Ontology highlight
ABSTRACT:
SUBMITTER: Luo Y
PROVIDER: S-EPMC3637047 | biostudies-literature | 2013 May
REPOSITORIES: biostudies-literature
Luo Yin Y Dinkel Paul P Yu Xiang X Margittai Martin M Zheng Jie J Nussinov Ruth R Wei Guanghong G Ma Buyong B
Chemical communications (Cambridge, England) 20130501 34
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. ...[more]