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Related Experiment Video

Updated: May 29, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
07:57

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

Detecting HSP90 phosphorylation.

Mehdi Mollapour1, Len Neckers

  • 1Urologic Oncology Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.

Methods in Molecular Biology (Clifton, N.J.)
|September 8, 2011
PubMed
Summary
This summary is machine-generated.

Heat-shock protein 90 (HSP90) is a crucial chaperone for cancer-related proteins. Its function relies on ATPase activity, regulated by co-chaperones and modifications like phosphorylation, which can be studied in yeast.

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Last Updated: May 29, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
07:57

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Published on: January 20, 2023

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
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Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

Published on: March 31, 2022

Area of Science:

  • Molecular biology
  • Biochemistry
  • Cellular biology

Background:

  • Heat-shock protein 90 (HSP90) is a vital molecular chaperone in eukaryotic cells.
  • HSP90 plays a critical role in the stabilization and function of proteins implicated in multistep carcinogenesis.
  • Its ATPase activity is fundamental to its chaperone function and is tightly regulated.

Purpose of the Study:

  • To investigate the regulatory mechanisms of HSP90's ATPase activity.
  • To explore the role of posttranslational modifications in HSP90 function.
  • To establish yeast as a model system for studying HSP90 phosphorylation.

Main Methods:

  • Expression and purification of HSP90 in yeast.
  • Utilizing pan-phosphoserine and phosphothreonine antibodies for detection.
  • Assessing HSP90 ATPase activity in conjunction with regulatory factors.

Main Results:

  • Yeast successfully expresses and purifies functional HSP90.
  • Phosphorylation of HSP90 was detected using specific antibodies.
  • Evidence suggests co-chaperones and posttranslational modifications modulate HSP90 ATPase activity.

Conclusions:

  • Yeast is a suitable model for studying HSP90 regulation and function.
  • Posttranslational modifications, particularly phosphorylation, are key regulators of HSP90.
  • Understanding HSP90 regulation is crucial for targeting cancer-related pathways.