Publications by authors named "Tien Ying Tsai"
Article Synopsis
- The study focuses on the role of the SERF1a factor in the fibrillization of huntingtin exon 1, which is crucial for understanding Huntington's disease.
- Researchers used various methods, including SEC-SWAXS, NMR, and molecular simulations, to show that SERF1a binds tightly to the N-terminal region of huntingtin's NT17 peptide.
- The findings suggest that the structure of these peptides affects how they interact with SERF1a, with more structured peptides having weaker binding, shedding light on the mechanism behind Httex1 fibrillization.
Alzheimer's disease (AD) is a devastating, progressive neurodegenerative disease affecting the elderly in the world. The pathological hallmark senile plaques are mainly composed of amyloid-β (Aβ), in which the main isoforms are Aβ40 and Aβ42. Aβ is prone to aggregate and ultimately forms amyloid fibrils in the brains of AD patients.
View Article and Find Full Text PDFAbnormal polyglutamine (polyQ) expansion and fibrillization occur in Huntington's disease (HD). Amyloid modifier SERF enhances amyloid formation, but the underlying mechanism is not revealed. Here, the fibrillization and toxicity effect of SERF1a on Htt-exon1 are examined.
View Article and Find Full Text PDF