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    NEIL3 nei like DNA glycosylase 3 [ Homo sapiens (human) ]

    Gene ID: 55247, updated on 7-Jul-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    NEIL3 promotes cell proliferation of ccRCC via the cyclin D1-Rb-E2F1 feedback loop regulation.

    NEIL3 promotes cell proliferation of ccRCC via the cyclin D1-Rb-E2F1 feedback loop regulation.
    Zhang M, Jiang Y, Wang J, Yue Y, Liu W, Wang L, Li Y, Wang W, Cai H, Yang Z, Ma M, Lu S, Fan J.

    01/3/2024
    [Overexpression of Nei endonuclease VIII-like protein 3 in hepatocellular carcinoma indicates increased levels of immune infiltration and an unfavorable prognosis].

    [Overexpression of Nei endonuclease VIII-like protein 3 in hepatocellular carcinoma indicates increased levels of immune infiltration and an unfavorable prognosis].
    Wang GN, Zhang YP, Wang MC, Han W, Zhang YC.

    11/1/2023
    EWSR1-induced circNEIL3 promotes glioma progression and exosome-mediated macrophage immunosuppressive polarization via stabilizing IGF2BP3.

    EWSR1-induced circNEIL3 promotes glioma progression and exosome-mediated macrophage immunosuppressive polarization via stabilizing IGF2BP3.
    Pan Z, Zhao R, Li B, Qi Y, Qiu W, Guo Q, Zhang S, Zhao S, Xu H, Li M, Gao Z, Fan Y, Xu J, Wang H, Wang S, Qiu J, Wang Q, Guo X, Deng L, Zhang P, Xue H, Li G., Free PMC Article

    04/2/2022
    CircNEIL3 regulatory loop promotes pancreatic ductal adenocarcinoma progression via miRNA sponging and A-to-I RNA-editing.

    CircNEIL3 regulatory loop promotes pancreatic ductal adenocarcinoma progression via miRNA sponging and A-to-I RNA-editing.
    Shen P, Yang T, Chen Q, Yuan H, Wu P, Cai B, Meng L, Huang X, Liu J, Zhang Y, Hu W, Miao Y, Lu Z, Jiang K., Free PMC Article

    12/4/2021
    DNA glycosylase Neil3 regulates vascular smooth muscle cell biology during atherosclerosis development.

    DNA glycosylase Neil3 regulates vascular smooth muscle cell biology during atherosclerosis development.
    Quiles-Jiménez A, Gregersen I, Segers FM, Skarpengland T, Kroustallaki P, Yang K, Kong XY, Lauritzen KH, Olsen MB, Karlsen TR, Nyman TA, Sagen EL, Bjerkeli V, Suganthan R, Nygård S, Scheffler K, Prins J, Van der Veer E, Øgaard JD, Fløisand Y, Jørgensen HF, Holven KB, Biessen EA, Nilsen H, Dahl TB, Holm S, Bennett MR, Aukrust P, Bjørås M, Halvorsen B.

    09/4/2021
    Deficiency of NEIL3 Enhances the Chemotherapy Resistance of Prostate Cancer.

    Deficiency of NEIL3 Enhances the Chemotherapy Resistance of Prostate Cancer.
    Wang Y, Xu L, Shi S, Wu S, Meng R, Chen H, Jiang Z., Free PMC Article

    05/15/2021
    An autoinhibitory role for the GRF zinc finger domain of DNA glycosylase NEIL3.

    An autoinhibitory role for the GRF zinc finger domain of DNA glycosylase NEIL3.
    Rodriguez AA, Wojtaszek JL, Greer BH, Haldar T, Gates KS, Williams RS, Eichman BF., Free PMC Article

    03/13/2021
    TRAIP is important for the recruitment of NEIL3 but not FANCD2, and knockdown of TRAIP promotes FA/BRCA pathway activation. Interestingly, TRAIP is non-epistatic with both NEIL3 and FA pathways in psoralen-ICL repair, suggesting that TRAIP may function upstream of the two pathways.

    Cooperation of the NEIL3 and Fanconi anemia/BRCA pathways in interstrand crosslink repair.
    Li N, Wang J, Wallace SS, Chen J, Zhou J, D'Andrea AD., Free PMC Article

    05/23/2020
    Results indicate that whilst specificity for 5-hydroxyuracil and thymine glycol was observed, NEIL3 preferentially excises oxidized bases from single stranded DNA and within open fork structures.

