E. B. Gralla

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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.

Bryan F. Shaw, A. Nersissian, J. Valentine, 2007, Journal of the American Chemical Society.

Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: A possible general mechanism for familial ALS

I. Bertini, J. Valentine, L. Banci, 2007, Proceedings of the National Academy of Sciences.

Delivering Copper Inside Yeast and Human Cells

J. Valentine, E. B. Gralla, 1997, Science.

Metalloprotein Ligand Redesign: Characterization of Copper-Cysteinate Proteins Derived from Yeast Copper-Zinc Superoxide Dismutase

J. Valentine, E. B. Gralla, Joan Selverstone Valentine, 1993 .

Copper-zinc superoxide dismutase and ALS.

J. Valentine, P. Hart, E. B. Gralla, 1999, Advances in experimental medicine and biology.

Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis.

J. Valentine, E. B. Gralla, C. Nishida, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells.

D. Borchelt, P. Wong, R. Gwinn, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein.

L. Ellerby, D. Bredesen, T. Lyons, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Null mutants of Saccharomyces cerevisiae Cu,Zn superoxide dismutase: characterization and spontaneous mutation rates

J. Valentine, E. B. Gralla, 1991, Journal of bacteriology.

Yeast lacking superoxide dismutase. Isolation of genetic suppressors.

J. Valentine, V. Culotta, P. Lapinskas, 1992, The Journal of biological chemistry.

Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase.

D. Thiele, L. Ellerby, J. Valentine, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Yeast Lacking Superoxide Dismutase(s) Show Elevated Levels of “Free Iron” as Measured by Whole Cell Electron Paramagnetic Resonance*

J. Valentine, J. Imlay, E. B. Gralla, 2000, The Journal of Biological Chemistry.

A Novel SOD1 Intermediate Oligomer, Role of Free Thiols and Disulfide Exchange

J. Valentine, J. Whitelegge, E. B. Gralla, 2021, Frontiers in Neuroscience.

Insights into the Role of the Unusual Disulfide Bond in Copper-Zinc Superoxide Dismutase*

Bryan F. Shaw, J. Valentine, P. Hart, 2014, The Journal of Biological Chemistry.

Copper and Zinc Metallation Status of Copper-Zinc Superoxide Dismutase from Amyotrophic Lateral Sclerosis Transgenic Mice*

D. Borchelt, J. Valentine, J. Whitelegge, 2010, The Journal of Biological Chemistry.

In vivo peroxidative activity of FALS-mutant human CuZnSODs expressed in yeast.

J. Valentine, J. J. Goto, E. B. Gralla, 2002, Free radical biology & medicine.

Loss of in Vitro Metal Ion Binding Specificity in Mutant Copper-Zinc Superoxide Dismutases Associated with Familial Amyotrophic Lateral Sclerosis*

A. Nersissian, J. Valentine, Haining Zhu, 2000, The Journal of Biological Chemistry.

Metabolic alterations in yeast lacking copper-zinc superoxide dismutase.

J. Valentine, V. Longo, E. B. Gralla, 2011, Free radical biology & medicine.

Induction of phenotypes resembling CuZn-superoxide dismutase deletion in wild-type yeast cells: an in vivo assay for the role of superoxide in the toxicity of redox-cycling compounds.

J. Valentine, J. Fukuto, E. B. Gralla, 2005, Chemical research in toxicology.

Only one of a wide assortment of manganese-containing SOD mimicking compounds rescues the slow aerobic growth phenotypes of both Escherichia coli and Saccharomyces cerevisiae strains lacking superoxide dismutase enzymes.

J. Valentine, J. Imlay, A. Durazo, 2007, Journal of inorganic biochemistry.

Exogenous manganous ion at millimolar levels rescues all known dioxygen-sensitive phenotypes of yeast lacking CuZnSOD

J. Valentine, E. B. Gralla, William H. Munroe, 2005, JBIC Journal of Biological Inorganic Chemistry.

Autoxidation of ubiquinol-6 is independent of superoxide dismutase.

L. Ellerby, J. Valentine, C. Clarke, 1996, Biochemistry.

A pH Switch Controls Zinc Binding in Tomato Copper-Zinc Superoxide Dismutase.

S. T. Thomas, J. Valentine, P. Hart, 2021, Biochemistry.

Cell death mechanisms in ALS

L. Ellerby, D. Bredesen, J. Valentine, 1996, Neurology.

A new SOD mimic, Mn(III) ortho N-butoxyethylpyridylporphyrin, combines superb potency and lipophilicity with low toxicity.

I. Batinic-Haberle, H. Sheng, D. Warner, 2012, Free radical biology & medicine.

Superoxide Inhibits 4Fe-4S Cluster Enzymes Involved in Amino Acid Biosynthesis

J. Valentine, V. Longo, E. B. Gralla, 2004, Journal of Biological Chemistry.

Measurement of "free" or electron paramagnetic resonance-detectable iron in whole yeast cells as indicator of superoxide stress.

