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Journal Abstract Search

214 related items for PubMed ID: 29167269

  • 1. Ring finger protein 126 (RNF126) suppresses ionizing radiation-induced p53-binding protein 1 (53BP1) focus formation.
    Lee NS, Chang HR, Kim S, Ji JH, Lee J, Lee HJ, Seo Y, Kang M, Han JS, Myung K, Kim Y, Kim H.
    J Biol Chem; 2018 Jan 12; 293(2):588-598. PubMed ID: 29167269
    [Abstract] [Full Text] [Related]

  • 2. RNF126 Quenches RNF168 Function in the DNA Damage Response.
    Zhang L, Wang Z, Shi R, Zhu X, Zhou J, Peng B, Xu X.
    Genomics Proteomics Bioinformatics; 2018 Dec 12; 16(6):428-438. PubMed ID: 30529286
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  • 6. Polo-like kinase 1 inhibits DNA damage response during mitosis.
    Benada J, Burdová K, Lidak T, von Morgen P, Macurek L.
    Cell Cycle; 2015 Dec 12; 14(2):219-31. PubMed ID: 25607646
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  • 7. USP3 counteracts RNF168 via deubiquitinating H2A and γH2AX at lysine 13 and 15.
    Sharma N, Zhu Q, Wani G, He J, Wang QE, Wani AA.
    Cell Cycle; 2014 Dec 12; 13(1):106-14. PubMed ID: 24196443
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  • 8. An RNF168 fragment defective for focal accumulation at DNA damage is proficient for inhibition of homologous recombination in BRCA1 deficient cells.
    Muñoz MC, Yanez DA, Stark JM.
    Nucleic Acids Res; 2014 Jul 12; 42(12):7720-33. PubMed ID: 24829461
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  • 9. Tumors overexpressing RNF168 show altered DNA repair and responses to genotoxic treatments, genomic instability and resistance to proteotoxic stress.
    Chroma K, Mistrik M, Moudry P, Gursky J, Liptay M, Strauss R, Skrott Z, Vrtel R, Bartkova J, Kramara J, Bartek J.
    Oncogene; 2017 Apr 27; 36(17):2405-2422. PubMed ID: 27841863
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  • 10. Histone H2A variants alpha1-extension helix directs RNF168-mediated ubiquitination.
    Kelliher JL, West KL, Gong Q, Leung JWC.
    Nat Commun; 2020 May 18; 11(1):2462. PubMed ID: 32424115
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  • 11. A small ubiquitin binding domain inhibits ubiquitin-dependent protein recruitment to DNA repair foci.
    Helchowski CM, Skow LF, Roberts KH, Chute CL, Canman CE.
    Cell Cycle; 2013 Dec 15; 12(24):3749-58. PubMed ID: 24107634
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  • 12. Ubiquitin Phosphorylation at Thr12 Modulates the DNA Damage Response.
    Walser F, Mulder MPC, Bragantini B, Burger S, Gubser T, Gatti M, Botuyan MV, Villa A, Altmeyer M, Neri D, Ovaa H, Mer G, Penengo L.
    Mol Cell; 2020 Nov 05; 80(3):423-436.e9. PubMed ID: 33022275
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  • 13. DNA damage-induced histone H1 ubiquitylation is mediated by HUWE1 and stimulates the RNF8-RNF168 pathway.
    Mandemaker IK, van Cuijk L, Janssens RC, Lans H, Bezstarosti K, Hoeijmakers JH, Demmers JA, Vermeulen W, Marteijn JA.
    Sci Rep; 2017 Nov 10; 7(1):15353. PubMed ID: 29127375
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  • 14. RNF168 promotes noncanonical K27 ubiquitination to signal DNA damage.
    Gatti M, Pinato S, Maiolica A, Rocchio F, Prato MG, Aebersold R, Penengo L.
    Cell Rep; 2015 Jan 13; 10(2):226-38. PubMed ID: 25578731
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  • 15. Ubiquitin-activating enzyme UBA1 is required for cellular response to DNA damage.
    Moudry P, Lukas C, Macurek L, Hanzlikova H, Hodny Z, Lukas J, Bartek J.
    Cell Cycle; 2012 Apr 15; 11(8):1573-82. PubMed ID: 22456334
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  • 16. DNA damage response is suppressed by the high cyclin-dependent kinase 1 activity in mitotic mammalian cells.
    Zhang W, Peng G, Lin SY, Zhang P.
    J Biol Chem; 2011 Oct 14; 286(41):35899-35905. PubMed ID: 21878640
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  • 17. USP11 Is a Negative Regulator to γH2AX Ubiquitylation by RNF8/RNF168.
    Yu M, Liu K, Mao Z, Luo J, Gu W, Zhao W.
    J Biol Chem; 2016 Jan 08; 291(2):959-67. PubMed ID: 26507658
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  • 20. Histone Ubiquitination by the DNA Damage Response Is Required for Efficient DNA Replication in Unperturbed S Phase.
    Schmid JA, Berti M, Walser F, Raso MC, Schmid F, Krietsch J, Stoy H, Zwicky K, Ursich S, Freire R, Lopes M, Penengo L.
    Mol Cell; 2018 Sep 20; 71(6):897-910.e8. PubMed ID: 30122534
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