Research Topics
| JOAN VALENTINESummaryAffiliation: University of California Country: USA Publications
Research Grants
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Detail Information
Publications
Copper-zinc superoxide dismutase and amyotrophic lateral sclerosisJoan Selverstone Valentine
Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095 1569, USA
Annu Rev Biochem 74:563-93. 2005....- Cloning, expression, and spectroscopic characterization of Cucumis sativus stellacyanin in its nonglycosylated formA M Nersissian
Department of Chemistry and Biochemistry, UCLA 90095, USA
Protein Sci 5:2184-92. 1996.... - The dark side of dioxygen biochemistryJ S Valentine
Department of Chemistry and Biochemistry, UCLA, Los Angeles, CA 90095 1569, USA
Curr Opin Chem Biol 2:253-62. 1998..These reactive oxygen species have historically been perceived almost exclusively as agents of the dark side, but it has recently become clear that they play beneficial roles as well... - Reactive oxygen species special featureJoan Selverstone Valentine
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-1569, USA
Proc Natl Acad Sci U S A 105:8178. 2008 - Do oxidatively modified proteins cause ALS?Joan Selverstone Valentine
Department of Chemistry and Biochemistry, University of California at Los Angeles, Los Angeles, CA 90095 1569, USA
Free Radic Biol Med 33:1314-20. 2002.... - Misfolded CuZnSOD and amyotrophic lateral sclerosisJoan Selverstone Valentine
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90025 1569, USA
Proc Natl Acad Sci U S A 100:3617-22. 2003.... - Initiation and elongation in fibrillation of ALS-linked superoxide dismutaseMadhuri Chattopadhyay
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA
Proc Natl Acad Sci U S A 105:18663-8. 2008..Our findings provide a rare glimpse into the specific changes in a protein that can lead to nucleation and into the ability of amyloid nuclei to recruit diverse forms of the same protein into fibrils... - Metal-free superoxide dismutase-1 and three different amyotrophic lateral sclerosis variants share a similar partially unfolded beta-barrel at physiological temperatureArmando Durazo
Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095, USA
J Biol Chem 284:34382-9. 2009..e. beta3 and beta4, residues 21-53). Together, these results show that human wild-type apo-SOD1 and variants have a partially unfolded beta-barrel at physiological temperature and unfold non-cooperatively... - Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALSMadhuri Chattopadhyay
Department of Chemistry and Biochemistry, University of California, Los Angeles, California, USA
Antioxid Redox Signal 11:1603-14. 2009..We here review the recent research on the significance, causes, and mechanisms of SOD1 fibril formation from a biophysical perspective... - 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 proteinSoshanna Zittin Potter
Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, CA 90095, USA
J Am Chem Soc 129:4575-83. 2007..The relevance of these findings to amyotrophic lateral sclerosis is discussed... - Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometryBryan Francis Shaw
Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, CA 90095, USA
J Biol Chem 281:18167-76. 2006..These local and global unfolding events could facilitate intermolecular protein-protein interactions that cause the aggregation or neurotoxicity of A4V SOD1... - In vivo peroxidative activity of FALS-mutant human CuZnSODs expressed in yeastJames A Roe
Department of Chemistry and Biochemistry, Loyola Marymount University, Los Angeles, CA 90045 8225, USA
Free Radic Biol Med 32:169-74. 2002..This study also presents an in vivo model system to study free radical production in FALS-associated CuZnSOD mutations... - How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein?Bryan F Shaw
Department of Chemistry and Biochemistry, University of California Los Angeles, Los Angeles, CA 90095, USA
Trends Biochem Sci 32:78-85. 2007..Thus, it seems likely that different ALS-associated mutations promote SOD1 aggregation by fundamentally distinct mechanisms. Understanding this complexity has implications for drug development and treatment of the disease... - Exogenous manganous ion at millimolar levels rescues all known dioxygen-sensitive phenotypes of yeast lacking CuZnSODRaylene J Sanchez
Department of Chemistry and Biochemistry, UCLA, 607 Charles E. Young Drive, East, Los Angeles, CA 90095-1569, USA
J Biol Inorg Chem 10:913-23. 2005..Mechanisms by which ionic manganese can effect this rescue, while the mimetic compounds do not, are discussed... - 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 compoundsMatthew Alan Wallace
Department of Chemistry and Biochemistry, University of California, Los Angeles, 607 Charles E. Young Drive East, Los Angeles, California 90095-1569, USA
Chem Res Toxicol 18:1279-86. 2005..Using this method, we analyzed the Parkinsonism-inducing compound 1-methyl-4-phenylpyridinium and found that redox cycling and superoxide toxicity are not the predominant factor in its toxic mechanism... - Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesisJorge A Rodriguez
Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA
