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Showing 1–9 of 9 results
Advanced filters: Author: Jayaraman Seetharaman Clear advanced filters

  • PXR is a receptor activated by diverse compounds that triggers detoxification pathways in the cell, and blocking this receptor may increase the effectiveness of certain drugs. Here, the authors present the structural basis of PXR inhibition.

    • Efren Garcia-Maldonado
    • Andrew D. Huber
    • Taosheng Chen
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-14

  • The authors show that the mechanism of BAK activation in mitochondrial apoptosis involves cooperation between direct activation by BH3-only protein BID and BAK autoactivation, providing a unifying basis for BAK triggering by BH3 ligands.

    • Geetika Singh
    • Cristina D. Guibao
    • Tudor Moldoveanu
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-15

  • De novo enzyme designs have generally tried to optimize multiple aspects of enzyme function simultaneously. Focusing only on positioning of active site residues to generate a nucleophilic serine as assessed by activity-based protein profiling now leads to a successful intermediate design.

    • Sridharan Rajagopalan
    • Chu Wang
    • David Baker
    Research
    Nature Chemical Biology
    Volume: 10, P: 386-391

  • UNC119 is a protein localized to the non-motile primary cilia. Here, Zhang et al. report the crystal structure of UNC119 and provide biochemical and cellular evidence that UNC119 is a lipid-binding protein that mediates G protein trafficking. The authors also show that that UNC119 function is conserved from GPCR trafficking in C. elegans olfactory neuron to transducin trafficking in mammalian photoreceptors.

    • Houbin Zhang
    • Ryan Constantine
    • Wolfgang Baehr
    Research
    Nature Neuroscience
    Volume: 14, P: 874-880

  • Methylthiolation by radical SAM enzymes is thought to include the sacrificial breakdown of a second Fe-S cluster to generate the sulfur cosubstrate. A biochemical, spectroscopic and structural study of two methylthiotransferases shows these enzymes retain their clusters, using exogenous thiols to modify their targets.

    • Farhad Forouhar
    • Simon Arragain
    • Marc Fontecave
    Research
    Nature Chemical Biology
    Volume: 9, P: 333-338