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Binding of a Single Zinc Ion to One Subunit of Copper−Zinc Superoxide Dismutase Apoprotein Substantially Influences the Structure and Stability of the Entire Homodimeric Protein

Journal of the American Chemical Society, 2007-04, Vol.129 (15), p.4575-4583

2007

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Destabilization of Apoprotein Is Insufficient to Explain Cu,Zn-Superoxide Dismutase-Linked ALS Pathogenesis

Proceedings of the National Academy of Sciences - PNAS, 2005-07, Vol.102 (30), p.10516-10521

2005

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Detergent-insoluble Aggregates Associated with Amyotrophic Lateral Sclerosis in Transgenic Mice Contain Primarily Full-length, Unmodified Superoxide Dismutase-1

The Journal of biological chemistry, 2008-03, Vol.283 (13), p.8340-8350

2008

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A Structure-Based Mechanism for Copper−Zinc Superoxide Dismutase

Biochemistry (Easton), 1999-02, Vol.38 (7), p.2167-2178

1999

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Local Unfolding in a Destabilized, Pathogenic Variant of Superoxide Dismutase 1 Observed with H/D Exchange and Mass Spectrometry

The Journal of biological chemistry, 2006-06, Vol.281 (26), p.18167-18176

2006

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Spectroscopic Investigation of Stellacyanin Mutants: Axial Ligand Interactions at the Blue Copper Site

Journal of the American Chemical Society, 2003-09, Vol.125 (37), p.11314-11328

2003

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Copper(2+) Binding to the Surface Residue Cysteine 111 of His46Arg Human Copper−Zinc Superoxide Dismutase, a Familial Amyotrophic Lateral Sclerosis Mutant

Biochemistry (Easton), 2000-07, Vol.39 (28), p.8125-8132

2000

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Metal-free Superoxide Dismutase-1 and Three Different Amyotrophic Lateral Sclerosis Variants Share a Similar Partially Unfolded β-Barrel at Physiological Temperature

The Journal of biological chemistry, 2009-12, Vol.284 (49), p.34382-34389

2009

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X-ray Absorption Edge and EXAFS Studies of the Blue Copper Site in Stellacyanin: Effects of Axial Amide Coordination

The journal of physical chemistry. B, 2000-11, Vol.104 (46), p.10814-10819

2000

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Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: Plant‐specific mononuclear blue copper proteins

Protein science, 1998-09, Vol.7 (9), p.1915-1929

1998

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Spectroscopic and Geometric Variations in Perturbed Blue Copper Centers: Electronic Structures of Stellacyanin and Cucumber Basic Protein

Journal of the American Chemical Society, 1998-09, Vol.120 (37), p.9621-9631

1998

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A missing link in cupredoxins: Crystal structure of cucumber stellacyanin at 1.6 Å resolution

Protein science, 1996-11, Vol.5 (11), p.2175-2183

1996

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Structural Information through NMR Hyperfine Shifts in Blue Copper Proteins

Journal of the American Chemical Society, 2000-04, Vol.122 (15), p.3701-3707

2000

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Subunit asymmetry in the three‐dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis

Protein science, 1998-03, Vol.7 (3), p.545-555

1998

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Cobalt(2+) Binding to Human and Tomato Copper Chaperone for Superoxide Dismutase: Implications for the Metal Ion Transfer Mechanism

Biochemistry (Easton), 2000-05, Vol.39 (18), p.5413-5421

2000

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Preliminary Characterization of Occipodins, Natural Product Anticoagulants from Hematophagous Marine Parasites, Isopod Elthusa vulgaris and Copepod Phrixocephalus Cincinnatus

Blood, 2016-12, Vol.128 (22), p.1443-1443

2016

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X-ray Crystallographic and Analytical Ultracentrifugation Analyses of Truncated and Full-Length Yeast Copper Chaperones for SOD (LYS7): A Dimer−Dimer Model of LYS7−SOD Association and Copper Delivery

Biochemistry (Easton), 2000-04, Vol.39 (13), p.3611-3623

2000

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Metal-free Superoxide Dismutase-1 and Three Different Amyotrophic Lateral Sclerosis Variants Share a Similar Partially Unfolded Î²-Barrel at Physiological Temperature

The Journal of biological chemistry, 2009-12, Vol.284 (49), p.34382

2009

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Metal-free Superoxide Dismutase-1 and Three Different Amyotrophic Lateral Sclerosis Variants Share a Similar Partially Unfolded b-Barrel at Physiological Temperature

