Results 1 to 10 of about 15,652 (205)

Pharmacological Targeting of IRE1 in Cancer [PDF]

Trends in Cancer, 2020
IRE1α (inositol requiring enzyme 1 alpha) is one of the main transducers of the unfolded protein response (UPR). IRE1α plays instrumental protumoral roles in several cancers, and high IRE1α activity has been associated with poorer prognoses. In this context, IRE1α has been identified as a potentially relevant therapeutic target.
Leif A Eriksson, Eric Chevet, Xavier Guillory   +2 more
exaly   +5 more sources

Structural and functional basis for RNA cleavage by Ire1 [PDF]

BMC Biology, 2011
Background The unfolded protein response (UPR) controls the protein folding capacity of the endoplasmic reticulum (ER). Central to this signaling pathway is the ER-resident bifunctional transmembrane kinase/endoribonuclease Ire1.
Stroud Robert M, Finer-Moore Janet, Egea Pascal F, Korostelev Andrei A, Korennykh Alexei V, Zhang Chao, Shokat Kevan M, Walter Peter   +7 more
doaj   +7 more sources

Chemically-induced degradation of the endoplasmic-reticulum stress sensor IRE1 by a VHL-recruiting chimera [PDF]

Nature Communications
The endoplasmic-reticulum (ER) transmembrane protein IRE1 mitigates ER stress through kinase-endoribonuclease and scaffolding activities. Cancer cells often co-opt IRE1 to facilitate growth.
Jin Du, Elisia Villemure, Matthew Johnson, Caleigh Azumaya, Catarina J. Gaspar, Scot Marsters, David Lawrence, Scott Foster, Alexis Rohou, Tommy K. Cheung, Christopher M. Rose, Thomas Garner, Soo Ro, Kevin Clark, Maureen H. Beresini, Marie-Gabrielle Braun, Joachim Rudolph, Peter Hsu, Avi Ashkenazi   +18 more
doaj   +2 more sources

Cytomegalovirus downregulates IRE1 to repress the unfolded protein response. [PDF]

PLoS Pathogens, 2013
During viral infection, a massive demand for viral glycoproteins can overwhelm the capacity of the protein folding and quality control machinery, leading to an accumulation of unfolded proteins in the endoplasmic reticulum (ER). To restore ER homeostasis,
Sebastian Stahl, Julia M Burkhart, Florian Hinte, Boaz Tirosh, Hermine Mohr, René P Zahedi, Albert Sickmann, Zsolt Ruzsics, Matthias Budt, Wolfram Brune   +9 more
doaj   +5 more sources

Signal sequence-triage is activated by translocon obstruction sensed by an ER stress sensor IRE1α

Cell Structure and Function, 2023
Secretory pathway proteins are cotranslationally translocated into the endoplasmic reticulum (ER) of metazoan cells through the protein channel, translocon.
Ashuei Sogawa, Ryota Komori, Kota Yanagitani, Miku Ohfurudono, Akio Tsuru, Koji Kadoi, Yukio Kimata, Hiderou Yoshida, Kenji Kohno   +8 more
doaj   +1 more source

Mechanism of Hsp70 specialized interactions in protein translocation and the unfolded protein response [PDF]

Open Biology, 2020
Hsp70 chaperones interact with substrate proteins in a coordinated fashion that is regulated by nucleotides and enhanced by assisting cochaperones.
Natacha Larburu, Christopher J. Adams, Chao-Sheng Chen, Piotr R. Nowak, Maruf M. U. Ali   +4 more
doaj   +1 more source

Icariin inhibits the expression of IL-1β, IL-6 and TNF-α induced by OGD/R through the IRE1/XBP1s pathway in microglia

Pharmaceutical Biology, 2021
Context Icariin (ICA), a flavonol glycoside extracted from Epimedium brevicornum Maxim (Berberidaceae), has been proven to inhibit inflammatory response in ischaemic rats in our laboratory's previous work.
Zhen-Tao Mo, Jie Zheng, Yu-ling Liao
doaj   +1 more source

Classical swine fever virus employs the PERK- and IRE1-dependent autophagy for viral replication in cultured cells.

Virulence, 2021
Endoplasmic reticulum stress (ERS)-mediated autophagy is indispensable for modulation of replication and pathogenesis of numerous mammalian viruses. We have previously shown that classical swine fever virus (CSFV) infection induces ERS-mediated autophagy
Erpeng Zhu, Huawei Wu, Wenxian Chen, Yuwei Qin, Jiameng Liu, Shuangqi Fan, Shengming Ma, Keke Wu, Qian Mao, Chaowei Luo, Yixian Qin, Lin Yi, Hongxing Ding, Mingqiu Zhao, Jinding Chen   +14 more
doaj   +1 more source

Quaternary structure analysis of IRE1

microPublication biology, 2023
IRE1 belongs to a type I transmembrane protein family harboring two functional domains, cytoplasmic domain with kinase and RNAse catalytic activity, and the luminal domain, which is involved in the sensing of unfolded proteins. IRE1 molecule undergoes dimerization in the lumenal domain, which functionally activates the catalytic C-terminal domain. IRE1
Bashir, Samirul, Pal, Debnath, Qadri, Ozaira, Banday, Mariam, Fazili, Khalid   +4 more
openaire   +2 more sources

Fat body Ire1 regulates lipid homeostasis through the Xbp1s-FoxO axis in Drosophila

iScience, 2021
Summary: The endoplasmic reticulum (ER)-resident transmembrane protein kinase/RNase Ire1 is a conserved sensor of the cellular unfolded protein response and has been implicated in lipid homeostasis, including lipid synthesis and transport, across species.
Peng Zhao, Ping Huang, Tongfu Xu, Xiaoxiang Xiang, Ying Sun, Jingqi Liu, Cheng Yan, Lei Wang, Jiamei Gao, Shang Cui, Xiangdong Wang, Lixing Zhan, Haiyun Song, Jingnan Liu, Wei Song, Yong Liu   +15 more
doaj   +1 more source