α-Synuclein in Central Nervous System and from Erythrocytes, Mammalian Cells, andEscherichia coliExists Predominantly as Disordered Monomer

Mimicking Phosphorylation at Serine 87 Inhibits the Aggregation of Human  -Synuclein and Protects against Its Toxicity in a Rat Model of Parkinson's Disease

(2012) A. Oueslati et al.   JOURNAL OF NEUROSCIENCE

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

(2011) Tim Bartels et al.   NATURE

Identification of Novel α-Synuclein Isoforms in Human Brain Tissue by using an Online NanoLC-ESI-FTICR-MS Method

(2011) Annika Öhrfelt et al.   NEUROCHEMICAL RESEARCH

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

Progressive accumulation of amyloid-β oligomers in Alzheimer’s disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins

(2010) Emiley Pham et al.   FEBS Journal

The Lipid-binding Domain of Wild Type and Mutant α-Synuclein

(2010) Elka R. Georgieva et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Phosphorylation at S87 Is Enhanced in Synucleinopathies, Inhibits  -Synuclein Oligomerization, and Influences Synuclein-Membrane Interactions

(2010) K. E. Paleologou et al.   JOURNAL OF NEUROSCIENCE

Metalloproteomics and metal toxicology of α-synuclein

(2010) Aaron Santner et al.   Metallomics

Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation

(2010) V. L. Anderson et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

19F NMR Studies of α-Synuclein Conformation and Fibrillation

(2009) Conggang Li et al.   BIOCHEMISTRY

Biophysics of Parkinsons Disease: Structure and Aggregation of α- Synuclein

(2009) Vladimir Uversky et al.   CURRENT PROTEIN & PEPTIDE SCIENCE

Phosphorylation of Synucleins by Members of the Polo-like Kinase Family

(2009) Martial K. Mbefo et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

E46K Parkinson’s-Linked Mutation Enhances C-Terminal-to-N-Terminal Contacts in α-Synuclein

(2009) Carla C. Rospigliosi et al.   JOURNAL OF MOLECULAR BIOLOGY

Structural Reorganization of α-Synuclein at Low pH Observed by NMR and REMD Simulations

(2009) Kuen-Phon Wu et al.   JOURNAL OF MOLECULAR BIOLOGY

α-Synuclein and neuronal cell death

(2009) Mark R Cookson   Molecular Neurodegeneration

Targeted overexpression of the parkin substrate Pael-R in the nigrostriatal system of adult rats to model Parkinson's disease

(2009) Julien Dusonchet et al.   NEUROBIOLOGY OF DISEASE

A comparative study of common techniques used to measure haemolysis in stored red cell concentrates

(2009) V. Han et al.   VOX SANGUINIS

Phosphorylation Does Not Prompt, Nor Prevent, the Formation of  -synuclein Toxic Species in a Rat Model of Parkinson's Disease

(2008) S. Azeredo da Silveira et al.   HUMAN MOLECULAR GENETICS

Phosphorylation at Ser-129 but Not the Phosphomimics S129E/D Inhibits the Fibrillation of α-Synuclein

(2008) Katerina E. Paleologou et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Characterization of Conformational and Dynamic Properties of Natively Unfolded Human and Mouse α-Synuclein Ensembles by NMR: Implication for Aggregation

(2008) Kuen-Phon Wu et al.   JOURNAL OF MOLECULAR BIOLOGY

Advanced glycation end products induce in vitro cross‐linking of α‐synuclein and accelerate the process of intracellular inclusion body formation

(2008) Shamim Shaikh et al.   JOURNAL OF NEUROSCIENCE RESEARCH

Highly Efficient Depletion Strategy for the Two Most Abundant Erythrocyte Soluble Proteins Improves Proteome Coverage Dramatically

(2008) Jeffrey H. Ringrose et al.   JOURNAL OF PROTEOME RESEARCH

Membrane-Bound α-Synuclein Forms an Extended Helix: Long-Distance Pulsed ESR Measurements Using Vesicles, Bicelles, and Rodlike Micelles

(2008) Elka R. Georgieva et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Tissue transglutaminase modulates α-synuclein oligomerization

(2008) Ine M.J. Segers-Nolten et al.   PROTEIN SCIENCE

Hydrogen exchange of monomeric α-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding inEscherichia coli

(2008) Robyn L. Croke et al.   PROTEIN SCIENCE