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Nuclear RNR-alpha antagonizes cell proliferation by directly inhibiting ZRANB3
Adenocarcinoma-specific mRNA expression levels of EZH2 and RRM1 are associated with poor post-surgical survival in the first set of patients, but not replicated in a clinically and pathologically matched independent validation set. This study highlights challenges associated with clinical translation of prognostic biomarkers.
overexpression of RRM1 was correlated with poor prognosis in metastatic bladder cancer patients who underwent gemcitabine-containing chemotherapy
The evaluation of RRM1 gene expression in cfRNA allows for estimation of the risk of severe oral mucositis (OM) in patients subjected to radiotherapy
The expression of RRM1 can be considered a predictor of poor survival in patients with pancreatic cancer receiving gemcitabine chemotherapy.
Our results therefore demonstrate that RRM1 is a novel therapeutic target in multiple myeloma in the preclinical setting and provide the basis for clinical evaluation of RRM1 inhibitor, alone or in combination with DNA-damaging agents, to improve patient outcome in multiple myeloma
three SNPs (corepressor interacting with RBPJ 1 (CIR1) rs13009079T>C, ribonucleotide reductase M1 (RRM1) rs1465952T>C and solute carrier family 38, member 4 (SLC38A4) rs2429467C>T), may play a role in the pathogenesis of lung cancer
TP53 mutant cancer cells had elevation of ribonucleotide reductase subunit 1 (RRM1) and 2 (RRM2), which was reduced by inhibition of mTORC1.
The genetic polymorphisms RRM1 -756T>C and -269C>A may not be a factor for susceptibility to cervical neoplasia
Based on the results of clinical trials, we conclude that Ribonucleotide reductase (RR) enzymes (RR1 and RR2)inhibitors are viable treatment options, either as a monotherapy or as a combination in cancer chemotherapy. With the recent advances made in cancer biology, further development of RR inhibitors with improved efficacy and reduced toxicity is possible for treatment of variety of cancers.
RRM1 single nucleotide polymorphism is associated with Non-Small-Cell Lung Cancer.
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.
findings suggest that the up-regulated RRM1 and hTrx1 in colorectal cancer directly interact with each other and promote RR activity, resulting in enhanced DNA synthesis and cancer malignancy.
RRM1 and ERCC1 expression levels did not show any relationship with overall survival.
RRM1 and ERCC wild type alleles are risk-reducing factor for Coronary artery disease (CAD). Also, carrying RRM1 A allele might have a protective effect for smokers.
Presence of rare AA (-37C>A) and CC (-524C>T) genotypes of the RRM1 may be favorable predictive factors for chemotherapy with platinum compounds and gemcitabine in non-small cell lung cancer patients.
study finds that ERCC1 and RRM1 are not independent prognostic factors of recurrence in stage I non-small cell lung cancer patients
mRNA expression of RRM1 was closely associated with cell proliferation and varied in seven non-Hodgkin lymphoma cell lines.
A significant association has been found between RRM1 rs12806698 (-269C>A) RRM1 genotype and the risk for developing non-small cell lung cancer.
Results underline the relevance of microRNA-101-3p-driven regulation of RRM1 in pancreatic ductal carcinoma gemcitabine resistance.
This study provides an improved understanding of the molecular basis (structure and dynamics) that governs the binding of the p54(nrb)/NonO RRM1 to one of its target RNAs.
This work reveals that binding of RRM1 to RRM2 is essential for mammalian cells and provides the first loss-of-function model of the ribonucleotide reductase complex for genetic studies.
analysis of transgenic overexpression of ribonucleotide reductase Rrm1 and Rrm2 improves cardiac performance
silencing RRM1 expression using siRNA could potentially be an effective strategy to overcome gemcitabine resistance.
Tip60-dependent recruitment of RNR plays an essential role in dNTP supply for DNA repair
The hexamer form of murine ribonucleotide reductase (mRR) large catalytic subunit mR1(6) predominates over the dimer form mR1(2) in the cytoplasm of normal cells, where the great majority of mRR activity is located.
overexpression of RRM1 in human and mouse lung cancer cell lines induced PTEN expression, reduced phosphorylation of focal adhesion kinase (FAK), suppressed migration, invasion, and metastasis formation, and increased survival in an animal model.
This gene encodes one of two non-identical subunits that constitute ribonucleoside-diphosphate reductase, an enzyme essential for the production of deoxyribonucleotides prior to DNA synthesis in S phase of dividing cells. It is one of several genes located in the imprinted gene domain of 11p15.5, an important tumor-suppressor gene region. Alterations in this region have been associated with the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocrotical carcinoma, and lung, ovarian, and breast cancer. This gene may play a role in malignancies and disease that involve this region.
ribonucleoside diphosphate reductase large subunit
, ribonucleoside diphosphate reductase M1 subunit
, ribonucleoside-diphosphate reductase large subunit
, ribonucleoside-diphosphate reductase M1 chain
, ribonucleotide reductase M1 polypeptide
, ribonucleotide reductase M1
, ribonucleoside-diphosphate reductase large subunit-like
, ribonucleoside-diphosphate reductase subunit M1
, ribonucleotide reductase, R1 subunit
, ribonucleotide reductase large subunit
, ribonucleotide reductase protein r1 class I