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PRDX1 and MTH1 (show NUDT1 Proteins) cooperate to prevent accumulation of oxidized guanine in the genome
Study uncovered a novel interaction between APE1 (show APEX1 Proteins) and PRDX1, which existed in both the nuclear and cytosolic fractions. Its knockdown enhances APE1 (show APEX1 Proteins) detection in the nucleus and stimulates IL-8 (show IL8 Proteins) expression. Also, in gastric cancer patients, PRDX1 mRNA expression level is reduced and correlates with poor survival.
Median PRDX1 levels were significantly higher in stroke patients compared to controls.
The epimutation is present in three generations and results from PRDX1 mutations that force antisense transcription of MMACHC (show MMACHC Proteins).
Peroxiredoxin I (Prx (show PRDX6 Proteins) I) increased in tumors of hepatocellular carcinoma (HCC (show FAM126A Proteins)) patients that aligned with overexpression of oncogenic H-ras (show HRAS Proteins).
Prx1 might play an oncogenic role in tobacco-related oral squamous cell carcinoma and thus serve as a target for chemopreventive and therapeutic interventions.
PRDX1 safeguards telomeres from oxygen radicals to counteract telomere damage and preserve telomeric DNA for elongation by telomerase.
infection results in S-nitrosylation of multiple host proteins, including Prx1.
circulating Prdx1 provides not only prognostic information but may be a promising target against ischemia/reperfusion injury.
our findings suggest that the tumor suppressor activity of SIRT2 (show SIRT2 Proteins) requires its ability to restrict the antioxidant activity of Prdx-1, thereby sensitizing breast cancer cells to reactive oxygen species -induced DNA damage and cell cytotoxicity
PRX1 and PRX5 (show PRDX5 Proteins) were upregulated in osteoblasts in the proximal tibial metaphysis of ovariectomized mice. Interestingly, PRX1 and PRX5 (show PRDX5 Proteins) showed different distribution patterns, with PRX1 mainly accumulated in cell nuclei and PRX5 (show PRDX5 Proteins) in the cytoplasm.
HDAC6 (show HDAC6 Proteins) inhibition and the regulation of Prx1 activity may play a significant role in protecting retinal cells and in particular photoreceptors.
This is the first report proclaiming that the ESAT-6 regulates Prdx-1 which is involved in the increase of mycobacterial uptake and survival. The intermediate mechanisms involve the increased Prdx-1 production in macrophages through the activation of p38 (show CRK Proteins) and NRF-2 (show NFE2L2 Proteins) dependent signaling.
in the absence of PAG, Csk becomes more associated with alternative partners; i.e., phosphatase PTPN22 and Dok adaptors. Combining PAG deficiency with PTPN22 or Dok adaptor deficiency further enhances effector T cell responses. Unlike PAG, Cbl ubiquitin ligases inhibit the activation of naive, but not of effector, T cells.
These findings suggest that extracellular Prx1-mediated TLR4 (show TLR4 Proteins)/NF-kappaB (show NFKB1 Proteins) pathway activation probably contributes to neuroinflammatory injury after ICH (show ACE Proteins), and thus blocking Prx1-TLR4 (show TLR4 Proteins) signaling might provide a novel anti-neuroinflammatory strategy with extended therapeutic window for hemorrhagic stroke
This study demonstrated that Prdx1 showed a distinct nuclear localization in the spinal cord also present in the nucleus of dorsal root ganglia (DRG) cells as well as in the sensory nerve root in embryonic development.
Prx I and Prx II appear to have a tight association with the mechanism underlying the protection of ESC stemness in developing teratomas.
Prx (show PRX Proteins) I is an antioxidant that is up-regulated in a reactive oxygen species/p38 MAPK (show MAPK14 Proteins)-dependent manner and governs the progression of neuroinflammation by suppressing microglial activation.
NO/SNO donors such as S-nitrosocysteine and S-nitrosoglutathione readily induced the S-nitrosylation of Prx1, causing structural and functional alterations
PrxI is not an effective protector against ozone-induced oxidative damage but plays a positive role in the initiation of lung inflammation following exposure.
These results suggest that PRX 1 is a novel mechanosensitive antioxidant, playing an important role in shear-dependent regulation of endothelial biology and atherosclerosis.
It was assumed that Prx1 plays a leading role in X. laevis early development.
The results suggested that scarless skin-wound healing may require activation of the prx1 limb enhancer, and competence to activate the enhancer is probably a prerequisite for epimorphic regeneration, such as limb regeneration.
HDAC6 (show HDAC6 Proteins) inhibition and the regulation of Prx1 (show PRRX1 Proteins) activity may play a significant role in protecting retinal cells and in particular photoreceptors.
Data suggest a role for peroxiredoxin1 (Prdx1) in vasculature and indicating that the antioxidant function of prdx1 is important.
This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells. This protein may have a proliferative effect and play a role in cancer development or progression. Four transcript variants encoding the same protein have been identified for this gene.
natural killer cell-enhancing factor A
, natural killer-enhancing factor A
, proliferation-associated gene A
, proliferation-associated gene protein
, thioredoxin peroxidase 2
, thioredoxin-dependent peroxide reductase 2
, Trx dependent peroxide reductase 2
, macrophage 23 Kd stress protein
, macrophage 23 kDa stress protein
, macrophage 23kDa stress protein
, macrophase stress protein 22kDa
, macrophase stress protein 23 kd
, osteoblast specific factor 3
, osteoblast-specific factor 3
, thioredoxin dependent peroxide reductase 2
, heme-binding 23 kDa protein
, peroxiredoxin 1
, Thioredoxin peroxidase 2
, thioredoxin peroxidase II