scispace - formally typeset
S

Shifeng Xiao

Researcher at Shenzhen University

Publications -  11
Citations -  275

Shifeng Xiao is an academic researcher from Shenzhen University. The author has contributed to research in topics: Tau protein & Medicine. The author has an hindex of 4, co-authored 8 publications receiving 180 citations. Previous affiliations of Shifeng Xiao include Cornell University.

Papers
More filters
Journal ArticleDOI

Discovery and characterization of stable and toxic Tau/phospholipid oligomeric complexes.

TL;DR: It is reported that the interaction of Tau with vesicles results in the formation of highly stable protein/phospholipid complexes, which are toxic to primary hippocampal cultures and are detected by MC-1, an antibody recognizing pathological Tau conformations.
Journal ArticleDOI

Tau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeats.

TL;DR: In this article, electron spin resonance spectroscopy was employed to investigate the secondary and long-range structural properties of the microtubule-binding domain (MBD) of three-repeat tau isoforms when bound to lipid vesicles and membrane mimetics.
Journal ArticleDOI

Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- and lipid-binding properties of Tau.

TL;DR: Tyr-310 phosphorylation has a unique role in the regulation of Tau aggregation, microtubule, and lipid interactions and is highlighted by NMR experiments indicated that these effects are mediated by a local decrease in β-sheet propensity of Tau's PHF6 domain.
Journal ArticleDOI

Fisetin inhibits tau aggregation by interacting with the protein and preventing the formation of β-strands.

TL;DR: Fisetin, a plant-derived polyphenol compound, can inhibit aggregation of the tau fragment, K18, and can disaggregate tau K18 filaments in vitro as discussed by the authors.
Posted ContentDOI

Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- and lipid-binding properties of Tau

TL;DR: These findings underscore the unique role of Y310 phosphorylation in the regulation of Tau aggregation, microtubule and lipid interactions and highlight the importance of conducting further studies to elucidate its role in theregulation of Tau normal functions and its pathogenic properties.