A5024842195- Protein purification and stability
- Redox biology and oxidative stress
- Free Radicals and Antioxidants
- Mass Spectrometry Techniques and Applications
- Viral Infectious Diseases and Gene Expression in Insects
- Monoclonal and Polyclonal Antibodies Research
- Sulfur Compounds in Biology
- Nitric Oxide and Endothelin Effects
- Electron Spin Resonance Studies
- Radical Photochemical Reactions
- Mitochondrial Function and Pathology
- Advanced Proteomics Techniques and Applications
- Ion channel regulation and function
- Biochemical effects in animals
- Analytical Chemistry and Chromatography
- Endoplasmic Reticulum Stress and Disease
- Computational Drug Discovery Methods
- Photochemistry and Electron Transfer Studies
- Alzheimer's disease research and treatments
- Metal-Catalyzed Oxygenation Mechanisms
- DNA and Nucleic Acid Chemistry
- Chemical Synthesis and Analysis
- Muscle metabolism and nutrition
- Enzyme Structure and Function
- Insect and Pesticide Research
University of Kansas
2016-2025
ETH Zurich
2004-2014
Vanguard University
2009-2011
University of Arizona
1997-2011
Amgen (United States)
1997-2010
University of Notre Dame
1997-2009
Leibniz Institute of Surface Engineering
2007-2009
Instytut Chemii i Techniki Jądrowej
1997-2007
The Heart Research Institute
2007
Rzeszów University of Technology
2007
Neurodegeneration in familial amyotrophic lateral sclerosis (ALS) is associated with enhanced redox stress caused by dominant mutations superoxide dismutase–1 (SOD1). SOD1 a cytosolic enzyme that facilitates the conversion of (O2•–) to H2O2. Here we demonstrate not just catabolic enzyme, but can also directly regulate NADPH oxidase–dependent (Nox-dependent) O2•– production binding Rac1 and inhibiting its GTPase activity. Oxidation H2O2 uncoupled reversible fashion, producing self-regulating...
The accumulation of covalently modified proteins is an important hallmark biological aging, but relatively few studies have addressed the detailed molecular-chemical changes and processes responsible for modification specific protein targets. Recently, Narayanan et al. [Narayanan, Jones, Xu Yu (1996) Am. J. Physiol. 271, C1032-C1040] reported that effects aging on skeletal-muscle function are muscle-specific, with a significant age-dependent change in ATP-supported Ca2+-uptake activity...
Oxidation is one of the major chemical degradation pathways for protein pharmaceuticals. Methionine, cysteine, histidine, tryptophan, and tyrosine are amino acid residues most susceptible to oxidation due their high reactivity with various reactive oxygen species. during processing storage can be induced by contaminating oxidants, catalyzed presence transition metal ions light. Oxidative modification depends on structural features proteins as well particular mechanisms inherent in oxidative...
Skeletal muscle contraction and relaxation is efficiently modulated through the reaction of reactive oxygen−nitrogen species with sarcoplasmic reticulum protein thiols in vivo. However, exact locations functionally important modifications are at present unknown. Here, we determine by HPLC−MS that modification one (out 24) Cys residue (SR) Ca-ATPase isoform SERCA1, Cys349, peroxynitrite sufficient for modulation enzyme activity. Despite size nature SR Ca-ATPase, a 110 kDa membrane protein,...
Proteomic techniques were used to identify cardiac proteins from whole heart homogenate and mitochondria of Fisher 344/Brown Norway F1 rats, which suffer protein nitration as a consequence biological aging. Soluble young (5 mo old) old (26 animals separated by one- two-dimensional gel electrophoresis. One- Western blots with an anti-nitrotyrosine antibody show age-related increase in the immunoresponse few specific proteins, identified nanoelectrospray ionization-tandem mass spectrometry...
The pathogenesis of Alzheimer's disease is strongly associated with the formation and deposition β-amyloid peptide (βAP) in brain. This contains a methionine (Met) residue C-terminal domain, which important for its neurotoxicity propensity to reduce transition metals form reactive oxygen species. Theoretical studies have proposed βAP Met radical cations as intermediates, but no experimental evidence regard reactivity these species available, largely due insolubility peptide. To define...
The nitration of protein tyrosine residues represents an important post-translational modification during development, oxidative stress, and biological aging. To rationalize any physiological changes with such modifications, the actual targets must be identified by proteomic methods. While several studies have used proteomics to screen for 3-nitrotyrosine-containing proteins in vivo, most these failed prove unambiguously through localization 3-nitrotyrosine specific sequences mass...
Methionine sulfoxide (MetSO) in calmodulin (CaM) was previously shown to be a substrate for bovine liver peptide methionine reductase (pMSR, EC 1.8.4.6), which can partially recover protein structure and function of oxidized CaM vitro. Here, we report the first time that pMSR selectively reduces D ‐sulfoxide diastereomer CaM‐bound L ‐MetSO ( ‐Met‐ ‐SO). After exhaustive reduction by pMSR, ratio ‐SO decreased about 1:25 hydrogen peroxide‐oxidized CaM, 1:10 free MetSO. The accumulation MetSO...
Tyrosine hydroxylase (TH) is modified by nitration after exposure of mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydrophenylpyridine. The temporal association tyrosine with inactivation TH activity<i>in vitro</i> suggests that this covalent post-translational modification responsible for the <i>in vivo</i> loss function (Ara, J., Przedborski, S., Naini, A. B., Jackson-Lewis, V., Trifiletti, R. R., Horwitz, and Ischiropoulos, H. (1998)<i>Proc. Natl. Acad. Sci. U. S. A.</i> 95, 7659–7663). Recent...
The oxidative inactivation of rabbit skeletal muscle Ca 2+-ATPase in sarcoplasmic reticulum (SR) vesicles by peroxynitrite (ONOO−) was investigated. exposure SR (10 mg/ml protein) to low concentrations (≤0.2 mM) resulted a decrease Ca2+-ATPase activity primarily through oxidation sulf-hydryl groups. Most this deactivation (ca. 70%) could be chemically reversed subsequent reduction the enzyme with either dithiothreitol (DTT) or sodium borohydride (NaBH4), indicating that free cysteine groups...