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Stefanie D Boyd

Showing results (1-10 of 11) with videos related to

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Journal of Proteomics & Bioinformatics|June 29, 2018
Quantifying the Interaction between Copper-Zinc Superoxide Dismutase (Sod1) and its Copper Chaperone (Ccs1)Stefanie D Boyd, Li Liu, Lee Bulla, et al.
Antioxidants (Basel, Switzerland)|June 11, 2020
Copper Sources for Sod1 ActivationStefanie D Boyd, Morgan S Ullrich, Amelie Skopp, et al.
Journal of Proteomics & Bioinformatics|February 12, 2019
"The Defined Toxin-binding Region of the Cadherin G-protein Coupled Receptor, BT-R<sub>1</sub>, for the Active Cry1Ab Toxin of <i>Bacillus thuringiensis</i>"Li Liu, Stefanie D Boyd, Lee A Bulla, et al.
Metallomics : Integrated Biometal Science|July 8, 2017
Oxygen-dependent activation of Cu,Zn-superoxide dismutase-1Morgan M Fetherolf, Stefanie D Boyd, Duane D Winkler, et al.
Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine|July 12, 2019
Copper-zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1Amélie Skopp, Stefanie D Boyd, Morgan S Ullrich, et al.
Biochemistry|August 5, 2024
Pathogenic R<sub>163</sub>W Variant of the Copper Chaperone for Sod1 (Ccs) Functions as an Anti-chaperoneBei Zhang, Stefanie D Boyd, Dannie Zhabilov, et al.
Molecules (Basel, Switzerland)|March 4, 2020
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)Stefanie D Boyd, Morgan S Ullrich, Jenifer S Calvo, et al.
The Journal of Biological Chemistry|December 12, 2018
The yeast copper chaperone for copper-zinc superoxide dismutase (CCS1) is a multifunctional chaperone promoting all levels of SOD1 maturationStefanie D Boyd, Jenifer S Calvo, Li Liu, et al.
Biochemistry|April 19, 2022
Functional and Structural Analysis of the Toxin-Binding Site of the Cadherin G-Protein-Coupled Receptor, BT-R<sub>1</sub>, for Cry1A Toxins of <i>Bacillus thuringiensis</i>Li Liu, Xander E Wilcox, Andrew J Fisher, et al.
The Journal of Biological Chemistry|May 24, 2017
Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry siteMorgan M Fetherolf, Stefanie D Boyd, Alexander B Taylor, et al.
Pageof 2

Showing results (1-10 of 11) with videos related to

Sort By:
Pageof 2
Journal of Proteomics & Bioinformatics|June 29, 2018
Quantifying the Interaction between Copper-Zinc Superoxide Dismutase (Sod1) and its Copper Chaperone (Ccs1)Stefanie D Boyd, Li Liu, Lee Bulla, et al.
Antioxidants (Basel, Switzerland)|June 11, 2020
Copper Sources for Sod1 ActivationStefanie D Boyd, Morgan S Ullrich, Amelie Skopp, et al.
Journal of Proteomics & Bioinformatics|February 12, 2019
"The Defined Toxin-binding Region of the Cadherin G-protein Coupled Receptor, BT-R<sub>1</sub>, for the Active Cry1Ab Toxin of <i>Bacillus thuringiensis</i>"Li Liu, Stefanie D Boyd, Lee A Bulla, et al.
Metallomics : Integrated Biometal Science|July 8, 2017
Oxygen-dependent activation of Cu,Zn-superoxide dismutase-1Morgan M Fetherolf, Stefanie D Boyd, Duane D Winkler, et al.
Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine|July 12, 2019
Copper-zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1Amélie Skopp, Stefanie D Boyd, Morgan S Ullrich, et al.
Biochemistry|August 5, 2024
Pathogenic R<sub>163</sub>W Variant of the Copper Chaperone for Sod1 (Ccs) Functions as an Anti-chaperoneBei Zhang, Stefanie D Boyd, Dannie Zhabilov, et al.
Molecules (Basel, Switzerland)|March 4, 2020
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)Stefanie D Boyd, Morgan S Ullrich, Jenifer S Calvo, et al.
The Journal of Biological Chemistry|December 12, 2018
The yeast copper chaperone for copper-zinc superoxide dismutase (CCS1) is a multifunctional chaperone promoting all levels of SOD1 maturationStefanie D Boyd, Jenifer S Calvo, Li Liu, et al.
Biochemistry|April 19, 2022
Functional and Structural Analysis of the Toxin-Binding Site of the Cadherin G-Protein-Coupled Receptor, BT-R<sub>1</sub>, for Cry1A Toxins of <i>Bacillus thuringiensis</i>Li Liu, Xander E Wilcox, Andrew J Fisher, et al.
The Journal of Biological Chemistry|May 24, 2017
Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry siteMorgan M Fetherolf, Stefanie D Boyd, Alexander B Taylor, et al.
Pageof 2