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3,764 results found
    1. Biochemistry and Chemical Biology
    2. Chromosomes and Gene Expression

    ICE1 promotes the link between splicing and nonsense-mediated mRNA decay

    Thomas D Baird et al.
    A whole-genome siRNA screen identifies ICE1 as a factor required for accurate sensing and quality control of mRNAs containing premature stop codons.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    An unfolded protein-induced conformational switch activates mammalian IRE1

    G Elif Karagöz et al.
    ER-stress sensing mechanism of the unfolded protein response sensor/transducer IRE1 is conserved from yeast to mammals, where in mammals, unfolded protein binding to IRE1's ER lumenal domain is coupled to its oligomerization and activation through an allosteric conformational change.
    1. Cell Biology

    Unstructured regions in IRE1α specify BiP-mediated destabilisation of the luminal domain dimer and repression of the UPR

    Niko Amin-Wetzel et al.
    Client protein-driven reversal of endoplasmic reticulum chaperone (BiP) mediated-repression is revealed as a principal component of the regulation of the unfolded protein response transducer IRE1 in cells.
    1. Cell Biology

    Regulated Ire1-dependent mRNA decay requires no-go mRNA degradation to maintain endoplasmic reticulum homeostasis in S. pombe

    Nicholas R Guydosh et al.
    A critical component of the cellular response to unfolded proteins is the widespread rescue of ribosomes that stall on endonucleolytically-cleaved mRNA transcripts.
    1. Cell Biology

    The unfolded protein response and endoplasmic reticulum protein targeting machineries converge on the stress sensor IRE1

    Diego Acosta-Alvear et al.
    The coordination of protein targeting to the endoplasmic reticulum and the unfolded protein response through the stress sensor IRE1 ensures quality control of the secreted and transmembrane proteomes.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    In vitro FRET analysis of IRE1 and BiP association and dissociation upon endoplasmic reticulum stress

    Megan C Kopp et al.
    Quantitative FRET UPR induction assay is used to measure IRE1 and BIP association and dissociation by a variety of ER misfolded proteins and by an important BiP substrate-binding domain mutant, significantly enhancing the evidence for the allosteric UPR induction model.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Noncanonical binding of BiP ATPase domain to Ire1 and Perk is dissociated by unfolded protein CH1 to initiate ER stress signaling

    Marta Carrara et al.
    The chaperone protein BiP forms complexes with Ire1 and Perk that dissociate when unfolded proteins bind to BiP to activate the unfolded protein response in the ER.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

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

    Eelco van Anken et al.
    Selective docking of HAC1 mRNA on Ire1 clusters at a site separate from the Ire1 RNase domain is key for endoplasmic reticulum stress signaling.
    1. Biochemistry and Chemical Biology

    Protomer alignment modulates specificity of RNA substrate recognition by Ire1

    Weihan Li et al.
    Biochemical analysis and computational modeling reveal how cells mechanistically control the quality of their proteomes and demonstrate that the precise alignment of subunits in oligomeric complexes can profoundly affect enzymatic properties.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Endoplasmic reticulum stress-independent activation of unfolded protein response kinases by a small molecule ATP-mimic

    Aaron S Mendez et al.
    A rationally designed small molecule ATP-mimetic activates IRE1 and PERK signaling in cells by inducing conformational changes that template the assembly of higher-order enzymatically active structures.

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