Related Experiment Video

Updated: May 13, 2026

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
09:22

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Molecular insights into the reversible formation of tau protein fibrils

Yin Luo1, Paul Dinkel, Xiang Yu

  • 1State Key Laboratory of Surface Physics, Department of Physics, Fudan University, Shanghai, PR China.

Chemical Communications (Cambridge, England)
|March 26, 2013
PubMed

More Related Videos

In Vitro Assay for Studying the Aggregation of Tau Protein and Drug Screening09:49

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

Published on: November 20, 2018

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

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, normally used to...
Protein Folding01:22

Protein Folding

Overview