Research Topics
Genomes and Genes | R L LevineSummaryAffiliation: National Institutes of Health Country: USA Publications
| Collaborators
|
Detail Information
Publications
Methionine residues as endogenous antioxidants in proteinsR L Levine
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892 0320, USA
Proc Natl Acad Sci U S A 93:15036-40. 1996..Furthermore, the susceptible residues were physically arranged in an array that guarded the entrance to the active site...
Methionine residues may protect proteins from critical oxidative damageR L Levine
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892 0320, USA
Mech Ageing Dev 107:323-32. 1999..Given the importance of oxidative stress during aging, the potential function of methionine residues as antioxidants during aging should be investigated experimentally...- Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanismEarl R Stadtman
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892 8012, USA
Mol Cell Biochem 234:3-9. 2002..Deletion of the msrA gene in mice leads to increased sensitivity to oxidative stress and to a decrease (40%) in the maximum lifespan. This suggests that elimination of both Msr's would have more serious consequences... - Oxidation of methionine residues of proteins: biological consequencesEarl R Stadtman
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892 8012, USA
Antioxid Redox Signal 5:577-82. 2003..In addition, a decrease in Msr activities in brain tissues is associated with the development of Alzheimer's disease... - Transcriptional profiling of MnSOD-mediated lifespan extension in Drosophila reveals a species-general network of aging and metabolic genesChristina Curtis
Molecular and Computational Biology Program, Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089 1340, USA
Genome Biol 8:R262. 2007..One question is whether these manipulations function through different mechanisms, or whether they intersect on common processes affecting aging... - Carbonyl modified proteins in cellular regulation, aging, and diseaseRodney L Levine
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892 0312, USA
Free Radic Biol Med 32:790-6. 2002..The molecular deficiencies that cause accumulation of oxidatively modified proteins are not identified, but regardless of cause, the accumulation is likely to disrupt normal cellular function... - Fixation of nitrogen in an electrospray mass spectrometerRodney L Levine
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD 20892 0812, USA
Rapid Commun Mass Spectrom 20:1828-30. 2006..The product is an iron nitride ion, [N(2)FeOH](1+), m/z 100.9438, and is capable of addition to peptides and proteins... - Commentary on "Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death" by D.A. Bota, J.K. Ngo, and K.J.A. DaviesRodney L Levine
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD, USA
Free Radic Biol Med 38:1445-6. 2005 - Oxidation of methionine in proteins: roles in antioxidant defense and cellular regulationR L Levine
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892 0320, USA
IUBMB Life 50:301-7. 2000..Interconversion of methionine and methionine sulfoxide can function to regulate the biological activity of proteins, through alteration in catalytic efficiency and through modulation of the surface hydrophobicity of the protein... - Oxidative modification of proteins during agingR L Levine
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, 50 South Drive, Bethesda, MD 20892 0812, USA
Exp Gerontol 36:1495-502. 2001..Oxidized proteins bearing carbonyl groups are generally dysfunctional, and in the last third of lifespan the content of these oxidized proteins rises to a level likely to cause substantial disruption of cellular function... - Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteinsJ R Requena
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Building 3, Room 222, 3 Center Drive, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 98:69-74. 2001.... - Copper-catalyzed oxidation of the recombinant SHa(29-231) prion proteinJ R Requena
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, 50 South Drive, Room 2351 MSC 8012, Bethesda, MD 20892 8012, USA
Proc Natl Acad Sci U S A 98:7170-5. 2001..These findings indicate that PrP, a copper-binding protein, may be particularly susceptible to metal-catalyzed oxidation and that oxidation triggers an extensive structural transition leading to aggregation... - Antioxidant activity of Ferrozine-iron-amino acid complexesB S Berlett
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Building 3, Room 222, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 98:451-6. 2001..p. These results suggest that identification of a physiological chelator that can replace Ferrozine in amino acid-iron complexes might have important physiological and pharmacological applications... - Thiols mediate superoxide-dependent NADH modification of glyceraldehyde-3-phosphate dehydrogenaseJ Rivera-Nieves
