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The expression of p53R2 was associated closely with the development and progression of lung sarcomatoid carcinoma.
p53R2 protein is overexpressed in early-stage cervical cancer and unravels some unconventional oncogenic functions of p53R2.
High RRM2B expression is associated with neoplasms.
Studied the expression of ribonucleotide reductase (RR) subunit p53R2 in nasopharyngeal carcinoma and its significance in the prognosis.
RRM1/RRM2B enzyme is capable of retaining activity in hypoxia and therefore is favored over RRM1/RRM2 in order to preserve ongoing replication and avoid the accumulation of DNA damage in hypoxic cells.
p53R2 acts as a positive regulator of TrxR2 activity in mitochondria both under normal physiological conditions and during the cellular response to DNA damage
Silencing of both PYCR1 and PYCR2 completely abolished anti-oxidation activity of RRM2B, demonstrating a functional collaboration of these metabolic enzymes in response to oxidative stress.
A newly discovered role of E2F1 in the regulation of p53R2 expression in DNA damage response.
analysis of caspase-dependent degradation of human R2 and p53R2 small subunits
in Turkish population p53R2 genotype distributions between head and neck squamous epithelial cell cancer patients and control groups were not statistically significantly different.
Data indicate that forkhead transcription factorsF OXO3 directly bound to and transcriptionally activated the promoter of ribonucleotide reductase subunit RRM2B, and induced the expression of RRM2B at RNA and protein levels.
we found no support of the hypothesis that aberrations of RRM1 or RRM2B, neither individually nor in combination, are associated with an altered clinical outcome following chemotherapy.
Ribonucleotide reductase M2B inhibits cell migration and spreading by early growth response protein 1-mediated phosphatase and tensin homolog/Akt1 pathway in hepatocellular carcinoma.
RRM2B expression may discriminate cervical cancer phenotype and radiochemotherapy outcome
RRM2B is highly induced in a p53-dependent manner during senescence and is expressed at higher levels in senescent precancerous human prostatic intraepithelial neoplasm lesions compared to adjacent normal prostate glands.
p53R2 could regulate matrix synthesis via Akt phosphorylation during chondrocyte mechanotransduction. Down-regulation of p53R2 may be a new therapeutic approach in OA therapy.
p53R2 is directly regulated by p53 and also by a MEK2 (ERK kinase 2/MAP kinase kinase 2)-dependent pathway.
Propose p53R2 as a therapeutic target to enhance the effectiveness of chemotherapy in patients with p53R2-positive melanoma.
These results confirm a role for p53R2 in both Clofarabine and decitabine mechanism of action
In nontransformed cells only during quiescence, protein p53R2 is required for maintenance of mitochondrial DNA and for optimal DNA repair after ultraviolet damage.
Rrm2b plays a crucial role in maintaining chromosomal stability and preventing chronic-inflammation-associated tumorigenesis.
Rrm2b deficiency caused higher rates of spontaneous mutation in the kidneys of Rrm2b-/- mice. p53R2 has a pivotal role in maintaining dNTP levels for repair of DNA in resting cells.
This gene encodes the small subunit of a p53-inducible ribonucleotide reductase. This heterotetrameric enzyme catalyzes the conversion of ribonucleoside diphosphates to deoxyribonucleoside diphosphates. The product of this reaction is necessary for DNA synthesis. Mutations in this gene have been associated with autosomal recessive mitochondrial DNA depletion syndrome, autosomal dominant progressive external ophthalmoplegia-5, and mitochondrial neurogastrointestinal encephalopathy. Alternatively spliced transcript variants have been described.
ribonucleotide reductase M2 B (TP53 inducible)
, ribonucleoside-diphosphate reductase subunit M2 B
, TP53-inducible ribonucleotide reductase M2 B
, p53-inducible ribonucleotide reductase small subunit 2 homolog
, p53-inducible ribonucleotide reductase small subunit 2 short form beta
, p53-inducible ribonucleotide reductase small subunit 2-like protein