The 140-residue protein α-synuclein (AS) is able to form amyloid fibrils and as such is the
main component of protein inclusions involved in Parkinson's disease. We have investigated …

The relation of α‐synuclein (αS) aggregation to Parkinson's disease (PD) has long been
recognized, but the mechanism of toxicity, the pathogenic species and its molecular …

CAMSAP and Patronin family members regulate microtubule minus-end stability and
localization and thus organize noncentrosomal microtubule networks, which are essential …

The polymerization of the microtubule-associated protein tau into paired helical filaments
(PHFs) represents one of the hallmarks of Alzheimer's disease. We employed solid-state …

Proteorhodopsin (PR) is a recently discovered ubiquitous eubacterial retinal-binding light-
driven proton pump. Almost 1000 PR variants are widely distributed in species of marine …

Protein misfolding and aggregation is linked to a large number of neurodegenerative and
systemic diseases. Prominent examples are the spongiform encephalopathies, Parkinson's …

Abstract We describe the principles and applications of dipolar recoupling in solid-state
NMR spectroscopy as a means to access information about molecular structure and transfer …

Gating the ion-permeation pathway in K+ channels requires conformational changes in
activation and inactivation gates. Here we have investigated the structural alterations …

Protein aggregation via polyglutamine stretches occurs in a number of severe
neurodegenerative diseases such as Huntington's disease. We have investigated fibrillar …

Fibrils from the Parkinson's-disease-related A53T mutant of α-synuclein were investigated
by solid-state NMR spectroscopy, electron microscopy, and atomic force microscopy …