Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Ninth BHD International Symposium: Advancing research through global collaboration.

Cell stress & chaperones·2026
Same author

Emw1/TTC27 is a chaperone required for folding of the eukaryotic elongation factor 2.

Cellular and molecular life sciences : CMLS·2026
Same author

Fanconi anemia complementation group C gene (FANCC) association with hereditary and sporadic renal tumors.

The oncologist·2026
Same author

Targeting and dissociating HIF2α from the molecular chaperone Hsp70 triggers apoptosis in kidney cancer.

Communications medicine·2026
Same author

c-KIT joins the TSC ToolKIT: a new driver of renal cystogenesis.

EMBO molecular medicine·2025
Same author

Ex vivo qualitative and quantitative analysis of fluorescently-labeled Hsp90 drug in human tumors.

Cell stress & chaperones·2025

Related Experiment Video

Updated: Aug 7, 2025

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
13:52

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae

Published on: July 9, 2013

10.4K

Saccharomyces cerevisiae as a tool for deciphering Hsp90 molecular chaperone function.

Sarah J Backe1,2, Mehdi Mollapour1,2,3, Mark R Woodford1,2,3

  • 1Department of Urology, SUNY Upstate Medical University, Syracuse, NY 13210, U.S.A.

Essays in Biochemistry
|March 13, 2023
PubMed
Summary

Saccharomyces cerevisiae, a yeast model, is crucial for understanding heat shock protein 90 (Hsp90) function. Its genetic tractability and similarity to higher eukaryotes facilitate discoveries in human health and disease.

Keywords:
Saccharomyces cerevisiaeheat shock proteinsmolecular chaperonespost translational modification

More Related Videos

Isolating Potentiated Hsp104 Variants Using Yeast Proteinopathy Models
08:44

Isolating Potentiated Hsp104 Variants Using Yeast Proteinopathy Models

Published on: November 11, 2014

8.2K
Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

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

Published on: July 21, 2021

2.8K

Related Experiment Videos

Last Updated: Aug 7, 2025

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
13:52

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae

Published on: July 9, 2013

10.4K
Isolating Potentiated Hsp104 Variants Using Yeast Proteinopathy Models
08:44

Isolating Potentiated Hsp104 Variants Using Yeast Proteinopathy Models

Published on: November 11, 2014

8.2K
Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

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

Published on: July 21, 2021

2.8K

Area of Science:

  • Molecular biology
  • Cellular biology
  • Biochemistry

Background:

  • Yeast, specifically Saccharomyces cerevisiae, is a powerful model organism.
  • Its genetic manipulability, rapid growth, and eukaryotic similarity aid biological research.
  • Saccharomyces cerevisiae has been instrumental in understanding complex proteins and pathways relevant to human health.

Purpose of the Study:

  • To provide an overview of the Saccharomyces cerevisiae model system.
  • To describe the application of this model in studying heat shock protein 90 (Hsp90) function.

Main Methods:

  • Review of existing literature on Saccharomyces cerevisiae as a model organism.
  • Analysis of studies utilizing Saccharomyces cerevisiae for heat shock protein 90 (Hsp90) research.

Main Results:

  • Saccharomyces cerevisiae offers significant advantages for genetic and functional studies.
  • Numerous key discoveries in heat shock protein 90 (Hsp90) biology originated from research in this yeast model.
  • The model system has been successfully employed to elucidate Hsp90 chaperone mechanisms.

Conclusions:

  • Saccharomyces cerevisiae is an effective eukaryotic model for investigating molecular chaperone functions.
  • Its application has led to critical insights into heat shock protein 90 (Hsp90) and its role in cellular signaling.