Duane D. Winkler

发表

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

E. L. Guenther, Michael R. Sawaya, Lisa M. Johnson, 2013, Proceedings of the National Academy of Sciences.

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

K. Luger, S. Fenn, G. Witte, 2012, Nucleic acids research.

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.

Disrupted zinc-binding sites in structures of pathogenic SOD1 variants D124V and H80R.

J. Valentine, P. Hart, Alexander B. Taylor, 2010, Biochemistry.

Structural and biophysical properties of the pathogenic SOD1 variant H46R/H48Q.

D. Borchelt, P. Hart, V. Culotta, 2009, Biochemistry.

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.

Copper–Zinc Superoxide Dismutase, Its Copper Chaperone, and Familial Amyotrophic Lateral Sclerosis

D. Borchelt, Celeste M. Karch, P. Hart, 2010 .

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.

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

Zhiguo Zhang, K. Luger, Hui Zhou, 2012, Nucleic acids research.

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

Zhiguo Zhang, K. Luger, Hui Zhou, 2012, Nucleic acids research.

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.

Quantifying chromatin-associated interactions: the HI-FI system.

K. Luger, Duane D. Winkler, Aaron R Hieb, 2012, Methods in enzymology.

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

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

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

K. Luger, Duane D. Winkler, 2011, The Journal of Biological Chemistry.

FACT is a sensor of DNA torsional stress in eukaryotic cells

K. Kirsanov, E. Lesovaya, M. Yakubovskaya, 2017, Nucleic acids research.

Evidence for monomeric actin function in INO80 chromatin remodeling

K. Luger, Xuetong Shen, Duane D. Winkler, 2013, Nature Structural &Molecular Biology.

Histone Chaperone FACT Coordinates Nucleosome Interaction through Multiple Synergistic Binding Events*

Uma M. Muthurajan, K. Luger, U. Muthurajan, 2011, The Journal of Biological 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.

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

K. Luger, J. DeLuca, J. Prenni, 2013, Nucleic acids research.

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

D. Borchelt, P. Hart, M. Prudencio, 2009, Proceedings of the National Academy of Sciences.

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.

The FACT Complex Promotes Avian Leukosis Virus DNA Integration

K. Beemon, M. Kvaratskhelia, Ross C. Larue, 2017, Journal of Virology.

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.

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

E. L. Guenther, D. Eisenberg, Stuart A. Sievers, 2013 .

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

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