𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Dynamics of α-synuclein aggregation and inhibition of pore-like oligomer development by β-synuclein

✍ Scribed by Igor F. Tsigelny; Pazit Bar-On; Yuriy Sharikov; Leslie Crews; Makoto Hashimoto; Mark A. Miller; Steve H. Keller; Oleksandr Platoshyn; Jason X.-J. Yuan; Eliezer Masliah

Book ID
111311876
Publisher
John Wiley and Sons
Year
2007
Tongue
English
Weight
985 KB
Volume
274
Category
Article
ISSN
1432-1327

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Inhibition of α-synuclein aggregation by
Inhibition of α-synuclein aggregation by small heat shock proteins
✍ Ilona B. Bruinsma; Kim A. Bruggink; Karsten Kinast; Alexandra A. M. Versleijen; 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 846 KB

## Abstract The fibrillization of α‐synuclein (α‐syn) is a key event in the pathogenesis of α‐synucleinopathies. Mutant α‐syn (A53T, A30P, or E46K), each linked to familial Parkinson's disease, has altered aggregation properties, fibril morphologies, and fibrillization kinetics. Besides α‐syn, Lewy

Baicalein Inhibits Formation of α-Synucl
Baicalein Inhibits Formation of α-Synuclein Oligomers within Living Cells and Prevents Aβ Peptide Fibrillation and Oligomerisation
✍ Jia-Hong Lu; Mustafa Taleb Ardah; Siva Sundara Kumar Durairajan; Liang-Feng Liu; 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 622 KB

## Abstract Abnormal protein aggregation in the brain is linked to the pathogenesis of neurodegenerative diseases, including Alzheimer's disease (AD) and Parkinson's disease (PD). Recent studies revealed that the oligomeric form of aggregates is most likely the toxic species, and thus could be a go