James Bardwell


Affiliation: University of Michigan
Country: USA


  1. Stull F, Hipp H, Stockbridge R, Bardwell J. In vivo chloride concentrations surge to proteotoxic levels during acid stress. Nat Chem Biol. 2018;: pubmed publisher
  2. Malik A, Mueller Schickert A, Bardwell J. Cytosolic selection systems to study protein stability. J Bacteriol. 2014;196:4333-43 pubmed publisher
    ..We demonstrate that our approach allows the in vivo analysis of protein stability in the cytosolic compartment without the need for prior structural and functional knowledge. ..
  3. Dahl J, Koldewey P, Salmon L, Horowitz S, Bardwell J, Jakob U. HdeB functions as an acid-protective chaperone in bacteria. J Biol Chem. 2015;290:65-75 pubmed publisher
    ..These studies demonstrate how two structurally homologous proteins with seemingly identical in vivo functions have evolved to provide bacteria with the means for surviving a range of acidic protein-unfolding conditions. ..
  4. Dahl J, Koldewey P, Bardwell J, Jakob U. Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo. J Vis Exp. 2016;: pubmed publisher
    ..Finally, survival studies were used to monitor the influence of HdeB's chaperone function in vivo. ..
  5. Sachsenhauser V, Bardwell J. Directed evolution to improve protein folding in vivo. Curr Opin Struct Biol. 2018;48:117-123 pubmed publisher
    ..These methods have the potential of not just leading to a better understanding of the in vivo folding process, they may also allow for improved production of proteins of biotechnological interest. ..
  6. Lennon C, Thamsen M, Friman E, Cacciaglia A, Sachsenhauser V, Sorgenfrei F, et al. Folding Optimization In Vivo Uncovers New Chaperones. J Mol Biol. 2015;427:2983-94 pubmed publisher
    ..By giving bacteria the stark choice between death and stabilizing a poorly folded protein, we have now generated designer bacteria selected for their ability to stabilize specific proteins. ..
  7. Koldewey P, Stull F, Horowitz S, Martin R, Bardwell J. Forces Driving Chaperone Action. Cell. 2016;166:369-379 pubmed publisher
    ..By allowing the client to fold itself, Spy circumvents the need for client-specific folding instructions. This mechanism might help explain how chaperones can facilitate the folding of various unrelated proteins. ..
  8. Horowitz S, Koldewey P, Stull F, Bardwell J. Folding while bound to chaperones. Curr Opin Struct Biol. 2018;48:1-5 pubmed publisher
    ..In this review, we discuss the salient features of folding while bound in the cases for which it has been observed and speculate about its biological importance and possible occurrence in other chaperones. ..
  9. Docter B, Horowitz S, Gray M, Jakob U, Bardwell J. Do nucleic acids moonlight as molecular chaperones?. Nucleic Acids Res. 2016;44:4835-45 pubmed publisher
    ..Our findings reveal a possible new role for nucleic acids within the cell: that nucleic acids directly participate in maintaining proteostasis by preventing protein aggregation. ..

More Information


  1. Koldewey P, Horowitz S, Bardwell J. Chaperone-client interactions: Non-specificity engenders multifunctionality. J Biol Chem. 2017;292:12010-12017 pubmed publisher
    ..Chaperone mechanism may be better understood by always considering it in the context of the client's folding pathway and biological function. ..
  2. Salmon L, Stull F, Sayle S, Cato C, Akgül S, Foit L, et al. The Mechanism of HdeA Unfolding and Chaperone Activation. J Mol Biol. 2018;430:33-40 pubmed publisher
    ..Overall, this study provides a detailed experimental investigation into the mechanism by which HdeA unfolds and activates. ..