Ubiquitination of -synuclein by Siah-1 promotes -synuclein aggregation and apoptotic cell death

Unveiling a Selective Mechanism for the Inhibition of α-Synuclein Aggregation by β-Synuclein

α-Synuclein (αS) is an intrinsically disordered protein that is associated with Parkinson's disease (PD) through its ability to self-assemble into oligomers and fibrils. Inhibition of this oligomerization cascade is an interesting approach to developing therapeutical strategies and β-synuclein (βS) has been described as a natural negative regulator of this process. However, the biological backg...

The Aggregation of Huntingtin and α-Synuclein

Huntington's and Parkinson's diseases are neurodegenerative disorders associated with unusual protein interactions. Although the origin and evolution of these diseases are completely different, characteristic deposits of protein aggregates (huntingtin and α-synuclein resp.), are a common feature in both diseases. After these observations, many studies are performed with both proteins. Some of t...

-Synuclein Reduces Proteasomal Inhibition by -Synuclein but Not -Synuclein*

From the ‡Department of Pharmacology, Loyola University Medical Center, Maywood, Illinois 60153, the §Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, the ¶Department of Pharmacology, Boston University School of Medicine, Boston, Massachussetts 02118, the Department of Neuroscience, University of California at San Diego, La Jolla...

Hsp70 Reduces alpha-Synuclein Aggregation and Toxicity.

Aggregation and cytotoxicity of misfolded alpha-synuclein is postulated to be crucial in the disease process of neurodegenerative disorders such as Parkinson's disease and DLB (dementia with Lewy bodies). In this study, we detected misfolded and aggregated alpha-synuclein in a Triton X-100 insoluble fraction as well as a high molecular weight product by gel electrophoresis of temporal neocortex...

Alpha-synuclein structure, aggregation and modulators