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

Biometals, 2019-08, Vol.32 (4), p.695-705

2019

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

The Journal of biological chemistry, 2017-07, Vol.292 (29), p.12025-12040

2017

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

The Journal of biological chemistry, 2019-02, Vol.294 (6), p.1956-1966

2019

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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)

Molecules (Basel, Switzerland), 2020-02, Vol.25 (5), p.1086

2020

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

Metallomics, 2017-08, Vol.9 (8), p.1047-1059

2017

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Copper Sources for Sod1 Activation

Antioxidants, 2020-06, Vol.9 (6), p.500

2020

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

Biochemistry (Easton), 2024-08, Vol.63 (16), p.2051-2062

2024

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Pathogenic R163W Variant of the Copper Chaperone for Sod1 (Ccs) Functions as an Anti-chaperone

Biochemistry (Easton), 2024-08, Vol.63 (16), p.2051-2062

2024

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

Journal of proteomics & bioinformatics, 2018, Vol.11 (11)

2018

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

Biochemistry (Easton), 2022-05, Vol.61 (9), p.752-766

2022

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Functional and Structural Analysis of the Toxin-Binding Site of the Cadherin G-Protein-Coupled Receptor, BT-R 1 , for Cry1A Toxins of Bacillus thuringiensis

Biochemistry (Easton), 2022-05, Vol.61 (9), p.752-766

2022

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Fluorescent Functionalization across Quaternary Structure in a Virus-like Particle

Bioconjugate chemistry, 2017-09, Vol.28 (9), p.2277-2283

2017

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

Journal of proteomics & bioinformatics, 2018, Vol.11 (4)

2018

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Increased food energy supply as a major driver of the obesity epidemic: a global analysis

Bulletin of the World Health Organization, 2015-07, Vol.93 (7), p.446-456

2015

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The healthiness of New Zealand school food environments: a national survey

Australian and New Zealand journal of public health, 2022-06, Vol.46 (3), p.325-331

2022

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

The Journal of biological chemistry, 2021-12, Vol.297 (6), p.101314-101314, Article 101314

2021

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Obesogenic Retail Food Environments Around New Zealand Schools

American journal of preventive medicine, 2016-09, Vol.51 (3), p.e57-e66

2016

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

Nanoscale, 2020-04, Vol.12 (16), p.9124-9132

2020

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Increased food energy supply as a major driver of the obesity epidemic: a global analysis/L'accroissement de la disponibilite energetique alimentaire comme facteur majeur de l'epidemie d'obesite: une analyse a l'echelle internationale/El aumento del suministro de energia alimentaria como el principal impulsor de la epidemia de obesidad: un analisis internacional

Bulletin of the World Health Organization, 2015-07, p.446

2015

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20 Years of ClO Measurements in the Antarctic Lower Stratosphere

Atmospheric chemistry and physics, 2016-08, Vol.16 (16), p.10725-10734

2016

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

Journal of proteomics & bioinformatics, 2018, Vol.11 (4)

2018

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Structural and Molecular Determinants of CCS-Mediated Copper Activation of MEK1/2

SSRN Electronic Journal

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

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

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

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)

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

Copper Sources for Sod1 Activation

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

Pathogenic R163W Variant of the Copper Chaperone for Sod1 (Ccs) Functions as an Anti-chaperone

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

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

Functional and Structural Analysis of the Toxin-Binding Site of the Cadherin G-Protein-Coupled Receptor, BT-R 1 , for Cry1A Toxins of Bacillus thuringiensis

Fluorescent Functionalization across Quaternary Structure in a Virus-like Particle

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

Increased food energy supply as a major driver of the obesity epidemic: a global analysis

The healthiness of New Zealand school food environments: a national survey

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

Obesogenic Retail Food Environments Around New Zealand Schools

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

20 Years of ClO Measurements in the Antarctic Lower Stratosphere

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

Structural and Molecular Determinants of CCS-Mediated Copper Activation of MEK1/2

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