1,574 results found
    1. Structural Biology and Molecular Biophysics

    Regulation of RUVBL1-RUVBL2 AAA-ATPases by the nonsense-mediated mRNA decay factor DHX34, as evidenced by Cryo-EM

    Andres López-Perrote et al.
    Cryo-EM reveals the regulation of RUVBL1 and RUVBL2 AAA-ATPases by DHX34, a helicase involved in nonsense-mediated mRNA decay (NMD), and suggests mechanisms for how RUVBL1 and RUVBL2 function in NMD.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Interactions between a subset of substrate side chains and AAA+ motor pore loops determine grip during protein unfolding

    Tristan A Bell et al.
    The AAA+ protein unfolding motor ClpX grips substrates with the uppermost part of its substrate-binding pore, and requires interactions with hydrophobic amino acid side chains to operate with optimal efficiency.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Structure of a AAA+ unfoldase in the process of unfolding substrate

    Zev A Ripstein et al.
    The structure of a substrate-engaged AAA+ unfoldase suggests a model for processive unfolding that is supported by biochemical data.
    1. Biochemistry and Chemical Biology

    Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control

    Marta Carroni et al.
    Head-to-head interactions of regulatory coiled-coil domains control activity of the central bacterial AAA+ protein ClpC by promoting formation of a reversible resting state.
    1. Cell Biology

    The AAA protein Msp1 mediates clearance of excess tail-anchored proteins from the peroxisomal membrane

    Nicholas R Weir et al.
    Msp1, a membrane-integral AAA ATPase at mitochondria and peroxisomes, selectively recognizes uncomplexed substrate molecules in vivo while avoiding substrates stabilized by binding partners.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Structure of Vps4 with circular peptides and implications for translocation of two polypeptide chains by AAA+ ATPases

    Han Han et al.
    Structural and biochemical studies indicate that AAA+ ATPase employ a general mechanism to translocate a variety of substrates, including extended polypeptides, hairpins, crosslinked chains, and chains conjugated to other molecules.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching

    Qiaozhen Ye et al.
    TRIP13 inactivates the spindle assembly checkpoint by converting MAD2 from its active ‘closed’ state to its inactive ‘open’ state.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Structural basis of protein translocation by the Vps4-Vta1 AAA ATPase

    Nicole Monroe et al.
    A cryo-electron microscopy structure of a substrate-bound Vps4-Vta1 AAA ATPase reveals an asymmetric hexameric ring and suggests how nucleotide-induced changes in subunit interfaces translocate polypeptides into the central pore.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets

    Han Han et al.
    A 3.2 Å resolution structure of Vps4 provides a detailed model for protein substrate binding and translocation by AAA ATPases.
    1. Plant Biology

    A chloroplast retrograde signal, 3’-phosphoadenosine 5’-phosphate, acts as a secondary messenger in abscisic acid signaling in stomatal closure and germination

    Wannarat Pornsiriwong et al.
    Molecular signals from chloroplasts can synergistically interact with the plant hormone, abscisic acid (ABA), to regulate non-canonical signaling pathways mediating fundamental cellular processes including stomatal closure, seed dormancy and germination.

Refine your results by:

Type
Research categories