Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–7 of 7 results
Advanced filters: Author: David P. Giedroc Clear advanced filters
  • The extent to which human bacterial pathogens broadly utilize ergothioneine as an antioxidant is unknown. Here, authors describe the discovery of a specific transporter for ergothioneine in a respiratory pathogen that is highly conserved among Firmicutes.

    • Yifan Zhang
    • Giovanni Gonzalez-Gutierrez
    • David P. Giedroc
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-15
  • Structural analyses reveal that CopA and CupA share a binuclear Cu(I) ion binding motif and that copper is trafficked from a low-affinity site on CupA to a high-affinity site in CopA, making CupA the first membrane-bound copper chaperone important in copper resistance.

    • Yue Fu
    • Ho-Ching Tiffany Tsui
    • David P Giedroc
    Research
    Nature Chemical Biology
    Volume: 9, P: 177-183
  • Structural and kinetic analyses of the transcriptional repressor SqrR in multiple states indicate that its persulfide selectivity is determined by structural frustration in the disulfide form, favoring formation of the tetrasulfide-bridged product.

    • Daiana A. Capdevila
    • Brenna J. C. Walsh
    • David P. Giedroc
    Research
    Nature Chemical Biology
    Volume: 17, P: 65-70
  • A crystal structure of the C. difficile toxin TcdA reveals a requirement for zinc during autoprocessing and a delivery domain involved in the pH-dependent pore formation that allows the toxin to exit the endosome.

    • Nicole M. Chumbler
    • Stacey A. Rutherford
    • D. Borden Lacy
    Research
    Nature Microbiology
    Volume: 1, P: 1-6
  • Blue copper proteins serve as models for understanding how proteins tune metal binding properties, however, the mechanism through which they do so remains unclear. Here, the authors investigate carbon-deuterium bond vibrations in Nostocplastocyanin to study key copper-ligand interactions in different redox states, and reveal specific impacts of perturbation to the cupredoxin scaffold on copper coordination and the redox properties of plastocyanin.

    • Claire C. Mammoser
    • Brynn E. LeMasters
    • Megan C. Thielges
    ResearchOpen Access
    Communications Chemistry
    Volume: 6, P: 1-9