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Journal Abstract Search

298 related items for PubMed ID: 18656483

  • 1. ZNF451 is a novel PML body- and SUMO-associated transcriptional coregulator.
    Karvonen U, Jääskeläinen T, Rytinki M, Kaikkonen S, Palvimo JJ.
    J Mol Biol; 2008 Oct 10; 382(3):585-600. PubMed ID: 18656483
    [Abstract] [Full Text] [Related]

  • 2. The SUMO2/3 specific E3 ligase ZNF451-1 regulates PML stability.
    Koidl S, Eisenhardt N, Fatouros C, Droescher M, Chaugule VK, Pichler A.
    Int J Biochem Cell Biol; 2016 Oct 10; 79():478-487. PubMed ID: 27343429
    [Abstract] [Full Text] [Related]

  • 3. Role of SUMO in RNF4-mediated promyelocytic leukemia protein (PML) degradation: sumoylation of PML and phospho-switch control of its SUMO binding domain dissected in living cells.
    Percherancier Y, Germain-Desprez D, Galisson F, Mascle XH, Dianoux L, Estephan P, Chelbi-Alix MK, Aubry M.
    J Biol Chem; 2009 Jun 12; 284(24):16595-16608. PubMed ID: 19380586
    [Abstract] [Full Text] [Related]

  • 4. SUMO deconjugation is required for arsenic-triggered ubiquitylation of PML.
    Fasci D, Anania VG, Lill JR, Salvesen GS.
    Sci Signal; 2015 Jun 09; 8(380):ra56. PubMed ID: 26060329
    [Abstract] [Full Text] [Related]

  • 5. Identification of a non-covalent ternary complex formed by PIAS1, SUMO1, and UBC9 proteins involved in transcriptional regulation.
    Mascle XH, Lussier-Price M, Cappadocia L, Estephan P, Raiola L, Omichinski JG, Aubry M.
    J Biol Chem; 2013 Dec 20; 288(51):36312-27. PubMed ID: 24174529
    [Abstract] [Full Text] [Related]

  • 6. RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation.
    Tatham MH, Geoffroy MC, Shen L, Plechanovova A, Hattersley N, Jaffray EG, Palvimo JJ, Hay RT.
    Nat Cell Biol; 2008 May 20; 10(5):538-46. PubMed ID: 18408734
    [Abstract] [Full Text] [Related]

  • 7. PML IV/ARF interaction enhances p53 SUMO-1 conjugation, activation, and senescence.
    Ivanschitz L, Takahashi Y, Jollivet F, Ayrault O, Le Bras M, de Thé H.
    Proc Natl Acad Sci U S A; 2015 Nov 17; 112(46):14278-83. PubMed ID: 26578773
    [Abstract] [Full Text] [Related]

  • 8. SUMO Ligase Protein Inhibitor of Activated STAT1 (PIAS1) Is a Constituent Promyelocytic Leukemia Nuclear Body Protein That Contributes to the Intrinsic Antiviral Immune Response to Herpes Simplex Virus 1.
    Brown JR, Conn KL, Wasson P, Charman M, Tong L, Grant K, McFarlane S, Boutell C.
    J Virol; 2016 Jul 01; 90(13):5939-5952. PubMed ID: 27099310
    [Abstract] [Full Text] [Related]

  • 9. Novel Role for Protein Inhibitor of Activated STAT 4 (PIAS4) in the Restriction of Herpes Simplex Virus 1 by the Cellular Intrinsic Antiviral Immune Response.
    Conn KL, Wasson P, McFarlane S, Tong L, Brown JR, Grant KG, Domingues P, Boutell C.
    J Virol; 2016 May 01; 90(9):4807-4826. PubMed ID: 26937035
    [Abstract] [Full Text] [Related]

