The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
about
The OXR domain defines a conserved family of eukaryotic oxidation resistance proteinsFunctional significance of the conserved residues for the 23-residue module among MTH1 and MutT family proteinsHuman MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATPAn oxidized purine nucleoside triphosphatase, MTH1, suppresses cell death caused by oxidative stressHuman MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine and deoxyguanosine diphosphates: comparison with MTH1 and MTH2A novel mechanism for preventing mutations caused by oxidation of guanine nucleotides.Spontaneous tumorigenesis in mice defective in the MTH1 gene encoding 8-oxo-dGTPaseCharacterization of a nudix hydrolase from Deinococcus radiodurans with a marked specificity for (deoxy)ribonucleoside 5'-diphosphatesProtection of pulmonary epithelial cells from oxidative stress by hMYH adenine glycosylaseA functional analysis of the DNA glycosylase activity of mouse MUTYH protein excising 2-hydroxyadenine opposite guanine in DNAThe Caenorhabditis elegans Y87G2A.14 Nudix hydrolase is a peroxisomal coenzyme A diphosphataseMammalian enzymes for preventing transcriptional errors caused by oxidative damage.MTH1 inhibition eradicates cancer by preventing sanitation of the dNTP poolStructural and Dynamic Features of the MutT Protein in the Recognition of Nucleotides with the Mutagenic 8-Oxoguanine BaseDiverse substrate recognition and hydrolysis mechanisms of human NUDT5Crystal structure of human MTH1 and the 8-oxo-dGMP product complexAn Organometallic Inhibitor for the Human Repair Enzyme 7,8-Dihydro-8-oxoguanosine TriphosphataseStereospecific targeting of MTH1 by (S)-crizotinib as an anticancer strategyA novel Nudix hydrolase for oxidized purine nucleoside triphosphates encoded by ORFYLR151c (PCD1 gene) in Saccharomyces cerevisiae.Mutations induced by 8-hydroxyguanine (8-oxo-7,8-dihydroguanine), a representative oxidized base, in mammalian cellsStructure of human MTH1, a Nudix family hydrolase that selectively degrades oxidized purine nucleoside triphosphatesCrystal structure, biochemical and cellular activities demonstrate separate functions of MTH1 and MTH28-Chloro-dGTP, a hypochlorous acid-modified nucleotide, is hydrolyzed by hMTH1, the human MutT homologOxidation of the guanine nucleotide pool underlies cell death by bactericidal antibioticsA role for oxidized DNA precursors in Huntington's disease-like striatal neurodegenerationMycobacterial MazG safeguards genetic stability via housecleaning of 5-OH-dCTPIdentification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multiple forms of hMYH located in nuclei and mitochondriaHouse cleaning, a part of good housekeeping.MTH1 Substrate Recognition--An Example of Specific Promiscuity.Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigenHypersensitivity of Escherichia coli Delta(uvrB-bio) mutants to 6-hydroxylaminopurine and other base analogs is due to a defect in molybdenum cofactor biosynthesis.2-Hydroxy-dATP is incorporated opposite G by Escherichia coli DNA polymerase III resulting in high mutagenicity.Critical amino acids in human DNA polymerases eta and kappa involved in erroneous incorporation of oxidized nucleotides.A Chimeric ATP-Linked Nucleotide Enables Luminescence Signaling of Damage Surveillance by MTH1, a Cancer Target.Urinary 8-oxo-2'-deoxyguanosine--source, significance and supplements.Involvement of oxidatively damaged DNA and repair in cancer development and aging.Erroneous incorporation of oxidized DNA precursors by Y-family DNA polymerases8-oxoguanine causes spontaneous de novo germline mutations in mice.Structural and Kinetic Studies of the Human Nudix Hydrolase MTH1 Reveal the Mechanism for Its Broad Substrate Specificity.The oxidized deoxynucleoside triphosphate pool is a significant contributor to genetic instability in mismatch repair-deficient cells
P2860
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P2860
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
@ast
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
@en
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
@en-gb
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
@nl
type
label
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
@ast
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
@en
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
@en-gb
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
@nl
prefLabel
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
@ast
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
@en
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
@en-gb
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
@nl
P2093
P921
P3181
P356
P1476
The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein
@en
P2093
P304
P3181
P356
10.1074/JBC.274.26.18201
P407
P577
1999-06-25T00:00:00Z