E. B. Gralla, C. Srinivasan, 2002, Methods in enzymology.

Metal ion reconstitution studies of yeast copper-zinc superoxide dismutase: the "phantom" subunit and the possible role of Lys7p

T. Lyons, A. Nersissian, J. Valentine, 1998, JBIC Journal of Biological Inorganic Chemistry.

ACE1,acopper-dependent transcription factor, activates expression oftheyeast copper, zincsuperoxide dismutase gene (gene expression/oxygen toxicity/metal regulation)

J. Valentine, E. B. Gralla, 1991 .

Copper-Zinc Superoxide Dismutase: Mechanistic and Biological Studies

L. Ellerby, J. Valentine, E. B. Gralla, 1995 .

Manganous phosphate acts as a superoxide dismutase.

J. Valentine, E. B. Gralla, D. Cabelli, 2008, Journal of the American Chemical Society.

The copper, zinc-superoxide dismutase gene of Saccharomyces cerevisiae: cloning, sequencing, and biological activity.

J. Valentine, E. B. Gralla, O. Bermingham-McDonogh, 1988, Proceedings of the National Academy of Sciences of the United States of America.

Biologically relevant mechanism for catalytic superoxide removal by simple manganese compounds

J. Valentine, E. B. Gralla, D. Cabelli, 2012, Proceedings of the National Academy of Sciences.

Mitochondrial superoxide decreases yeast survival in stationary phase.

J. Valentine, V. Longo, E. B. Gralla, 1999, Archives of biochemistry and biophysics.

Yeast copper–zinc superoxide dismutase can be activated in the absence of its copper chaperone

J. Valentine, A. Durazo, E. B. Gralla, 2013, JBIC Journal of Biological Inorganic Chemistry.

Molecular genetics of superoxide dismutases in yeasts and related fungi.

D. Kosman, E. B. Gralla, Edith Butler Gralla, 1992, Advances in genetics.

The dark side of dioxygen biochemistry.

T. Lyons, J. Valentine, J. J. Goto, 1998, Current opinion in chemical biology.

Copper-containing proteins

J. Valentine, E. B. Gralla, 2002 .

The redesign of a type 2 into a type 1 copper protein: construction and characterization of yeast copper, zinc superoxide dismutase mutants

Yunfeng Lu, J. Valentine, Yunfeng Lu, 1992 .

Reactions of Hydrogen Peroxide with Familial Amyotrophic Lateral Sclerosis Mutant Human Copper-Zinc Superoxide Dismutases Studied by Pulse Radiolysis*

J S Valentine, J. Valentine, J. J. Goto, 1998, The Journal of Biological Chemistry.

Altered Reactivity of Superoxide Dismutase in Familial Amyotrophic Lateral Sclerosis

D. Bredesen, J. Valentine, S. Rabizadeh, 1996, Science.

Comparison of two yeast MnSODs: mitochondrial Saccharomyces cerevisiae versus cytosolic Candida albicans.

J. Valentine, D. Cascio, R. D. Britt, 2011, Journal of the American Chemical Society.

Investigation of the highly active manganese superoxide dismutase from Saccharomyces cerevisiae.

J. Valentine, R. D. Britt, T. A. Stich, 2010, Journal of the American Chemical Society.

Tetramerization Reinforces the Dimer Interface of MnSOD

J. Valentine, D. Cascio, A. Durazo, 2013, PloS one.

Superoxide Dismutase Activity Is Essential for Stationary Phase Survival in Saccharomyces cerevisiae

J S Valentine, J. Valentine, V. Longo, 1996, The Journal of Biological Chemistry.

Radioprotective effects of manganese-containing superoxide dismutase mimics on ataxia-telangiectasia cells.

J. Valentine, R. Gatti, I. Batinic-Haberle, 2009, Free radical biology & medicine.

Probing in vivo Mn2+ speciation and oxidative stress resistance in yeast cells with electron-nuclear double resonance spectroscopy

J. Valentine, V. Culotta, Ajay Sharma, 2010, Proceedings of the National Academy of Sciences.

Bcl-2 inhibition of neural death: decreased generation of reactive oxygen species.

D. Bredesen, J. Valentine, E. B. Gralla, 1993, Science.

Superoxide is a mediator of an altruistic aging program in Saccharomyces cerevisiae

A. Diaspro, V. Longo, E. B. Gralla, 2004, The Journal of cell biology.

SOD2 functions downstream of Sch9 to extend longevity in yeast.

A. Diaspro, J. Valentine, V. Longo, 2003, Genetics.

Human Bcl-2 Reverses Survival Defects in Yeast Lacking Superoxide Dismutase and Delays Death of Wild-Type Yeast

L. Ellerby, D. Bredesen, J. Valentine, 1997, The Journal of cell biology.

Superoxide Dismutase: Studies in the Yeast Saccharomyces cerevisiae

E. B. Gralla, 1997 .

Copper(2+) binding to the surface residue cysteine 111 of His46Arg human copper-zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant.

