Compounds > methionine sulfoxide

methionine sulfoxide and dithiothreitol

methionine sulfoxide has been researched along with dithiothreitol in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (20.00)18.2507
2000's3 (60.00)29.6817
2010's1 (20.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Borchardt, RT; Schöneich, C; Wilson, GS; Zhao, F1
Azza, S; Boschi-Muller, S; Branlant, G; Sanglier-Cianferani, S; Talfournier, F; Van Dorsselear, A1
Bechtold, U; Boelens, WC; Gustavsson, N; Härndahl, U; Kokke, BP; Murphy, D; Poghosyan, Z; Silow, M; Sundby, C1
Kim, HY; Lee, TH1
Ando, Y; Hirota, S; Nagao, S; Nugraheni, AD; Ren, C; Wang, Z1

Other Studies

5 other study(ies) available for methionine sulfoxide and dithiothreitol

ArticleYear
Iron-thiolate induced oxidation of methionine to methionine sulfoxide in small model peptides. Intramolecular catalysis by histidine.
    Biochimica et biophysica acta, 1993, Nov-28, Volume: 1158, Issue:3

    Topics: Amino Acid Sequence; Binding Sites; Catalysis; Chlorides; Dithiothreitol; Ferric Compounds; Histidine; Hydrogen-Ion Concentration; Methionine; Molecular Sequence Data; Oxidation-Reduction; Peptides

1993
A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli.
    The Journal of biological chemistry, 2000, Nov-17, Volume: 275, Issue:46

    Topics: Binding Sites; Catalysis; Cysteine; Disulfides; Dithionitrobenzoic Acid; Dithiothreitol; Escherichia coli; Methionine; Methionine Sulfoxide Reductases; Models, Chemical; Molecular Weight; Mutation; Oxidoreductases; Peptides; Reducing Agents; Spectrometry, Mass, Electrospray Ionization; Sulfenic Acids; Sulfhydryl Compounds; Thioredoxins

2000
A peptide methionine sulfoxide reductase highly expressed in photosynthetic tissue in Arabidopsis thaliana can protect the chaperone-like activity of a chloroplast-localized small heat shock protein.
    The Plant journal : for cell and molecular biology, 2002, Volume: 29, Issue:5

    Topics: Arabidopsis; Arabidopsis Proteins; Chloroplasts; Citrate (si)-Synthase; Dithiothreitol; Escherichia coli; Gene Expression; Heat-Shock Proteins; Isoenzymes; Methionine; Methionine Sulfoxide Reductases; Molecular Chaperones; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Oxidative Stress; Oxidoreductases; Plant Leaves; Plastids; Recombinant Proteins; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

2002
An anaerobic bacterial MsrB model reveals catalytic mechanisms, advantages, and disadvantages provided by selenocysteine and cysteine in reduction of methionine-R-sulfoxide.
    Archives of biochemistry and biophysics, 2008, Oct-15, Volume: 478, Issue:2

    Topics: Amino Acid Sequence; Bacterial Proteins; Base Sequence; Catalytic Domain; Cell Line; Clostridium; Cysteine; Dithiothreitol; DNA Primers; Humans; Kinetics; Methionine; Methionine Sulfoxide Reductases; Models, Biological; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Recombinant Proteins; Selenocysteine; Sequence Homology, Amino Acid; Thioredoxins

2008
Self-oxidation of cytochrome c at methionine80 with molecular oxygen induced by cleavage of the Met-heme iron bond.
    Molecular bioSystems, 2014, Volume: 10, Issue:12

    Topics: Cytochromes c; Dithiothreitol; Heme; Humans; Iron; Liposomes; Methionine; Oxidation-Reduction; Oxygen; Protein Conformation; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

2014