Residue Histidine 50 Plays a Key Role in Protecting α-Synuclein from Aggregation at Physiological pH

Structures of the E46K Mutant-Type α-Synuclein Protein and Impact of E46K Mutation on the Structures of the Wild-Type α-Synuclein Protein

(2013) Olivia Wise-Scira et al.   ACS Chemical Neuroscience

The Parkinson’s Disease-Associated H50Q Mutation Accelerates α-Synuclein Aggregation in Vitro

(2013) Dhiman Ghosh et al.   BIOCHEMISTRY

α-Synuclein as an intrinsically disordered monomer - fact or artefact?

(2013) Eduardo Coelho-Cerqueira et al.   FEBS Journal

Alpha-synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease

(2013) Silke Appel-Cresswell et al.   MOVEMENT DISORDERS

A novel  -synuclein missense mutation in Parkinson disease

(2013) C. Proukakis et al.   NEUROLOGY

100 years of Lewy pathology

(2012) Michel Goedert et al.   Nature Reviews Neurology

Role of C-terminal negative charges and tyrosine residues in fibril formation of α-synuclein

(2012) Yasutaka Izawa et al.   Brain and Behavior

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

(2011) Tim Bartels et al.   NATURE

A soluble  -synuclein construct forms a dynamic tetramer

(2011) W. Wang et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Impact of Tyr to Ala mutations on α-synuclein fibrillation and structural properties

(2008) Nataša Poklar Ulrih et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE

Selective loss of nigral dopamine neurons induced by overexpression of truncated human α-synuclein in mice

(2006) Masaki Wakamatsu et al.   NEUROBIOLOGY OF AGING