Corrigendum: The disease associated Tau35 fragment has an increased propensity to aggregate compared to full-length

Related Experiment Video

Updated: Jul 15, 2025

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening
09:49

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening

Published on: November 20, 2018

18.7K

Chen Lyu1, Stefano Da Vela2, Youssra Al-Hilaly3

  • 1Department of Basic and Clinical Neuroscience, King's College London, London, United Kingdom.

Frontiers in Molecular Biosciences
|October 4, 2023
PubMed

Keywords:
biophysical studiesdementiahybrid methodsintrinsically disordered proteinsneurodegenerationsmall angle x-ray scatteringtau truncationtauopathy

More Related Videos

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

18.4K
An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons05:51

An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

Published on: May 23, 2019

6.0K

Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
9.6K