Proc Natl Acad Sci U S A 102:10516-21. 2005..Thus, the ALS mutant Cu,Zn-superoxide dismutase apoproteins do not all share reduced global stability, and additional properties must be identified and understood to explain the toxicity of all of the mutant proteins... - The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease)Soshanna Zittin Potter
Department of Chemistry and Biochemistry, UCLA, Los Angeles, CA 90095 1569, USA
J Biol Inorg Chem 8:373-80. 2003..Results and implications of the role of CuZnSOD in FALS are discussed... - Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stabilityPeter A Doucette
Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095, USA
J Biol Chem 279:54558-66. 2004..By combining the sedimentation data with previous crystallographic results, a molecular explanation is provided for the existence of different SOD1 macromolecular shapes and multiple SOD1 dimeric species with different stabilities... - SOD2 functions downstream of Sch9 to extend longevity in yeastPaola Fabrizio
Andrus Gerontology Center and Department of Biological Sciences, University of Southern California, Los Angeles, California 90089 0191, USA
Genetics 163:35-46. 2003..cerevisiae to superoxide dismutases and suggest that the induction of other stress-resistance genes regulated by Msn2/4 and Rim15 is required for maximum longevity extension... - 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 enzymesWilliam Munroe
Department of Chemistry and Biochemistry, UCLA, Los Angeles, CA 90095 1569, USA
J Inorg Biochem 101:1875-82. 2007..Our results suggest the possibility that the beneficial effects of some of the so-called "SOD mimic drugs" may be due to some property other than in vivo superoxide dismutase activity... - Superoxide inhibits 4Fe-4S cluster enzymes involved in amino acid biosynthesis. Cross-compartment protection by CuZn-superoxide dismutaseMatthew Alan Wallace
Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095-1569, USA
J Biol Chem 279:32055-62. 2004..Thus, we conclude that when Sod1p is absent a lysine auxotrophy is induced because Lys4p is inactivated in the matrix by superoxide that originates in the intermembrane space and diffuses across the inner membrane... - Manganous phosphate acts as a superoxide dismutaseKevin Barnese
Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095 1569, USA
J Am Chem Soc 130:4604-6. 2008.... - Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant His46ArgSvetlana Antonyuk
Molecular Biophysics Group, CCLRC Daresbury Laboratory, Warrington, Cheshire, WA4 4AD, UK
Protein Sci 14:1201-13. 2005.... - SOD1 and amyotrophic lateral sclerosis: mutations and oligomerizationLucia Banci
Magnetic Resonance Center CERM, Department of Chemistry, University of Florence, Florence, Italy
PLoS ONE 3:e1677. 2008..The mechanism here proposed for SOD1 mutant oligomerization is absolutely general and it provides a common unique picture for the behaviors of the many SOD1 mutants, of different nature and distributed all over the protein... - Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosisXiaohang Cao
Department of Biochemistry and the X ray Crystallography Core Laboratory, The University of Texas Health Ssience Center, San Antonio, Texas 78229, USA
J Biol Chem 283:16169-77. 2008..These findings support the notion that metal-deficient and/or disulfide-reduced mutant SOD1 species contribute to toxicity in SOD1-linked amyotrophic lateral sclerosis... - Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosisLawrence J Hayward
Department of Neurology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA
J Biol Chem 277:15923-31. 2002..Further characterization of these as-isolated SOD1 proteins may provide new insights regarding mutant SOD1 enzyme toxicity in ALS... - Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALSJennifer Stine Elam
Department of Biochemistry and the Center for Biomolecular Structure Analysis, The University of Texas, Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, Texas 78229 3900, USA
Nat Struct Biol 10:461-7. 2003..Loss of this protection through conformational rearrangement in the metal-deficient enzyme could be a toxic property common to mutants of SOD1 linked to FALS... - Metalation of the amyotrophic lateral sclerosis mutant glycine 37 to arginine superoxide dismutase (SOD1) apoprotein restores its structural and dynamical properties in solution to those of metalated wild-type SOD1Lucia Banci
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 46:9953-62. 2007..These results suggest further that it is the metal-free apo forms of the mutant SOD1 protein that are the agents of its toxicity... - Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALSLucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Italy
Proc Natl Acad Sci U S A 104:11263-7. 2007..Although we cannot exclude other mechanisms in SOD1-linked familial ALS, the one proposed here has the strength of explaining how a large and diverse set of SOD1 mutant proteins all could lead to disease through the same mechanism... - An alternative mechanism of bicarbonate-mediated peroxidation by copper-zinc superoxide dismutase: rates enhanced via proposed enzyme-associated peroxycarbonate intermediateJennifer Stine Elam
Department of Biochemistry and the X ray Crystallography Core Laboratory, University of Texas Health Science Center, San Antonio, Texas 78229 3900, USA
