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Cyclin F and ribonucleotide reductase family member 2 (RRM2) compose a functional axis responsible for nucleotide metabolism. Impairment in this pathway may contribute to increased DNA damage repair and drug resistance. Additionally, we analyzed the expression of RRM2 mRNA and discovered that high expression of RRM2 is associated with worse overall survival.
overexpression of RRM2 is associated with the genesis and progression of neuroblastoma, and may be a potential chemotherapeutic target
Data suggest that targeting of breast cancer 1, early onset protein (BRCA1)-ribonucleotide reductase regulatory subunit M2 (RRM2) axis may represent a paradigm for therapeutic intervention in glioblastoma (GBM).
These results demonstrate that gambogic acid sensitizes pancreatic cancer cells to gemcitabine in vitro and in vivo by inhibiting the activation of the ERK/E2F1/RRM2 signaling pathway.
OX2 and RRM2 are suggested to be prominent markers for breast cancer metastasis.
SLFN11 contributes to the sensitivity of Ewing sarcoma cells to inhibition of ribonucleotide reductase M2
TP53 mutant cancer cells had elevation of ribonucleotide reductase subunit 1 (RRM1) and 2 (RRM2), which was reduced by inhibition of mTORC1.
Results indicate CREB1 as a critical transcription factor of RRM2 which promotes tumor aggressiveness, and imply a significant correlation between CREB1 and RRM2 in CRC specimens.
These findings suggest that the identified APLP2, RRM2, and PRC1 signature could be useful for distinguishing between benign (follicular adenoma) and malignant (follicular carcionma and follicular variant of papillary carcinoma) tumors of the thyroid follicular epithelium.
Data show that inhibition of sphingosine kinase-2 by ABC294640 is synergistically cytotoxic with gemcitabine toward three pancreatic cancer cell lines, resulting in decreased expression of both ribonucleotide reductase regulatory subunit M2 (RRM2) and c-MYC protein (Myc) in all three cell lines.
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.
Here we designed UC-rich and CU-rich 10-nt sequences for engagement of both RRM2 and RRM3 and demonstrated that the TIA-1 RRM23 construct preferentially binds the UC-rich RNA ligand. Together our data support a specific mode of TIA-1 RRM23 interaction with target oligonucleotides consistent with the role of TIA-1 in binding RNA to regulate gene expression
These data suggest that VASH2 reduces the chemosensitivity to gemcitabine in pancreatic cancer cells via JUN-dependent transactivation of RRM2.
HPV31 regulates RRM2 levels through expression of E7 and activation of the ATR-Chk1-E2F1 DNA damage response, which is essential to combat replication stress upon entry into S-phase.
To the best of our knowledge, this is the first study that investigated the relationship of RRM1 and RRM2 gene polymorphisms and Coronary artery disease (CAD).
The SCYL1- BP1 affects the cell cycle through increasing steady state levels of Cyclin F and RRM2 proteins, thus constituting a dual regulatory circuit.
A significant association has been found between RRM2 rs6759180 (located in the 5'UTR, 10126436G>A) and the risk for developing non-small cell lung cancer.
Data show that ribonucleotide reductase M2 (RRM2) is associated with increased nuclear factor kappa B (NF-kappaB) activity.
our findings establish a signaling role for RRM2 in gastric cancer cells and identify that the RRM2/AKT/NF-kappaB signaling pathway is essential for tumor invasiveness in gastric cancer cells
HBV exploits the Chk1-E2F1 axis of the DNA damage response pathway to induce R2 expression in a cell cycle-independent manner.
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.
mice carrying extra alleles of the RNR regulatory subunit RRM2 (Rrm2(TG)) present supraphysiological RNR activity and reduced chromosomal breakage at fragile sites
R2 expression may discriminate cervical cancer phenotype and radiochemotherapy outcome
analysis of transgenic overexpression of ribonucleotide reductase Rrm1 and Rrm2 improves cardiac performance
Cinobufotalin significantly inhibits the growth of the xenografts of endometrial carcinoma Ishikawa in nude mice by inhibiting RRM2 expression.
Data suggest that RRM2 may be an important effector of progesterone signaling to induce cell proliferation and decidualization in uterus.
exclusion as candidate congenital polycystic kidney gene
illegitimate recombination initiated by c-Myc
Adrenergic stimulation of brown adipocytes elevates ribonucleotide reductase subunit R2 in the proliferative stage of adipocyte development; mediating pathways include cAMP/PKA cascades, Src and Erk Map Kinases.
Cobalt substitution of mouse R2 ribonucleotide reductase as a model for the reactive diferrous state.
The small subunit R2 of murine ribonucleotide reductase (RR) may be important for nuclear RR activity and for RR activity in cells having abnormally low ATP levels, such as cancer cells.
S Phase-specific transcription of the mouse ribonucleotide reductase R2 gene requires both a proximal repressive E2F-binding site and an upstream promoter activating region
x-ray crystallographic analysis of the native dinuclear iron center of ribonucleotide reductase protein R2
Results, supported by molecular modeling, strongly suggest that Arg265 of ribonucleotide reductase R2 is involved in the proton-coupled electron transfer pathway and may act as a proton mediator during catalysis.
Chk1 is required for DNA replication at least through regulating RNR2 gene transcription.
results indicate that the affinity of the RNR R2 proteins for binding metals is determined by the nature of one specific residue in the vicinity of the dimetal site, namely the one that carries the tyrosyl radical in class Ia and Ib R2 proteins
The structure of the active site of ribonucleotide reductase M2 (PDB 1XSM) in the radical state (tyrosyl radical) was studied using EPR.
multilayered mechanisms control the differential expression and function of zebrafish R2 gene during cell cycle and under genotoxic stress.
This gene encodes one of two non-identical subunits for ribonucleotide reductase. This reductase catalyzes the formation of deoxyribonucleotides from ribonucleotides. Synthesis of the encoded protein (M2) is regulated in a cell-cycle dependent fashion. Transcription from this gene can initiate from alternative promoters, which results in two isoforms that differ in the lengths of their N-termini. Related pseudogenes have been identified on chromosomes 1 and X.
ribonucleoside-diphosphate reductase subunit M2
, ribonucleotide reductase M2 polypeptide
, ribonucleotide reductase small chain
, ribonucleotide reductase small subunit
, ribonucleoside-diphosphate reductase M2 chain
, Ribonucleotide reductase 2
, reductase M2 polypeptide variant 1
, reductase M2 polypeptide variant 2
, reductase M2 polypeptide variant 3a
, reductase M2 polypeptide variant 3b
, reductase M2 polypeptide variant 3c
, reductase M2 polypeptide variant 3d
, ribonucleotide reductase protein r2 class I