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

What causes cell death in Parkinson's disease?

(2010) Amitabh Gupta et al.   ANNALS OF NEUROLOGY

Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses

(2010) Stephen Connelly et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Distinct Region-Specific  -Synuclein Oligomers in A53T Transgenic Mice: Implications for Neurodegeneration

(2010) E. Tsika et al.   JOURNAL OF NEUROSCIENCE

Missing pieces in the Parkinson's disease puzzle

(2010) Jose A Obeso et al.   NATURE MEDICINE

Brain α-synuclein accumulation in multiple system atrophy, Parkinson's disease and progressive supranuclear palsy: a comparative investigation

(2009) Junchao Tong et al.   BRAIN

Formation of a High Affinity Lipid-Binding Intermediate during the Early Aggregation Phase of α-Synuclein†

(2008) David P. Smith et al.   BIOCHEMISTRY

The two faces of protein misfolding: gain- and loss-of-function in neurodegenerative diseases

(2008) Konstanze F Winklhofer et al.   EMBO JOURNAL

Cryoelectron Microscopy Structure of Purified γ-Secretase at 12 Å Resolution

(2008) Pamela Osenkowski et al.   JOURNAL OF MOLECULAR BIOLOGY

Aggregates Assembled From Overexpression of Wild-Type α-Synuclein are not Toxic to Human Neuronal Cells

(2008) Li-wen Ko et al.   JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY

GATA transcription factors directly regulate the Parkinson's disease-linked gene  -synuclein

(2008) C. R. Scherzer et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA