Endoplasmic reticulum stress in malignancy.
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Clarke, H. J., Chambers, J., Liniker, E., & Marciniak, S. (2014). Endoplasmic reticulum stress in malignancy.. Cancer Cell, 25 (5), 563-573. https://doi.org/10.1016/j.ccr.2014.03.015
The combination of relative nutrient deprivation and dysregulation of protein synthesis make malignant cells especially prone to protein misfolding. Endoplasmic reticulum stress, which results from protein misfolding within the secretory pathway, has a profound effect on cancer cell proliferation and survival. In this review, we examine the evidence implicating endoplasmic reticulum dysfunction in the pathology of cancer and discuss how recent findings may help to identify novel therapeutic targets.
Endoplasmic Reticulum, Humans, Neoplasms, Neovascularization, Pathologic, Boronic Acids, Pyrazines, Endoribonucleases, Protein-Serine-Threonine Kinases, eIF-2 Kinase, Antineoplastic Agents, Cell Proliferation, Cell Survival, Protein Folding, Activating Transcription Factor 6, Unfolded Protein Response, Endoplasmic Reticulum Stress, Bortezomib
Medical Research Council (G1002610)
Medical Research Council (G0601840)
Wellcome Trust (100140/Z/12/Z)
External DOI: https://doi.org/10.1016/j.ccr.2014.03.015
This record's URL: https://www.repository.cam.ac.uk/handle/1810/301417
Attribution-NonCommercial-NoDerivatives 4.0 International
Licence URL: https://creativecommons.org/licenses/by-nc-nd/4.0/