1,437 results found
    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. Cell Biology
    2. Developmental Biology

    The Sec14-like phosphatidylinositol transfer proteins Sec14l3/SEC14L2 act as GTPase proteins to mediate Wnt/Ca2+ signaling

    Bo Gong et al.
    Sec14l3/SEC14L2 respond to upstream Wnt/Frizzled/Dvl stimulation to recruit and activate phospholipase Cδ4a (Plcδ4a) to further initiate calcium release.
    1. Structural Biology and Molecular Biophysics
    2. Human Biology and Medicine

    The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding

    Simon Mysling et al.
    Building on previous work (Mysling et al., 2016), it is shown that angiopoietin-like protein 4 (ANGPTL4) inhibits lipoprotein lipase activity by catalyzing the unfolding of its hydrolase domain.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    Efficient protein targeting to the inner nuclear membrane requires Atlastin-dependent maintenance of ER topology

    Sumit Pawar et al.
    Efficient targeting of membrane proteins from the endoplasmic reticulum (ER) to the inner nuclear membrane depends on GTP hydrolysis by Atlastin GTPases and their function in maintaining an interconnected topology of the ER network.
    1. Cell Biology

    Cooperation of mitochondrial and ER factors in quality control of tail-anchored proteins

    Verena Dederer et al.
    The endoplasmic reticulum E3 ubiquitin ligase Doa10 and the mitochondrial AAA-ATPase Msp1 govern targeting fidelity of outer mitochondrial tail-anchored proteins by controlling cytoplasmic concentration and extracting mistargeted and orphan species.
    1. Biochemistry and Chemical Biology

    Prefabrication of a ribosomal protein subcomplex essential for eukaryotic ribosome formation

    Cohue Peña et al.
    The ATPase Fap7 prefabricates a uS11:eS26 ribosomal protein complex for ribosome assembly.
    1. Structural Biology and Molecular Biophysics
    2. Human Biology and Medicine

    The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain

    Simon Mysling et al.
    Intravascular triglyceride hydrolysis by lipoprotein lipase is crucial for delivering lipid nutrients to vital tissues, such as the heart, skeletal muscle, and adipose tissue.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Structural basis for activation and non-canonical catalysis of the Rap GTPase activating protein domain of plexin

    Yuxiao Wang et al.
    The crystal structures of the intracellular part of the plexin receptor in the active dimer form, and its complex with a key downstream signalling protein Rap, provide insights into how plexin initiates a signalling cascade involved in axon guidance.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    ATPase activity of the DEAD-box protein Dhh1 controls processing body formation

    Christopher Frederick Mugler et al.
    The ATPase Dhh1 controls processing body formation and disassembly in yeast cells, and processing body dynamics can be recapitulated in vitro with recombinant Dhh1, ATP and RNA.
    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.

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