J S Valentine, H. Zhu, J. Valentine, 2000, Biochemistry.

New Type 2 Copper-Cysteinate Proteins. Copper Site Histidine-to-Cysteine Mutants of Yeast Copper-Zinc Superoxide Dismutase.

Ivano Bertini, Lucia Banci, Christopher J. Bender, 1996, Inorganic chemistry.

ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene.

D. Thiele, J. Valentine, E. B. Gralla, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Yeast Lacking Cu-Zn Superoxide Dismutase Show Altered Iron Homeostasis

J. Valentine, E. B. Gralla, R. Meneghini, 2000, The Journal of Biological Chemistry.

Initiation and elongation in fibrillation of ALS-linked superoxide dismutase

Julian P. Whitelegge, Armando Durazo, J. Valentine, 2008, Proceedings of the National Academy of Sciences.

Cellular role of yeast Apn1 apurinic endonuclease/3'-diesterase: repair of oxidative and alkylation DNA damage and control of spontaneous mutation

E. B. Gralla, B. Demple, D. Ramotar, 1991, Molecular and cellular biology.

D. Borchelt, J. Valentine, J. Whitelegge, 2013, Proceedings of the National Academy of Sciences.

Superoxide dismutase 1 modulates expression of transferrin receptor

C. Crosio, A. Ludolph, J. Valentine, 2006, JBIC Journal of Biological Inorganic Chemistry.

Differential localization and potency of manganese porphyrin superoxide dismutase-mimicking compounds in Saccharomyces cerevisiae

J. Valentine, I. Batinic-Haberle, I. Spasojević, 2014, Redox biology.

Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials

C. Crosio, J. Valentine, G. Rotilio, 2006, Proceedings of the National Academy of Sciences.

Construction of a blue copper site at the native zinc site of yeast copper-zinc superoxide dismutase

Edward I. Solomon, Michael D. Lowery, Christopher J. Bender, 1993 .

Time dependence of the frequency and amplitude of the local nanomechanical motion of yeast.

James K Gimzewski, J. Gimzewski, E. B. Gralla, 2005, Nanomedicine : nanotechnology, biology, and medicine.

Local Nanomechanical Motion of the Cell Wall of Saccharomyces cerevisiae

Andrew E. Pelling, James K. Gimzewski, J. Gimzewski, 2004, Science.

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

Bryan F. Shaw, D. Borchelt, A. Nersissian, 2008, Journal of Biological Chemistry.

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

Matteo Pellegrini, David Eisenberg, D. Eisenberg, 1998, Protein science : a publication of the Protein Society.

The interaction of nitric oxide (NO) with the yeast transcription factor Ace1: A model system for NO-protein thiol interactions with implications to metal metabolism.

D. Thiele, J. Valentine, C. Switzer, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Biological chemistry of copper-zinc superoxide dismutase and its link to amyotrophic lateral sclerosis.

T. Lyons, J. Valentine, E. B. Gralla, 1999, Metal ions in biological systems.

BIOCHEMISTRY: Delivering Copper Inside Yeast and Human Cells

J. Valentine, E. B. Gralla, 1997 .

The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation*

J. Valentine, J. Whitelegge, E. B. Gralla, 2015, The Journal of Biological Chemistry.

Accumulation of Porphyrin-based SOD Mimics in Mitochondria is Proportional to Their Lipophilicity: S. cerevisiae Study of ortho Mn(III) N-alkylpyridylporphyrins

J. Valentine, I. Batinic-Haberle, I. Spasojević, 2010 .

The metal binding properties of the zinc site of yeast copper-zinc superoxide dismutase: implications for amyotrophic lateral sclerosis

T. Lyons, A. Nersissian, J. Valentine, 2000, JBIC Journal of Biological Inorganic Chemistry.

Evidence for a Novel Role of Copper-Zinc Superoxide Dismutase in Zinc Metabolism*

J. Valentine, E. B. Gralla, C. Srinivasan, 2001, The Journal of Biological Chemistry.

Cobalt(2+) binding to human and tomato copper chaperone for superoxide dismutase: implications for the metal ion transfer mechanism.

H. Zhu, J. Valentine, P. Hart, 2000, Biochemistry.

Effects of nitric oxide on the copper-responsive transcription factor Ace1 in Saccharomyces cerevisiae: cytotoxic and cytoprotective actions of nitric oxide.

D. Thiele, J. Valentine, C. Switzer, 2000, Archives of biochemistry and biophysics.

A new SOD mimic, Mn(III) ortho N-butoxyethylpyridylporphyrin, combines superb potency and lipophilicity with low toxicity.

I. Batinic-Haberle, H. Sheng, D. Warner, 2012, Free radical biology & medicine.

Superoxide Inhibits 4Fe-4S Cluster Enzymes Involved in Amino Acid Biosynthesis

J. Valentine, V. Longo, E. B. Gralla, 2004, Journal of Biological Chemistry.