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  • Journal article

  • The role of glutathione in periplasmic redox homeostasis and oxidative protein folding in Escherichia coli

    • Authors : Knoke, Lisa R. (2023)

  • The thiol redox balance in the periplasm of E. coli depends on the DsbA/B pair for oxidative 14 power and the DsbC/D system as its complement for isomerization of non-native disulfides. 15 While the standard redox potentials of those systems are known, the in vivo redox potential 16 imposed onto protein thiol disulfide pairs in the periplasm remains unknown. Here, we used 17 genetically encoded redox probes (roGFP2 ...
  • Journal article

  • A conformational-dependent interdomain redox relay at the core of Protein Disulfide Isomerase activity

    • Authors : Melo, Eduardo P. (2023)

  • Protein disulfide isomerases (PDIs) are a family of molecular chaperones resident in the endoplasmic reticulum (ER) emerging as important factors in disease. In addition to an holdase function, some members catalyse disulfide bond formation and isomerization, a crucial step for native folding and prevention of aggregation of misfolded proteins. PDIs are characterized by a modular arrangement of thioredoxin-like domains, with the canonical, first identified PDIA1, ...
  • Journal article

  • The role of glutathione in periplasmic redox homeostasis and oxidative protein folding in Escherichia coli

    • Authors : Knoke, Lisa R. (2023)

  • The thiol redox balance in the periplasm of E. coli depends on the DsbA/B pair for oxidative 14 power and the DsbC/D system as its complement for isomerization of non-native disulfides. 15 While the standard redox potentials of those systems are known, the in vivo redox potential 16 imposed onto protein thiol disulfide pairs in the periplasm remains unknown. Here, we used 17 genetically encoded redox probes (roGFP2 ...
  • Journal article

  • Deubiquitinase-Targeting Chimeras for Targeted Protein Stabilization

    • Authors : Henning, Nathaniel J. (2021)

  • Targeted protein degradation is a powerful therapeutic modality that uses heterobifunctional small-molecules to induce proximity between E3 ubiquitin ligases and target proteins to ubiquitinate and degrade specific proteins of interest. However, many proteins are ubiquitinated and degraded to drive disease pathology; in these cases targeted protein stabilization (TPS), rather than degradation, of the actively degraded target using a smallmolecule would be ther...