D. S. Eisenberg

The paper presents a cryo-EM structure of RNA-bound tau fibrils, revealing a small C-terminal core that may nucleate fibril formation and is essential for fibril integrity.

This study investigates how SARS-CoV-2 nucleocapsid protein binds RNA, finding it preferentially interacts with structured and long RNAs, and proposes a mechanism linking packaging to RNA recognition.

The paper identifies LARKS as a common structural motif in amyloid-like fibrils across six organisms and shows their abundance in M. tuberculosis, D. melanogaster, and H. sapiens.

This study uses cryoEM to determine how EGCG binds to AD tau fibrils and initiates their disaggregation by wedging into a cleft and causing charge repulsions.

This study determines the cryo-EM structure of human IAPP fibrils and designs inhibitors to delay aggregation, offering insights into T2D pathology and therapeutic strategies.

This study determines the cryoEM structure of α-synuclein fibrils with the E46K mutation, revealing a more stable and pathogenic fibril structure compared to wild-type.

This study determines cryo-EM structures of alpha-synuclein fibrils with the H50Q mutation, revealing two new polymorphs and structural changes linked to disease mechanisms.

This study determines the cryo-EM structures of four polymorphic TDP-43 amyloid cores, revealing structural features that distinguish reversible from irreversible aggregation and how a mutation may enhance pathology.

The paper identifies two independent amyloid-driving segments in Ig light chain variable domains that drive fibril formation in AL amyloidosis and are potential therapeutic targets.