The Journal of biological chemistry, 2009-12, Vol.284 (49)

2009

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Blue copper-binding domains

Advances in Protein Chemistry, 2002, Vol.60, p.271-340

2002

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Detergent-insoluble Aggregates Associated with Amyotrophic Lateral Sclerosis in Transgenic Mice Contain Primarily Full-length, Unmodified Superoxide Dismutase-1S

The Journal of biological chemistry, 2008-03, Vol.283 (13), p.8340-8350

2008

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Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form

Protein science, 1996-11, Vol.5 (11), p.2184-2192

1996

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Particles of photosystem 2 contain plantacyanin

Biochemical and biophysical research communications, 1990-04, Vol.168 (1), p.232-239

1990

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Studies on plantacyanin. III. Structural data obtained by CD and MCD methods and antigenic properties of the protein

Biochimica et biophysica acta, Protein structure and molecular enzymology, 1988-01, Vol.957 (3), p.446-453

1988

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Studies on plantacyanin. IV. Reconstitution with Cu-thionein, oxidation by cytochrome oxidase and autooxidation in the presence of cardiolipin

Biochimica et biophysica acta, Protein structure and molecular enzymology, 1991-01, Vol.1076 (3), p.337-342

1991

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Binding of a Single Zinc Ion to One Subunit of Copper−Zinc Superoxide Dismutase Apoprotein Substantially Influences the Structure and Stability of the Entire Homodimeric Protein

Destabilization of Apoprotein Is Insufficient to Explain Cu,Zn-Superoxide Dismutase-Linked ALS Pathogenesis

Detergent-insoluble Aggregates Associated with Amyotrophic Lateral Sclerosis in Transgenic Mice Contain Primarily Full-length, Unmodified Superoxide Dismutase-1

A Structure-Based Mechanism for Copper−Zinc Superoxide Dismutase

Local Unfolding in a Destabilized, Pathogenic Variant of Superoxide Dismutase 1 Observed with H/D Exchange and Mass Spectrometry

Spectroscopic Investigation of Stellacyanin Mutants: Axial Ligand Interactions at the Blue Copper Site

Copper(2+) Binding to the Surface Residue Cysteine 111 of His46Arg Human Copper−Zinc Superoxide Dismutase, a Familial Amyotrophic Lateral Sclerosis Mutant

Metal-free Superoxide Dismutase-1 and Three Different Amyotrophic Lateral Sclerosis Variants Share a Similar Partially Unfolded β-Barrel at Physiological Temperature

X-ray Absorption Edge and EXAFS Studies of the Blue Copper Site in Stellacyanin: Effects of Axial Amide Coordination

Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: Plant‐specific mononuclear blue copper proteins

Spectroscopic and Geometric Variations in Perturbed Blue Copper Centers: Electronic Structures of Stellacyanin and Cucumber Basic Protein

A missing link in cupredoxins: Crystal structure of cucumber stellacyanin at 1.6 Å resolution

Structural Information through NMR Hyperfine Shifts in Blue Copper Proteins

Subunit asymmetry in the three‐dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis

Cobalt(2+) Binding to Human and Tomato Copper Chaperone for Superoxide Dismutase: Implications for the Metal Ion Transfer Mechanism

Preliminary Characterization of Occipodins, Natural Product Anticoagulants from Hematophagous Marine Parasites, Isopod Elthusa vulgaris and Copepod Phrixocephalus Cincinnatus

X-ray Crystallographic and Analytical Ultracentrifugation Analyses of Truncated and Full-Length Yeast Copper Chaperones for SOD (LYS7): A Dimer−Dimer Model of LYS7−SOD Association and Copper Delivery

Metal-free Superoxide Dismutase-1 and Three Different Amyotrophic Lateral Sclerosis Variants Share a Similar Partially Unfolded Î²-Barrel at Physiological Temperature

Metal-free Superoxide Dismutase-1 and Three Different Amyotrophic Lateral Sclerosis Variants Share a Similar Partially Unfolded b-Barrel at Physiological Temperature

Blue copper-binding domains

Detergent-insoluble Aggregates Associated with Amyotrophic Lateral Sclerosis in Transgenic Mice Contain Primarily Full-length, Unmodified Superoxide Dismutase-1S

Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated form

Particles of photosystem 2 contain plantacyanin

Studies on plantacyanin. III. Structural data obtained by CD and MCD methods and antigenic properties of the protein

Studies on plantacyanin. IV. Reconstitution with Cu-thionein, oxidation by cytochrome oxidase and autooxidation in the presence of cardiolipin

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