M
Marianne Koritzinsky
Researcher at Princess Margaret Cancer Centre
Publications - 89
Citations - 7701
Marianne Koritzinsky is an academic researcher from Princess Margaret Cancer Centre. The author has contributed to research in topics: Unfolded protein response & Cancer. The author has an hindex of 38, co-authored 76 publications receiving 6899 citations. Previous affiliations of Marianne Koritzinsky include Maastricht University & Maastricht University Medical Centre.
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Journal ArticleDOI
Hypoxia signalling through mTOR and the unfolded protein response in cancer
TL;DR: Growing evidence suggests that HIF-, mTOR- and UPR-dependent responses to hypoxia act in an integrated way, influencing each other and common downstream pathways that affect gene expression, metabolism, cell survival, tumorigenesis and tumour growth.
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The unfolded protein response protects human tumor cells during hypoxia through regulation of the autophagy genes MAP1LC3B and ATG5
Kasper M.A. Rouschop,Twan van den Beucken,Ludwig Dubois,Hanneke E.C. Niessen,Johan Bussink,Kim G.M. Savelkouls,Tom G. Keulers,Hilda Mujcic,Willy Landuyt,Jan Willem Voncken,Philippe Lambin,Albert J. van der Kogel,Marianne Koritzinsky,Bradly G. Wouters +13 more
TL;DR: It is demonstrated that the UPR is an important mediator of the hypoxic tumor microenvironment and that it contributes to resistance to treatment through its ability to facilitate autophagy.
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ER stress‐regulated translation increases tolerance to extreme hypoxia and promotes tumor growth
Meixia Bi,Christine Naczki,Marianne Koritzinsky,Diane Fels,Jaime D. Blais,Nianping Hu,Heather P. Harding,Isabelle Novoa,Mahesh A. Varia,James A. Raleigh,Donalyn Scheuner,Randal J. Kaufman,John C. Bell,David Ron,Bradly G. Wouters,Constantinos Koumenis +15 more
TL;DR: It is demonstrated that cells cultured under hypoxic/anoxic conditions and transformed cells in hypoxic areas of tumors activate a translational control program known as the integrated stress response (ISR), which adapts cells to endoplasmic reticulum (ER) stress and suggests that this pathway is an attractive target for antitumor modalities.
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Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase perk and phosphorylation of the translation initiation factor eif2alpha
Constantinos Koumenis,Christine Naczki,Marianne Koritzinsky,Sally Rastani,Alan J. Diehl,Nahum Sonenberg,Antonis E. Koromilas,Bradly G. Wouters +7 more
TL;DR: Results indicate that adaptation of cells to hypoxic stress requires activation of PERK and phosphorylation of eIF2α and suggest that the mechanism of hypoxia-induced translational attenuation may be linked to ER stress and the unfolded-protein response.
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Hypoxia-mediated down-regulation of Bid and Bax in tumors occurs via hypoxia-inducible factor 1-dependent and -independent mechanisms and contributes to drug resistance.
Janine T. Erler,Christopher Cawthorne,Kaye J. Williams,Marianne Koritzinsky,Bradley G Wouters,Claire Wilson,Crispin J. Miller,Costas Demonacos,Ian J. Stratford,Caroline Dive +9 more
TL;DR: The contribution of Bid and/or Bax down-regulation to drug responsiveness was demonstrated by the relative resistance of normoxic cells that had no or reduced expression of Bid or Bax and by the finding that forcedexpression of Bid in hypoxic cells resulted in increased sensitivity to the topoisomerase II inhibitor etoposide.