Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione.
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Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensorRedox Regulation in Cancer Stem CellsProtein-thiol oxidation and cell death: regulatory role of glutaredoxinsCytoprotective Nrf2 pathway is induced in chronically txnrd 1-deficient hepatocytesSolution nuclear magnetic resonance structure of a protein disulfide oxidoreductase from Methanococcus jannaschiiAtomic-resolution crystal structure of thioredoxin from the acidophilic bacterium Acetobacter acetiUtility of Synechocystis sp. PCC 6803 glutaredoxin A as a platform to study high-resolution mutagenesis of proteinsMycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of MycobacteriaAtomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxinsA protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold unitsTwo isoforms of Saccharomyces cerevisiae glutaredoxin 2 are expressed in vivo and localize to different subcellular compartmentsRole of yeast glutaredoxins as glutathione S-transferases.The yeast Saccharomyces cerevisiae contains two glutaredoxin genes that are required for protection against reactive oxygen species.Redox regulation by reversible protein S-thiolation in bacteriaThioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signalingParadoxical Roles of Antioxidant Enzymes: Basic Mechanisms and Health ImplicationsGlutaredoxin modulates platelet-derived growth factor-dependent cell signaling by regulating the redox status of low molecular weight protein-tyrosine phosphataseMolecular mechanisms of thioredoxin and glutaredoxin as hydrogen donors for Mammalian s phase ribonucleotide reductasePlasmodium falciparum possesses a classical glutaredoxin and a second, glutaredoxin-like protein with a PICOT homology domainMouse glutaredoxin - cDNA cloning, high level expression in E. coli and its possible implication in redox regulation of the DNA binding activity in transcription factor PEBP2.A genetic investigation of the essential role of glutathione: mutations in the proline biosynthesis pathway are the only suppressors of glutathione auxotrophy in yeast.The gene for a novel protein, a member of the protein disulphide isomerase/form I phosphoinositide-specific phospholipase C family, is amplified in hydroxyurea-resistant cells.Cloning, sequencing, and characterization of alternatively spliced glutaredoxin 1 cDNA and its genomic gene: chromosomal localization, mrna stability, and origin of pseudogenes.Molecular mapping of functionalities in the solution structure of reduced Grx4, a monothiol glutaredoxin from Escherichia coli.Plant thioredoxin CDSP32 regenerates 1-cys methionine sulfoxide reductase B activity through the direct reduction of sulfenic acid.The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasmConstruction and characterization of glutaredoxin-negative mutants of Escherichia coli.Glutaredoxins: roles in iron homeostasisRedox regulation of cell survival by the thioredoxin superfamily: an implication of redox gene therapy in the heart.Redox regulation of ischemic limb neovascularization - What we have learned from animal studiesDifferential expression of islet glutaredoxin 1 and 5 with high reactive oxygen species production in a mouse model of diabesityMechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulationReactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction.Hepatocytes lacking thioredoxin reductase 1 have normal replicative potential during development and regeneration.Exercise-induced oxidative stress: cellular mechanisms and impact on muscle force productionRedox control systems in the nucleus: mechanisms and functions.Hypoxia increases the dependence of glioma cells on glutathioneLigand interactions of the ArsC arsenate reductase.Tandem use of selenocysteine: adaptation of a selenoprotein glutaredoxin for reduction of selenoprotein methionine sulfoxide reductase.Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria.
