Results 131 to 140 of about 67,514 (293)

Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. [PDF]

open access: yesPLoS Biology, 2006
The protein folding capacity of the endoplasmic reticulum (ER) is regulated by the unfolded protein response (UPR). The UPR senses unfolded proteins in the ER lumen and transmits that information to the cell nucleus, where it drives a transcriptional ...
Sebastián Bernales   +2 more
doaj   +1 more source

Inhibition of IRE1α-mediated XBP1 mRNA cleavage by XBP1 reveals a novel regulatory process during the unfolded protein response [PDF]

open access: yes, 2017
Background: The mammalian endoplasmic reticulum (ER) continuously adapts to the cellular secretory load by the activation of an unfolded protein response (UPR).
Bulleid, Neil J.   +4 more
core   +2 more sources

A New Role for Estrogen Receptor α in Cell Proliferation and Cancer: Activating the Anticipatory Unfolded Protein Response

open access: yesFrontiers in Endocrinology, 2018
Cells react to a variety of stresses, including accumulation of unfolded or misfolded protein, by activating the endoplasmic reticulum (EnR) stress sensor, the unfolded protein response (UPR).
Mara Livezey   +3 more
doaj   +1 more source

Unveiling the complexity of cellular senescence in cancers: From mechanism to therapeutic opportunities

open access: yesBMEMat, EarlyView.
This review highlights the complex roles of cellular senescence in cancer progression and suppression, discusses the mechanisms and regulatory pathways involved, and evaluates the efficacy of the “One‐Two punch” sequential treatment approach while addressing emerging challenges in this novel therapeutic strategy.
Qiuming Pan   +12 more
wiley   +1 more source

Methods for Monitoring Endoplasmic Reticulum Stress and the Unfolded Protein Response

open access: yesInternational Journal of Cell Biology, 2010
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 ...
Afshin Samali   +3 more
doaj   +1 more source

Yeast Bax Inhibitor, Bxi1p, Is an ER-Localized Protein that Links the Unfolded Protein Response and Programmed Cell Death in \u3cem\u3eSaccharomyces cerevisiae\u3c/em\u3e [PDF]

open access: yes, 2011
Bax inhibitor-1 (BI-1) is an anti-apoptotic gene whose expression is upregulated in a wide range of human cancers. Studies in both mammalian and plant cells suggest that the BI-1 protein resides in the endoplasmic reticulum and is involved in the ...
Austriaco, Nicanor   +4 more
core   +1 more source

Uterine Endoplasmic Reticulum Stress and Its Unfolded Protein Response May Regulate Caspase 3 Activation in the Pregnant Mouse Uterus [PDF]

open access: yes, 2013
We have previously proposed that uterine caspase-3 may modulate uterine contractility in a gestationally regulated fashion. The objective of this study was to determine the mechanism by which uterine caspase-3 is activated and consequently controlled in ...
Condon, Jennifer C.   +5 more
core   +3 more sources

Bee‐Derived Antioxidants as a Protective Strategy Against Doxorubicin‐Induced Ovarian Damage

open access: yesChemistry &Biodiversity, EarlyView.
Graphical abstract of Bee‐Derived Antioxidants as a Protective Strategy Against Doxorubicin‐Induced Ovarian Damage ABSTRACT Antineoplastic agents can induce tissue damage through oxidative stress mechanisms. Doxorubicin, a widely used chemotherapeutic agent, has been shown to cause permanent damage to reproductive tissues.
Meltem Arıkan Malkoc   +3 more
wiley   +1 more source

Unfolding the role of stress response signaling in endocrine resistant breast cancers

open access: yesFrontiers in Oncology, 2015
The unfolded protein response (UPR) is an ancient stress response that enables a cell to manage the energetic stress that accompanies protein folding.
Robert eClarke, Katherine L Cook
doaj   +1 more source

tRNA ligase structure reveals kinetic competition between non-conventional mRNA splicing and mRNA decay. [PDF]

open access: yes, 2019
Yeast tRNA ligase (Trl1) is an essential trifunctional enzyme that catalyzes exon-exon ligation during tRNA biogenesis and the non-conventional splicing of HAC1 mRNA during the unfolded protein response (UPR).
Peschek, Jirka, Walter, Peter
core  

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