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    1. Cell Biology
    2. Neuroscience

    Ubiquitin-interacting motifs of ataxin-3 regulate its polyglutamine toxicity through Hsc70-4-dependent aggregation

    Sean L Johnson et al.
    Pathogenesis in Spinocerebellar Ataxia Type 3 is enhanced by the heat-shock protein family member, Hsc70-4, uncovering new mechanisms of toxicity for this disease and suggesting pleiotropic roles for chaperones.
    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. Cancer Biology
    2. Cell Biology

    Methylglyoxal, a glycolysis side-product, induces Hsp90 glycation and YAP-mediated tumor growth and metastasis

    Marie-Julie Nokin et al.
    Carbonyl stress mediated by Methylglyoxal affects Hsp90 activity, inhibits the Hippo pathway and promotes tumor growth and metastasis in breast cancer.
    1. Physics of Living Systems
    2. Structural Biology and Molecular Biophysics

    Efficient conversion of chemical energy into mechanical work by Hsp70 chaperones

    Salvatore Assenza et al.
    A multiscale modeling approach reveals how the energy from ATP hydrolysis is used by Hsp70 chaperones to remodel the conformation of their substrates through a novel force-generating mechanism.
    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. Biochemistry and Chemical Biology

    Controlling protein function by fine-tuning conformational flexibility

    Sonja Schmid, Thorsten Hugel
    Specific and non-specific conformational confinement, via point mutation or cochaperone interaction or macro-molecular crowding, stimulates protein function in Hsp90 by reducing non-productive conformational flexibility.
    1. Computational and Systems Biology
    2. Genetics and Genomics

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

    Zoltán Farkas et al.
    Protein biosynthesis and protein quality control jointly determine protein production costs.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation

    Marta Carroni et al.
    Overcoming image-processing problems in the analysis of the ClpB chaperone provides a new structural model and regulatory mechanism, based on clear density for the coiled-coil domain and supported by various biochemical data.
    1. Biochemistry and Chemical Biology
    2. Physics of Living Systems

    Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption

    Paolo De Los Rios, Alessandro Barducci
    ATP consumption enables chaperones to exploit the different kinetic properties of their conformational states to exhibit a non-equilibrium affinity for their substrates that is orders of magnitude higher than its equilibrium value.
    1. Cell Biology

    Glucose intake hampers PKA-regulated HSP90 chaperone activity

    Yu-Chen Chen et al.
    Food overconsumption impairs cellular protein folding through a novel aging-related signaling pathway.