Lothar Gremer

This study provides direct evidence of transient binding between α-synuclein C-terminus and synaptobrevin-2 using NMR and other biophysical methods, suggesting a role in neuronal exocytosis.

This paper shows lecanemab binds to amyloid-β fibrils from Alzheimer's disease mouse models with flexible N-termini, including type-I, type-II, and Arctic folds, but not those with fixed N-termini like in tg-SwDI mice.

This paper expresses and characterizes native-like human prion protein with GPI-anchoring and glycosylation using Leishmania tarentolae, confirming its structural homogeneity and monomeric conformation.

This paper develops all-D-peptide ligands that disassemble alpha-syn preformed fibrils into monomers, showing potential for treating Parkinson's disease.

The paper presents cryo-EM structures of Aβ fibrils from Alzheimer's disease mouse models and compares them to human fibrils.

This study uses solid-state MAS NMR to investigate the structure of Aβ oligomers bound to huPrP, revealing conformational heterogeneity and β-strand content.