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Related Experiment Video

Updated: May 10, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Reconstructing the Hsp90/Tau Machine.

Umesh K Jinwal¹, John Koren, Chad A Dickey

¹Department of Molecular Medicine, USF Health Byrd Alzheimer's Institute, Tampa, Florida 33613.

Current Enzyme Inhibition

|June 27, 2013

Summary

This summary is machine-generated.

Cellular protein imbalance drives aging diseases. Targeting Hsp90 co-chaperones may treat neurodegenerative diseases like Alzheimer's by managing tau protein buildup.

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Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

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Published on: July 21, 2021

Area of Science:

Molecular biology
Neuroscience
Aging research

Background:

Cellular protein homeostasis is crucial for health, with imbalances linked to aging and neurodegenerative diseases.
Accumulation of toxic protein aggregates, such as tau, is a hallmark of tauopathies, including Alzheimer's disease (AD).
Age-related alterations in the cellular chaperone system, particularly Hsp90 co-chaperones, influence tau protein stability and aggregation.

Purpose of the Study:

To investigate the role of Hsp90 co-chaperones in regulating tau protein.
To identify potential therapeutic targets within the Hsp90 co-chaperone network for treating tauopathies.

Main Methods:

Analysis of the Hsp90 co-chaperone repertoire's impact on tau protein.
Evaluation of tau protein stability and clearance mechanisms influenced by co-chaperones.

Main Results:

Hsp90 co-chaperones exhibit varied effects on tau protein, with some promoting stabilization and others facilitating clearance.
The Hsp90 co-chaperone network represents a potential avenue for therapeutic intervention in tauopathies.

Conclusions:

Targeting individual Hsp90 co-chaperones offers a promising, potentially safer therapeutic strategy for neurodegenerative diseases compared to direct Hsp90 inhibition.
Modulating Hsp90 co-chaperone activity could restore protein homeostasis and mitigate neurotoxic tau accumulation in aging-related diseases.