Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 19, pp. 7355 - 7366
Methionine residues in proteins provide antioxidant defense by reacting with oxidizing species, which oxidize methionine to methionine sulfoxide. Reduction of...
STARD3 | CELLS | COMPLEX | DOMAIN | ACTIN | APOLIPOPROTEINS AI | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | DAMAGE | endosome | protein myristoylation | methionine | oxidation-reduction (redox) | RESIDUES | oxidative stress | methionine sulfoxide reductase A | HIGH-DENSITY-LIPOPROTEINS | oxidation–reduction (redox) | Cell Biology
STARD3 | CELLS | COMPLEX | DOMAIN | ACTIN | APOLIPOPROTEINS AI | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | DAMAGE | endosome | protein myristoylation | methionine | oxidation-reduction (redox) | RESIDUES | oxidative stress | methionine sulfoxide reductase A | HIGH-DENSITY-LIPOPROTEINS | oxidation–reduction (redox) | Cell Biology
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2011, Volume 108, Issue 26, pp. 10472 - 10477
Methionine sulfoxide reductase A (MsrA) catalyzes the reduction of methionine sulfoxide to methionine and is specific for the S epimer of methionine sulfoxide....
Oxidases | Proteins | Enzymes | Molecules | Oxygen | Sulfenic acids | Active sites | Sulfoxides | Oxidation | Physiological regulation | THIOLS | OXIDATIVE STRESS | ENZYME | MECHANISM | ANTIOXIDANT DEFENSE | MULTIDISCIPLINARY SCIENCES | NEISSERIA-MENINGITIDIS | ESCHERICHIA-COLI | GLUTAMINE-SYNTHETASE | PROTEIN-BOUND METHIONINE | RESIDUES | Methionine Sulfoxide Reductases - metabolism | Biocatalysis | Oxidation-Reduction | Stereoisomerism | Mass Spectrometry | Substrate Specificity | Chromatography, High Pressure Liquid | Sulfur compounds | Health aspects | Methionine | Biological Sciences
Oxidases | Proteins | Enzymes | Molecules | Oxygen | Sulfenic acids | Active sites | Sulfoxides | Oxidation | Physiological regulation | THIOLS | OXIDATIVE STRESS | ENZYME | MECHANISM | ANTIOXIDANT DEFENSE | MULTIDISCIPLINARY SCIENCES | NEISSERIA-MENINGITIDIS | ESCHERICHIA-COLI | GLUTAMINE-SYNTHETASE | PROTEIN-BOUND METHIONINE | RESIDUES | Methionine Sulfoxide Reductases - metabolism | Biocatalysis | Oxidation-Reduction | Stereoisomerism | Mass Spectrometry | Substrate Specificity | Chromatography, High Pressure Liquid | Sulfur compounds | Health aspects | Methionine | Biological Sciences
Journal Article
Methods in Molecular Biology, ISSN 1064-3745, 2018, Volume 1661, pp. 285 - 299
The sulfur-containing amino acid methionine (Met) plays critical roles in protein synthesis, methylation, and sulfur metabolism. Both in its free form and in...
Fluorescent microscopy | Oxidative stress | Methionine sulfoxide reductase | Protein oxidation | Genetically encoded fluorescent sensors | HPLC | Life Sciences | fluorescent microscopy | genetically encoded fluorescent sensors | methionine sulfoxide reductase | oxidative stress | protein oxidation
Fluorescent microscopy | Oxidative stress | Methionine sulfoxide reductase | Protein oxidation | Genetically encoded fluorescent sensors | HPLC | Life Sciences | fluorescent microscopy | genetically encoded fluorescent sensors | methionine sulfoxide reductase | oxidative stress | protein oxidation
Journal Article
Antioxidants & Redox Signaling, ISSN 1523-0864, 09/2013, Volume 19, Issue 9, pp. 958 - 969
Significance: Selenium is utilized in the methionine sulfoxide reduction system that occurs in most organisms. Methionine sulfoxide reductases (Msrs), MsrA and...