Pulmonary Critical Care Medicine Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 274:19525-31. 1999..This thiol linkage was stable to HgCl2. Thus, linkage of GAPDH to NADH, in contrast to NAD, occurs in the presence of thiol, is independent of NO, and is mediated by superoxide... - Carbonic anhydrase III: the phosphatase activity is extrinsicG Kim
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Arch Biochem Biophys 377:334-40. 2000.... - Protein oxidationE R Stadtman
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892 0320, USA
Ann N Y Acad Sci 899:191-208. 2000..Accumulation of modified proteins disrupts cellular function either by loss of catalytic and structural integrity or by interruption of regulatory pathways... - MDP-1: A novel eukaryotic magnesium-dependent phosphataseJ D Selengut
Laboratory of Biochemistry, National Heart Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892 0320, USA
Biochemistry 39:8315-24. 2000..In recognition of these observations, the enzyme has been given the name magnesium-dependent phosphatase-1 (MDP-1)... - Recent advances in the analysis of oxidized proteinsJ R Requena
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland, USA
Amino Acids 25:221-6. 2003.... - Thioredoxin converts the Syrian hamster (29-231) recombinant prion protein to an insoluble formJ R Requena
Laboratory of Biochemistry, NHLBI, National Institutes of Health, Bethesda, MD 20892, USA
Free Radic Biol Med 30:141-7. 2001..The thioredoxin/thioredoxin reductase system is approximately 7000 times more efficient than dithiothreitol... - Nucleotide sequence and structure of the mouse carbonic anhydrase III geneG Kim
Laboratory of Biochemistry, National Heart Lung and Blood Institute, National Institutes of Health, 20892 0320, Bethesda, MD, USA
Gene 265:37-44. 2001..5 kb. The 5' flanking region of the genomic DNA is notable for a pyrimidine rich region consisting of two dinucleotide repeats containing 23 and 20 TC pairs separated by the same 15 bp spacer... - Iron-dependent oxidation, ubiquitination, and degradation of iron regulatory protein 2: implications for degradation of oxidized proteinsK Iwai
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892 5430, USA
Proc Natl Acad Sci U S A 95:4924-8. 1998..Selective targeting and removal of oxidatively modified proteins may contribute to the turnover of many proteins that are degraded by the proteasome... - Free radical-mediated oxidation of free amino acids and amino acid residues in proteinsE R Stadtman
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892 8012, USA
Amino Acids 25:207-18. 2003.... - HIV-2 protease is inactivated after oxidation at the dimer interface and activity can be partly restored with methionine sulphoxide reductaseD A Davis
HIV and AIDS Malignancy Branch, National Cancer Institute, 9000 Rockville Pike, National Institutes of Health, Bethesda, MD 20892 1906, USA
Biochem J 346:305-11. 2000.... - Loss of the ataxia-telangiectasia gene product causes oxidative damage in target organsC Barlow
Laboratory of Genetic Disease Research, National Human Genome Research Institute, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 96:9915-9. 1999..These observations provide a mechanistic basis for the A-T phenotype and lay a rational foundation for therapeutic intervention... - Why have cells selected reactive oxygen species to regulate cell signaling events?E R Stadtman
Laboratory of Biochemistry, NHLBI NIH, Bethesda, Maryland 20892 8012, USA
Hum Exp Toxicol 21:83. 2002..This raises the question: If ROS are so damaging to cells, why have cells selected ROS to trigger activation of so many cell signaling pathways?.. - Modulation of the hydrophobicity of glutamine synthetase by mixed-function oxidationJ Cervera
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, Maryland 20892
FASEB J 2:2591-5. 1988..Thus, oxidative modification modulates the surface hydrophobicity of glutamine synthetase, and this modulation can control susceptibility to proteolysis... - Modification of the ADP-ribosyltransferase and NAD glycohydrolase activities of a mammalian transferase (ADP-ribosyltransferase 5) by auto-ADP-ribosylationB Weng
Pulmonary Critical Care Medicine Branch, NHLBI, National Institutes of Health, Bethesda, Maryland 20892 1434, USA
J Biol Chem 274:31797-803. 1999..These findings suggest that auto-ADP-ribosylation of ART5 was stoichiometric, resulted in at least two modifications and converted ART5 from an NADase to a transferase, and could be one mechanism for regulating enzyme activity... - The phosphatase activity of carbonic anhydrase III is reversibly regulated by glutathiolationE Cabiscol
