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PMID: 8287967 Published · ppublish English Journal Article

Assembly of Alzheimer-like filaments from full-length tau protein.

FEBS letters ·Vol. 337 ·No. 2 ·1994-01-10 ·Pages 135-8

Crowther RA, Olesen OF, Smith MJ, Jakes R, Goedert M

Abstract

The principal fibrous component of neurofibrillary pathology in Alzheimer's disease, the paired helical filament, is formed from hyperphosphorylated microtubule-associated protein tau. Here we show that recombinant tau protein either in a non-phosphorylated state or following phosphorylation with brain extract can be assembled in vitro into filaments resembling those seen in Alzheimer's disease.

MeSH Terms
Alzheimer Disease/pathology Cloning, Molecular Escherichia coli Humans Immunoblotting Microscopy, Electron Phosphorylation Recombinant Proteins/biosynthesis,isolation & purification,ultrastructure tau Proteins/biosynthesis,isolation & purification,ultrastructure
Chemicals
Recombinant Proteins tau Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Crowther R A
Medical Research Council, Laboratory of Molecular Biology, Cambridge, UK.
Olesen O F
Smith M J
Jakes R
Goedert M
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1994-01-10
Pages
135-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
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