5,454 results found
    1. Computational and Systems Biology

    Quantitative time-resolved analysis reveals intricate, differential regulation of standard- and immuno-proteasomes

    Juliane Liepe, Hermann-Georg Holzhütter ... Michele Mishto
    Experimental and computational analyses reveal how proteasomal hydrolysis is regulated and show that peptide transport is the rate-limiting step and the main differentiating factor between human standard- and immuno-proteasomes.
    1. Cell Biology
    2. Developmental Biology

    Proteasome dysfunction triggers activation of SKN-1A/Nrf1 by the aspartic protease DDI-1

    Nicolas J Lehrbach, Gary Ruvkun
    Post-translational processing of the SKN-1A/Nrf1 transcription factor regulates proteasome expression.
    1. Biochemistry and Chemical Biology

    A cryptic K48 ubiquitin chain binding site on UCH37 is required for its role in proteasomal degradation

    Jiale Du, Sandor Babik ... Eric Strieter
    The proteasomal deubiquitinase UCHL5/UCH37 uses a face distinct from the canonical ubiquitin binding site to engage K48-linked ubiquitin chains and catalyze chain debranching.
    1. Biochemistry and Chemical Biology

    The aspartyl protease DDI2 activates Nrf1 to compensate for proteasome dysfunction

    Shun Koizumi, Taro Irie ... Shigeo Murata
    Peptidase activity of DDI2 is required to activate Nrf1 in order to enable proteasome recovery in response to proteasome inhibition.
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    1. Structural Biology and Molecular Biophysics

    Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition

    Corey M Dambacher, Evan J Worden ... Gabriel C Lander
    Within the isolated lid sub-complex of the proteasome, a finely tuned network of interactions maintains the deubiquitinase in an inhibited conformation; dramatic rearrangements of the lid subunits upon incorporation into the holoenzyme lead to the deubiquitinase’s activation.
    1. Cell Biology

    p97-dependent retrotranslocation and proteolytic processing govern formation of active Nrf1 upon proteasome inhibition

    Senthil K Radhakrishnan, Willem den Besten, Raymond J Deshaies
    The enzyme p97/VCP regulates the activity of the transcription factor Nrf1 to promote increased transcription of genes that encode proteasome subunits following inhibition of the proteasome.
    1. Physics of Living Systems
    2. Structural Biology and Molecular Biophysics

    An empirical energy landscape reveals mechanism of proteasome in polypeptide translocation

    Rui Fang, Jason Hon ... Ying Lu
    Empirical energy landscape allows simulating the structural dynamics of the proteasomal ATPase complex, which yields predictions that are widely consistent with experimental observations and reveals the functional mechanism of the proteasome in substrate degradation.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Branched ubiquitin chain binding and deubiquitination by UCH37 facilitate proteasome clearance of stress-induced inclusions

    Aixin Song, Zachary Hazlett ... Tingting Yao
    Through interactions with both ubiquitin units that emanate from a branch point in polyubiquitin, UCH37 recognizes and hydrolyzes branched chains to promote proteasome-mediated degradation upon proteolytic stresses.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    RETRACTED: Proteasome storage granules protect proteasomes from autophagic degradation upon carbon starvation

    Richard S Marshall, Richard D Vierstra
    Proteasomes are protected from autophagic elimination upon carbon starvation by sequestration into cytoplasmic storage granules, which aid cell fitness by providing a cache of proteasomes that can be rapidly remobilized when carbon availability improves.
    1. Cell Biology

    Compromising the 19S proteasome complex protects cells from reduced flux through the proteasome

    Peter Tsvetkov, Marc L Mendillo ... Susan Lindquist
    Reducing the expression of 19S subunits shifts the ratio of 20S/26S proteasome complexes and provides a powerful survival advantage in the face of lethal proteasome inhibition.

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