Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 A resolution
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Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionineDifferent catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductasesThe methionine sulfoxide reduction system: selenium utilization and methionine sulfoxide reductase enzymes and their functionsStructure–function analysis of the 3′ phosphatase component of T4 polynucleotide kinase/phosphataseStructural and kinetic analysis of an MsrA-MsrB fusion protein fromStreptococcus pneumoniaeStructural Plasticity of the Thioredoxin Recognition Site of Yeast Methionine S-Sulfoxide Reductase Mxr1Selenoprotein R is a zinc-containing stereo-specific methionine sulfoxide reductase.Activity, tissue distribution and site-directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: hCBS1E. coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxideRat peptide methionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during agingArsenic binding to proteinsEvidence for the dimerization-mediated catalysis of methionine sulfoxide reductase A from Clostridium oremlandiiIdentification of a new functional splice variant of the enzyme methionine sulphoxide reductase A (MSRA) expressed in rat vascular smooth muscle cellsCharacterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis.The high resolution crystal structure of a native thermostable serpin reveals the complex mechanism underpinning the stressed to relaxed transition.Tandem use of selenocysteine: adaptation of a selenoprotein glutaredoxin for reduction of selenoprotein methionine sulfoxide reductase.Corynebacterium glutamicum methionine sulfoxide reductase A uses both mycoredoxin and thioredoxin for regeneration and oxidative stress resistance.Essential role of the C-terminal helical domain in active site formation of selenoprotein MsrA from Clostridium oremlandii.Crystallization and preliminary X-ray crystallographic analysis of the methionine sulfoxide reductase A domain of MsrAB from Haemophilus influenzaeA low pKa cysteine at the active site of mouse methionine sulfoxide reductase AInsights into the role of the metal binding site in methionine-R-sulfoxide reductases B.Maintenance of proteins and aging: the role of oxidized protein repair.Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase.Reaction mechanism, evolutionary analysis, and role of zinc in Drosophila methionine-R-sulfoxide reductase.Structural and kinetic analysis of free methionine-R-sulfoxide reductase from Staphylococcus aureus: conformational changes during catalysis and implications for the catalytic and inhibitory mechanisms.Corynebacterium diphtheriae methionine sulfoxide reductase a exploits a unique mycothiol redox relay mechanism.Methionine sulfoxide reduction and assimilation in Escherichia coli: new role for the biotin sulfoxide reductase BisCImportant role for methionine sulfoxide reductase in the oxidative stress response of Xanthomonas campestris pv. phaseoli.Methionine sulfoxide reductase in Helicobacter pylori: interaction with methionine-rich proteins and stress-induced expression.Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases.Repair of oxidized proteins. Identification of a new methionine sulfoxide reductase.Thioredoxin and peptide methionine sulfoxide reductase: convergence of similar structure and function in distinct structural folds.Characterization of the amino acids from Neisseria meningitidis MsrA involved in the chemical catalysis of the methionine sulfoxide reduction step.Kinetic characterization of the chemical steps involved in the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitidis.The N-terminal domain of PILB from Neisseria meningitidis is a disulfide reductase that can recycle methionine sulfoxide reductases.Functional and structural aspects of poplar cytosolic and plastidial type a methionine sulfoxide reductases.The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases.
P2860
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P2860
Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 A resolution
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2000 nî lūn-bûn
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2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
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2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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name
Crystal structure of the Esche ...... reductase at 1.9 A resolution
@ast
Crystal structure of the Esche ...... reductase at 1.9 A resolution
@en
Crystal structure of the Esche ...... reductase at 1.9 A resolution
@nl
type
label
Crystal structure of the Esche ...... reductase at 1.9 A resolution
@ast
Crystal structure of the Esche ...... reductase at 1.9 A resolution
@en
Crystal structure of the Esche ...... reductase at 1.9 A resolution
@nl
prefLabel
Crystal structure of the Esche ...... reductase at 1.9 A resolution
@ast
Crystal structure of the Esche ...... reductase at 1.9 A resolution
@en
Crystal structure of the Esche ...... reductase at 1.9 A resolution
@nl
P2093
P1433
P1476
Crystal structure of the Esche ...... reductase at 1.9 A resolution
@en
P2093
F Tête-Favier
G Branlant
S Boschi-Muller
P304
P356
10.1016/S0969-2126(00)00526-8
P577
2000-11-15T00:00:00Z