    The Biochemical Role of the Human NEIL1 and NEIL3 DNA Glycosylases on Model DNA Replication Forks.
    Albelazi MS, Martin PR, Mohammed S, Mutti L, Parsons JL, Elder RH., Free PMC Article

    01/11/2020
    NEIL3 cleaves psoralen-induced DNA-DNA cross-links in three-stranded and four-stranded DNA substrates to generate unhooked DNA fragments containing either an abasic site or a psoralen-thymine monoadduct. Nei and NEIL1 also cleave a psoralen-induced four-stranded DNA substrate to generate 2 unhooked DNA duplexes with a nick; NEIL3 targets both DNA strands in interstrand cross-links without generating single-strand breaks.

    The Human DNA glycosylases NEIL1 and NEIL3 Excise Psoralen-Induced DNA-DNA Cross-Links in a Four-Stranded DNA Structure.
    Martin PR, Couvé S, Zutterling C, Albelazi MS, Groisman R, Matkarimov BT, Parsons JL, Elder RH, Saparbaev MK., Free PMC Article

    08/3/2019
    NEIL1 and NEIL3 may protect cells against cytotoxic and mutagenic effects of NM-Fapy-dG, but NEIL1 may have a unique role in initiation of base excision repair of AFB1-Fapy-dG

    Processing of N(5)-substituted formamidopyrimidine DNA adducts by DNA glycosylases NEIL1 and NEIL3.
    Minko IG, Christov PP, Li L, Stone MP, McCullough AK, Lloyd RS., Free PMC Article

    07/20/2019
    This study identifies the NEIL3 promoter possessing a G-rich element that can adopt a G4 fold, and when 8-oxo-7,8-dihydroguanine is incorporated, the sequence can lock into a more stable G4 fold via recruitment of the fifth track of Gs.

    The Fifth Domain in the G-Quadruplex-Forming Sequence of the Human NEIL3 Promoter Locks DNA Folding in Response to Oxidative Damage.
    Omaga CA, Fleming AM, Burrows CJ., Free PMC Article

    09/15/2018
    Results suggest a novel role for the DNA glycosylase Neil3 in atherogenesis in balancing lipid metabolism and macrophage function, potentially independently of genome-wide canonical base excision repair of oxidative DNA damage.

    Neil3-dependent base excision repair regulates lipid metabolism and prevents atherosclerosis in Apoe-deficient mice.
    Skarpengland T, Holm S, Scheffler K, Gregersen I, Dahl TB, Suganthan R, Segers FM, Østlie I, Otten JJ, Luna L, Ketelhuth DF, Lundberg AM, Neurauter CG, Hildrestrand G, Skjelland M, Bjørndal B, Svardal AM, Iversen PO, Hedin U, Nygård S, Olstad OK, Krohg-Sørensen K, Slupphaug G, Eide L, Kuśnierczyk A, Folkersen L, Ueland T, Berge RK, Hansson GK, Biessen EA, Halvorsen B, Bjørås M, Aukrust P., Free PMC Article

    06/2/2018
    NEIL3 protects genome stability through targeted repair of oxidative damage in telomeres during S/G2 phase.

    NEIL3 Repairs Telomere Damage during S Phase to Secure Chromosome Segregation at Mitosis.
    Zhou J, Chan J, Lambelé M, Yusufzai T, Stumpff J, Opresko PL, Thali M, Wallace SS., Free PMC Article

    05/5/2018
    NEIL3-dependent modulation of DNA methylation regulates cardiac fibroblast proliferation and thereby affects extracellular matrix modulation after myocardial infarction.

    NEIL3-Dependent Regulation of Cardiac Fibroblast Proliferation Prevents Myocardial Rupture.
    Olsen MB, Hildrestrand GA, Scheffler K, Vinge LE, Alfsnes K, Palibrk V, Wang J, Neurauter CG, Luna L, Johansen J, Øgaard JDS, Ohm IK, Slupphaug G, Kuśnierczyk A, Fiane AE, Brorson SH, Zhang L, Gullestad L, Louch WE, Iversen PO, Østlie I, Klungland A, Christensen G, Sjaastad I, Sætrom P, Yndestad A, Aukrust P, Bjørås M, Finsen AV.

    11/25/2017
    Data indicate that DNA glycosylases MYH, UNG2, MPG, NTH1, NEIL1, 2 and 3 on nascent DNA.

    Monitoring of the spatial and temporal dynamics of BER/SSBR pathway proteins, including MYH, UNG2, MPG, NTH1 and NEIL1-3, during DNA replication.
    Bj Rås KØ, Sousa MML, Sharma A, Fonseca DM, S Gaard CK, Bj Rås M, Otterlei M., Free PMC Article

    10/28/2017
    These findings demonstrate that deficiency in NEIL3 is associated with increased lymphocyte apoptosis, autoantibodies, and predisposition to autoimmunity.

