Refolding of helical soluble α-synuclein through transient interaction with lipid interfaces

Parkinson disease

(2017) Werner Poewe et al.   Nature Reviews Disease Primers

New insights into cellular α-synuclein homeostasis in health and disease

(2016) Ulf Dettmer et al.   CURRENT OPINION IN NEUROBIOLOGY

Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation

(2015) Ulf Dettmer et al.   Nature Communications

α-Synuclein Multimers Cluster Synaptic Vesicles and Attenuate Recycling

(2014) Lina Wang et al.   CURRENT BIOLOGY

α-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formation

(2014) Jacqueline Burré et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Solid-State 13C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein α-Synuclein

(2013) Avigdor Leftin et al.   JOURNAL OF MOLECULAR BIOLOGY

The Function of α-Synuclein

(2013) Jacob T. Bendor et al.   NEURON

α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

(2011) Tim Bartels et al.   NATURE

Targeted Amino-Terminal Acetylation of Recombinant Proteins in E. coli

(2010) Matthew Johnson et al.   PLoS One

Linking folding and binding

(2009) Peter E Wright et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY