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Article

Tau aggregation is driven by a transition from random coil to beta sheet structure.

Biochimica et biophysica acta - 3 Jan 2005

von Bergen Martin, Barghorn Stefan, Biernat Jacek, Mandelkow Eva-Maria, Mandelkow Eckhard

Abstract excerpt

The abnormal aggregation of the microtubule associated protein tau into paired helical filaments (PHFs) is one the hallmarks of Alzheimer's disease. The soluble protein is one of the longest natively unfolded proteins, lacking significant amounts of secondary structure over a sequence of 441 amino acids in the longest isoform. Furthermore, the unfolded character is consistent with some notable features of the...

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Source

Identifiers

PMID: 15615635
DOI: 10.1016/j.bbadis.2004.09.010

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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