Browse the search results

Page 2 of 74
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    The neuronal calcium sensor NCS-1 regulates the phosphorylation state and activity of the Gα chaperone and GEF Ric-8A

    Daniel Muñoz-Reyes, Levi J McClelland ... Maria Jose Sanchez-Barrena
    Biochemical, biophysical, and structural approach to determine the molecular basis of the calcium-sensitive regulation of the Gα chaperone and guanine exchange factor Ric-8A by the neuronal calcium sensor NCS-1.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Calcium dependence of both lobes of calmodulin is involved in binding to a cytoplasmic domain of SK channels

    David B Halling, Ashley E Philpo, Richard W Aldrich
    Calcium drives interactions for both calcium-binding domains of calmodulin in complex with KCa2.1 peptides and both domains are required for normal channel function.
    1. Biochemistry and Chemical Biology
    2. Evolutionary Biology

    How did UGA codon translation as tryptophan evolve in certain ciliates? A critique of Kachale et al. 2023 Nature

    Estienne Carl Swart, Christiane Emmerich ... Aditi Singh
    Not revised
    Reviewed Preprint v1
    • Valuable
    • Solid
    1. Biochemistry and Chemical Biology
    2. Neuroscience

    Somatostatin binds to the human amyloid β peptide and favors the formation of distinct oligomers

    Hansen Wang, Lisa D Muiznieks ... Gerold Schmitt-Ulms
    The cyclic neuropeptide somatostatin binds to human Aβ1-42 through an interface that critically relies on a specific tryptophan, thereby blocking the propensity of Aβ to aggregate, a critical step in the pathobiology of Alzheimer's disease.
    1. Structural Biology and Molecular Biophysics

    Structural basis for mammalian nucleotide sugar transport

    Shivani Ahuja, Matthew R Whorton
    Crystal structures of the mouse CMP-sialic acid transporter in complex with both CMP and CMP-sialic acid reveal the mechanisms of substrate selectivity and transport.
    1. Immunology and Inflammation
    2. Medicine

    Oral supplementation of gut microbial metabolite indole-3-acetate alleviates diet-induced steatosis and inflammation in mice

    Yufang Ding, Karin Yanagi ... Arul Jayaraman
    A microbiome metabolite alleviates liver steatosis and inflammation, and shows its potential as a therapeutic modality for non-alcoholic fatty liver disease.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Rate-limiting transport of positively charged arginine residues through the Sec-machinery is integral to the mechanism of protein secretion

    William J Allen, Robin A Corey ... Ian Collinson
    The time it takes to secrete a protein is dominated by diffusion of positively charged arginines through the channel across the membrane, but lysines avoid this problem as they are neutralised before transport.
    1. Biochemistry and Chemical Biology
    2. Genetics and Genomics

    Evolution of substrate specificity in a retained enzyme driven by gene loss

    Ana Lilia Juárez-Vázquez, Janaka N Edirisinghe ... Francisco Barona-Gómez
    An integrated biochemical and evolutionary analysis shows how enzyme specificity evolves after gene loss during genome decay, implicating relaxation of purifying selection as a driving force for functional divergence.
    1. Chromosomes and Gene Expression

    Serotonin signaling mediates protein valuation and aging

    Jennifer Ro, Gloria Pak ... Scott D Pletcher
    Serotonin modulates diet-dependent lifespan in flies.
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    The dimerization equilibrium of a ClC Cl/H+ antiporter in lipid bilayers

    Rahul Chadda, Venkatramanan Krishnamani ... Janice L Robertson
    Measuring the equilibrium dimerization of a polytopic membrane protein in lipid bilayers forms the basis of a new system for studying the physical forces that stabilize membrane protein association in membranes.