Stefanie Boyd

发表

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)

Gabriele Meloni, F. Behnia, Duane D. Winkler, 2020, Molecules.

Functional and Structural Analysis of the Toxin-Binding Site of the Cadherin G-Protein-Coupled Receptor, BT-R1, for Cry1A Toxins of Bacillus thuringiensis.

A. Fisher, L. Bulla, Duane D. Winkler, 2022, Biochemistry.

Interaction of Fluorescently Labeled Cadherin G Protein-coupled Receptor with the Cry1Ab Toxin of Bacillus thuringiensis

Li Liu, L. Bulla, Duane D. Winkler, 2018, Journal of proteomics & bioinformatics.

“The Defined Toxin-binding Region of the Cadherin G-protein Coupled Receptor, BT-R1, for the Active Cry1Ab Toxin of Bacillus thuringiensis”

Li Liu, L. Bulla, Duane D. Winkler, 2018, Journal of proteomics & bioinformatics.

Using FRET to measure the time it takes for a cell to destroy a virus.

J. Gassensmith, Zhuo Chen, C. Benjamin, 2019, Nanoscale.

Copper Sources for Sod1 Activation

Duane D. Winkler, Stefanie Boyd, Morgan S. Ullrich, 2020, Antioxidants.

Oxygen-dependent activation of Cu,Zn-superoxide dismutase-1.

D. Winge, Duane D. Winkler, Stefanie Boyd, 2017, Metallomics : integrated biometal science.

Structural and molecular determinants of CCS-mediated copper activation of MEK1/2

R. Marmorstein, P. Wittung-Stafshede, M. Matthews, 2020, bioRxiv.

Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site

D. Winge, P. Hart, J. Wohlschlegel, 2017, The Journal of Biological Chemistry.

Quantifying the Interaction between Copper-Zinc Superoxide Dismutase (Sod1) and its Copper Chaperone (Ccs1)

Li Liu, L. Bulla, Duane D. Winkler, 2018, Journal of proteomics & bioinformatics.

Fluorescent Functionalization across Quaternary Structure in a Virus-like Particle.

J. Gassensmith, Gabriele Meloni, Zhuo Chen, 2017, Bioconjugate chemistry.

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

R. Marmorstein, P. Wittung-Stafshede, George M. Burslem, 2021, The Journal of biological chemistry.

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

Li Liu, Duane D. Winkler, Stefanie Boyd, 2019, BioMetals.

The yeast copper chaperone for copper-zinc superoxide dismutase (CCS1) is a multifunctional chaperone promoting all levels of SOD1 maturation

Li Liu, Gabriele Meloni, Duane D. Winkler, 2018, The Journal of Biological Chemistry.

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

Li Liu, Duane D. Winkler, Stefanie Boyd, 2019, BioMetals.

Oxygen-dependent activation of Cu,Zn-superoxide dismutase-1.

D. Winge, Duane D. Winkler, Stefanie Boyd, 2017, Metallomics : integrated biometal science.