The activities of amyloids from a structural perspective von Riek, Roland, Eisenberg, David S.

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Structural Studies of Amyloid Proteins at the Molecular Level von Eisenberg, David S, Sawaya, Michael R

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Propagation of Tau Aggregates and Neurodegeneration von Goedert, Michel, Eisenberg, David S, Crowther, R. Anthony

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The expanding amyloid family: Structure, stability, function, and pathogenesis von Sawaya, Michael R., Hughes, Michael P., Rodriguez, Jose A., Riek, Roland, Eisenberg, David S.

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Cryo-EM structures of four polymorphic TDP-43 amyloid cores von Cao, Qin, Boyer, David R., Sawaya, Michael R., Ge, Peng, Eisenberg, David S.

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Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel von Li, Binsen, Ge, Peng, Murray, Kevin A., Sheth, Phorum, Zhang, Meng, Nair, Gayatri, Sawaya, Michael R., Shin, Woo Shik, Boyer, David R., Ye, Shulin, Eisenberg, David S., Zhou, Z. Hong, Jiang, Lin

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Half a century of amyloids: past, present and future von Ke, Pu Chun, Zhou, Ruhong, Serpell, Louise C, Riek, Roland, Knowles, Tuomas P. J, Lashuel, Hilal A, Gazit, Ehud, Hamley, Ian W, Davis, Thomas P, Fändrich, Marcus, Otzen, Daniel Erik, Chapman, Matthew R, Dobson, Christopher M, Eisenberg, David S, Mezzenga, Raffaele

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CryoEM structure of the low-complexity domain of hnRNPA2 and its conversion to pathogenic amyloid von Lu, Jiahui, Cao, Qin, Hughes, Michael P., Sawaya, Michael R., Boyer, David R., Cascio, Duilio, Eisenberg, David S.

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Structure-based discovery of small molecules that disaggregate Alzheimer’s disease tissue derived tau fibrils in vitro von Seidler, Paul M., Murray, Kevin A., Boyer, David R., Ge, Peng, Sawaya, Michael R., Hu, Carolyn J., Cheng, Xinyi, Abskharon, Romany, Pan, Hope, DeTure, Michael A., Williams, Christopher K., Dickson, Dennis W., Vinters, Harry V., Eisenberg, David S.

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TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle von Vogler, Thomas O., Wheeler, Joshua R., Nguyen, Eric D., Hughes, Michael P., Britson, Kyla A., Lester, Evan, Rao, Bhalchandra, Betta, Nicole Dalla, Whitney, Oscar N., Ewachiw, Theodore E., Gomes, Edward, Shorter, James, Lloyd, Thomas E., Eisenberg, David S., Taylor, J. Paul, Johnson, Aaron M., Olwin, Bradley B., Parker, Roy

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Atomic-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2 von Guenther, Elizabeth L., Ge, Peng, Trinh, Hamilton, Sawaya, Michael R., Cascio, Duilio, Boyer, David R., Gonen, Tamir, Zhou, Z. Hong, Eisenberg, David S.

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Expanding metabolism for biosynthesis of nonnatural alcohols von Zhang, Kechun, Sawaya, Michael R, Eisenberg, David S, Liao, James C

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Uncovering the Mechanism of Aggregation of Human Transthyretin von Saelices, Lorena, Johnson, Lisa M., Liang, Wilson Y., Sawaya, Michael R., Cascio, Duilio, Ruchala, Piotr, Whitelegge, Julian, Jiang, Lin, Riek, Roland, Eisenberg, David S.

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Amyloid seeding of transthyretin by ex vivo cardiac fibrils and its inhibition von Saelices, Lorena, Chung, Kevin, Lee, Ji H., Cohn, Whitaker, Whitelegge, Julian P., Benson, Merrill D., Eisenberg, David S.

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Toxicity of Eosinophil MBP Is Repressed by Intracellular Crystallization and Promoted by Extracellular Aggregation von Soragni, Alice, Yousefi, Shida, Stoeckle, Christina, Soriaga, Angela B., Sawaya, Michael R., Kozlowski, Evelyne, Schmid, Inès, Radonjic-Hoesli, Susanne, Boutet, Sebastien, Williams, Garth J., Messerschmidt, Marc, Seibert, M. Marvin, Cascio, Duilio, Zatsepin, Nadia A., Burghammer, Manfred, Riekel, Christian, Colletier, Jacques-Philippe, Riek, Roland, Eisenberg, David S., Simon, Hans-Uwe

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Ab initio structure determination from prion nanocrystals at atomic resolution by MicroED von Sawaya, Michael R., Rodriguez, Jose, Cascio, Duilio, Collazo, Michael J., Shi, Dan, Reyes, Francis E., Hattne, Johan, Gonen, Tamir, Eisenberg, David S.

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Designed amyloid fibers as materials for selective carbon dioxide capture von Dan Li, Furukawa, Hiroyasu, Deng, Hexiang, Liu, Cong, Yaghi, Omar M., Eisenberg, David S.

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The structured core domain of αB-crystallin can prevent amyloid fibrillation and associated toxicity von Hochberg, Georg K. A., Ecroyd, Heath, Liu, Cong, Cox, Dezerae, Cascio, Duilio, Sawaya, Michael R., Collier, Miranda P., Stroud, James, Carver, John A., Baldwin, Andrew J., Robinson, Carol V., Eisenberg, David S., Benesch, Justin L. P., Laganowsky, Arthur

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Non-proteinaceous hydrolase comprised of a phenylalanine metallo-supramolecular amyloid-like structure von Makam, Pandeeswar, Yamijala, Sharma S. R. K. C., Tao, Kai, Shimon, Linda J. W., Eisenberg, David S., Sawaya, Michael R., Wong, Bryan M., Gazit, Ehud

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Structure-based inhibitors halt prion-like seeding by Alzheimer’s disease–and tauopathy–derived brain tissue samples von Seidler, Paul Matthew, Boyer, David R., Murray, Kevin A., Yang, Tianxiao P., Bentzel, Megan, Sawaya, Michael R., Rosenberg, Gregory, Cascio, Duilio, Williams, Christopher Kazu, Newell, Kathy L., Ghetti, Bernardino, DeTure, Michael A., Dickson, Dennis W., Vinters, Harry V., Eisenberg, David S.

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