P2860
Q24529525-4CE3024E-FBA2-4C67-BD85-72B2A6EA4E02Q26798198-81783656-ED19-46A1-8A1B-42A23CDE975DQ26852767-6F8CACFD-7B23-4108-9D1B-E3F6C68F40A2Q27346748-7B0F8D9D-A134-409B-8C0D-4E7D9CEA972BQ27630806-CE303429-12AA-47C6-BBFB-BA0D7E8099B8Q27640985-9530FC9B-2A3F-43A3-BCAD-58BD16D1FE33Q27680743-B1E73C54-9FEE-48F7-9CE6-CFC001A70782Q27682237-1A9DDC15-4109-4F4C-B376-85B831C06B75Q27688885-95DE77C5-BBD4-4713-960D-7DABF056A25FQ27764581-2D8AAF0B-FB03-4A72-B09B-F2B47C5FB480Q27931122-E412A5E8-8A39-4201-AA5F-FD8F177733B0Q27931430-4B335A77-D4AB-4E47-A307-6D23ABD49B9EQ27933841-6F0DD923-47DE-44B5-BF6E-3200DFDE15B1Q28083854-3CAE76D0-B33C-4778-9A82-4E8D73A187CFQ28389739-F39823B7-A747-4050-A267-E395A38798E6Q28392715-B2597F38-2FDB-4967-819B-F7BAE71DE6BDQ28580369-A829B51E-9165-47BB-B651-EB07C48F8A8AQ28594627-43825EB1-4859-4018-B482-15CCC7131DB4Q30042295-84CF9DF6-5188-4F92-90D6-7D0D2E99C681Q30789277-663C0B18-EAA9-4FFD-A7F7-73591511ACFFQ30964979-CB289597-97D8-4C13-86BE-4BF170D6712CQ30982469-A8E26C90-0AB1-4218-BD97-917AFD2C4920Q33210647-FCF8E6BB-9916-4AB5-9BE5-30F649EC163DQ33214225-9CF15989-B18B-4711-8C22-15FA1F82DBCCQ33541792-18FDD5A7-C83F-47AC-BCCF-B2B1DBDB383DQ33551316-830BCBD9-669E-41C1-8316-0A5D8287B9AEQ33552014-35CEC7CC-C255-4AA7-8054-C041640F0C89Q33636455-97497D11-03E8-426B-B64A-B5B91C3AFE3DQ33649846-101F65F1-9D58-4962-996D-105F27FE4AF7Q33681553-21708C40-6F1A-4319-9463-797BB6B5F19CQ33724707-24A0130C-E776-4DED-96DD-D225AFEE63BFQ33741131-A5FF05B8-487D-4BBF-9DC5-2B126ADA08B7Q33883304-CCD86B35-0F03-47C4-ADC6-76B57B70BDA4Q33951227-C6D96292-D22D-4B07-8D10-FA31E64C60CAQ34016655-7600731F-1682-40AC-9792-38C713F12F96Q34110120-4C26A378-CBC7-4B90-894C-4E0339BE5746Q34333783-8303F1B4-0C6B-4478-8000-EDE732E7A37FQ34435846-A6164119-AE5C-4A8D-A19A-BD1E4E8323B9Q34706984-617D4054-C8E4-43CC-9AA2-0BA1D04B68D3Q34743720-342F6818-470E-4EA8-8E26-598B554DA26C
P2860
Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione.
description
1976 nî lūn-bûn
@nan
1976 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1976 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1976年の論文
@ja
1976年論文
@yue
1976年論文
@zh-hant
1976年論文
@zh-hk
1976年論文
@zh-mo
1976年論文
@zh-tw
1976年论文
@wuu
name
Hydrogen donor system for Esch ...... se dependent upon glutathione.
@ast
Hydrogen donor system for Esch ...... se dependent upon glutathione.
@en
type
label
Hydrogen donor system for Esch ...... se dependent upon glutathione.
@ast
Hydrogen donor system for Esch ...... se dependent upon glutathione.
@en
prefLabel
Hydrogen donor system for Esch ...... se dependent upon glutathione.
@ast
Hydrogen donor system for Esch ...... se dependent upon glutathione.
@en
P2860
P356
P1476
Hydrogen donor system for Esch ...... se dependent upon glutathione.
@en
P2093
Holmgren A
P2860
P304
P356
10.1073/PNAS.73.7.2275
P407
P577
1976-07-01T00:00:00Z