Eisenberg, D. S. (2020) Crystal structure of a conformational antibody that binds tau oligomers and inhibits pathological seeding by extracts from donors with Alzheimer's disease. J Biol Chem. 10.1074/jbc.RA120.013638
2021
Gray, A. L. H., Sawaya, M. R., Acharyya, D., Lou, J., Edington, E. M., Best, M. D., Prosser, R. A., Eisenberg, D. S., and Do, T. D. (2021) Atomic view of an amyloid dodecamer exhibiting selective cellular toxic vulnerability in acute brain slices. Protein Sci. 10.1002/pro.4268
Tayeb-Fligelman, E., Cheng, X., Tai, C., Bowler, J. T., Griner, S., Sawaya, M. R., Seidler, P. M., Jiang, Y. Xiao, Lu, J., Rosenberg, G. M., Salwinski, L., Abskharon, R., Zee, C. - T., Hou, K., Li, Y., Boyer, D. R., Murray, K. A., Falcon, G., Anderson, D. H., Cascio, D., Saelices, L., Damoiseaux, R., Guo, F., and Eisenberg, D. S. (2021) Inhibition of amyloid formation of the Nucleoprotein of SARS-CoV-2. bioRxiv. 10.1101/2021.03.05.434000
2022
Murray, K. A., Hughes, M. P., Hu, C. J., Sawaya, M. R., Salwinski, L., Pan, H., French, S. W., Seidler, P. M., and Eisenberg, D. S. (2022) Identifying amyloid-related diseases by mapping mutations in low-complexity protein domains to pathologies. Nat Struct Mol Biol. 29, 529-536

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