Forum Review Articles | LIFE-SPAN | OXIDATIVE STRESS | SELENOCYSTEINE INSERTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | R-SULFOXIDE | ESCHERICHIA-COLI | ENDOCRINOLOGY & METABOLISM | ENDOPLASMIC-RETICULUM | PROTEIN-BOUND METHIONINE | HYDROGEN-SULFIDE | CATALYTIC MECHANISM | SACCHAROMYCES-CEREVISIAE | Selenocysteine - metabolism | Oxidation-Reduction | Methionine - metabolism | Humans | Substrate Specificity | Eukaryotic Cells - metabolism | Mammals | Selenoproteins - metabolism | Methionine Sulfoxide Reductases - metabolism | Animals | Selenium - metabolism | Metabolic Networks and Pathways | Methionine - analogs & derivatives | Catalysis | Aging - metabolism | Physiological aspects | Selenium | Research | Selenoproteins | Redox potential | Methionine | Forum Review
Forum Review Articles | LIFE-SPAN | OXIDATIVE STRESS | SELENOCYSTEINE INSERTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | R-SULFOXIDE | ESCHERICHIA-COLI | ENDOCRINOLOGY & METABOLISM | ENDOPLASMIC-RETICULUM | PROTEIN-BOUND METHIONINE | HYDROGEN-SULFIDE | CATALYTIC MECHANISM | SACCHAROMYCES-CEREVISIAE | Selenocysteine - metabolism | Oxidation-Reduction | Methionine - metabolism | Humans | Substrate Specificity | Eukaryotic Cells - metabolism | Mammals | Selenoproteins - metabolism | Methionine Sulfoxide Reductases - metabolism | Animals | Selenium - metabolism | Metabolic Networks and Pathways | Methionine - analogs & derivatives | Catalysis | Aging - metabolism | Physiological aspects | Selenium | Research | Selenoproteins | Redox potential | Methionine | Forum Review
Journal Article
Free Radical Biology and Medicine, ISSN 0891-5849, 02/2019, Volume 131, pp. 154 - 161
Mouse, human, and methionine sulfoxide reductase A (MSRA) stereospecifically catalyze both the reduction of S-methionine sulfoxide to methionine and the...
Methionine sulfoxide reductase | Methionine oxidase | Drosophila | Calmodulin | OXIDATION | LIFE-SPAN | ACID | ACTIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CYSTEINE | PROTECTS | ENDOCRINOLOGY & METABOLISM | NITROGEN | RESIDUES | EXPRESSION
Methionine sulfoxide reductase | Methionine oxidase | Drosophila | Calmodulin | OXIDATION | LIFE-SPAN | ACID | ACTIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CYSTEINE | PROTECTS | ENDOCRINOLOGY & METABOLISM | NITROGEN | RESIDUES | EXPRESSION
Journal Article
Biochemical Journal, ISSN 0264-6021, 12/2018, Volume 475, Issue 23, pp. 3779 - 3795
Methionine (Met) is prone to oxidation and can be converted to Met sulfoxide (MetO), which exists as R- and S-diastereomers. MetO can be reduced back to Met by...
SYSTEM | RESPIRATORY-CHAIN | OXIDATIVE STRESS | ARABIDOPSIS-THALIANA | REPAIR | BIOCHEMISTRY & MOLECULAR BIOLOGY | OXIDIZED PROTEINS | ESCHERICHIA-COLI | PURIFICATION | SINGLET OXYGEN | IDENTIFICATION | Amino Acid Sequence | Rhodobacter sphaeroides - enzymology | Oxidation-Reduction | Isoenzymes - genetics | Methionine - metabolism | Stereoisomerism | Bacterial Proteins - genetics | Substrate Specificity | Methionine Sulfoxide Reductases - genetics | Methionine Sulfoxide Reductases - metabolism | Methionine - analogs & derivatives | Isoenzymes - metabolism | Methionine - chemistry | Periplasmic Proteins - genetics | Rhodobacter sphaeroides - metabolism | Bacterial Proteins - metabolism | Rhodobacter sphaeroides - genetics | Periplasmic Proteins - metabolism | Mutation | Life Sciences | Biochemistry, Molecular Biology
SYSTEM | RESPIRATORY-CHAIN | OXIDATIVE STRESS | ARABIDOPSIS-THALIANA | REPAIR | BIOCHEMISTRY & MOLECULAR BIOLOGY | OXIDIZED PROTEINS | ESCHERICHIA-COLI | PURIFICATION | SINGLET OXYGEN | IDENTIFICATION | Amino Acid Sequence | Rhodobacter sphaeroides - enzymology | Oxidation-Reduction | Isoenzymes - genetics | Methionine - metabolism | Stereoisomerism | Bacterial Proteins - genetics | Substrate Specificity | Methionine Sulfoxide Reductases - genetics | Methionine Sulfoxide Reductases - metabolism | Methionine - analogs & derivatives | Isoenzymes - metabolism | Methionine - chemistry | Periplasmic Proteins - genetics | Rhodobacter sphaeroides - metabolism | Bacterial Proteins - metabolism | Rhodobacter sphaeroides - genetics | Periplasmic Proteins - metabolism | Mutation | Life Sciences | Biochemistry, Molecular Biology
Journal Article
PROGRESS IN CHEMISTRY, ISSN 1005-281X, 10/2018, Volume 30, Issue 10, pp. 1496 - 1502
Selenoproteins represent a category of proteins that possess selenocysteine as the active center, by taking advantage of robust reducing ability of selenium,...
