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Related Experiment Video

Updated: Mar 17, 2026

Assays for the Degradation of Misfolded Proteins in Cells

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

Modulating protein quality control.

Lars Plate^1,2, Ryan J Paxman¹, R Luke Wiseman^2,3

¹Department of Chemistry, The Scripps Research Institute, La Jolla, United States.

|July 21, 2016

Summary

This summary is machine-generated.

Small molecules targeting the unfolded protein response may offer new treatments for protein misfolding diseases. This approach holds promise for various human conditions caused by protein aggregation.

Keywords:

ATF6-alpha ER stress cell biology endoplasmic reticulum human site-1-protease small molecule screening unfolded protein response

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Last Updated: Mar 17, 2026

Assays for the Degradation of Misfolded Proteins in Cells

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Area of Science:

Biochemistry
Molecular Biology
Pharmacology

Background:

Protein misfolding diseases result from the accumulation of misfolded proteins.
The unfolded protein response (UPR) is a cellular stress response pathway.
Dysregulation of the UPR is implicated in the pathogenesis of many protein misfolding diseases.

Purpose of the Study:

To explore the therapeutic potential of small molecules that modulate the unfolded protein response (UPR).
To investigate the role of UPR modulators in treating human protein misfolding diseases.

Main Methods:

Utilizing small molecule screening to identify UPR modulators.
Employing cell-based assays to assess the impact of molecules on UPR pathways.
Investigating the efficacy of identified compounds in disease models.

Main Results:

Identification of novel small molecules capable of modulating the UPR.
Demonstration that these molecules can alleviate cellular stress associated with protein misfolding.
Evidence suggesting therapeutic potential in preclinical models.

Conclusions:

Small molecules targeting the UPR represent a promising therapeutic strategy.
Modulating the UPR could offer a viable treatment approach for diverse protein misfolding disorders.
Further research into UPR-targeted therapies is warranted.