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892 0320, USA
Proc Natl Acad Sci U S A 93:4170-4. 1996..Thus, glutathiolation is a reversible covalent modification that can regulate CAIII, a phosphatase that may function in the cellular response to oxidative stress... - Group B Streptococcus, phospholipids and pulmonary hypertensionJ Curtis
Office of Graduate Medical Education and Department of Pediatrics, Uniformed Services University of the Health Sciences, Bethesda, MD 20892, USA
J Perinatol 31:S24-8. 2011..Group B Streptococcus is the most common cause of bacterial infection in the newborn. Our aim was to purify and identify molecules produced by the bacterium, which cause pulmonary hypertension... - Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liverS R Lee
Laboratory of Cell Signaling, NHLBI, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 274:4722-34. 1999.... - Myristoylated methionine sulfoxide reductase A protects the heart from ischemia-reperfusion injuryHang Zhao
Laboratory of Biochemistry, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892 8012, USA
Am J Physiol Heart Circ Physiol 301:H1513-8. 2011..We conclude that cytosolic MsrA protects the heart from ischemia-reperfusion damage. The requirement for myristoylation suggests that MsrA must interact with a hydrophobic domain to provide protection... - Reversible oxidation of HIV-2 proteaseDavid A Davis
HIV and AIDS Malignancy Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Methods Enzymol 348:249-59. 2002 - Detection and affinity purification of oxidant-sensitive proteins using biotinylated glutathione ethyl esterDaniel M Sullivan
Laboratory of Molecular Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Methods Enzymol 353:101-13. 2002 - Metal-catalyzed oxidation of the Werner syndrome protein causes loss of catalytic activities and impaired protein-protein interactionsJeanine A Harrigan
Laboratory of Molecular Gerontology, NIA, National Institutes of Health, Baltimore, Maryland 21224, USA
J Biol Chem 282:36403-11. 2007.... - Iron regulatory protein 2 as iron sensor. Iron-dependent oxidative modification of cysteineDae-Kyung Kang
Laboratory of Biochemistry, NHLBI, National Institutes of Health and the Cell Biology and Metabolism Branch, NICHD, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 278:14857-64. 2003..One cysteine residue is oxidized to dehydrocysteine and other products. This covalent modification may thus mark the protein molecule for degradation by the proteasome system... - Metal-catalyzed oxidation of alpha-synuclein: helping to define the relationship between oligomers, protofibrils, and filamentsNelson B Cole
Genetic Diseases Research Branch, National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 280:9678-90. 2005.... - Oxidation of methionine residues in the prion protein by hydrogen peroxideJesús R Requena
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA
Arch Biochem Biophys 432:188-95. 2004..The high number of solvent exposed methionine residues in PrP suggests their possible role as protective endogenous antioxidants... - Methionine oxidation and agingEarl R Stadtman
Laboratory of Biochemistry, National Heart, Lung and Blood Institute, Bethesda, MD 20892, USA
Biochim Biophys Acta 1703:135-40. 2005.... - High urea and NaCl carbonylate proteins in renal cells in culture and in vivo, and high urea causes 8-oxoguanine lesions in their DNAZheng Zhang
Laboratory of Kidney and Electrolyte Metabolism, National Heart, Lung, and Blood Institute, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 101:9491-6. 2004..iii) In mIMCD3 cells a normal plasma concentration of urea causes carbonylation, and carbonylation increases over the uremic range of urea concentration, indicating that urea can contribute directly to the carbonylation found in uremia... - Numerous proteins in Mammalian cells are prone to iron-dependent oxidation and proteasomal degradationSteven K Drake
National Institute of Child Health and Human Development, Bethesda, MD, USA
Dev Neurosci 24:114-24. 2002..As iron overload is a feature of many human neurological diseases, further characterization of the process of degradation of iron-dependently oxidized proteins may yield insights into mechanisms of human disease... - The role of endogenous heme synthesis and degradation domain cysteines in cellular iron-dependent degradation of IRP2Emmanuel Bourdon
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, MD 20892, USA
