Results 51 to 60 of about 15,549 (206)

BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response.

PLoS Biology, 2010
The unfolded protein response (UPR) is an intracellular signaling pathway that counteracts variable stresses that impair protein folding in the endoplasmic reticulum (ER). As such, the UPR is thought to be a homeostat that finely tunes ER protein folding
David Pincus, Michael W Chevalier, Tomás Aragón, Eelco van Anken, Simon E Vidal, Hana El-Samad, Peter Walter   +6 more
doaj   +1 more source

Targeting IRE1 with small molecules counteracts progression of atherosclerosis [PDF]

Proceedings of the National Academy of Sciences, 2017
Significance Endoplasmic reticulum (ER) stress is linked to the development of complex metabolic diseases, including diabetes, obesity, and atherosclerosis. Irremediable ER stress can push the unfolded protein response (UPR) toward proinflammatory and proapoptotic signaling.
Ozlem Tufanli, Pelin Telkoparan Akillilar, Diego Acosta-Alvear, Begum Kocaturk, Umut Inci Onat, Syed Muhammad Hamid, Ismail Çimen, Peter Walter, Christian Weber, Ebru Erbay   +9 more
openaire   +6 more sources

Enteroviruses Manipulate the Unfolded Protein Response through Multifaceted Deregulation of the Ire1-Xbp1 Pathway

Viruses, 2022
Many viruses are known to trigger endoplasmic reticulum (ER) stress in host cells, which in turn can develop a protective unfolded protein response (UPR). Depending on the conditions, the UPR may lead to either cell survival or programmed cell death. One
Anna Shishova, Ilya Dyugay, Ksenia Fominykh, Victoria Baryshnikova, Alena Dereventsova, Yuriy Turchenko, Anna A. Slavokhotova, Yury Ivin, Sergey E. Dmitriev, Anatoly Gmyl   +9 more
doaj   +1 more source

Specificity in endoplasmic reticulum-stress signaling in yeast entails a step-wise engagement of HAC1 mRNA to clusters of the stress sensor Ire1

eLife, 2014
Insufficient protein-folding capacity in the endoplasmic reticulum (ER) induces the unfolded protein response (UPR). In the ER lumen, accumulation of unfolded proteins activates the transmembrane ER-stress sensor Ire1 and drives its oligomerization.
Eelco van Anken, David Pincus, Scott Coyle, Tomás Aragón, Christof Osman, Federica Lari, Silvia Gómez Puerta, Alexei V Korennykh, Peter Walter   +8 more
doaj   +1 more source

Pharmacological inhibition of the PERK pathway modulates hepatocellular carcinoma growth and immune signaling

FEBS Open Bio, EarlyView.
Pharmacological inhibition of PERK in a DEN‐induced mouse model of liver cancer does not reduce tumor burden but alters cellular stress signaling. Despite blocking PERK activity, downstream stress responses, including CHOP expression, remain active, suggesting compensatory mechanisms within the unfolded protein response that may influence tumor ...
Ada Lerma‐Clavero, Maria Kopsida, Nathalie Arendt, Hans Lennernäs, Markus Sjöblom, Femke Heindryckx   +5 more
wiley   +1 more source

Effects of Ire1 gene on virulence and pathogenicity of Candida albicans

Open Life Sciences
With the extensive utilization of antifungal drugs, the drug resistance of Candida albicans is progressively intensifying, and the effect of empirical treatment for C. albicans infection is not evident.
Zhao Huihai, Qin Lixia, Li Mengyan, Jiang Mengyu, Cui Mengge, Wang Hua, Hou Baohua, Wang Fukun, Jia Keran   +8 more
doaj   +1 more source

Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1

BMC Biology, 2011
Background Ire1 is a signal transduction protein in the endoplasmic reticulum (ER) membrane that serves to adjust the protein-folding capacity of the ER according to the needs of the cell.
Stroud Robert M, Finer-Moore Janet, Korostelev Andrei A, Egea Pascal F, Korennykh Alexei V, Zhang Chao, Shokat Kevan M, Walter Peter   +7 more
doaj   +1 more source

RNA sequencing identifies novel regulated IRE1-dependent decay targets that affect multiple myeloma survival and proliferation

Experimental Hematology & Oncology, 2022
Background IRE1 is an unfolded protein response (UPR) sensor with kinase and endonuclease activity. It plays a central role in the endoplasmic reticulum (ER) stress response through unconventional splicing of XBP1 mRNA and regulated IRE1-dependent decay (
Dalia Quwaider, Luis A. Corchete, Marta Martín-Izquierdo, Jesús M. Hernández-Sánchez, Elizabeta A. Rojas, Ignacio J. Cardona-Benavides, Ramón García-Sanz, Ana B. Herrero, Norma C. Gutiérrez   +8 more
doaj   +1 more source

Malectin Alleviates Endoplasmic Reticulum Stress in Gestational Diabetes Mellitus via Glycoprotein Quality Control Mechanisms

Advanced Science, EarlyView.
Malectin alleviates high glucose‐induced ER stress and damage in placental trophoblasts, a function dependent on its six critical carbohydrate‐binding residues. In a GDM mouse model, administration of TAT‐Malectin ameliorated hyperglycemia and placental ER stress and prevented fetal macrosomia.
Jiahui Zhu, Yumeng Zhang, Ye Wang, Xiaoyu Zhu, Ailin Yuan, Weijing Yin, Huangmin Yu, Xuemin Pang, Yufeng He, Yuchen Wang, Tong Wang, Yong Li, Yunlong Si   +12 more
wiley   +1 more source

Dual RNase activity of IRE1 as a target for anticancer therapies

Journal of Cell Communication and Signaling, 2023
AbstractThe unfolded protein response (UPR) is a cellular mechanism that protects cells during stress conditions in which there is an accumulation of misfolded proteins in the endoplasmic reticulum (ER). UPR activates three signaling pathways that function to alleviate stress conditions and promote cellular homeostasis and cell survival.
Sylwia Bartoszewska, Jakub Sławski, James F. Collawn, Rafał Bartoszewski   +3 more
openaire   +2 more sources