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Showing 1–8 of 8 results
Advanced filters: Author: Craig Bingman Clear advanced filters

  • Epistasis plays an important role in the evolution of novel protein functions because it determines the mutational path a protein takes. Here, the authors combine functional, structural and biophysical analyses to characterize epistasis in a computationally redesigned ligand-inducible allosteric transcription factor and found that epistasis creates distinct biophysical and biological functional landscapes.

    • Kyle K. Nishikawa
    • Nicholas Hoppe
    • Srivatsan Raman
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-14

  • Here, the structure of poly(UG) RNA reveals an unusual left-handed quadruplex, or ‘pUG fold’. The pUG fold marks RNAs as vectors for gene silencing in C. elegans by recruiting RNA-dependent RNA polymerase for siRNA synthesis.

    • Saeed Roschdi
    • Jenny Yan
    • Samuel E. Butcher
    Research
    Nature Structural & Molecular Biology
    Volume: 29, P: 1113-1121

  • Murray et al. identified and characterized a small-molecule inhibitor of human COQ8A, which belongs to the UbiB protein family and is essential for coenzyme Q biosynthesis.

    • Nathan H. Murray
    • Christopher R. M. Asquith
    • David J. Pagliarini
    Research
    Nature Chemical Biology
    Volume: 19, P: 230-238

  • Enantioselective C–C bond-forming reactions are underdeveloped in the biocatalysis toolbox. Now, engineering an efficient and promiscuous decarboxylative aldolase enzyme provides a solution to facilitate the convenient synthesis of non-standard γ-hydroxy amino acids from simple building blocks.

    • Jonathan M. Ellis
    • Meghan E. Campbell
    • Andrew R. Buller
    Research
    Nature Catalysis
    Volume: 5, P: 136-143

  • Nematode P granules are cytoplasmic RNA–protein biomolecule condensates central to germ cell development. Here the authors show that dimerization of the PGL-1 scaffolding protein is crucial to granule formation and mRNA repression, and that the WAGO-1 Argonaute protein is a cofactor in repressing PGL-1 bound mRNAs.

    • Scott Takeo Aoki
    • Tina R. Lynch
    • Judith Kimble
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-14

  • The synthetic ABA agonist pyrabactin helped identify the PYR/PYL family of ABA receptors. Now the selectivity of pyrabactin toward specific members of this family is explained using genetic, chemical and structural approaches. Subtle differences in the binding pockets of the receptors lead to productive or nonproductive conformations upon pyrabactin binding.

    • Francis C Peterson
    • E Sethe Burgie
    • Brian F Volkman
    Research
    Nature Structural & Molecular Biology
    Volume: 17, P: 1109-1113