Ask about this productRelated genes to: NUDT18 antibody
- Gene:
- NUDT18 NIH gene
- Name:
- nudix hydrolase 18
- Previous symbol:
- -
- Synonyms:
- FLJ22494, MTH3
- Chromosome:
- 8p21.3
- Locus Type:
- gene with protein product
- Date approved:
- 2005-07-07
- Date modifiied:
- 2016-10-25
Related products to: NUDT18 antibody
Related articles to: NUDT18 antibody
- Nudix hydrolase 18 (NUDT18) belongs to the family of nudix hydrolases. This study aimed to clarify the relationship between NUDT18 and endometrial cancer (EC) and whether it is a prognostic factor for EC. - Source: PubMed
Publication date: 2025/07/25
Hua YueMiao MengdanWang YanZhou Huaijun - Isoprene pyrophosphates play a crucial role in the synthesis of a diverse array of essential nonsterol and sterol biomolecules and serve as substrates for posttranslational isoprenylation of proteins, enabling specific anchoring to cellular membranes. Hydrolysis of isoprene pyrophosphates would be a means to modulate their levels, downstream products, and protein isoprenylation. While NUDIX hydrolases from plants have been described to catalyze the hydrolysis of isoprene pyrophosphates, homologous enzymes with this function in animals have not yet been reported. In this study, we screened an extensive panel of human NUDIX hydrolases for activity in hydrolyzing isoprene pyrophosphates. We found that human nucleotide triphosphate diphosphatase NUDT15 and 8-oxo-dGDP phosphatase NUDT18 efficiently catalyze the hydrolysis of several physiologically relevant isoprene pyrophosphates. Notably, we demonstrate that geranyl pyrophosphate is an excellent substrate for NUDT18, with a catalytic efficiency of 2.1 × 10 m·s, thus making it the best substrate identified for NUDT18 to date. Similarly, geranyl pyrophosphate proved to be the best isoprene pyrophosphate substrate for NUDT15, with a catalytic efficiency of 4.0 × 10 M·s. LC-MS analysis of NUDT15 and NUDT18 catalyzed isoprene pyrophosphate hydrolysis revealed the generation of the corresponding monophosphates and inorganic phosphate. Furthermore, we solved the crystal structure of NUDT15 in complex with the hydrolysis product geranyl phosphate at a resolution of 1.70 Å. This structure revealed that the active site nicely accommodates the hydrophobic isoprenoid moiety and helped identify key binding residues. Our findings imply that isoprene pyrophosphates are endogenous substrates of NUDT15 and NUDT18, suggesting they are involved in animal isoprene pyrophosphate metabolism. - Source: PubMed
Publication date: 2024/06/29
Scaletti Emma RUnterlass Judith EAlmlöf IngridKoolmeister TobiasVallin Karl SKapsitidou DespinaTsuber ViktoriiaHelleday ThomasStenmark PålJemth Ann-Sofie - Multiple sclerosis (MS), a chronic auto-immune, inflammatory, and degenerative disease of the central nervous system, affects both males and females; however, females suffer from a higher risk of developing MS (2-3:1 ratio relative to males). The precise sex-based factors influencing risk of MS are currently unknown. Here, we explore the role of sex in MS to identify molecular mechanisms underlying observed MS sex differences that may guide novel therapeutic approaches tailored for males or females. - Source: PubMed
Publication date: 2023/04/05
Català-Senent José FranciscoAndreu ZoraidaHidalgo Marta RSoler-Sáez IreneRoig Francisco JoséYanguas-Casás NataliaNeva-Alejo AlmudenaLópez-Cerdán Adolfode la Iglesia-Vayá MaríaStranger Barbara EGarcía-García Francisco - Green feed diet in ruminants exerts a beneficial effect on rumen metabolism and enhances the content of milk nutraceutical quality. At present, a comprehensive analysis focused on the identification of genes, and therefore, biological processes modulated by the green feed in buffalo rumen has never been reported. We performed RNA-sequencing in the rumen of buffaloes fed a total mixed ration (TMR) + the inclusion of 30% of ryegrass green feed (treated) or TMR (control), and identified differentially expressed genes (DEGs) using EdgeR and NOISeq tools. - Source: PubMed
Publication date: 2023/03/20
Salzano AngelaFioriniello SalvatoreD'Onofrio NunziaBalestrieri Maria LuisaAiese Cigliano RiccardoNeglia GianlucaDella Ragione FlorianaCampanile Giuseppe - Remdesivir and molnupiravir have gained considerable interest because of their demonstrated activity against SARS-CoV-2. These antivirals are converted intracellularly to their active triphosphate forms remdesivir-TP and molnupiravir-TP. Cellular hydrolysis of these active metabolites would consequently decrease the efficiency of these drugs; however, whether endogenous enzymes that can catalyze this hydrolysis exist is unknown. Here, we tested remdesivir-TP as a substrate against a panel of human hydrolases and found that only Nudix hydrolase (NUDT) 18 catalyzed the hydrolysis of remdesivir-TP with notable activity. The k/K value of NUDT18 for remdesivir-TP was determined to be 17,700 sM, suggesting that NUDT18-catalyzed hydrolysis of remdesivir-TP may occur in cells. Moreover, we demonstrate that the triphosphates of the antivirals ribavirin and molnupiravir are also hydrolyzed by NUDT18, albeit with lower efficiency than Remdesivir-TP. Low activity was also observed with the triphosphate forms of sofosbuvir and aciclovir. This is the first report showing that NUDT18 hydrolyzes triphosphates of nucleoside analogs of exogenous origin, suggesting that NUDT18 can act as a cellular sanitizer of modified nucleotides and may influence the antiviral efficacy of remdesivir, molnupiravir, and ribavirin. As NUDT18 is expressed in respiratory epithelial cells, it may limit the antiviral efficacy of remdesivir and molnupiravir against SARS-CoV-2 replication by decreasing the intracellular concentration of their active metabolites at their intended site of action. - Source: PubMed
Publication date: 2022/06/19
Jemth Ann-SofieScaletti Emma RoseHoman EvertStenmark PålHelleday ThomasMichel Maurice