Publications

Found 28 results
Filters: Author is Eisenberg, David S  [Clear All Filters]
Journal Article
Ivanova, M. I., Sievers, S. A., Guenther, E. L., Johnson, L. M., Winkler, D. D., Galaleldeen, A., Sawaya, M. R., P Hart, J., and Eisenberg, D. S. (2014) Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS. Proc Natl Acad Sci U S A. 111, 197-201
McPartland, L., Heller, D. M., Eisenberg, D. S., Hochschild, A., and Sawaya, M. R. (2018) Atomic insights into the genesis of cellular filaments by globular proteins. Nat Struct Mol Biol. 25, 705-714
Sangwan, S., Zhao, A., Adams, K. L., Jayson, C. K., Sawaya, M. R., Guenther, E. L., Pan, A. C., Ngo, J., Moore, D. M., Soriaga, A. B., Do, T. D., Goldschmidt, L., Nelson, R., Bowers, M. T., Koehler, C. M., Shaw, D. E., Novitch, B. G., and Eisenberg, D. S. (2017) Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS). Proc Natl Acad Sci U S A. 114, 8770-8775
Sangwan, S., Sawaya, M. R., Murray, K. A., Hughes, M. P., and Eisenberg, D. S. (2018) Atomic structures of corkscrew-forming segments of SOD1 reveal varied oligomer conformations. Protein Sci. 10.1002/pro.3391
Krotee, P., Rodriguez, J. A., Sawaya, M. R., Cascio, D., Reyes, F. E., Shi, D., Hattne, J., Nannenga, B. L., Oskarsson, M. E., Philipp, S., Griner, S., Jiang, L., Glabe, C. G., Westermark, G. T., Gonen, T., and Eisenberg, D. S. (2017) Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity.. Elife. 10.7554/eLife.19273
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
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
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
Miallau, L., Jain, P., Arbing, M. A., Cascio, D., Phan, T., Ahn, C. J., Chan, S., Chernishof, I., Maxson, M., Chiang, J., Jacobs, W. R., and Eisenberg, D. S. (2013) Comparative proteomics identifies the cell-associated lethality of M. tuberculosis RelBE-like toxin-antitoxin complexes. Structure. 21, 627-37
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
Saelices, L., Sievers, S. A., Sawaya, M. R., and Eisenberg, D. S. (2018) Crystal Structures of Amyloidogenic Segments of Human Transthyretin. Protein Sci. 10.1002/pro.3420
Soragni, A., Janzen, D. M., Johnson, L. M., Lindgren, A. G., Nguyen, A. Thai- Quynh, Tiourin, E., Soriaga, A. B., Lu, J., Jiang, L., Faull, K. F., Pellegrini, M., Memarzadeh, S., and Eisenberg, D. S. (2016) A Designed Inhibitor of p53 Aggregation Rescues p53 Tumor Suppression in Ovarian Carcinomas. Cancer Cell. 29, 90-103
Do, T. D., Sangwan, S., de Almeida, N. E. C., Ilitchev, A. I., Giammona, M., Sawaya, M. R., Buratto, S. K., Eisenberg, D. S., and Bowers, M. T. (2018) Distal Amyloid β-Protein Fragments Template Amyloid Assembly.. Protein Sci. 10.1002/pro.3375
Do, T. D., LaPointe, N. E., Sangwan, S., Teplow, D. B., Feinstein, S. C., Sawaya, M. R., Eisenberg, D. S., and Bowers, M. T. (2014) Factors that drive peptide assembly from native to amyloid structures: experimental and theoretical analysis of [leu-5]-enkephalin mutants. J Phys Chem B. 118, 7247-56
Brumshtein, B., Esswein, S. R., Landau, M., Ryan, C. M., Whitelegge, J. P., Phillips, M. L., Cascio, D., Sawaya, M. R., and Eisenberg, D. S. (2014) Formation of amyloid fibers by monomeric light chain variable domains. J Biol Chem. 289, 27513-25
Brumshtein, B., Esswein, S. R., Sawaya, M. R., Rosenberg, G., Ly, A. T., Landau, M., and Eisenberg, D. S. (2018) Identification of two principal amyloid-driving segments in variable domains of Ig light chains in systemic light chain amyloidosis. J Biol Chem. 10.1074/jbc.RA118.004142
Cao, Q., Shin, W. Shik, Chan, H., Vuong, C. K., Dubois, B., Li, B., Murray, K. A., Sawaya, M. R., Feigon, J., Black, D. L., Eisenberg, D. S., and Jiang, L. (2018) Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design.. Nat Chem. 10.1038/s41557-018-0147-z
Brumshtein, B., Esswein, S. R., Salwinski, L., Phillips, M. L., Ly, A. T., Cascio, D., Sawaya, M. R., and Eisenberg, D. S. (2015) Inhibition by small-molecule ligands of formation of amyloid fibrils of an immunoglobulin light chain variable domain. Elife. 4, e10935
Basavalingappa, V., Bera, S., Xue, B., Azuri, I., Tang, Y., Tao, K., Shimon, L. J. W., Sawaya, M. R., Kolusheva, S., Eisenberg, D. S., Kronik, L., Cao, Y., Wei, G., and Gazit, E. (2019) Mechanically rigid supramolecular assemblies formed from an Fmoc-guanine conjugated peptide nucleic acid. Nat Commun. 10, 5256
Makam, P., Yamijala, S. S. R. K. C., Tao, K., Shimon, L. J. W., Eisenberg, D. S., Sawaya, M. R., Wong, B. M., and Gazit, E. (2019) Non-proteinaceous hydrolase comprised of a phenylalanine metallo-supramolecular amyloid-like structure. Nat Catal. 2, 977-985
Sawaya, M. R., Cascio, D., Gingery, M., Rodriguez, J., Goldschmidt, L., Colletier, J. - P., Messerschmidt, M. M., Boutet, S., Koglin, J. E., Williams, G. J., Brewster, A. S., Nass, K., Hattne, J., Botha, S., R Doak, B., Shoeman, R. L., DePonte, D. P., Park, H. - W., Federici, B. A., Sauter, N. K., Schlichting, I., and Eisenberg, D. S. (2014) Protein crystal structure obtained at 2.9 Å resolution from injecting bacterial cells into an X-ray free-electron laser beam.. Proc Natl Acad Sci U S A. 111, 12769-74
Rodriguez, J. A., Ivanova, M. I., Sawaya, M. R., Cascio, D., Reyes, F. E., Shi, D., Sangwan, S., Guenther, E. L., Johnson, L. M., Zhang, M., Jiang, L., Arbing, M. A., Nannenga, B. L., Hattne, J., Whitelegge, J., Brewster, A. S., Messerschmidt, M., Boutet, S., Sauter, N. K., Gonen, T., and Eisenberg, D. S. (2015) Structure of the toxic core of α-synuclein from invisible crystals.. Nature. 525, 486-90
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
Hochberg, G. K. A., Ecroyd, H., Liu, C., Cox, D., Cascio, D., Sawaya, M. R., Collier, M. P., Stroud, J., Carver, J. A., Baldwin, A. J., Robinson, C. V., Eisenberg, D. S., Benesch, J. L. P., and Laganowsky, A. (2014) The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity.. Proc Natl Acad Sci U S A. 111, E1562-70

Pages