Publications

Found 25 results
Filters: Author is Eisenberg, David  [Clear All Filters]
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Liu, C., Sawaya, M. R., and Eisenberg, D. (2011) β₂-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.. Nat Struct Mol Biol. 18, 49-55
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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
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Landau, M., Sawaya, M. R., Faull, K. F., Laganowsky, A., Jiang, L., Sievers, S. A., Liu, J., Barrio, J. R., and Eisenberg, D. (2011) Towards a pharmacophore for amyloid. PLoS Biol. 9, e1001080
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Zhao, M., Cascio, D., Sawaya, M. R., and Eisenberg, D. (2011) Structures of segments of α-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation.. Protein Sci. 20, 996-1004
Wagner, J. M., Chan, S., Evans, T. J., Kahng, S., Kim, J., Arbing, M. A., Eisenberg, D., and Korotkov, K. V. (2016) Structures of EccB1 and EccD1 from the core complex of the mycobacterial ESX-1 type VII secretion system. BMC Struct Biol. 16, 5
Sievers, S. A., Karanicolas, J., Chang, H. W., Zhao, A., Jiang, L., Zirafi, O., Stevens, J. T., Münch, J., Baker, D., and Eisenberg, D. (2011) Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation. Nature. 475, 96-100
Miallau, L., Faller, M., Chiang, J., Arbing, M., Guo, F., Cascio, D., and Eisenberg, D. (2009) Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. J Biol Chem. 284, 276-83
Tuukkanen, A. T., Freire, D., Chan, S., Arbing, M. A., Reed, R. W., Evans, T. J., Zenkeviciutė, G., Kim, J., Kahng, S., Sawaya, M. R., Chaton, C. T., Wilmanns, M., Eisenberg, D., Parret, A. H. A., and Korotkov, K. V. (2018) Structural Variability of EspG Chaperones from Mycobacterial ESX-1, ESX-3 and ESX-5 Type VII Secretion Systems. J Mol Biol. 10.1016/j.jmb.2018.11.003
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Hazari, A., Sawaya, M. R., Vlahakis, N., Johnstone, T. C., Boyer, D., Rodriguez, J., Eisenberg, D., and Raskatov, J. A. (2022) The rippled β-sheet layer configuration-a novel supramolecular architecture based on predictions by Pauling and Corey.. Chem Sci. 13, 8947-8952
Teng, P. K., Anderson, N. J., Goldschmidt, L., Sawaya, M. R., Sambashivan, S., and Eisenberg, D. (2012) Ribonuclease A suggests how proteins self-chaperone against amyloid fiber formation. Protein Sci. 21, 26-37
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Liu, C., Zhao, M., Jiang, L., Cheng, P. - N., Park, J., Sawaya, M. R., Pensalfini, A., Gou, D., Berk, A. J., Glabe, C. G., Nowick, J., and Eisenberg, D. (2012) Out-of-register β-sheets suggest a pathway to toxic amyloid aggregates.. Proc Natl Acad Sci U S A. 109, 20913-8
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Wiltzius, J. J. W., Landau, M., Nelson, R., Sawaya, M. R., Apostol, M. I., Goldschmidt, L., Soriaga, A. B., Cascio, D., Rajashankar, K., and Eisenberg, D. (2009) Molecular mechanisms for protein-encoded inheritance. Nat Struct Mol Biol. 16, 973-8
Ivanova, M. I., Sievers, S. A., Sawaya, M. R., Wall, J. S., and Eisenberg, D. (2009) Molecular basis for insulin fibril assembly. Proc Natl Acad Sci U S A. 106, 18990-5
Colletier, J. - P., Laganowsky, A., Landau, M., Zhao, M., Soriaga, A. B., Goldschmidt, L., Flot, D., Cascio, D., Sawaya, M. R., and Eisenberg, D. (2011) Molecular basis for amyloid-beta polymorphism. Proc Natl Acad Sci U S A. 108, 16938-43
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Arbing, M. A., Chan, S., Harris, L., Kuo, E., Zhou, T. T., Ahn, C. J., Nguyen, L., He, Q., Lu, J., Menchavez, P. T., Shin, A., Holton, T., Sawaya, M. R., Cascio, D., and Eisenberg, D. (2013) Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. PLoS One. 8, e81753
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Murray, K. A., Evans, D., Hughes, M. P., Sawaya, M. R., Hu, C. J., Houk, K. N., and Eisenberg, D. (2022) Extended β-Strands Contribute to Reversible Amyloid Formation.. ACS Nano. 16, 2154-2163
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Apostol, M. I., Sawaya, M. R., Cascio, D., and Eisenberg, D. (2010) Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease. J Biol Chem. 285, 29671-5
Laganowsky, A., Benesch, J. L. P., Landau, M., Ding, L., Sawaya, M. R., Cascio, D., Huang, Q., Robinson, C. V., Horwitz, J., and Eisenberg, D. (2010) Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function. Protein Sci. 19, 1031-43
Soriaga, A. B., Sangwan, S., Macdonald, R., Sawaya, M. R., and Eisenberg, D. (2016) Crystal Structures of IAPP Amyloidogenic Segments Reveal a Novel Packing Motif of Out-of-Register Beta Sheets. J Phys Chem B. 120, 5810-6
Min, A. B., Miallau, L., Sawaya, M. R., Habel, J., Cascio, D., and Eisenberg, D. (2012) The crystal structure of the Rv0301-Rv0300 VapBC-3 toxin-antitoxin complex from M. tuberculosis reveals a Mg²⁺ ion in the active site and a putative RNA-binding site.. Protein Sci. 21, 1754-67
Arbing, M. A., Kaufmann, M., Phan, T., Chan, S., Cascio, D., and Eisenberg, D. (2010) The crystal structure of the Mycobacterium tuberculosis Rv3019c-Rv3020c ESX complex reveals a domain-swapped heterotetramer. Protein Sci. 19, 1692-703
Liu, C., Sawaya, M. R., Cheng, P. - N., Zheng, J., Nowick, J. S., and Eisenberg, D. (2011) Characteristics of amyloid-related oligomers revealed by crystal structures of macrocyclic β-sheet mimics.. J Am Chem Soc. 133, 6736-44
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Laganowsky, A., Liu, C., Sawaya, M. R., Whitelegge, J. P., Park, J., Zhao, M., Pensalfini, A., Soriaga, A. B., Landau, M., Teng, P. K., Cascio, D., Glabe, C., and Eisenberg, D. (2012) Atomic view of a toxic amyloid small oligomer. Science. 335, 1228-31
Wiltzius, J. J. W., Sievers, S. A., Sawaya, M. R., and Eisenberg, D. (2009) Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process. Protein Sci. 18, 1521-30
Cheng, P. - N., Liu, C., Zhao, M., Eisenberg, D., and Nowick, J. S. (2012) Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity.. Nat Chem. 4, 927-33