Glutathione-dependent hydrogen donor system for calf thymus ribonucleoside-diphosphate reductase.
about
Cysteine specific targeting of the functionally distinct peroxiredoxin and glutaredoxin proteins by the investigational disulfide BNP7787Thioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signalingGlutathione synthesis is essential for mouse development but not for cell growth in cultureMolecular 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 domainCloning, sequencing, and characterization of alternatively spliced glutaredoxin 1 cDNA and its genomic gene: chromosomal localization, mrna stability, and origin of pseudogenes.Knockdown of cytosolic glutaredoxin 1 leads to loss of mitochondrial membrane potential: implication in neurodegenerative diseasesHepatocytes lacking thioredoxin reductase 1 have normal replicative potential during development and regeneration.Hypoxia increases the dependence of glioma cells on glutathioneHepatocyte DNA replication in growing liver requires either glutathione or a single allele of txnrd1.Regulation of cell physiology and pathology by protein S-glutathionylation: lessons learned from the cardiovascular system.Purification, crystallization and preliminary diffraction studies of an ectromelia virus glutaredoxin.Transforming growth factor β suppresses glutamate-cysteine ligase gene expression and induces oxidative stress in a lung fibrosis modelThioredoxin, glutaredoxin, and thioredoxin reductase from cultured HeLa cells.Glutathione defense mechanism in liver injury: insights from animal models.Regulatory properties of a fructose 1,6-bisphosphatase from the cyanobacterium Anacystis nidulans.Complete 1H, 13C, and 15N NMR resonance assignments and secondary structure of human glutaredoxin in the fully reduced formPhosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins.Alternative mRNAs arising from trans-splicing code for mitochondrial and cytosolic variants of Echinococcus granulosus thioredoxin Glutathione reductase.The A to Z of modulated cell patterning by mammalian thioredoxin reductases.Molecular cloning and characterization of Fasciola gigantica thioredoxin-glutathione reductase.Animal and plant mitochondria contain specific thioredoxins.
P2860
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P2860
Glutathione-dependent hydrogen donor system for calf thymus ribonucleoside-diphosphate reductase.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 1979
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Glutathione-dependent hydrogen ...... leoside-diphosphate reductase.
@en
Glutathione-dependent hydrogen ...... leoside-diphosphate reductase.
@nl
type
label
Glutathione-dependent hydrogen ...... leoside-diphosphate reductase.
@en
Glutathione-dependent hydrogen ...... leoside-diphosphate reductase.
@nl
prefLabel
Glutathione-dependent hydrogen ...... leoside-diphosphate reductase.
@en
Glutathione-dependent hydrogen ...... leoside-diphosphate reductase.
@nl
P2093
P2860
P356
P1476
Glutathione-dependent hydrogen ...... leoside-diphosphate reductase.
@en
P2093
Eriksson S
Holmgren A
Thelander L
P2860
P304
P356
10.1073/PNAS.76.5.2158
P407
P577
1979-05-01T00:00:00Z