ARAN - Access to Research at NUI Galway

Methods for Monitoring Endoplasmic Reticulum Stress and the Unfolded Protein Response

ARAN - Access to Research at NUI Galway

Show simple item record Samali, Afshin en FitzGerald, Una en Deegan, Shane en Gupta, Sanjeev en 2010-08-20T10:40:23Z en 2010-08-20T10:40:23Z en 2010 en
dc.identifier.citation Samali, A., Fitzgerald, U., Deegan, S., & Gupta, S. Methods (2010) for monitoring endoplasmic reticulum stress and the unfolded protein response. Int J Cell Biol, 830307. en
dc.identifier.uri en
dc.description.abstract The endoplasmic reticulum (ER) is the site of folding of membrane and secreted proteins in the cell. Physiological or pathological processes that disturb protein folding in the endoplasmic reticulum cause ER stress and activate a set of signaling pathways termed the Unfolded Protein Response (UPR). The UPR can promote cellular repair and sustained survival by reducing the load of unfolded proteins through upregulation of chaperones and global attenuation of protein synthesis. Research into ER stress and the UPR continues to grow at a rapid rate as many new investigators are entering the field. There are also many researchers not working directly on ER stress, but who wish to determine whether this response is activated in the system they are studying: thus, it is important to list a standard set of criteria for monitoring UPR in different model systems. Here, we discuss approaches that can be used by researchers to plan and interpret experiments aimed at evaluating whether the UPR and related processes are activated. We would like to emphasize that no individual assay is guaranteed to be the most appropriate one in every situation and strongly recommend the use of multiple assays to verify UPR activation. en
dc.format application/pdf en
dc.language.iso en en
dc.subject Biochemistry en
dc.title Methods for Monitoring Endoplasmic Reticulum Stress and the Unfolded Protein Response en
dc.type Article en
dc.local.publishedsource en
dc.local.publisherstatement application/pdf en
dc.description.peer-reviewed peer-reviewed en
dc.contributor.funder Science Foundation Ireland en
dc.contributor.funder Health Research Board en
dc.contributor.funder Enterprise Ireland en

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