David S Eisenberg

The paper identifies a founder variant in ADAP1 associated with increased risk of schizophrenia and bipolar disorder in a Colombian genetic isolate.

The paper determines the cryo-EM structures of three neuropathy-associated ATTR variants and reveals a shared amyloid core despite different mutations and clinical phenotypes.

This study develops a structure-guided antibody that detects SOD1 oligomers in various ALS genotypes and shows its ability to alleviate cytotoxic effects in cell cultures.

The paper shows a D-peptide disassembles AD-tau fibrils via a strain-relief mechanism involving oppositely twisted fibrils.

The paper uses cryo-electron microscopy to show that cardiac ATTR amyloid fibrils are structurally polymorphic, independent of genotype and phenotype, challenging the one-fibril-fold-per-disease paradigm.

The paper identifies TMEM106B, not TDP-43, as the protein composing amyloid fibrils in FTLD-TDP using cryo-EM.

This paper presents the cryoEM structure of hnRNPA2 LCD fibrils, showing structural differences from pathogenic amyloid and how mutations convert it to a pathogenic form.

The paper evaluates peptide inhibitors in Drosophila models of neuropathic ATTR, finding TabFH2 most effective in improving motor function and reducing TTR deposition.