Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Assembly of Complex Microtubule Structures

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.

Microtubule Associated Proteins (MAPs)

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Diagnostic impact of tau versus amyloid PET in patients with cognitive symptoms.

Brain : a journal of neurology·2026

Same author

Methods for characterizing the individual filament structures of amyloid peptide assemblies using atomic force microscopy.

Methods in enzymology·2026

Same author

Assessment of clinical and neuroimaging efficacy of treatment targeting tau pathology in mild cognitive impairment and mild to moderate Alzheimer's disease with hydromethylthionine mesylate using external control data.

The journal of prevention of Alzheimer's disease·2026

Same author

Atypical population pharmacokinetics of hydromethylthionine in patients with Alzheimer's disease explains unexpected phase 3 trial results.

British journal of clinical pharmacology·2026

Same author

Human FUS is toxic via association with RNA polymerase II in Drosophila.

Cell death & disease·2026

Same author

Amyloid and the Cross-Beta Architecture.

Journal of visualized experiments : JoVE·2026

Search research articles

Related Experiment Video

Updated: Aug 23, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

An Additive-Free Model for Tau Self-Assembly.

Youssra K Al-Hilaly^1,2, Karen E Marshall³, Liisa Lutter^4,5

¹Chemistry Department, College of Science, Mustansiriyah University, Baghdad, Iraq. youssra.alhilaly@uomustansiriyah.edu.iq.

Methods in Molecular Biology (Clifton, N.J.)

|October 31, 2022

Summary

This summary is machine-generated.

Researchers developed methods to create tau protein filaments in vitro, crucial for studying Alzheimer's disease (AD) pathology. This work provides a new model system for investigating tau misfolding and self-assembly in AD.

Keywords:

Atomic force microscopy Circular dichroism Cross-beta Electron microscopy Paired helical filament Self-assembly Tau Thioflavin S fluorescence Tyrosine fluorescence X-ray fibre diffraction

More Related Videos

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

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 Neurons

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

Published on: May 23, 2019

Related Experiment Videos

Last Updated: Aug 23, 2025

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

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

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 Neurons

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

Published on: May 23, 2019

Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Tau protein is essential for microtubule stability.
Misfolded tau protein self-assembles into filaments (PHFs and SFs) in Alzheimer's disease (AD).
Full-length tau assembly is limited in vitro without additives like heparin.

Purpose of the Study:

To describe methods for preparing in vitro paired helical filaments (PHFs) and straight filaments (SFs) from a truncated tau protein (297-391), named dGAE.
To establish an alternative in vitro PHF model system.
To discuss techniques for monitoring tau filament assembly and structure.

Main Methods:

Utilized a truncated tau protein (297-391) for self-assembly.
Developed methods to prepare in vitro PHFs and SFs.
Employed various biophysical and biochemical techniques to analyze filament assembly and structure.

Main Results:

Successfully prepared in vitro PHFs and SFs from the truncated tau protein (dGAE) without additives.
Demonstrated the self-assembly capability of the truncated tau form.
Established a novel in vitro model system for tau filament formation.

Conclusions:

The truncated tau protein (dGAE) provides a valuable tool for studying tauopathies like AD.
The developed methods facilitate the investigation of tau self-assembly mechanisms.
Further research can utilize these in vitro models to explore therapeutic strategies for AD.