J Biol Chem 278:21032-9. 2003..The orientation of the enzyme-associated oxyanion suggests that both the self-oxidative and external oxidative pathways can proceed through an enzyme-associated peroxycarbonate intermediate... - Mechanisms for activating Cu- and Zn-containing superoxide dismutase in the absence of the CCS Cu chaperoneMark C Carroll
Department of Environmental Health Sciences, Bloomberg School of Public Health, The Johns Hopkins University, Baltimore, MD 21218, USA
Proc Natl Acad Sci U S A 101:5964-9. 2004..The possible implications of multiple pathways for SOD1 activation are discussed in the context of SOD1 evolutionary biology and familial amyotrophic lateral sclerosis... - Mutations in Saccharomyces cerevisiae iron-sulfur cluster assembly genes and oxidative stress relevant to Cu,Zn superoxide dismutaseLaran T Jensen
Department of Environmental Health Sciences, Johns Hopkins University, Bloomberg School of Public Health, Baltimore, Maryland 21205, USA
J Biol Chem 279:29938-43. 2004..By comparison, the sod1Delta lysine auxotrophy appears to be reversed in the seo mutants by increased expression of genes in the lysine biosynthetic pathway, perhaps through sensing of mitochondrial damage by the retrograde response... - Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymesRichard W Strange
Molecular Biophysics Group, CCLRC Daresbury Laboratory, Warrington, Cheshire WA4 4AD, UK
J Mol Biol 356:1152-62. 2006..These data raise the possibility that in a cellular environment with low availability of free copper, Zn-Zn may be the preferred metallation state of SOD1 prior to its interaction with the copper chaperone... - Fully metallated S134N Cu,Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solutionLucia Banci
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
J Biol Chem 280:35815-21. 2005..We have here also established that the two free cysteines (6 and 111) do not play a role in this behavior... - Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosisEric L Shipp
Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 42:1890-9. 2003..Alternatively, a motor neuron-specific substrate may bind this region of the protein, leading to deleterious modifications and/or reactions... - Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentialsAlberto Ferri
Institute of Neuroscience, Department of Psychobiology and Psychopharmacology, Consiglio Nazionale delle Ricerche, 00100 Rome, Italy
Proc Natl Acad Sci U S A 103:13860-5. 2006.... - Superoxide dismutase 1 modulates expression of transferrin receptorRuth Danzeisen
Department of Neurology, University of Ulm, Ulm, Germany
J Biol Inorg Chem 11:489-98. 2006..We propose that changes in superoxide levels due to alteration of SOD1 activity affect iron metabolism in glial and neuronal cells from higher eukaryotes and that this may be relevant to diseases of the nervous system... - Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutantsMichael A Hough
Molecular Biophysics Group, Council for the Central Laboratory of the Research Councils, Daresbury Laboratory, Warrington, Cheshire WA4 4AD, United Kingdom
Proc Natl Acad Sci U S A 101:5976-81. 2004....
Research Grants
- FUNCTIONAL STUDIES OF CYTOSOLIC ANTIOXIDANT PROTEINSJoan Selverstone Valentine; Fiscal Year: 2010..Together, these studies will shed light on the complex interactions of small molecules and proteins that all eukaryotes use to protect their mitochondria from superoxide-mediated damage. ..
- FUNCTIONAL STUDIES OF CYTOSOLIC ANTIOXIDANT PROTEINSJOAN VALENTINE; Fiscal Year: 2001..The roles played by the different metal ions will also be examined in yeast model systems designed to investigate processes related to aging, cell death and disease. ..
- HISTIDYL IMIDAZOLE LIGAND IN METALLOPROTEINSJOAN VALENTINE; Fiscal Year: 2001..Finally, new metalloproteins will be designed, based on CuZn SOD and stellacyanin. They will be prepared using site-directed mutagenesis, expressed, and purified and their new properties will be characterized. ..
- Molecular Mechanisms of SOD1-linked ALS (P01)JOAN VALENTINE; Fiscal Year: 2007..Through our combined efforts we will be able to define structure and disease-function relationships at an unprecedented level. ..
- FUNCTIONAL STUDIES OF CYTOSOLIC ANTIOXIDANT PROTEINSJOAN VALENTINE; Fiscal Year: 2007..Together, these studies will shed light on the complex interactions of small molecules and proteins that all eukaryotes use to protect their mitochondria from superoxide-mediated damage. ..
- THE HISTIDYL IMIDAZOLE LIGAND IN METALLOPROTEINSJOAN VALENTINE; Fiscal Year: 2005....
- FUNCTIONAL STUDIES OF CYTOSOLIC ANTIOXIDANT PROTEINSJOAN VALENTINE; Fiscal Year: 2005....
- FUNCTIONAL STUDIES OF CYTOSOLIC ANTIOXIDANT PROTEINSJOAN VALENTINE; Fiscal Year: 1993..We believe that our results will be highly relevant to some of the fundamental processes that lead to cancer...
- THE HISTIDYL IMIDAZOLE LIGAND IN METALLOPROTEINSJOAN VALENTINE; Fiscal Year: 1980..Such information about superoxide dismutase may facilitate development of new treatments for disorders which are believed to involve superoxide anion such as rheumatoid arthritis...
- THE HISTIDYL IMIDAZOLE LIGAND IN METALLOPROTEINSJOAN VALENTINE; Fiscal Year: 1993..Information gained from this project will add to our understanding of the mechanism of reactions of CuZnSOD and of its physical properties as well as of metalloproteins in general...