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    PARG poly(ADP-ribose) glycohydrolase [ Homo sapiens (human) ]

    Gene ID: 8505, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    PARG Promotes Esophagus Cancer Cell Metastasis by Activation of the Wnt/beta-Catenin Pathway.

    PARG Promotes Esophagus Cancer Cell Metastasis by Activation of the Wnt/β-Catenin Pathway.
    Yan J, Zhou Y, Wang Y, Liu Y.

    05/22/2024
    O-GlcNAc has crosstalk with ADP-ribosylation via PARG.

    O-GlcNAc has crosstalk with ADP-ribosylation via PARG.
    Li J, Liu X, Peng B, Feng T, Zhou W, Meng L, Zhao S, Zheng X, Wu C, Wu S, Chen X, Xu X, Sun J, Li J., Free PMC Article

    03/15/2024
    Upregulation of PARG in prostate cancer cells suppresses their malignant behavior and downregulates tumor-promoting genes.

    Upregulation of PARG in prostate cancer cells suppresses their malignant behavior and downregulates tumor-promoting genes.
    Karpova Y, Johnson SJ, Bordet G, Guo D, Ghatak A, Markov DA, Tulin AV.

    10/1/2022
    Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease.

    Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease.
    Prokhorova E, Agnew T, Wondisford AR, Tellier M, Kaminski N, Beijer D, Holder J, Groslambert J, Suskiewicz MJ, Zhu K, Reber JM, Krassnig SC, Palazzo L, Murphy S, Nielsen ML, Mangerich A, Ahel D, Baets J, O'Sullivan RJ, Ahel I., Free PMC Article

    07/24/2021
    PARG overexpression partially but significantly inhibited ASK3 dephosphorylation under hyperosmotic stress, while the glycohydrolase-inactive PARG mutant did not.

    Cells recognize osmotic stress through liquid-liquid phase separation lubricated with poly(ADP-ribose).
    Watanabe K, Morishita K, Zhou X, Shiizaki S, Uchiyama Y, Koike M, Naguro I, Ichijo H., Free PMC Article

    03/4/2021
    Regulation of ALT-associated homology-directed repair by polyADP-ribosylation.

    Regulation of ALT-associated homology-directed repair by polyADP-ribosylation.
    Hoang SM, Kaminski N, Bhargava R, Barroso-González J, Lynskey ML, García-Expósito L, Roncaioli JL, Wondisford AR, Wallace CT, Watkins SC, James DI, Waddell ID, Ogilvie D, Smith KM, da Veiga Leprevost F, Mellacharevu D, Nesvizhskii AI, Li J, Ray-Gallet D, Sobol RW, Almouzni G, O'Sullivan RJ., Free PMC Article

    02/13/2021
    PARG has a robust endo-glycohydrolase activity that releases protein-free poly(ADP-ribose) chains.

    PARG has a robust endo-glycohydrolase activity that releases protein-free poly(ADP-ribose) chains.
    Pourfarjam Y, Kasson S, Tran L, Ho C, Lim S, Kim IK.

    01/23/2021
    PARG, an enzyme family that hydrolyzes poly(ADP-ribose), is sufficient to dissociate damaged DNA-rich compartments in vitro and initiates the nucleocytoplasmic shuttling of FUS in cells.

    PARP-1 Activation Directs FUS to DNA Damage Sites to Form PARG-Reversible Compartments Enriched in Damaged DNA.
    Singatulina AS, Hamon L, Sukhanova MV, Desforges B, Joshi V, Bouhss A, Lavrik OI, Pastré D.

    07/4/2020
    PARG role in the pancreatic ductal adenocarcinoma.

    Poly (ADP) Ribose Glycohydrolase Can Be Effectively Targeted in Pancreatic Cancer.
    Jain A, Agostini LC, McCarthy GA, Chand SN, Ramirez A, Nevler A, Cozzitorto J, Schultz CW, Lowder CY, Smith KM, Waddell ID, Raitses-Gurevich M, Stossel C, Gorman YG, Atias D, Yeo CJ, Winter JM, Olive KP, Golan T, Pishvaian MJ, Ogilvie D, James DI, Jordan AM, Brody JR., Free PMC Article

    06/20/2020
    Oncogenic activity of poly (ADP-ribose) glycohydrolase

    Oncogenic activity of poly (ADP-ribose) glycohydrolase.
    Marques M, Jangal M, Wang LC, Kazanets A, da Silva SD, Zhao T, Lovato A, Yu H, Jie S, Del Rincon S, Mackey J, Damaraju S, Alaoui-Jamali M, Witcher M., Free PMC Article

    05/4/2019
    PARG is acetylated at multiple sites.PARG interacts with PCNA via a non-canonical PIP-box.

    A novel non-canonical PIP-box mediates PARG interaction with PCNA.
    Kaufmann T, Grishkovskaya I, Polyansky AA, Kostrhon S, Kukolj E, Olek KM, Herbert S, Beltzung E, Mechtler K, Peterbauer T, Gotzmann J, Zhang L, Hartl M, Zagrovic B, Elsayad K, Djinovic-Carugo K, Slade D., Free PMC Article

    10/28/2017
    PARG inhibition leads to stalled replication forks and increased homologous recombination (HRR). The lack of HRR proteins at PARG inhibitor-induced replication stalling that induces cell death.

    Specific killing of DNA damage-response deficient cells with inhibitors of poly(ADP-ribose) glycohydrolase.
    Gravells P, Grant E, Smith KM, James DI, Bryant HE., Free PMC Article

    08/5/2017
    Data show that poly-(ADP-ribose) polymerase 1 (PARP1) opposes the function of poly-(ADP-ribose) glycohydrolase (PARG) during regulation of bone morphogenetic protein target gene expression.

