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Showing 1–6 of 6 results
Advanced filters: Author: William M. Marsiglia Clear advanced filters

  • X-ray crystallography, solution NMR and biochemical and cell-based analyses reveal a model where catalytically repressed receptor tyrosine kinases accomplish activation loop (A-loop) tyrosine transphosphorylation.

    • Lingfeng Chen
    • William M. Marsiglia
    • Moosa Mohammadi
    Research
    Nature Chemical Biology
    Volume: 16, P: 267-277

  • This Perspective highlights advances in bioluminescence resonance energy transfer technologies for measuring intracellular drug–target engagement, expanding their use to analyze kinetics, permeability and complex mechanisms in chemical biology.

    • Jacob L. Capener
    • Martin P. Schwalm
    • Matthew B. Robers
    Reviews
    Nature Chemical Biology
    P: 1-11

  • Crystal structures of the MEK kinase bound to the scaffold protein KSR and various MEK inhibitors, including the anti-cancer drug trametinib, reveal the molecular and functional mechanisms behind MEK inhibition.

    • Zaigham M. Khan
    • Alexander M. Real
    • Arvin C. Dar
    Research
    Nature
    Volume: 588, P: 509-514

  • Here, the authors reveal the protonation of a single membrane embedded glutamate residue within the homodimer of the efflux transporter EmrE modulates the structure and dynamics in an allosteric manner using NMR spectroscopy.

    • Jianping Li
    • Ampon Sae Her
    • Nathaniel J. Traaseth
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-14

  • Development of live-cell target engagement approaches to query MEK-bound binary and ternary complexes reveals the distinct pharmacology of clinical MEK inhibitors at specific assemblies composed of MEK, RAF, KSR and 14-3-3.

    • William M. Marsiglia
    • Arthur Chow
    • Arvin C. Dar
    Research
    Nature Chemical Biology
    Volume: 20, P: 373-381