  • 10. Nucleus accumbens associated 1 is recruited within the promyelocytic leukemia nuclear body through SUMO modification.
    Tatemichi Y, Shibazaki M, Yasuhira S, Kasai S, Tada H, Oikawa H, Suzuki Y, Takikawa Y, Masuda T, Maesawa C.
    Cancer Sci; 2015 Jul 01; 106(7):848-56. PubMed ID: 25891951
    [Abstract] [Full Text] [Related]

  • 11. A non-covalent interaction between small ubiquitin-like modifier-1 and Zac1 regulates Zac1 cellular functions.
    Liu ST, Chang YL, Wang WM, Chung MH, Lin WS, Chou WY, Huang SM.
    Int J Biochem Cell Biol; 2012 Mar 01; 44(3):547-55. PubMed ID: 22227369
    [Abstract] [Full Text] [Related]

  • 12. ZNF198, a zinc finger protein rearranged in myeloproliferative disease, localizes to the PML nuclear bodies and interacts with SUMO-1 and PML.
    Kunapuli P, Kasyapa CS, Chin SF, Caldas C, Cowell JK.
    Exp Cell Res; 2006 Nov 15; 312(19):3739-51. PubMed ID: 17027752
    [Abstract] [Full Text] [Related]

  • 13. Transcriptional activity of peroxisome proliferator-activated receptor gamma is modulated by SUMO-1 modification.
    Ohshima T, Koga H, Shimotohno K.
    J Biol Chem; 2004 Jul 09; 279(28):29551-7. PubMed ID: 15123625
    [Abstract] [Full Text] [Related]

  • 14. Arsenic degrades PML or PML-RARalpha through a SUMO-triggered RNF4/ubiquitin-mediated pathway.
    Lallemand-Breitenbach V, Jeanne M, Benhenda S, Nasr R, Lei M, Peres L, Zhou J, Zhu J, Raught B, de Thé H.
    Nat Cell Biol; 2008 May 09; 10(5):547-55. PubMed ID: 18408733
    [Abstract] [Full Text] [Related]

  • 15. The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA.
    Rabellino A, Carter B, Konstantinidou G, Wu SY, Rimessi A, Byers LA, Heymach JV, Girard L, Chiang CM, Teruya-Feldstein J, Scaglioni PP.
    Cancer Res; 2012 May 01; 72(9):2275-84. PubMed ID: 22406621
    [Abstract] [Full Text] [Related]

  • 16. The ND10 Component Promyelocytic Leukemia Protein Acts as an E3 Ligase for SUMOylation of the Major Immediate Early Protein IE1 of Human Cytomegalovirus.
    Reuter N, Schilling EM, Scherer M, Müller R, Stamminger T.
    J Virol; 2017 May 15; 91(10):. PubMed ID: 28250117
    [Abstract] [Full Text] [Related]

  • 17. SUMOylation of HMGA2: selective destabilization of promyelocytic leukemia protein via proteasome.
    Cao X, Clavijo C, Li X, Lin HH, Chen Y, Shih HM, Ann DK.
    Mol Cancer Ther; 2008 Apr 15; 7(4):923-34. PubMed ID: 18413806
    [Abstract] [Full Text] [Related]

  • 18. PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases.
    Kotaja N, Karvonen U, Jänne OA, Palvimo JJ.
    Mol Cell Biol; 2002 Jul 15; 22(14):5222-34. PubMed ID: 12077349
    [Abstract] [Full Text] [Related]

  • 19. SUMO pathway dependent recruitment of cellular repressors to herpes simplex virus type 1 genomes.
    Cuchet-Lourenço D, Boutell C, Lukashchuk V, Grant K, Sykes A, Murray J, Orr A, Everett RD.
    PLoS Pathog; 2011 Jul 15; 7(7):e1002123. PubMed ID: 21779164
    [Abstract] [Full Text] [Related]

  • 20. BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes in its nuclear body.
    Kuwata T, Nakamura T.
    Genes Cells; 2008 Sep 15; 13(9):931-40. PubMed ID: 18681895
    [Abstract] [Full Text] [Related]

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