D. R. Boyer

DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity

This paper identifies an aromatic-rich motif in DNAJB8 that mediates oligomerization and shows that disrupting this motif affects oligomerization but not substrate activity.

Structure of a reversible amyloid fibril formed by the CPEB3 prion-like domain reveals a core sequence involved in translational regulation

This study identifies an amyloidogenic segment in CPEB3's prion domain that is critical for its function in translational regulation and long-term memory.

Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation

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.

Why amyloid fibrils have a limited width

The paper investigates why amyloid fibrils have a limited width, finding that helical symmetry causes hydrogen bonds to weaken at the fibril edges, preventing lateral growth beyond 10-20 nm.

CryoEM reveals how the small molecule EGCG binds to AD brain-derived tau fibrils and initiates fibril disaggregation

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.

Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils

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.

The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure

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.

Cryo-EM structures of alpha-synuclein fibrils with the H50Q hereditary mutation reveal new polymorphs

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.

Cryo-EM Structures of Four Polymorphic TDP-43 Amyloid Cores

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.