selenoprotein R | neurodegenerative diseases | ACTIVATION | methionine sulfoxide reductase | PROTEIN | CHEMISTRY, MULTIDISCIPLINARY | central nervous system
selenoprotein R | neurodegenerative diseases | ACTIVATION | methionine sulfoxide reductase | PROTEIN | CHEMISTRY, MULTIDISCIPLINARY | central nervous system
Journal Article
8.
Full Text
Alkyl Hydroperoxide Reductase Repair by Helicobacter pylori Methionine Sulfoxide Reductase
Journal of Bacteriology, ISSN 0021-9193, 12/2013, Volume 195, Issue 23, pp. 5396 - 5401
Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
ALKYLHYDROPEROXIDE REDUCTASE | CATALASE | SYSTEM | PROTEIN | GASTRITIS | ESCHERICHIA-COLI | TRANSCRIPTION | NEUTROPHILS | MICROBIOLOGY | CHAPERONE | STRESS | Peroxiredoxins - metabolism | Bacterial Proteins - genetics | Gene Expression Regulation, Enzymologic - physiology | Methionine Sulfoxide Reductases - genetics | Gene Expression Regulation, Bacterial - physiology | Methionine Sulfoxide Reductases - metabolism | Peroxiredoxins - genetics | Helicobacter pylori - enzymology | Hypochlorous Acid | Peroxidases - metabolism | Bacterial Proteins - metabolism | Mutation | Peroxidases - genetics | Microbial enzymes | Helicobacter pylori | Bacterial proteins | Physiological aspects | Influence | Research | Gene expression | Index Medicus
ALKYLHYDROPEROXIDE REDUCTASE | CATALASE | SYSTEM | PROTEIN | GASTRITIS | ESCHERICHIA-COLI | TRANSCRIPTION | NEUTROPHILS | MICROBIOLOGY | CHAPERONE | STRESS | Peroxiredoxins - metabolism | Bacterial Proteins - genetics | Gene Expression Regulation, Enzymologic - physiology | Methionine Sulfoxide Reductases - genetics | Gene Expression Regulation, Bacterial - physiology | Methionine Sulfoxide Reductases - metabolism | Peroxiredoxins - genetics | Helicobacter pylori - enzymology | Hypochlorous Acid | Peroxidases - metabolism | Bacterial Proteins - metabolism | Mutation | Peroxidases - genetics | Microbial enzymes | Helicobacter pylori | Bacterial proteins | Physiological aspects | Influence | Research | Gene expression | Index Medicus
Journal Article
Free Radical Biology and Medicine, ISSN 0891-5849, 12/2019, Volume 145, pp. 374 - 384
Oxidation of methionine residues to methionine sulfoxide scavenges reactive species, thus protecting against oxidative stress. Reduction of the sulfoxide back...
Ischemia-reperfusion | Methionine sulfoxide reductases | Oxidative stress | Paraquat | Oxidative defenses | Methionine-methionine sulfoxide signaling | CELLS | ACTIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | RECEPTOR | PROTECTS | DELETION | HEART | S-NITROSYLATION | REDOX REGULATION | ROLES | ENDOCRINOLOGY & METABOLISM
Ischemia-reperfusion | Methionine sulfoxide reductases | Oxidative stress | Paraquat | Oxidative defenses | Methionine-methionine sulfoxide signaling | CELLS | ACTIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | RECEPTOR | PROTECTS | DELETION | HEART | S-NITROSYLATION | REDOX REGULATION | ROLES | ENDOCRINOLOGY & METABOLISM
Journal Article
Progress in Chemistry, ISSN 1005-281X, 10/2018, Volume 30, Issue 10, pp. 1496 - 1502
Journal Article
Free Radical Biology and Medicine, ISSN 0891-5849, 08/2013, Volume 61, pp. 257 - 264
Methionine sulfoxide reductase A has long been known to reduce -methionine sulfoxide, both as a free amino acid and within proteins. Recently the enzyme was...
