Now showing items 1-3 of 3

    • Copper-Zinc Superoxide Dismutase Is Activated through a Sulfenic Acid Intermediate at a Copper Ion Entry Site 

      Fetherolf, M. M.; Boyd, Stefanie D.; Taylor, A. B.; Kim, H. J.; Wohlschlegel, J. A.; Blackburn, N. J.; Hart, P. J.; Winge, D. R.; Winkler, Duane D. (American Society for Biochemistry and Molecular Biology Inc, 2018-08-20)
      Metallochaperones are a diverse family of trafficking molecules that provide metal ions to protein targets for use as cofactors. The copper chaperone for superoxide dismutase (Ccs1) activates immature copper-zinc superoxide ...
    • FACT Is a Sensor of DNA Torsional Stress in Eukaryotic Cells 

      Safina, A.; Cheney, P.; Pal, M.; Brodsky, L.; Ivanov, A.; Kirsanov, K.; Lesovaya, E.; Naberezhnov, D.; Nesher, E.; Koman, I.; Wang, D.; Wang, J.; Yakubovskaya, M.; Winkler, Duane D.; Gurova, K. (2018-09-24)
      Transitions of B-DNA to alternative DNA structures (ADS) can be triggered by negative torsional strain, which occurs during replication and transcription, and may lead to genomic instability. However, how ADS are recognized ...
    • Quantifying the Interaction between Copper-Zinc Superoxide Dismutase (Sod1) and Its Copper Chaperone (Ccs1) 

      Boyd, Stefanie D.; Liu, Li; Bulla, Lee A.; Winkler, Duane D.
      Immature copper-zinc superoxide dismutase (Sod1) is activated by its copper chaperone (Ccs1). Ccs1 delivers a single copper ion and catalyzes oxidation of an intra-subunit disulfide bond within each Sod1 monomer through a ...