341 results found
    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 et al.
    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. Biochemistry and Chemical Biology
    2. Cell Biology

    An unexpected role for the yeast nucleotide exchange factor Sil1 as a reductant acting on the molecular chaperone BiP

    Kevin D Siegenthaler et al.
    Building on previous work (Wang et al., 2014), it is shown that the nucleotide exchange factor of the chaperone BiP (Sil1) unexpectedly facilitates the reduction of oxidized BiP.
    1. Structural Biology and Molecular Biophysics

    Molecular Chaperones: Confirmation for conformational selection

    Yajun Jiang, Charalampos G Kalodimos
    NMR studies settle part of a long-standing debate about the mechanism used by the Hsp70 chaperone to recognize substrates.
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    1. Cell Biology

    CHIP as a membrane-shuttling proteostasis sensor

    Yannick Kopp et al.
    The mechanism is revealed that connects the protein degradation machinery to cellular membrane-bound compartments during proteostasis stress in mammalian cells.
    1. Cell Biology

    Unfolded protein response transducer IRE1-mediated signaling independent of XBP1 mRNA splicing is not required for growth and development of medaka fish

    Tokiro Ishikawa et al.
    The unfolded protein response sensor/transducer IRE1-mediated splicing of XBP1 mRNA encoding its active downstream transcription factor to maintain the homeostasis of the endoplasmic reticulum is sufficient for growth and development of medaka fish.
    1. Structural Biology and Molecular Biophysics

    Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles

    Rina Rosenzweig et al.
    Multiple chaperone binding sites on substrates suggest a mechanism by which the Hsp70 chaperone can circumvent kinetic traps in protein folding.
    1. Structural Biology and Molecular Biophysics

    Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions

    Ashok Sekhar et al.
    NMR-based flux measurements show that both bacterial and human Hsp70 chaperones interact with helical, as well as sheet substrates predominantly through a conformational selection mechanism.
    1. Structural Biology and Molecular Biophysics
    2. Computational and Systems Biology

    Modeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysis

    Duccio Malinverni et al.
    Integration of complementary computational approaches reveals an evolutionarily conserved interaction interface between molecular chaperones Hsp70 and Hsp40, rationalizing previous observations.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    AMPylation matches BiP activity to client protein load in the endoplasmic reticulum

    Steffen Preissler et al.
    Attaching a molecule of adenosine mono-phosphate (AMP) to the BiP protein at threonine 518 regulates its chaperone activity in the endoplasmic reticulum.
    1. Structural Biology and Molecular Biophysics
    2. Cell Biology

    Small molecule-mediated refolding and activation of myosin motor function

    Michael B Radke et al.
    The small molecule EMD 57033 is one of a new class of pharmacological chaperones that stabilize, enhance the activity of, and correct stress-induced misfolding of myosin proteins.

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