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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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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Structure-based inhibitors of amyloid beta core suggest a common interface with tau von Griner, Sarah L, Seidler, Paul, Bowler, Jeannette, Murray, Kevin A, Yang, Tianxiao Peter, Sahay, Shruti, Sawaya, Michael R, Cascio, Duilio, Rodriguez, Jose A, Philipp, Stephan, Sosna, Justyna, Glabe, Charles G, Gonen, Tamir, Eisenberg, David S

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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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Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation von Shin, Woo Shik, Di, Jing, Cao, Qin, Li, Binsen, Seidler, Paul M, Murray, Kevin A, Bitan, Gal, Jiang, Lin

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Inhibition of synucleinopathic seeding by rationally designed inhibitors von Sangwan, Smriti, Sahay, Shruti, Murray, Kevin A, Morgan, Sophie, Guenther, Elizabeth L, Jiang, Lin, Williams, Christopher K, Vinters, Harry V, Goedert, Michel, Eisenberg, David S

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Atomic structures of corkscrew‐forming segments of SOD1 reveal varied oligomer conformations von Sangwan, Smriti, Sawaya, Michael R., Murray, Kevin A., Hughes, Michael P., Eisenberg, David S.

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Low complexity domains of the nucleocapsid protein of SARS-CoV-2 form amyloid fibrils von Tayeb-Fligelman, Einav, Bowler, Jeannette T., Tai, Christen E., Sawaya, Michael R., Jiang, Yi Xiao, Garcia, Gustavo, Griner, Sarah L., Cheng, Xinyi, Salwinski, Lukasz, Lutter, Liisa, Seidler, Paul M., Lu, Jiahui, Rosenberg, Gregory M., Hou, Ke, Abskharon, Romany, Pan, Hope, Zee, Chih-Te, Boyer, David R., Li, Yan, Anderson, Daniel H., Murray, Kevin A., Falcon, Genesis, Cascio, Duilio, Saelices, Lorena, Damoiseaux, Robert, Arumugaswami, Vaithilingaraja, Guo, Feng, Eisenberg, David S.

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Different Amyloid-β Self-Assemblies Have Distinct Effects on Intracellular Tau Aggregation von Shin, Woo Shik, Di, Jing, Murray, Kevin A, Sun, Chuanqi, Li, Binsen, Bitan, Gal, Jiang, Lin

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Correction to: Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregation von Shin, Woo Shik, Di, Jing, Cao, Qin, Li, Binsen, Seidler, Paul M, Murray, Kevin A, Bitan, Gal, Jiang, Lin

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De novo designed protein inhibitors of amyloid aggregation and seeding von Murray, Kevin A., Hu, Carolyn J., Griner, Sarah L., Pan, Hope, Bowler, Jeannette T., Abskharon, Romany, Rosenberg, Gregory M., Cheng, Xinyi, Seidler, Paul M., Eisenberg, David S.

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Cryo-EM structures of hIAPP fibrils seeded by patient-extracted fibrils reveal new polymorphs and conserved fibril cores von Cao, Qin, Boyer, David R., Sawaya, Michael R., Abskharon, Romany, Saelices, Lorena, Nguyen, Binh A., Lu, Jiahui, Murray, Kevin A., Kandeel, Fouad, Eisenberg, David S.

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Bioinformatic identification of previously unrecognized amyloidogenic proteins von Rosenberg, Gregory M., Murray, Kevin A., Salwinski, Lukasz, Hughes, Michael P., Abskharon, Romany, Eisenberg, David S.

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Small molecules disaggregate alpha-synuclein and prevent seeding from patient brain-derived fibrils von Murray, Kevin A, Hu, Carolyn J, Pan, Hope, Lu, Jiahui, Abskharon, Romany, Bowler, Jeannette T, Rosenberg, Gregory M, Williams, Christopher K, Elezi, Gazmend, Balbirnie, Melinda, Faull, Kym F, Vinters, Harry V, Seidler, Paul M, Eisenberg, David S

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Extended β-Strands Contribute to Reversible Amyloid Formation von Murray, Kevin A, Evans, Declan, Hughes, Michael P, Sawaya, Michael R, Hu, Carolyn J, Houk, Kendall N, Eisenberg, David

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Identifying amyloid-related diseases by mapping mutations in low-complexity protein domains to pathologies von Murray, Kevin A., Hughes, Michael P., Hu, Carolyn J., Sawaya, Michael R., Salwinski, Lukasz, Pan, Hope, French, Samuel W., Seidler, Paul M., Eisenberg, David S.

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Inhibiting amyloid-β cytotoxicity through its interaction with the cell surface receptor LilrB2 by structure-based design von Cao, Qin, Shin, Woo Shik, Chan, Henry, Vuong, Celine K., Dubois, Bethany, Li, Binsen, Murray, Kevin A., Sawaya, Michael R., Feigon, Juli, Black, Douglas L., Eisenberg, David S., Jiang, Lin

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Structure-based design of nanobodies that inhibit seeding of Alzheimer's patient-extracted tau fibrils von Abskharon, Romany, Pan, Hope, Sawaya, Michael R, Seidler, Paul M, Olivares, Eileen J, Chen, Yu, Murray, Kevin A, Zhang, Jeffrey, Lantz, Carter, Bentzel, Megan, Boyer, David R, Cascio, Duilio, Nguyen, Binh A, Hou, Ke, Cheng, Xinyi, Pardon, Els, Williams, Christopher K, Nana, Alissa L, Vinters, Harry V, Spina, Salvatore, Grinberg, Lea T, Seeley, William W, Steyaert, Jan, Glabe, Charles G, Ogorzalek Loo, Rachel R, Loo, Joseph A, Eisenberg, David S

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Toward Functional Type III [Fe]-Hydrogenase Biomimics for H2 Activation: Insights from Computation von Murray, Kevin A., Wodrich, Matthew D., Hu, Xile, Corminboeuf, Clémence

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Toward Functional TypeIII [Fe]-Hydrogenase Biomimics for H2 Activation: Insights from Computation von Murray, Kevin A, Wodrich, Matthew D, Hu, Xile, Corminboeuf, Clémence

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