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    NUDT5 nudix hydrolase 5 [ Homo sapiens (human) ]

    Gene ID: 11164, updated on 2-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    The novel phosphatase NUDT5 is a critical regulator of triple-negative breast cancer growth.

    The novel phosphatase NUDT5 is a critical regulator of triple-negative breast cancer growth.
    Qian J, Ma Y, Tahaney WM, Moyer CL, Lanier A, Hill J, Coleman D, Koupaei N, Hilsenbeck SG, Savage MI, Page BDG, Mazumdar A, Brown PH., Free PMC Article

    03/11/2024
    NUDT5-Determines the fate of head and neck squamous cell carcinoma cells under endoplasmic reticulum stress by catalyzing nuclear ATP production to promote DNA repair.

    NUDT5-Determines the fate of head and neck squamous cell carcinoma cells under endoplasmic reticulum stress by catalyzing nuclear ATP production to promote DNA repair.
    Ding H, Wu C, Sun W, Zhan Q, Huang Y, Liao N, Jiang Z, Wang K, Li Y.

    05/23/2023
    Silencing of Nudix type 5 represses proliferation and invasion and enhances chemosensitivity of gastric carcinoma cells by affecting the AKT/GSK-3beta/beta-catenin pathway.

    Silencing of Nudix type 5 represses proliferation and invasion and enhances chemosensitivity of gastric carcinoma cells by affecting the AKT/GSK-3β/β-catenin pathway.
    Tan D, Zhang Y.

    05/7/2022
    The high expression of NUDT5 indicates poor prognosis of breast cancer by modulating AKT / Cyclin D signaling.

    The high expression of NUDT5 indicates poor prognosis of breast cancer by modulating AKT / Cyclin D signaling.
    Zhang H, Zhang LQ, Yang CC, Li J, Tian XY, Li DN, Cui J, Cai JP., Free PMC Article

    07/31/2021
    The high expression of MTH1 and NUDT5 promotes tumor metastasis and indicates a poor prognosis in patients with non-small-cell lung cancer.

    The high expression of MTH1 and NUDT5 promotes tumor metastasis and indicates a poor prognosis in patients with non-small-cell lung cancer.
    Li DN, Yang CC, Li J, Ou Yang QG, Zeng LT, Fan GQ, Liu TH, Tian XY, Wang JJ, Zhang H, Dai DP, Cui J, Cai JP.

    04/17/2021
    Data suggest that targeting nudix hydrolase 5 (NUDT5) may represent a promising new therapeutic approach for breast cancer treatment.

    Targeted NUDT5 inhibitors block hormone signaling in breast cancer cells.
    Page BDG, Valerie NCK, Wright RHG, Wallner O, Isaksson R, Carter M, Rudd SG, Loseva O, Jemth AS, Almlöf I, Font-Mateu J, Llona-Minguez S, Baranczewski P, Jeppsson F, Homan E, Almqvist H, Axelsson H, Regmi S, Gustavsson AL, Lundbäck T, Scobie M, Strömberg K, Stenmark P, Beato M, Helleday T., Free PMC Article

    03/3/2018
    In the presence of pyrophosphate, ADP-ribose is used by the pyrophosphatase NUDIX5 to generate nuclear ATP.

    ADP-ribose-derived nuclear ATP synthesis by NUDIX5 is required for chromatin remodeling.
    Wright RH, Lioutas A, Le Dily F, Soronellas D, Pohl A, Bonet J, Nacht AS, Samino S, Font-Mateu J, Vicent GP, Wierer M, Trabado MA, Schelhorn C, Carolis C, Macias MJ, Yanes O, Oliva B, Beato M.

    07/2/2016
    The NUDT5 protein could play significant roles in the prevention of RNA oxidation and survival in human fibroblast cells.

    Lowered Nudix type 5 expression leads to cellular senescence in IMR-90 fibroblast cells.
    Zhang L, Song XN, Dai DP, Zhou XY, Gan W, Takagi Y, Hayakawa H, Sekiguchi M, Cai JP.

    09/27/2014
    Results suggest that the NUDT5 protein may play significant roles in regulating the G1-S transition in HeLa cells.

    Lowered nudix type 5 (NUDT5) expression leads to cell cycle retardation in HeLa cells.
    Zhang LQ, Dai DP, Gan W, Takagi Y, Hayakawa H, Sekiguchi M, Cai JP.

    07/7/2012
    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.

    Cleavage of oxidized guanine nucleotide and ADP sugar by human NUDT5 protein.
    Ito R, Sekiguchi M, Setoyama D, Nakatsu Y, Yamagata Y, Hayakawa H.

    02/4/2012
    The broad substrate specificity of hNUDT5 is achieved by a diversity of not only substrate recognition, but also hydrolysis mechanisms.

    Diverse substrate recognition and hydrolysis mechanisms of human NUDT5.
    Arimori T, Tamaoki H, Nakamura T, Kamiya H, Ikemizu S, Takagi Y, Ishibashi T, Harashima H, Sekiguchi M, Yamagata Y., Free PMC Article

    01/21/2012
    human MTH1, MTH2, and NUDT5 proteins act as a defense against the mutagenesis induced by oxidized dGTP.

    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.
    Hori M, Satou K, Harashima H, Kamiya H.

    06/28/2010
    NUDT5 protein eliminates various oxidized deoxyribonucleoside diphosphates from the nucleotide pool and prevents their toxic effects.

    NUDT5 hydrolyzes oxidized deoxyribonucleoside diphosphates with broad substrate specificity.
    Kamiya H, Hori M, Arimori T, Sekiguchi M, Yamagata Y, Harashima H.

    01/25/2010
    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.

    Molecular mechanism of ADP-ribose hydrolysis by human NUDT5 from structural and kinetic studies.
    Zha M, Guo Q, Zhang Y, Yu B, Ou Y, Zhong C, Ding J.

    01/21/2010
    degrades 8-oxo-dGDP to 8-oxo-dGMP, an unusable form for DNA synthesis, and promotes the cleavage of 8-oxo-dGTP by MTH1 to yield 8-oxo-dGMP also

    A novel mechanism for preventing mutations caused by oxidation of guanine nucleotides.
    Ishibashi T, Hayakawa H, Sekiguchi M., Free PMC Article

    01/21/2010
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