    Deficiency of base excision repair enzyme NEIL3 drives increased predisposition to autoimmunity.
    Massaad MJ, Zhou J, Tsuchimoto D, Chou J, Jabara H, Janssen E, Glauzy S, Olson BG, Morbach H, Ohsumi TK, Schmitz K, Kyriacos M, Kane J, Torisu K, Nakabeppu Y, Notarangelo LD, Chouery E, Megarbane A, Kang PB, Al-Idrissi E, Aldhekri H, Meffre E, Mizui M, Tsokos GC, Manis JP, Al-Herz W, Wallace SS, Geha RS., Free PMC Article

    09/2/2017
    SNPs in NEIL3 are associated with impulsivity in Native American sample.

    Single nucleotide polymorphisms in the REG-CTNNA2 region of chromosome 2 and NEIL3 associated with impulsivity in a Native American sample.
    Ehlers CL, Gizer IR, Bizon C, Slutske W, Peng Q, Schork NJ, Wilhelmsen KC., Free PMC Article

    05/20/2017
    Single nucleotide polymorphism (SNP) rs142310826 near the NEIL3 gene showed a genome-wide significant interaction with caffeine consumption .There was no gender difference for this interaction (P = 0.64 for heterogeneity). NEIL3, a gene belonging to the base excision DNA repair pathway, encodes a DNA glycosylase that recognizes and removes lesions produced by oxidative stress.

    A genome-wide analysis of gene-caffeine consumption interaction on basal cell carcinoma.
    Li X, Cornelis MC, Liang L, Song F, De Vivo I, Giovannucci E, Tang JY, Han J., Free PMC Article

    05/20/2017
    The abnormal expressions of NEIL1, NEIL2, and NEIL3 are involved in cancer through their association with the somatic mutation load.

    Abnormal Expressions of DNA Glycosylase Genes NEIL1, NEIL2, and NEIL3 Are Associated with Somatic Mutation Loads in Human Cancer.
    Shinmura K, Kato H, Kawanishi Y, Igarashi H, Goto M, Tao H, Inoue Y, Nakamura S, Misawa K, Mineta H, Sugimura H., Free PMC Article

    03/4/2017
    NEIL3 rs12645561 SNP TT genotype was associated with increased risk of myocardial infarction.

    Genetic variants in the DNA repair gene NEIL3 and the risk of myocardial infarction in a nested case-control study. The HUNT Study.
    Skarpengland T, Laugsand LE, Janszky I, Luna L, Halvorsen B, Platou CG, Wang W, Vatten LJ, Damås JK, Aukrust P, Bjørås M, Åsvold BO.

    01/23/2016
    Polymorphisms within FLT3, EGFR, NEIL3, and ALOX5 may contribute to the occurrence of GBM.

    Association of polymorphisms in FLT3, EGFR, ALOX5, and NEIL3 with glioblastoma in the Han Chinese population.
    Jin TB, Li XL, Yang H, Jiri M, Shi XG, Yuan DY, Kang LL, Li SQ.

    09/6/2014
    Results show that the base excision and strand incision activities of NEIL3 exhibited a non-concerted action, indicating that NEIL3 mainly operates as a monofunctional DNA glycosylase.

    Human NEIL3 is mainly a monofunctional DNA glycosylase removing spiroimindiohydantoin and guanidinohydantoin.
    Krokeide SZ, Laerdahl JK, Salah M, Luna L, Cederkvist FH, Fleming AM, Burrows CJ, Dalhus B, Bjørås M., Free PMC Article

    07/19/2014
    one role for Neil3 and NEIL1 is to repair DNA base damages in telomeres in vivo and that Neil3 and Neil1 may function in quadruplex-mediated cellular events, such as gene regulation via removal of damaged bases from quadruplex DNA.

    Neil3 and NEIL1 DNA glycosylases remove oxidative damages from quadruplex DNA and exhibit preferences for lesions in the telomeric sequence context.
    Zhou J, Liu M, Fleming AM, Burrows CJ, Wallace SS., Free PMC Article

    11/30/2013
    Here we report the construction of bicistronic expression vectors for expressing in Escherichia coli the full-length mouse Neil3 (MmuNeil3), its glycosylase domain (MmuNeil3Delta324), as well as the glycosylase domain of human Neil3 (NEIL3Delta324).

    Expression and purification of active mouse and human NEIL3 proteins.
    Liu M, Bandaru V, Holmes A, Averill AM, Cannan W, Wallace SS., Free PMC Article

    12/22/2012
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