Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure.

By M. Bergen, Peter Friedhoff, J. Biernat, J. Heberle, E. Mandelkow. Proceedings of the National Academy of Sciences of the United States of America, 2000

938 citations recorded by the source corpus.

Subfields: Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/ee46242176405bd3a4b394721282037e243ebaee

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Citations in the corpus

Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020, background): “tifs in the second repeat and VQIVYK in the third repeat within the tau microtubule-binding domain are crucial for the formation of β-sheet structures and consequent tau aggregation [221, 222].”
Tau pathology in Alzheimer disease and other tauopathies. (2005, methodology): “…SF and PHF-like structures has been achieved under different conditions, such as urea treatment for 60 h, incubations with unsaturated free fatty acids, tRNA, heparin or polyglutamic acid, employing a tau fragment, tau concentrations up to 12 mg/ml, and incubation times up to several days [62–72].”
Tau protein liquid–liquid phase separation can initiate tau aggregation (2018, neutral): “The in vitro aggregation of tau into amyloid-like fibrils has been manifold described by several authors, mostly with emphasis on aggregation kinetics and aggregate structure (von Bergen et al , 2000; Tepper et al , 2014).”
Role of tau protein in both physiological and pathological conditions. (2004, background): “However, it has also been suggested that filament formation is also partially dependent on the presence of certain -sheet structures within tau (284).”
Post-translational modifications of tau protein: implications for Alzheimer's disease. (2011, neutral): “Tau phosphorylation, probably at specific epitopes decreases tau binding to microtubules and alters microtubule stability and then free tau (unbound tau) can self-aggregate (Fischer et al., 2009; Kopke et al., 1993; von Bergen et al., 2000).”
Tau in Alzheimer Disease and Related Tauopathies (2010, background): “The β-structure in tau is concentrated only in repeats R2 and R3 which can self-assemble into filaments [70] and co-assemble with heparin [71].”
Mechanisms of tau-induced neurodegeneration (2009, neutral): “The b-structure in tau is concentrated only in repeats R2 and R3, which can selfassemble into filaments [194] and co-assemble with heparin [14].”
Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. (2005, methodology): “A recent report has suggested that the minimal interaction motif of tau that gives rise to aggregation is a 43 residue segment (PHF43, or N265-E338DR2) corresponding to the third microtubule-binding repeat sequence along with a number of adjacent residues.(96) In addition, a spot membrane-binding as”