Results 21 to 30 of about 15,094 (184)
IRE1 signaling exacerbates Alzheimer’s disease pathogenesis
Acta Neuropathologica, 2017 Altered proteostasis is a salient feature of Alzheimer's disease (AD), highlighting the occurrence of endoplasmic reticulum (ER) stress and abnormal protein aggregation. ER stress triggers the activation of the unfolded protein response (UPR), a signaling pathway that enforces adaptive programs to sustain proteostasis or eliminate terminally damaged ...
Durán Aniotz, Claudia +14 more
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IRE1‐mediated miRNA maturation in macrophage phosphoinositide signaling [PDF]
EMBO reports, 2020 Endoplasmic reticulum (ER) stress signaling has long been associated with various pathological states in particular with the development of diseases with an underlying inflammation, such as diabetes, liver or cardiovascular dysfunctions, and cancer. ER stress signaling is mediated by three stress sensors.
Tony Avril, Eric Chevet
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The UPR Transducer IRE1 Promotes Breast Cancer Malignancy by Degrading Tumor Suppressor microRNAs
iScience, 2020 Summary: Dysregulation of inositol-requiring enzyme 1 (IRE1), the primary transducer of Unfolded Protein Response (UPR), has been observed in tumor initiation and progression, but the underlying mechanism remains to be further elucidated.
Kezhong Zhang +7 more
doaj +1 more source
Ire1 Has Distinct Catalytic Mechanisms for XBP1/HAC1 Splicing and RIDD
Cell Reports, 2014 An evolutionarily conserved unfolded protein response (UPR) component, IRE1, cleaves XBP1/HAC1 introns in order to generate spliced mRNAs that are translated into potent transcription factors.
Arvin B. Tam +2 more
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The Journal of Cell Biology, 2007 When demands on the protein folding machinery get too great, how does the cell know? Using a series of yeast mutants, [Kimata et al.][1] now suggest that oligomerization allows an ER stress sensor protein to recognize unfolded protein and signal distress.
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Structure-Based Drug Discovery of IRE1 Modulators
, 2022 IRE1α (inositol-requiring enzyme 1 alpha, referred to IRE1 hereafter) is an Endoplasmic Reticulum (ER) resident transmembrane enzyme with cytosolic kinase/RNAse activities. Upon ER stress IRE1 is activated through trans-autophosphorylation and oligomerization, resulting in a conformational change of the RNase domain, thereby promoting two signaling ...
Pelizzari Raymundo, Diana +3 more
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Decoding non-canonical mRNA decay by the endoplasmic-reticulum stress sensor IRE1α
Nature Communications, 2021 IRE1 helps mitigate endoplasmic-reticulum stress by cleaving specific mRNAs at a conserved sequence endomotif via regulated IRE1-dependent decay (RIDD). Here the authors discover a more promiscuous IRE1 activity dubbed RIDD lacking endomotif (RIDDLE).
Adrien Le Thomas +16 more
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Inhibition of IRE1 modifies effect of glucose deprivation on the expression of TNFα-related genes in U87 glioma cells [PDF]
The Ukrainian Biochemical Journal, 2015 Inhibition of IRE1 (inositol requiring enzyme-1), the major signaling pathway of endoplasmic reticulum stress, significantly decreases glioma cell proliferation and tumor growth.
I. V. Kryvdiuk +5 more
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Structural and functional basis for RNA cleavage by Ire1
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 +7 more
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Differential Ire1 determines loser cell fate in tumor-suppressive cell competition
Cell Reports, 2023 Summary: Tumor-suppressive cell competition (TSCC) is a conserved surveillance mechanism in which neighboring cells actively eliminate oncogenic cells.
Jiadong Zheng +5 more
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