Found 31 results
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Journal Article
Saelices, L., Johnson, L. M., Liang, W. Y., Sawaya, M. R., Cascio, D., Ruchala, P., Whitelegge, J., Jiang, L., Riek, R., and Eisenberg, D. S. (2015) Uncovering the Mechanism of Aggregation of Human Transthyretin. J Biol Chem. 290, 28932-43
Soragni, A., Yousefi, S., Stoeckle, C., Soriaga, A. B., Sawaya, M. R., Kozlowski, E., Schmid, I., Radonjic-Hoesli, S., Boutet, S., Williams, G. J., Messerschmidt, M., M Seibert, M., Cascio, D., Zatsepin, N. A., Burghammer, M., Riekel, C., Colletier, J. - P., Riek, R., Eisenberg, D. S., and Simon, H. - U. (2015) Toxicity of eosinophil MBP is repressed by intracellular crystallization and promoted by extracellular aggregation. Mol Cell. 57, 1011-21
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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