Results 31 to 40 of about 15,094 (184)

IRE1α Promotes Zika Virus Infection via XBP1

open access: yesViruses, 2020
Zika virus (ZIKV) is an emergent member of the Flaviviridae family which causes severe congenital defects and other major sequelae, but the cellular processes that support ZIKV replication are incompletely understood.
Elena P. Kolpikova   +5 more
doaj   +1 more source

OVEREXPRESSION OF DOMINANT-NEGATIVE IRE1 ENZYME IN H1299-shE6AP CELLS INCREASES HEAT SHOCK ELEMENT-DEPENDENT TRANSCRIPTION [PDF]

open access: yesBiotechnologia Acta, 2015
To investigate IRE1-dependent branch of endoplasmic reticulum stress pathway in various cancer cells we created cDNA-constructs for expression of dominant-negative inositol-requiring enzyme – 1 IRE1 and cytosolic domain of IRE1 fused on a C-terminus with
D. O. , О. H.
doaj   +1 more source

sMEK1 promotes crosstalk between IRE1 and Akt signalling pathways: Evidence for a novel IRE1/sMEK1/Akt complex [PDF]

open access: yes, 2021
AbstractThe Unfolded Protein Response (UPR) is a dynamic cellular pathway that helps maintain proteostasis during endoplasmic reticulum (ER) stress. One of the key UPR sensors is IRE1, which plays a central role in managing ER stress and interacts with other cellular pathways to regulate cell homeostasis.
Ozaira Qadri   +4 more
openaire   +1 more source

Engineering ER-stress dependent non-conventional mRNA splicing

open access: yeseLife, 2018
The endoplasmic reticulum (ER) protein folding capacity is balanced with the protein folding burden to prevent accumulation of un- or misfolded proteins.
Weihan Li   +6 more
doaj   +1 more source

IRE1: ER stress sensor and cell fate executor [PDF]

open access: yesTrends in Cell Biology, 2013
Cells operate a signaling network termed the unfolded protein response (UPR) to monitor protein-folding capacity in the endoplasmic reticulum (ER). Inositol-requiring enzyme 1 (IRE1) is an ER transmembrane sensor that activates the UPR to maintain the ER and cellular function.
Yani, Chen, Federica, Brandizzi
openaire   +2 more sources

In vitro RNA Cleavage Assays to Characterize IRE1-dependent RNA Decay

open access: yesBio-Protocol, 2019
The kinase/RNase IRE1 is a key effector of the cellular response to endoplasmic reticulum stress. The RNase activity of IRE1 can be measured in cells or in the test tube.
G. Karagöz   +3 more
doaj   +1 more source

CCDC170 affects breast cancer apoptosis through IRE1 pathway

open access: yesAging, 2020
Genome-wide association studies have revealed that multiple single-nucleotide polymorphisms in the intergenic region between estrogen receptor 1 and coiled-coil domain containing 170 (CCDC170) are associated with breast cancer risk. We performed microarray and bioinformatics analyses to identify genes that were induced upon CCDC170 overexpression, and ...
Wang, Qiong   +8 more
openaire   +2 more sources

Inhibition of IRE1 results in decreased scar formation [PDF]

open access: yesWound Repair and Regeneration, 2017
AbstractWound healing is characterized by the production of large amounts of protein necessary to replace lost cellular mass and extracellular matrix. The unfolded protein response (UPR) is an important adaptive cellular response to increased protein synthesis.
Tatiana V. Boyko   +8 more
openaire   +2 more sources

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

open access: yesPLoS 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   +6 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

open access: yeseLife, 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   +8 more
doaj   +1 more source

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