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DCTP pyrophosphatase 1

dCTPase, XTP3-transactivated protein A
Top mentioned proteins: dUTPase, CAN, ACID, POLYMERASE, pyrophosphatase
Papers on dCTPase
Discovery of the first potent and selective inhibitors of the human dCTP pyrophosphatase 1 (dCTPase).
Helleday et al., In J Med Chem, Feb 2016
UNASSIGNED: The dCTPase pyrophosphatase 1 (dCTPase) regulates the intracellular nucleotide pool through hydrolytic degradation of canonical and non-canonical nucleotide triphosphates (dNTPs).
Human dCTP pyrophosphatase 1 promotes breast cancer cell growth and stemness through the modulation on 5-methyl-dCTP metabolism and global hypomethylation.
Wang et al., Shanghai, China. In Oncogenesis, 2014
Human DCTPP1 (dCTP pyrophosphatase 1), also known as XTP3-transactivated protein A, belongs to MazG-like nucleoside triphosphate pyrophosphatase (NTP-PPase) superfamily.
The NTP pyrophosphatase DCTPP1 contributes to the homoeostasis and cleansing of the dNTP pool in human cells.
González-Pacanowska et al., Granada, Spain. In Biochem J, 2014
Human cells possess an all-α NTP (nucleoside triphosphate) pyrophosphatase named DCTPP1 [dCTP pyrophosphatase 1; also known as XTP3-TPA (XTP3-transactivated protein A)].
Protein profiling and transcript expression levels of heat shock proteins in 17beta-estradiol-treated human MCF-7 breast cancer cells.
Kim et al., Taejŏn, South Korea. In Cell Biol Int, 2006
When the transcript levels of these proteins and another Hsps were measured by real-time PCR, the transcripts encoding 6 proteins (Hsp56, Hsp90alpha, Hsp110, protein disulfide isomerase related protein, XTP3-transactivated protein A and stathmin 1) were significantly up-regulated and that encoding aminoacylase 1 was down-regulated by E2 in cells cultured with or without serum.
Mitogenic estrogen metabolites alter the expression of 17beta-estradiol-regulated proteins including heat shock proteins in human MCF-7 breast cancer cells.
Min et al., Taejŏn, South Korea. In Mol Cells, 2006
Levels of the transcripts of 3 E2-upregulated proteins (XTP3-transactivated protein A, protein disulfide isomerase-associated 4 protein and stathmin 1) and an E2-downregulated protein (aminoacylase 1) were also affected by the E2 metabolites.
Dimeric dUTPases, HisE, and MazG belong to a new superfamily of all-alpha NTP pyrophosphohydrolases with potential "house-cleaning" functions.
Galperin et al., York, United Kingdom. In J Mol Biol, 2005
Structure-guided analysis of the new dimeric dUTPase family revealed its sequence relationship to the phage T4 dCTPase, phosphoribosyl-ATP pyrophosphatase HisE, NTP pyrophosphatase MazG, and several uncharacterized protein families, including the human protein XTP3TPA (RS21-C6), which is overexpressed in embryonic and cancer cells.
The crystal structure of a complex of Campylobacter jejuni dUTPase with substrate analogue sheds light on the mechanism and suggests the "basic module" for dimeric d(C/U)TPases.
Wilson et al., York, United Kingdom. In J Mol Biol, 2004
Homologues of the C.jejuni dUTPase have been identified in several other bacteria and bacteriophages, including the dCTPase of phage T4.
Escherichia coli nucleoside diphosphate kinase interactions with T4 phage proteins of deoxyribonucleotide synthesis and possible regulatory functions.
Mathews et al., Corvallis, United States. In J Biol Chem, 2004
By means of optical biosensor analysis, fluorescence spectroscopy, immunoprecipitation, and glutathione S-transferase pull-down assays, we have shown that E. coli NDP kinase interacts directly with T4 thymidylate synthase, aerobic ribonucleotide reductase, dCTPase-dUTPase, gene 32 single-strand DNA-binding protein, and deoxycytidylate hydroxymethylase.
Trypanosomal dUTPases as potential targets for drug design.
González-Pazanowska et al., Granada, Spain. In Curr Protein Pept Sci, 2001
However, limited similarity was identified for three motifs present in an enzyme related in function the dCTPase-dUTPase from T phages and 35 percent identity with a putative dUTPase identified in the eubacteria Campylobacter jejuni.
Several new bacteriophage T4 genes, mapped by sequencing deletion endpoints between genes 56 (dCTPase) and dda (a DNA-dependent ATPase-helicase) modulate transcription.
Pietz et al., India. In Gene, 1998
We have analyzed DNA of wild-type T4 and of 13 independent large viable deletions isolated by Homyk and Weil (Virology 61 (1974) 505-523) and by Little (Virology 53 (1973) 47-59), by sequencing, cloning, and expression studies.
A species barrier between bacteriophages T2 and T4: exclusion, join-copy and join-cut-copy recombination and mutagenesis in the dCTPase genes.
Mosig et al., Nashville, United States. In Genetics, 1998
Our results argue against a role of the dCTPase protein in this exclusion and implicate instead DNA sequence differences as major contributors to the apparent species barrier.
T4 phage gene 32 protein as a candidate organizing factor for the deoxyribonucleoside triphosphate synthetase complex.
Mathews et al., Corvallis, United States. In J Biol Chem, 1996
In this paper we describe similar analysis of five more proteins: dihydrofolate reductase, dCTPase-dUTPase, deoxyribonucleoside monophosphokinase, ribonucleotide reductase, and E. coli nucleoside diphosphokinase,.
In vivo cleavage of cytosine-containing bacteriophage T4 DNA to genetically distinct, discretely sized fragments.
Wiberg et al., In J Virol, 1983
Mutants of bacteriophage T4D that are defective in genes 42 (dCMP hydroxymethylase), 46 (DNA exonuclease), and 56 (dCTPase) produce limited amounts of phage DNA in Escherichia coli B. In this DNA, glucoylated 5-hydroxymethylcytosine is completely replaced by cytosine.
Partial exclusion of bacteriophage T2 by bacteriophage T4: an exclusion-resistant mutation in gene 56 of T2.
Bom et al., In J Gen Virol, 1981
Additional evidence for location of exr(56)1 within gene 56 was provided by the decrease in the activity of the gene 56 product (dCTPase: EC
T4 ribonucleotide reductase. Physical and kinetic linkage to other enzymes of deoxyribonucleotide biosynthesis.
Mathews et al., In J Biol Chem, 1980
These studies have also confirmed the existence of dCTPase-dUTPase and dCMP deaminase activities in the putative complex.
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