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Showing 1–5 of 5 results
Advanced filters: Author: John D. Bagert Clear advanced filters

  • Combined use of a DNA-barcoded nucleosome library and a humanized yeast library allows the identification of histone globular domain mutations that affect histone exchange and nucleosome sliding processes, as well as cancer-associated gene pathways.

    • John D. Bagert
    • Michelle M. Mitchener
    • Tom W. Muir
    Research
    Nature Chemical Biology
    Volume: 17, P: 403-411

  • Proteins that interact with histone post-translational modifications have now been identified using an approach based on split-intein mediated histone semisynthesis. Histone modifications and disease-relevant mutations were installed into native chromatin with an adjacent photocross-linker to enable in situ cross-linking. This strategy enabled the determination of chromatin-relevant interactomes and represents a powerful tool for exploring epigenetic regulation and dysregulation at the molecular level.

    • Antony J. Burton
    • Michael Haugbro
    • Tom W. Muir
    Research
    Nature Chemistry
    Volume: 12, P: 520-527

  • The characterization of missense histone mutations that occur across several cancer types provides insight into the potential role of these mutations in altering chromatin structure and potentially contributing to tumour development.

    • Benjamin A. Nacev
    • Lijuan Feng
    • C. David Allis
    Research
    Nature
    Volume: 567, P: 473-478

  • Chemical approaches to site-specifically ubiquitylate a target protein allow investigation of the biochemical effects of this modification, but they often destabilize the protein. Here, the authors report on a synthetic conjugation strategy that leads to protein ubiquitylation in non-denaturing conditions.

    • Caroline E. Weller
    • Abhinav Dhall
    • Champak Chatterjee
    ResearchOpen Access
    Nature Communications
    Volume: 7, P: 1-10