Can any “non-specific charge modification within microtubule binding domains of Tau” be a prerequisite of the protein amyloid aggregation? An in vitro study on the 1N4R isoform

The aggregation of Tau into amyloid fibrils is a hallmark of neurodegenerative diseases such as Alzheimer’s disease (AD). Compared to the Aβ peptide, tau pathology more closely tracks changes in brain function that are responsible for the onset of early symptoms in AD. Tau belongs to the class of in...

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Veröffentlicht in:	International journal of biological macromolecules 2018-04, Vol.109, p.188-204
Hauptverfasser:	Jangholi, Abolfazl, Ashrafi-Kooshk, Mohammad Reza, Arab, Seyed Shahriar, Karima, Saeed, Poorebrahim, Mansour, Ghadami, Seyyed Abolghasem, Moosavi-Movahedi, Ali Akbar, Khodarahmi, Reza
Format:	Artikel
Sprache:	eng
Schlagworte:	Amyloid aggregation Charge modification Tau protein
Online-Zugang:	Volltext
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