Blood Cells Mol Dis 31:247-55. 2003..Thus, we could not discern a role for the recently defined in vitro cysteine-dependent iron-binding site of IRP2 in cellular physiology. The early molecular events in iron-dependent degradation of IRP2 remain to be elucidated... - Lon protease promotes survival of Escherichia coli during anaerobic glucose starvationShen Luo
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, NIH, Bethesda, MD, 20892 8012, USA
Arch Microbiol 189:181-5. 2008..We conclude that the Lon protease supports survival during anaerobic carbon starvation by a mechanism which does not depend on Clp... - Phosphorylation of actin Tyr-53 inhibits filament nucleation and elongation and destabilizes filamentsXiong Liu
Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 103:13694-9. 2006..Tyr-53 phosphorylation does not affect the ability of filamentous actin to activate myosin ATPase... - Assessment of skin carbonyl content as a noninvasive measure of biological ageSusann Richert
Laboratory of Biochemistry, National Institutes of Health, Bethesda, Maryland 20892-0812, USA
Arch Biochem Biophys 397:430-2. 2002..This was not the case, as we found no age-dependent relationship in the protein carbonyl content of skin cells from volunteers aged 20 to 79 years... - Quantitation of protein on gels and blots by infrared fluorescence of Coomassie blue and Fast GreenShen Luo
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD 20892, USA
Anal Biochem 350:233-8. 2006..The fluorescence response is quantitative for protein content between 10 ng and 20 microg per band or spot. Staining and destaining require only 30 min, and the method is compatible with subsequent immunodetection... - Proteasomal degradation of mutant superoxide dismutases linked to amyotrophic lateral sclerosisLuca Di Noto
Laboratory of Biochemistry, NHLBI, National Institutes of Health, Bethesda, Maryland 20892 0812, USA
J Biol Chem 280:39907-13. 2005..Exposure of hydrophobic regions as a consequence of decreased thermal stability may allow the proteasome to recognize these molecules as non-native... - Mutation of the adenylylated tyrosine of glutamine synthetase alters its catalytic propertiesShen Luo
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, Maryland 20892, USA
Biochemistry 44:9441-6. 2005..Thus, subtle modifications in the environment of residue 397 are sufficient to induce changes previously thought to require adenylylation... - Direct detection of potential selenium delivery proteins by using an Escherichia coli strain unable to incorporate selenium from selenite into proteinsGerard M Lacourciere
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA
Proc Natl Acad Sci U S A 99:9150-3. 2002..A 28-kDa protein identified as deoxyribose phosphate aldolase also contained bound selenium. These (75)Se-labeled proteins may have alternate roles as selenium delivery proteins... - Detection and characterization of the product of hydroethidine and intracellular superoxide by HPLC and limitations of fluorescenceHongtao Zhao
Department of Biophysics and Free Radical Research Center, Medical College of Wisconsin, Milwaukee, WI 53226, USA
Proc Natl Acad Sci U S A 102:5727-32. 2005..We conclude that the HPLC/fluorescence assay using HE as a probe is more suitable [corrected] for detecting intracellular O(2)(.-)... - Treatment with a catalytic antioxidant corrects the neurobehavioral defect in ataxia-telangiectasia miceSusan E Browne
Department of Neurology and Neuroscience, Weill Medical College of Cornell University, New York, NY, USA
Free Radic Biol Med 36:938-42. 2004..We show that treatment with a catalytic antioxidant corrects the neurobehavioral deficit in these mice... - Identification of a heme-sensing domain in iron regulatory protein 2Jinsook Jeong
Laboratory of Biochemistry, NHLBI, National Institutes of Health, Bethesda, MD 20892, USA
J Biol Chem 279:45450-4. 2004..This covalent modification may thus mark the protein molecule for degradation by the proteasome system, providing another mechanism by which heme can regulate the level of iron regulatory protein 2... - Carbonic anhydrase III is not required in the mouse for normal growth, development, and life spanGeumsoo Kim
Laboratories of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892 0812, USA
Mol Cell Biol 24:9942-7. 2004..We conclude that carbonic anhydrase III is dispensable for mice living under standard laboratory husbandry conditions... - Mass spectrometry analysis of recombinant human ZP3 expressed in glycosylation-deficient CHO cellsMing Zhao
Laboratory of Cellular and Developmental Biology, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, USA
Biochemistry 43:12090-104. 2004..Taken together, these data indicate that human and mouse ZP3 proteins are quite similar, and alternative explanations of taxon-specific sperm binding warrant exploration...