    Regulation of Bone Morphogenetic Protein Signaling by ADP-ribosylation.
    Watanabe Y, Papoutsoglou P, Maturi V, Tsubakihara Y, Hottiger MO, Heldin CH, Moustakas A., Free PMC Article

    12/17/2016
    Poly(ADP-ribosyl) glycohydrolase (PARG) is involved in cell proliferation and DNA synthesis, with depletion leading to replication-coupled H2AX phosphorylation. In addition, PARG depletion or inhibition slows down individual replication forks similarly to mild chemotherapeutic treatment.

    Poly(ADP-ribosyl) glycohydrolase prevents the accumulation of unusual replication structures during unperturbed S phase.
    Ray Chaudhuri A, Ahuja AK, Herrador R, Lopes M., Free PMC Article

    11/2/2015
    Studies indicate that poly (ADP-ribose) glycohydrolase (PARG) and terminal ADP-ribose glycohydrolase 1 (TARG1) are key enzymes in poly(ADP-ribose) polymerases (PARPs)-mediated ADP-ribosylation.

    Structures and Mechanisms of Enzymes Employed in the Synthesis and Degradation of PARP-Dependent Protein ADP-Ribosylation.
    Barkauskaite E, Jankevicius G, Ahel I.

    09/26/2015
    Nuclear Smad function is negatively regulated by PARP-1 that is assisted by PARP-2 and positively regulated by PARG during the course of TGFB signaling.

    Fine-tuning of Smad protein function by poly(ADP-ribose) polymerases and poly(ADP-ribose) glycohydrolase during transforming growth factor β signaling.
    Dahl M, Maturi V, Lönn P, Papoutsoglou P, Zieba A, Vanlandewijck M, van der Heide LP, Watanabe Y, Söderberg O, Hottiger MO, Heldin CH, Moustakas A., Free PMC Article

    05/16/2015
    Radiation-induced G2/M arrest was largely suppressed by PARG siRNA in PC-14 and A427 cells, which exhibited significantly enhanced radiosensitivity in response to PARG knockdown.

    Silencing of poly(ADP-ribose) glycohydrolase sensitizes lung cancer cells to radiation through the abrogation of DNA damage checkpoint.
    Nakadate Y, Kodera Y, Kitamura Y, Tachibana T, Tamura T, Koizumi F.

    04/5/2014
    The amount of poly(ADP-ribose) in a cell is regulated under the control of PARP1/PARG gene expression balance.

    PARP1 gene expression is downregulated by knockdown of PARG gene.
    Uchiumi F, Watanabe T, Ohta R, Abe H, Tanuma S., Free PMC Article

    03/8/2014
    PARG knockdown enhances sensitivity to MMS in MIAPaCa2 and RKO tumor cell lines.

    PARG dysfunction enhances DNA double strand break formation in S-phase after alkylation DNA damage and augments different cell death pathways.
    Shirai H, Poetsch AR, Gunji A, Maeda D, Fujimori H, Fujihara H, Yoshida T, Ogino H, Masutani M., Free PMC Article

    03/1/2014
    poly(ADP-ribose) glycohydrolase is crucial for Trypanosoma cruzi infection cycle.

    Host cell poly(ADP-ribose) glycohydrolase is crucial for Trypanosoma cruzi infection cycle.
    Vilchez Larrea SC, Schlesinger M, Kevorkian ML, Flawiá MM, Alonso GD, Fernández Villamil SH., Free PMC Article

    01/25/2014
    Therefore, strategies that target PAR metabolism for the improved treatment of cancer may be required to target PARP-1 and PARG individually in order to optimize cancer cell death.

    Inhibition of poly(ADP-ribose) polymerase-1 or poly(ADP‑ribose) glycohydrolase individually, but not in combination, leads to improved chemotherapeutic efficacy in HeLa cells.
    Feng X, Koh DW., Free PMC Article

    01/11/2014
    PARG silencing could inhibit the ability of HUVEC migration and proliferation by downregulating the activity of NF-kappaB in LoVo cells that in turn decreases angiogenic factors such as VEGF, b-FGF, ICAM-1, MMP-9, as well as phosphorylation of p38 and ERK.

    Effect of silencing PARG in human colon carcinoma LoVo cells on the ability of HUVEC migration and proliferation.
    Pan J, Fauzee NJ, Wang YL, Sheng YT, Tang Y, Wang JQ, Wu WQ, Yan JX, Xu J.

    04/13/2013
    Silencing of Apoptosis-Inducing factor and poly(ADP-ribose) glycohydrolase reveals novel roles in breast cancer cell death after chemotherapy.

    Silencing of Apoptosis-Inducing factor and poly(ADP-ribose) glycohydrolase reveals novel roles in breast cancer cell death after chemotherapy.
    Feng X, Zhou Y, Proctor AM, Hopkins MM, Liu M, Koh DW., Free PMC Article

    03/23/2013
    Results define PARG as a coactivator regulating chromatin remodeling during retinoic acid receptor-dependent gene expression.

    Poly (ADP-ribose) glycohydrolase regulates retinoic acid receptor-mediated gene expression.
    Le May N, Iltis I, Amé JC, Zhovmer A, Biard D, Egly JM, Schreiber V, Coin F.

    02/23/2013
    inhibition of PARG leads to an accumulation of PAR polymers, the collapse of replication forks and the induction of homologous recombination in wild-type cells.

    Inhibition of poly(ADP-ribose) glycohydrolase (PARG) specifically kills BRCA2-deficient tumor cells.
    Fathers C, Drayton RM, Solovieva S, Bryant HE.

    01/5/2013
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