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Showing 1–4 of 4 results
Advanced filters: Author: Ian Sitarik Clear advanced filters

  • Non-covalent lasso entanglements are pervasive structural features of increasing importance. Here, the authors show that these entanglements are associated with in vitro misfolding across the E. coli proteome and that chaperones preferentially rescue such misfolding in essential proteins.

    • Ian Sitarik
    • Quyen V. Vu
    • Edward P. O’Brien
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-14

  • How soluble misfolded proteins can bypass chaperones is unknown. Utilizing a meta-analysis, multi-scale modelling, and new experimental data it is found that this phenomena is common and arises from misfolded states that are native-like and long-lived due to protein self-entanglements.

    • Ritaban Halder
    • Daniel A. Nissley
    • Edward P. O’Brien
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-17

  • Enzymes with identical sequences of amino acids can display varying activities when encoded with mRNA with different properties, but why this is the case has been a mystery. Now, it has been shown that synonymous mutations in mRNA alter the partitioning of proteins into long-lived soluble misfolded states with varying activities.

    • Yang Jiang
    • Syam Sundar Neti
    • Edward P. O’Brien
    Research
    Nature Chemistry
    Volume: 15, P: 308-318