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Misincorporation of oxidized nucleoside triphosphates into DNA/RNA during replication and transcription can cause mutations that may result in carcinogenesis or neurodegeneration. Zusätzlich bieten wir Ihnen NUDT1 Antikörper (66) und NUDT1 Kits (10) und viele weitere Produktgruppen zu diesem Protein an.
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overall our cell viability data indicates that targeting MTH1 will likely not be an across-the-board effective non-small cell lung cancer therapeutic strategy; rather it induces non-cytotoxic DNA damage that could promote cancer heterogeneity and evolution.
MTH1 is required for maintaining migration and invasion potential of human thyroid cancer cells.
PRDX1 (zeige PRDX1 Proteine) and MTH1 cooperate to prevent accumulation of oxidized guanine in the genome
Results provide evidence that MTH1 is not essential for cancer cell survival.
CDT1 (zeige CDT1 Proteine), MCM7 (zeige MCM7 Proteine), and NUDT1 were shown to be up-regulated in hepatocellular carcinoma tissues and provide a more accurate diagnosis than alpha-fetal protein alone.
Our results reveal a novel antitumor mechanism of (S)-crizotinib in NSCLC which involves activation of ROS (zeige ROS1 Proteine)-dependent ER stress apoptotic pathway and is independent of MTH1 inhibition
this study showed that MTH1 protein expression was closely related to factors associated with a high malignant potential and poor patient survival
method for predicting individual residue contributions to enzyme specificity and binding-site energies, and its application to MTH1.
Data indicate the specificity of the enzyme 8-oxo-dGTPase MTH1 toward the substrate 8-oxo-dGTP.
We demonstrate that in order to kill cancer cells MTH1 inhibitors must also introduce oxidized nucleotides into DNA. Furthermore, we describe TH1579 as a best-in-class MTH1 inhibitor, which we expect to be useful in order to further validate the MTH1 inhibitor concept.
Increased cytotoxicity following MTH1 knockout or treatment with MTH1 inhibitor suggests the oxidation of precursor nucleotides.
The crystal structures of mouse MTH1 in complex with inhibitor TH588 and dog MTH1 elucidate the structural and sequence basis for the observed difference in their affinities for TH588. Amino acid residue 116 in MTH1 is an important determinant of TH588 affinity. The structure of mouse MTH1 in complex with the substrate 8-oxo-dGTP is presented.
These results suggest that MTH1 deficiency might be a causative factor for aging and age-related disorders.
MTH1 protects cells from H2O2-induced cell dysfunction and death by hydrolyzing oxidized purine nucleotides including 8-oxo-dGTP and 2-OH-dATP.
MTH1 efficiently suppresses the accumulation of 8-oxoG in both cellular DNA and RNA in the hippocampus, especially in microglia, caused by excitotoxicity.
Misincorporation of oxidized nucleoside triphosphates into DNA/RNA during replication and transcription can cause mutations that may result in carcinogenesis or neurodegeneration. The protein encoded by this gene is an enzyme that hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP, 8-oxo-dATP, 2-hydroxy-dATP, and 2-hydroxy rATP, to monophosphates, thereby preventing misincorporation. The encoded protein is localized mainly in the cytoplasm, with some in the mitochondria, suggesting that it is involved in the sanitization of nucleotide pools both for nuclear and mitochondrial genomes. Several alternatively spliced transcript variants, some of which encode distinct isoforms, have been identified. Additional variants have been observed, but their full-length natures have not been determined. A single-nucleotide polymorphism that results in the production of an additional, longer isoform (p26) has been described.
, 2-hydroxy-dATP diphosphatase
, 8-oxo-7,8-dihydrodeoxyguanosine triphosphatase
, 8-oxo-7,8-dihydroguanosine triphosphatase
, mutT human homolog 1
, nucleoside diphosphate-linked moiety X motif 1
, nucleoside diphosphate-linked moiety X-type motif 1
, nudix motif 1
, mutT human homolog (8-oxo-dGTPase)
, nudix-type motif 1