Hyperphosphorylation of Intrinsically Disordered Tau Protein Induces an Amyloidogenic Shift in Its Conformational Ensemble

PLoS ONE - United States
doi 10.1371/journal.pone.0120416
Full Text
Abstract

Available in full text

Date
Authors
Publisher

Public Library of Science (PLoS)

Related search

Conformational Recognition of an Intrinsically Disordered Protein

Biophysical Journal
Biophysics
2014English

Water in Amyloidogenic Intrinsically Disordered Proteins: Interplay of Conformational Preference and Amyloid Aggregation

Biophysical Journal
Biophysics
2016English

Automatic Assignment of the Intrinsically Disordered Protein Tau With 441-Residues

Journal of the American Chemical Society
BiochemistryColloidCatalysisChemistrySurface Chemistry
2010English

Prediction of the Effects of the Val66Met Polymorphism on the Conformational Ensemble of an Intrinsically Disordered Protein, Brain-Derived Neurotrophic Factor

Biophysical Journal
Biophysics
2014English

Different Conformational Subensembles of the Intrinsically Disordered Protein Synuclein in Cells

English

CIDER: Classification of Intrinsically Disordered Ensemble Regions

Biophysical Journal
Biophysics
2015English

Prediction of the Effects of the Val66Met Polymorphism and Adjacent Structured Domains on the Conformational Ensemble of an Intrinsically Disordered Protein, Brain-Derived Neurotrophic Factor

Biophysical Journal
Biophysics
2015English

Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and Upon Multisite Phosphorylation

Biophysical Journal
Biophysics
2017English

Interfacial Properties of N TAIL , an Intrinsically Disordered Protein

Biophysical Journal
Biophysics
2017English

Amanote Research

Note-taking for researchers

Follow Amanote

© 2024 Amaplex Software S.P.R.L. All rights reserved.

Privacy PolicyRefund Policy