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Updated: Jun 5, 2026

Measuring Endoplasmic Reticulum Stress and Unfolded Protein Response in HIV-1 Infected T-Cells and Analyzing its Role in HIV-1 Replication
Published on: June 14, 2024
Assays for detecting the unfolded protein response
Karen Cawley1, Shane Deegan, Afshin Samali
1Apoptosis Research Centre, School of Natural Sciences (Biochemistry), National University of Ireland Galway, Ireland.
This study details methods for assessing endoplasmic reticulum (ER) stress and the unfolded protein response (UPR) in cells. These techniques help researchers understand cellular adaptation and repair mechanisms during protein folding disturbances.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The endoplasmic reticulum (ER) is crucial for protein folding.
- Disruptions in ER protein folding trigger ER stress and the unfolded protein response (UPR).
- The UPR activates adaptive cellular responses, including enhanced protein folding and degradation.
Purpose of the Study:
- To describe experimental methods for studying the UPR in tissue culture cells.
- To provide guidelines for researchers evaluating UPR activation.
- To aid in the interpretation of UPR-related experimental data.
Main Methods:
- Utilizing established cell culture techniques.
- Implementing assays to monitor UPR signaling pathways.
- Analyzing transcriptional activation of UPR target genes.
Main Results:
- The described methods allow for the evaluation of UPR activation.
- These techniques facilitate the assessment of cellular responses to ER stress.
- The study provides a framework for understanding UPR dynamics.
Conclusions:
- The UPR is a critical cellular defense mechanism against ER stress.
- Standardized methods are essential for consistent UPR research.
- These guidelines support new investigators in the field of ER stress biology.
Related Concept Videos
The Unfolded Protein Response
Regulation of the Unfolded Protein Response
Protein Folding Quality Check in the RER

