Boyd S - Search Results

1

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

Benjamin CE , Chen Z , Brohlin OR , Lee H , Shahrivarkevishahi A , Boyd S , Winkler DD , Gassensmith JJ . Benjamin CE , et al. Among authors: boyd s. Nanoscale. 2020 Apr 28;12(16):9124-9132. doi: 10.1039/c9nr09816j. Epub 2020 Apr 15. Nanoscale. 2020. PMID: 32292962

2

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

Chen Z, Boyd SD, Calvo JS, Murray KW, Mejia GL, Benjamin CE, Welch RP, Winkler DD, Meloni G, D'Arcy S, Gassensmith JJ. Chen Z, et al. Among authors: boyd sd. Bioconjug Chem. 2017 Sep 20;28(9):2277-2283. doi: 10.1021/acs.bioconjchem.7b00305. Epub 2017 Aug 22. Bioconjug Chem. 2017. PMID: 28787574

3

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

Skopp A, Boyd SD, Ullrich MS, Liu L, Winkler DD. Skopp A, et al. Among authors: boyd sd. Biometals. 2019 Aug;32(4):695-705. doi: 10.1007/s10534-019-00206-3. Epub 2019 Jul 10. Biometals. 2019. PMID: 31292775 Free PMC article.

4

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

Boyd SD, Liu L, Bulla L, Winkler DD. Boyd SD, et al. J Proteomics Bioinform. 2018;11(4):473. doi: 10.4172/jpb.1000473. Epub 2018 May 14. J Proteomics Bioinform. 2018. PMID: 29950795 Free PMC article.

5

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

Liu L, Boyd SD, Bulla LA Jr, Winkler DD. Liu L, et al. J Proteomics Bioinform. 2018;11(11):201-210. doi: 10.4172/0974-276X.1000487. Epub 2018 Dec 11. J Proteomics Bioinform. 2018. PMID: 30740004 Free PMC article.

6

Copper Sources for Sod1 Activation.

Boyd SD, Ullrich MS, Skopp A, Winkler DD. Boyd SD, et al. Antioxidants (Basel). 2020 Jun 7;9(6):500. doi: 10.3390/antiox9060500. Antioxidants (Basel). 2020. PMID: 32517371 Free PMC article. Review.

7

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

Liu L, Boyd S, Kavoussi M, Bulla LA Jr, Winkler DD. Liu L, et al. Among authors: boyd s. J Proteomics Bioinform. 2018;11(4):104-0110. doi: 10.4172/jpb.1000474. Epub 2018 May 14. J Proteomics Bioinform. 2018. PMID: 30026652 Free PMC article.

8

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

Boyd SD, Calvo JS, Liu L, Ullrich MS, Skopp A, Meloni G, Winkler DD. Boyd SD, et al. J Biol Chem. 2019 Feb 8;294(6):1956-1966. doi: 10.1074/jbc.RA118.005283. Epub 2018 Dec 10. J Biol Chem. 2019. PMID: 30530491 Free PMC article.

9

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).

Boyd SD, Ullrich MS, Calvo JS, Behnia F, Meloni G, Winkler DD. Boyd SD, et al. Molecules. 2020 Feb 28;25(5):1086. doi: 10.3390/molecules25051086. Molecules. 2020. PMID: 32121118 Free PMC article.

10

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

Liu L, Wilcox XE, Fisher AJ, Boyd SD, Zhi J, Winkler DD, Bulla LA Jr. Liu L, et al. Biochemistry. 2022 May 3;61(9):752-766. doi: 10.1021/acs.biochem.2c00089. Epub 2022 Apr 19. Biochemistry. 2022. PMID: 35438971

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