Pathogenic R 163 W Variant of the Copper Chaperone for Sod1 (Ccs) Functions as an Anti-chaperone.

Autor: Zhang B; Department of Biological Sciences, The University of Texas at Dallas, Richardson, Texas 75083, United States., Boyd SD; Department of Biological Sciences, The University of Texas at Dallas, Richardson, Texas 75083, United States., Zhabilov D; Department of Biological Sciences, The University of Texas at Dallas, Richardson, Texas 75083, United States., Ullrich M; Department of Biological Sciences, The University of Texas at Dallas, Richardson, Texas 75083, United States., Blackburn NJ; Department of Chemical Physiology and Biochemistry, Oregon Health and Sciences University, Portland, Oregon 97239, United States., Winkler DD; Department of Biological Sciences, The University of Texas at Dallas, Richardson, Texas 75083, United States.

Publikováno v: Biochemistry [Biochemistry] 2024 Aug 20; Vol. 63 (16), pp. 2051-2062. Date of Electronic Publication: 2024 Aug 04.

The copper chaperone CCS facilitates copper binding to MEK1/2 to promote kinase activation.

Autor: Grasso M; Department of Chemistry, School of Arts and Sciences, University of Pennsylvania, Philadelphia, Pennsylvania, USA; Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA., Bond GJ; Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA; Biochemistry Major Program, College of Arts and Sciences, University of Pennsylvania, Philadelphia, Pennsylvania, USA; Department of Cancer Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA., Kim YJ; Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA; Department of Cancer Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA., Boyd S; Department of Biological Sciences, University of Texas at Dallas, Richardson, Texas, USA., Matson Dzebo M; Department of Biology and Biological Engineering, Chalmers University of Technology, Gothenburg, Sweden., Valenzuela S; Department of Biology and Biological Engineering, Chalmers University of Technology, Gothenburg, Sweden., Tsang T; Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA; Department of Cancer Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA; Cell and Molecular Biology Graduate Group, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA., Schibrowsky NA; Department of Chemistry, School of Arts and Sciences, University of Pennsylvania, Philadelphia, Pennsylvania, USA; Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA., Alwan KB; Department of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health and Science University, Portland, Oregon, USA., Blackburn NJ; Department of Chemical Physiology and Biochemistry, School of Medicine, Oregon Health and Science University, Portland, Oregon, USA., Burslem GM; Department of Cancer Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA; Department of Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA., Wittung-Stafshede P; Department of Biology and Biological Engineering, Chalmers University of Technology, Gothenburg, Sweden., Winkler DD; Department of Biological Sciences, University of Texas at Dallas, Richardson, Texas, USA., Marmorstein R; Department of Chemistry, School of Arts and Sciences, University of Pennsylvania, Philadelphia, Pennsylvania, USA; Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA; Department of Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA., Brady DC; Abramson Family Cancer Research Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA; Department of Cancer Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania, USA. Electronic address: bradyd@pennmedicine.upenn.edu.

Publikováno v: The Journal of biological chemistry [J Biol Chem] 2021 Dec; Vol. 297 (6), pp. 101314. Date of Electronic Publication: 2021 Oct 27.

Copper Sources for Sod1 Activation.

Autor: Boyd SD; Department of Biological Sciences, the University of Texas at Dallas, 800 W. Campbell Rd., Richardson, TX 75080, USA., Ullrich MS; Department of Biological Sciences, the University of Texas at Dallas, 800 W. Campbell Rd., Richardson, TX 75080, USA., Skopp A; Department of Biological Sciences, the University of Texas at Dallas, 800 W. Campbell Rd., Richardson, TX 75080, USA., Winkler DD; Department of Biological Sciences, the University of Texas at Dallas, 800 W. Campbell Rd., Richardson, TX 75080, USA.

Publikováno v: Antioxidants (Basel, Switzerland) [Antioxidants (Basel)] 2020 Jun 07; Vol. 9 (6). Date of Electronic Publication: 2020 Jun 07.

Mutations in Superoxide Dismutase 1 (Sod1) Linked to Familial Amyotrophic Lateral Sclerosis Can Disrupt High-Affinity Zinc-Binding Promoted by the Copper Chaperone for Sod1 (Ccs).

Autor: Boyd SD; Department of Biological Sciences, the University of Texas at Dallas, 800 W. Campbell Rd., Richardson, TX 75080, USA., Ullrich MS; Department of Biological Sciences, the University of Texas at Dallas, 800 W. Campbell Rd., Richardson, TX 75080, USA., Calvo JS; Department of Chemistry and Biochemistry, the University of Texas at Dallas, 800 W. Campbell Rd., Richardson, TX 75080, USA., Behnia F; Department of Biological Sciences, the University of Texas at Dallas, 800 W. Campbell Rd., Richardson, TX 75080, USA., Meloni G; Department of Chemistry and Biochemistry, the University of Texas at Dallas, 800 W. Campbell Rd., Richardson, TX 75080, USA., Winkler DD; Department of Biological Sciences, the University of Texas at Dallas, 800 W. Campbell Rd., Richardson, TX 75080, USA.

Publikováno v: Molecules (Basel, Switzerland) [Molecules] 2020 Feb 28; Vol. 25 (5). Date of Electronic Publication: 2020 Feb 28.

Copper-zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1.

Autor: Skopp A; Department of Biological Sciences, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, TX, 75080, USA., Boyd SD; Department of Biological Sciences, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, TX, 75080, USA., Ullrich MS; Department of Biological Sciences, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, TX, 75080, USA., Liu L; Department of Biological Sciences, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, TX, 75080, USA., Winkler DD; Department of Biological Sciences, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, TX, 75080, USA. duane.winkler@utdallas.edu.

Publikováno v: Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine [Biometals] 2019 Aug; Vol. 32 (4), pp. 695-705. Date of Electronic Publication: 2019 Jul 10.