746 results found
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Misfolded proteins bind and activate death receptor 5 to trigger apoptosis during unresolved endoplasmic reticulum stress

    Mable Lam, Scot A Marsters ... Peter Walter
    Death receptor 5 can directly sense misfolded proteins downstream of the endoplasmic reticulum to provide a quality control mechanism that executes apoptosis and prevents further production of misfolded proteins.
    1. Cell Biology

    The proteasome biogenesis regulator Rpn4 cooperates with the unfolded protein response to promote ER stress resistance

    Rolf M Schmidt, Julia P Schessner ... Sebastian Schuck
    Endoplasmic reticulum stress in yeast activates not only the UPR but also Rpn4, promoting the clearance of misfolded proteins from the cytosol as part of a modular cross-compartment stress response.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    An unfolded protein-induced conformational switch activates mammalian IRE1

    G Elif Karagöz, Diego Acosta-Alvear ... Peter Walter
    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. Biochemistry and Chemical Biology

    Translation attenuation by minocycline enhances longevity and proteostasis in old post-stress-responsive organisms

    Gregory M Solis, Rozina Kardakaris ... Michael Petrascheck
    Directly targeting the ribosome to attenuate translation partly mimics the integrated stress response, increasing lifespan and preserving protein folding capacity even in older individuals with dysfunctional stress response signaling.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Redox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stress

    Jie Wang, Kristeen A Pareja ... Carolyn S Sevier
    Direct modification by endogenous peroxide of a conserved cysteine in the molecular chaperone BiP decouples its ATPase and peptide-binding activities, allowing for enhanced polypeptide holdase activity during oxidative stress.
    1. Cell Biology
    2. Genetics and Genomics

    Targeting DNA topoisomerases or checkpoint kinases results in an overload of chaperone systems, triggering aggregation of a metastable subproteome

    Wouter Huiting, Suzanne L Dekker ... Steven Bergink
    Various genotoxic stresses trigger widespread aggregation of abundant, liquid-liquid phase separation-prone proteins, suggesting that genotoxic stress is a potential driver of disease-associated protein aggregation.
    1. Developmental Biology
    2. Plant Biology

    Mechanical stress contributes to the expression of the STM homeobox gene in Arabidopsis shoot meristems

    Benoît Landrein, Annamaria Kiss ... Olivier Hamant
    Mechanical stress promotes the expression of the homeobox gene and meristem master regulator STM, synergistically and independently from auxin depletion.
    1. Computational and Systems Biology
    2. Genetics and Genomics

    Hsp70-associated chaperones have a critical role in buffering protein production costs

    Zoltán Farkas, Dorottya Kalapis ... Csaba Pál
    Protein biosynthesis and protein quality control jointly determine protein production costs.
    1. Cell Biology
    2. Evolutionary Biology

    tRNA genes rapidly change in evolution to meet novel translational demands

    Avihu H Yona, Zohar Bloom-Ackermann ... Yitzhak Pilpel
    Experimental evolution and systematic sequence analysis of transfer RNA genes reveal that anticodon mutations provide adaptive plasticity to the translation machinery.
    1. Microbiology and Infectious Disease

    Lipoprotein DolP supports proper folding of BamA in the bacterial outer membrane promoting fitness upon envelope stress

    David Ranava, Yiying Yang ... Raffaele Ieva
    The envelope stress factor DolP associates with the outer membrane protein assembly machinery and supports proper folding and functioning of BamA contributing to preserve envelope integrity.

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