title: Molecular insights into the reversible formation of tau protein fibrils.
abstract: We computationally and experimentally showed that tau protein fibrils can be formed at high temperature. When cooled, the fibrils dissociate back to monomers. Heparin promotes tau fibril formation and prevents its reversion. Our results revealed the physicochemical mechanism of reversible formation of tau fibrils.
authors.affiliation: State Key Laboratory of Surface Physics, Department of Physics, Fudan University, Shanghai, PR China.
authors.forename: Yin
authors.initials: Y
authors.lastname: Luo
authors.forename: Paul
authors.initials: P
authors.lastname: Dinkel
authors.forename: Xiang
authors.initials: X
authors.lastname: Yu
authors.forename: Martin
authors.initials: M
authors.lastname: Margittai
authors.forename: Jie
authors.initials: J
authors.lastname: Zheng
authors.forename: Ruth
authors.initials: R
authors.lastname: Nussinov
authors.forename: Guanghong
authors.initials: G
authors.lastname: Wei
authors.forename: Buyong
authors.initials: B
authors.lastname: Ma
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D006493:Heparin / Q000737:chemistry; D006358:Hot Temperature; D016875:tau Proteins / Q000737:chemistry*
chemical_list: D000682:Amyloid; D016875:tau Proteins; D006493:Heparin