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    Methods for monitoring endoplasmic reticulum stress and the unfolded protein response.

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    Authors
    Samali, Afshin
    Fitzgerald, Una
    Deegan, Shane
    Gupta, Sanjeev
    Affiliation
    Department of Biochemistry, National University of Ireland, Galway, Galway, Ireland.
    Issue Date
    2010
    
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    Citation
    Methods for monitoring endoplasmic reticulum stress and the unfolded protein response. 2010, 2010:830307 Int J Cell Biol
    Journal
    International journal of cell biology
    URI
    http://hdl.handle.net/10147/93853
    DOI
    10.1155/2010/830307
    PubMed ID
    20169136
    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.
    Language
    en
    ISSN
    1687-8884
    ae974a485f413a2113503eed53cd6c53
    10.1155/2010/830307
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