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The Histone Chaperone FACT: Structural Insights and Mechanisms for Nucleosome Reorganization

The Journal of biological chemistry, 2011-05, Vol.286 (21), p.18369-18374

2011

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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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Histone Chaperone FACT Coordinates Nucleosome Interaction through Multiple Synergistic Binding Events

The Journal of biological chemistry, 2011-12, Vol.286 (48), p.41883-41892

2011

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Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS

Proceedings of the National Academy of Sciences - PNAS, 2014-01, Vol.111 (1), p.197-201

2014

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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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Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS

Proceedings of the National Academy of Sciences - PNAS, 2009-05, Vol.106 (19), p.7774-7779

2009

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Copper Sources for Sod1 Activation

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

2020

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Structure of Actin-related protein 8 and its contribution to nucleosome binding

Nucleic acids research, 2012-11, Vol.40 (21), p.11036-11046

2012

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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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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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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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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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Yeast CAF-1 assembles histone (H3-H4)2 tetramers prior to DNA deposition

Nucleic acids research, 2012-11, Vol.40 (20), p.10139-10149

2012

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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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Yeast CAF-1 assembles histone (H3-H4) 2 tetramers prior to DNA deposition

Nucleic acids research, 2017-09, Vol.45 (16), p.9811-9812

2017

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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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Linker histone H1.0 interacts with an extensive network of proteins found in the nucleolus

Nucleic acids research, 2013-04, Vol.41 (7), p.4026-4035

2013

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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 chromatin-associated interactions: the HI-FI system

Methods in enzymology, 2012, Vol.512, p.243-274

2012

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Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

Biochemistry (Easton), 2010-07, Vol.49 (27), p.5714-5725

2010

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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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The Histone Chaperone FACT: Structural Insights and Mechanisms for Nucleosome Reorganization

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

Histone Chaperone FACT Coordinates Nucleosome Interaction through Multiple Synergistic Binding Events

Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS

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

Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS

Copper Sources for Sod1 Activation

Structure of Actin-related protein 8 and its contribution to nucleosome binding

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

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

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

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

Yeast CAF-1 assembles histone (H3-H4)2 tetramers prior to DNA deposition

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

Yeast CAF-1 assembles histone (H3-H4) 2 tetramers prior to DNA deposition

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

Linker histone H1.0 interacts with an extensive network of proteins found in the nucleolus

Fluorescent Functionalization across Quaternary Structure in a Virus-like Particle

Quantifying chromatin-associated interactions: the HI-FI system

Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R

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

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