Signaling | Methionine sulfoxide reductase | Free radicals | Methionine reduction | Calmodulin | Methionine oxidation | CELLS | MEMBRANE CA-ATPASE | ACTIVATION | TERMINAL DOMAIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | TARGET RECOGNITION | DAMAGE | PROTECTS | ENDOCRINOLOGY & METABOLISM | CALCINEURIN | STRESS | Methionine Sulfoxide Reductases - metabolism | Chromatography, Affinity | Immunoprecipitation | Oxidation-Reduction | Calcium - metabolism | Stereoisomerism | Calmodulin - chemistry | Enzymes | Amino acids | Oxidation-reduction reaction | Chemical properties | methionine oxidation | methionine sulfoxide reductase | signaling | methionine reduction
Signaling | Methionine sulfoxide reductase | Free radicals | Methionine reduction | Calmodulin | Methionine oxidation | CELLS | MEMBRANE CA-ATPASE | ACTIVATION | TERMINAL DOMAIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | TARGET RECOGNITION | DAMAGE | PROTECTS | ENDOCRINOLOGY & METABOLISM | CALCINEURIN | STRESS | Methionine Sulfoxide Reductases - metabolism | Chromatography, Affinity | Immunoprecipitation | Oxidation-Reduction | Calcium - metabolism | Stereoisomerism | Calmodulin - chemistry | Enzymes | Amino acids | Oxidation-reduction reaction | Chemical properties | methionine oxidation | methionine sulfoxide reductase | signaling | methionine reduction
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2/2013, Volume 110, Issue 9, pp. 3633 - 3638
Seeds are in a natural oxidative context leading to protein oxidation. Although inevitable for proper progression from maturation to germination, protein...
Protein isoforms | Antioxidants | Seeds | Germination | Sulfoxides | Oxidation | Plants | Longevity | Seed longevity | Genotypes | Redox systems | Seed deterioration | Seed viability | Antioxidant enzymes | ENZYME-ACTIVITIES | LIFE-SPAN | MEDICAGO-TRUNCATULA SEEDS | OXIDATIVE STRESS | ARABIDOPSIS-THALIANA | MULTIDISCIPLINARY SCIENCES | OXIDIZED PROTEINS | antioxidant enzymes | GERMINATION | seed viability | HEAT-SHOCK-PROTEIN | MESSENGER-RNAS | redox systems | HYDROGEN-PEROXIDE | seed deterioration | Medicago truncatula - physiology | Arabidopsis - physiology | Methionine Sulfoxide Reductases - metabolism | Arabidopsis - enzymology | Seeds - growth & development | Seeds - physiology | Base Sequence | Seeds - enzymology | Databases, Genetic | Medicago truncatula - enzymology | Physiological aspects | Aging | Research | Oxidoreductases | Methionine | Life Sciences | Biological Sciences
Protein isoforms | Antioxidants | Seeds | Germination | Sulfoxides | Oxidation | Plants | Longevity | Seed longevity | Genotypes | Redox systems | Seed deterioration | Seed viability | Antioxidant enzymes | ENZYME-ACTIVITIES | LIFE-SPAN | MEDICAGO-TRUNCATULA SEEDS | OXIDATIVE STRESS | ARABIDOPSIS-THALIANA | MULTIDISCIPLINARY SCIENCES | OXIDIZED PROTEINS | antioxidant enzymes | GERMINATION | seed viability | HEAT-SHOCK-PROTEIN | MESSENGER-RNAS | redox systems | HYDROGEN-PEROXIDE | seed deterioration | Medicago truncatula - physiology | Arabidopsis - physiology | Methionine Sulfoxide Reductases - metabolism | Arabidopsis - enzymology | Seeds - growth & development | Seeds - physiology | Base Sequence | Seeds - enzymology | Databases, Genetic | Medicago truncatula - enzymology | Physiological aspects | Aging | Research | Oxidoreductases | Methionine | Life Sciences | Biological Sciences
Journal Article
Experimental Neurology, ISSN 0014-4886, 08/2019, Volume 318, pp. 145 - 156
Methionine sulfoxide reductase B2 (MSRB2) is a mitochondrial protein that protects cell from oxidative stress. The antioxidant activity suggests that MSRB2 may...
Oxidative stress | APP | Methionine sulfoxide reductase B2 | Phosphorylation | APP/PS1 mice | Transcription | JNK | Tau | LIFE-SPAN | ACTIVATION | NEUROSCIENCES | OVEREXPRESSION | GLUTATHIONE | ANTIOXIDANT DEFENSE | AMYLOID-BETA | NEURONAL CELLS | PRECURSOR PROTEIN | GAMMA-SECRETASE | EXPRESSION
Oxidative stress | APP | Methionine sulfoxide reductase B2 | Phosphorylation | APP/PS1 mice | Transcription | JNK | Tau | LIFE-SPAN | ACTIVATION | NEUROSCIENCES | OVEREXPRESSION | GLUTATHIONE | ANTIOXIDANT DEFENSE | AMYLOID-BETA | NEURONAL CELLS | PRECURSOR PROTEIN | GAMMA-SECRETASE | EXPRESSION
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 12/2001, Volume 276, Issue 52, pp. 48915 - 48920
Oxidation of methionine residues to methionine sulfoxide can lead to inactivation of proteins. Methionine sulfoxide reductase (MsrA) has been known for a long...
