Publications

Found 11 results
Filters: Author is Boyer, David R  [Clear All Filters]
Journal Article
Hanczyc, P., Mikhailovsky, A., Boyer, D. R., Sawaya, M. R., Heeger, A., and Eisenberg, D. (2018) Ultrafast Time-Resolved Studies on Fluorescein for Recognition Strands Architecture in Amyloid Fibrils. J Phys Chem B. 122, 8-18
Gallagher-Jones, M., Glynn, C., Boyer, D. R., Martynowycz, M. W., Hernandez, E., Miao, J., Zee, C. - T., Novikova, I. V., Goldschmidt, L., McFarlane, H. T., Helguera, G. F., Evans, J. E., Sawaya, M. R., Cascio, D., Eisenberg, D. S., Gonen, T., and Rodriguez, J. A. (2018) Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp.. Nat Struct Mol Biol. 10.1038/s41594-017-0018-0
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
Abskharon, R., Pan, H., Sawaya, M. R., Seidler, P. M., Olivares, E. J., Chen, Y., Murray, K. A., Zhang, J., Lantz, C., Bentzel, M., Boyer, D. R., Cascio, D., Nguyen, B. A., Hou, K., Cheng, X., Pardon, E., Williams, C. K., Nana, A. L., Vinters, H. V., Spina, S., Grinberg, L. T., Seeley, W. W., Steyaert, J., Glabe, C. G., Loo, R. R. Ogorzale, Loo, J. A., and Eisenberg, D. S. (2023) Structure-based design of nanobodies that inhibit seeding of Alzheimer's patient-extracted tau fibrils. Proc Natl Acad Sci U S A. 120, e2300258120
Tayeb-Fligelman, E., Bowler, J. T., Tai, C. E., Sawaya, M. R., Jiang, Y. Xiao, Garcia, G., Griner, S. L., Cheng, X., Salwinski, L., Lutter, L., Seidler, P. M., Lu, J., Rosenberg, G. M., Hou, K., Abskharon, R., Pan, H., Zee, C. - T., Boyer, D. R., Li, Y., Anderson, D. H., Murray, K. A., Falcon, G., Cascio, D., Saelices, L., Damoiseaux, R., Arumugaswami, V., Guo, F., and Eisenberg, D. S. (2023) Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils. Nat Commun. 14, 2379
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
Ryder, B. D., Boyer, D. R., Ustyantseva, E., Mendoza-Oliva, A., Kuska, M. I., Wydorski, P. M., Sawaya, M., Diamond, M. I., Eisenberg, D. S., Kampinga, H. H., and Joachimiak, L. A. (2023) DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity. bioRxiv. 10.1101/2023.03.06.531355
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
Guenther, E. L., Ge, P., Trinh, H., Sawaya, M. R., Cascio, D., Boyer, D. R., Gonen, T., Z Zhou, H., and Eisenberg, D. S. (2018) Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2. Nat Struct Mol Biol. 10.1038/s41594-018-0045-5
Guenther, E. L., Cao, Q., Trinh, H., Lu, J., Sawaya, M. R., Cascio, D., Boyer, D. R., Rodriguez, J. A., Hughes, M. P., and Eisenberg, D. S. (2018) Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation. Nat Struct Mol Biol. 10.1038/s41594-018-0064-2
Hughes, M. P., Sawaya, M. R., Boyer, D. R., Goldschmidt, L., Rodriguez, J. A., Cascio, D., Chong, L., Gonen, T., and Eisenberg, D. S. (2018) Atomic structures of low-complexity protein segments reveal kinked β sheets that assemble networks.. Science. 359, 698-701