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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.


NUDT5, Ysa1, ADP-sugar pyrophosphatase
Nudix hydrolases, such as NUDT5, eliminate toxic nucleotide derivatives from the cell and regulate the levels of important signaling nucleotides and their metabolites (McLennan, 1999 [PubMed 10373642]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: pyrophosphatase, CAN, ACID, V1a, fibrillin-1
Papers on NUDT5
Molecular dynamics study on conformational differences between dGMP and 8-oxo-dGMP: Effects of metal ions.
Amisaki et al., Yonago, Japan. In J Mol Graph Model, 2014
Nucleotide-sanitizing enzymes, such as the MutT homolog-1 (MTH1) and nudix-type motif 5 (NUDT5), selectively remove 8-oxo-G from the cellular pool of nucleotides.
A Nudix Hydrolase Protein, Ysa1, Regulates Oxidative Stress Response and Antifungal Drug Susceptibility in Cryptococcus neoformans.
Bahn et al., Seoul, South Korea. In Mycobiology, 2014
A nucleoside diphosphate-linked moiety X (Nudix) hydrolase-like gene, YSA1, has been identified as one of the gromwell plant extract-responsive genes in Cryptococcus neoformans.
Global transcriptome analysis of eukaryotic genes affected by gromwell extract.
Bahn et al., Seoul, South Korea. In J Sci Food Agric, 2014
Among the GE-responsive genes that are also evolutionarily conserved in the human genome, the expression patterns of YSA1, TPO2, CFO1 and PZF1 were confirmed by northern blot analysis.
Proteomic analysis of endothelial progenitor cells exposed to oxidative stress.
Hu et al., Dalian, China. In Int J Mol Med, 2013
The results revealed that triosephosphate isomerase and ADP-sugar pyrophosphatase were downregulated, while peroxiredoxin-2, thioredoxin-dependent peroxide reductase, mitochondrial (Prx‑3), peroxiredoxin-6, EGF-containing fibulin-like extracellular matrix protein 1, vimentin and Rab GDP dissociation inhibitor α were upregulated in the H2O2-treated EPCs.
Genome-wide association study of genetic predictors of overall survival for non-small cell lung cancer in never smokers.
Yang et al., Houston, United States. In Cancer Res, 2013
An additional six variants (rs4237904, rs7976914, rs4970833, rs954785, rs485411, and rs10906104) were validated through eQTL analysis that identified significant correlations with expression levels of six genes (LEMD3, TMBIM, ATXN7L2, SHE, ITIH2, and NUDT5, respectively) in normal lung tissue.
Lowered Nudix type 5 expression leads to cellular senescence in IMR-90 fibroblast cells.
Cai et al., Beijing, China. In Free Radic Res, 2013
Human Nudix type 5 (NUDT5), a MutT-related protein, catalyzes the hydrolysis of 8-oxoGDP to 8-oxoGMP, thereby preventing the misincorporation of 8-oxoGua into RNA.
Lowered nudix type 5 (NUDT5) expression leads to cell cycle retardation in HeLa cells.
Cai et al., Beijing, China. In Mol Cell Biochem, 2012
Results suggest that the NUDT5 protein may play significant roles in regulating the G1-S transition in HeLa cells.
NDX-1 protein hydrolyzes 8-oxo-7, 8-dihydrodeoxyguanosine-5'-diphosphate to sanitize oxidized nucleotides and prevent oxidative stress in Caenorhabditis elegans.
Zhang-Akiyama et al., Kyoto, Japan. In J Biochem, 2011
Human NUDT5 as well as human MTH1 hydrolyze 8-oxo-dGDP to 8-oxo-dGMP.
Diverse substrate recognition and hydrolysis mechanisms of human NUDT5.
Yamagata et al., Kumamoto, Japan. In Nucleic Acids Res, 2011
The broad substrate specificity of hNUDT5 is achieved by a diversity of not only substrate recognition, but also hydrolysis mechanisms.
Cleavage of oxidized guanine nucleotide and ADP sugar by human NUDT5 protein.
Hayakawa et al., Fukuoka, Japan. In J Biochem, 2011
The human NUDT5, which has an intrinsic activity to cleave ADP sugars to AMP and sugar phosphate, possesses the ability to degrade 8-oxo-dGDP to the monophosphate.
Suppression of mutagenesis by 8-hydroxy-2'-deoxyguanosine 5'-triphosphate (7,8-dihydro-8-oxo-2'-deoxyguanosine 5'-triphosphate) by human MTH1, MTH2, and NUDT5.
Kamiya et al., Sapporo, Japan. In Free Radic Biol Med, 2010
human MTH1, MTH2, and NUDT5 proteins act as a defense against the mutagenesis induced by oxidized dGTP.
NUDT5 hydrolyzes oxidized deoxyribonucleoside diphosphates with broad substrate specificity.
Harashima et al., Sapporo, Japan. In Dna Repair (amst), 2009
NUDT5 protein eliminates various oxidized deoxyribonucleoside diphosphates from the nucleotide pool and prevents their toxic effects.
Molecular mechanism of ADP-ribose hydrolysis by human NUDT5 from structural and kinetic studies.
Ding et al., Shanghai, China. In J Mol Biol, 2008
Results report the crystal structure of hNUDT5 in complex with a non-hydrolyzable ADPR analogue, alpha,beta-methyleneadenosine diphosphoribose, and three Mg(2+) ions representing the transition state of the enzyme during catalysis.
Activation of NUDT5, an ADP-ribose pyrophosphatase, by nitric oxide-mediated ADP-ribosylation.
Kim et al., Chŏnju, South Korea. In Biochem Biophys Res Commun, 2007
The ADP-ribose (ADPR) pyrophosphatase (ADPRase) NUDT5, a member of a superfamily of Nudix hydrolases, hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'-phosphate.
Escherichia coli AspP activity is enhanced by macromolecular crowding and by both glucose-1,6-bisphosphate and nucleotide-sugars.
Pozueta-Romero et al., Spain. In Febs Lett, 2007
Escherichia coli ADP-sugar pyrophosphatase (AspP) is a "Nudix" hydrolase that catalyzes the hydrolytic breakdown of ADP-glucose linked to glycogen biosynthesis.
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