OXIDATION | GENE | CLONING | ENZYMATIC REDUCTION | CALMODULIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CATALYTIC MECHANISM | EXPRESSION | RESIDUES | SITE-SPECIFIC MUTAGENESIS | Calmodulin - metabolism | Escherichia coli - enzymology | Oxidation-Reduction | Oxidoreductases - metabolism | Methionine - metabolism | Oxidoreductases - genetics | Humans | Methionine Sulfoxide Reductases | Cadmium - metabolism | Spectroscopy, Fourier Transform Infrared | Animals | Methionine - analogs & derivatives | Escherichia coli - genetics | Escherichia coli - metabolism | Life Sciences | Microbiology and Parasitology | Biomolecules | Biochemistry, Molecular Biology | Bacteriology
OXIDATION | GENE | CLONING | ENZYMATIC REDUCTION | CALMODULIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CATALYTIC MECHANISM | EXPRESSION | RESIDUES | SITE-SPECIFIC MUTAGENESIS | Calmodulin - metabolism | Escherichia coli - enzymology | Oxidation-Reduction | Oxidoreductases - metabolism | Methionine - metabolism | Oxidoreductases - genetics | Humans | Methionine Sulfoxide Reductases | Cadmium - metabolism | Spectroscopy, Fourier Transform Infrared | Animals | Methionine - analogs & derivatives | Escherichia coli - genetics | Escherichia coli - metabolism | Life Sciences | Microbiology and Parasitology | Biomolecules | Biochemistry, Molecular Biology | Bacteriology
Journal Article
BBA - General Subjects, ISSN 0304-4165, 2009, Volume 1790, Issue 11, pp. 1471 - 1477
Methionine sulfoxide reductases (Msrs) are thiol-dependent enzymes which catalyze conversion of methionine sulfoxide to methionine. Three Msr families, MsrA,...
Antioxidants | MsrA | Selenoprotein | fRMsr | Methionine sulfoxide | ROS | MsrB1 | Selenocysteine | Aging | MsrB3 | MsrB2 | LIFE-SPAN | OXIDATIVE DNA-DAMAGE | A MSRA | IODOTHYRONINE DEIODINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | R-SULFOXIDE | ESCHERICHIA-COLI | TRANSGENIC DROSOPHILA-MELANOGASTER | SACCHAROMYCES-CEREVISIAE | BIOPHYSICS | SMOOTH-MUSCLE-CELLS | SUPEROXIDE-DISMUTASE | Mammals - genetics | Mammals - metabolism | Oxidoreductases - metabolism | Selenoproteins - genetics | Oxidoreductases - genetics | Humans | Oxidoreductases - classification | Methionine Sulfoxide Reductases | Oxidoreductases - physiology | Selenoproteins - metabolism | Selenoproteins - classification | Animals | Aging - physiology | Models, Biological | Mammals - physiology | Catalysis | Selenoproteins - physiology | Aging - metabolism | Evolution, Molecular
Antioxidants | MsrA | Selenoprotein | fRMsr | Methionine sulfoxide | ROS | MsrB1 | Selenocysteine | Aging | MsrB3 | MsrB2 | LIFE-SPAN | OXIDATIVE DNA-DAMAGE | A MSRA | IODOTHYRONINE DEIODINASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | R-SULFOXIDE | ESCHERICHIA-COLI | TRANSGENIC DROSOPHILA-MELANOGASTER | SACCHAROMYCES-CEREVISIAE | BIOPHYSICS | SMOOTH-MUSCLE-CELLS | SUPEROXIDE-DISMUTASE | Mammals - genetics | Mammals - metabolism | Oxidoreductases - metabolism | Selenoproteins - genetics | Oxidoreductases - genetics | Humans | Oxidoreductases - classification | Methionine Sulfoxide Reductases | Oxidoreductases - physiology | Selenoproteins - metabolism | Selenoproteins - classification | Animals | Aging - physiology | Models, Biological | Mammals - physiology | Catalysis | Selenoproteins - physiology | Aging - metabolism | Evolution, Molecular
Journal Article