BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

172 related articles for article (PubMed ID: 11371618)

  • 1. Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4.
    Liu J; Prickett TD; Elliott E; Meroni G; Brautigan DL
    Proc Natl Acad Sci U S A; 2001 Jun; 98(12):6650-5. PubMed ID: 11371618
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Active transport of the ubiquitin ligase MID1 along the microtubules is regulated by protein phosphatase 2A.
    Aranda-Orgillés B; Aigner J; Kunath M; Lurz R; Schneider R; Schweiger S
    PLoS One; 2008; 3(10):e3507. PubMed ID: 18949047
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Mig12, a novel Opitz syndrome gene product partner, is expressed in the embryonic ventral midline and co-operates with Mid1 to bundle and stabilize microtubules.
    Berti C; Fontanella B; Ferrentino R; Meroni G
    BMC Cell Biol; 2004 Feb; 5():9. PubMed ID: 15070402
    [TBL] [Abstract][Full Text] [Related]  

  • 4. MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation.
    Trockenbacher A; Suckow V; Foerster J; Winter J; Krauss S; Ropers HH; Schneider R; Schweiger S
    Nat Genet; 2001 Nov; 29(3):287-94. PubMed ID: 11685209
    [TBL] [Abstract][Full Text] [Related]  

  • 5. MID1 and MID2 homo- and heterodimerise to tether the rapamycin-sensitive PP2A regulatory subunit, alpha 4, to microtubules: implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disorders.
    Short KM; Hopwood B; Yi Z; Cox TC
    BMC Cell Biol; 2002; 3():1. PubMed ID: 11806752
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Developmental expression of alpha4 protein phosphatase regulatory subunit in tissues affected by Opitz syndrome.
    Everett AD; Brautigan DL
    Dev Dyn; 2002 Aug; 224(4):461-4. PubMed ID: 12203739
    [TBL] [Abstract][Full Text] [Related]  

  • 7. MID1 catalyzes the ubiquitination of protein phosphatase 2A and mutations within its Bbox1 domain disrupt polyubiquitination of alpha4 but not of PP2Ac.
    Du H; Wu K; Didoronkute A; Levy MV; Todi N; Shchelokova A; Massiah MA
    PLoS One; 2014; 9(9):e107428. PubMed ID: 25207814
    [TBL] [Abstract][Full Text] [Related]  

  • 8. The Opitz syndrome gene product, MID1, associates with microtubules.
    Schweiger S; Foerster J; Lehmann T; Suckow V; Muller YA; Walter G; Davies T; Porter H; van Bokhoven H; Lunt PW; Traub P; Ropers HH
    Proc Natl Acad Sci U S A; 1999 Mar; 96(6):2794-9. PubMed ID: 10077590
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Solution structure of the microtubule-targeting COS domain of MID1.
    Wright KM; Du H; Dagnachew M; Massiah MA
    FEBS J; 2016 Aug; 283(16):3089-102. PubMed ID: 27367845
    [TBL] [Abstract][Full Text] [Related]  

  • 10. The Opitz syndrome gene product MID1 assembles a microtubule-associated ribonucleoprotein complex.
    Aranda-Orgillés B; Trockenbacher A; Winter J; Aigner J; Köhler A; Jastrzebska E; Stahl J; Müller EC; Otto A; Wanker EE; Schneider R; Schweiger S
    Hum Genet; 2008 Mar; 123(2):163-76. PubMed ID: 18172692
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Structural and functional observations of the P151L MID1 mutation reveal alpha4 plays a significant role in X-linked Opitz Syndrome.
    Wright KM; Du H; Massiah MA
    FEBS J; 2017 Jul; 284(14):2183-2193. PubMed ID: 28548391
    [TBL] [Abstract][Full Text] [Related]  

  • 12. The MID1 E3 ligase catalyzes the polyubiquitination of Alpha4 (α4), a regulatory subunit of protein phosphatase 2A (PP2A): novel insights into MID1-mediated regulation of PP2A.
    Du H; Huang Y; Zaghlula M; Walters E; Cox TC; Massiah MA
    J Biol Chem; 2013 Jul; 288(29):21341-21350. PubMed ID: 23740247
    [TBL] [Abstract][Full Text] [Related]  

  • 13. A structure-function study of MID1 mutations associated with a mild Opitz phenotype.
    Mnayer L; Khuri S; Merheby HA; Meroni G; Elsas LJ
    Mol Genet Metab; 2006 Mar; 87(3):198-203. PubMed ID: 16378742
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Cytokine activation of p38 mitogen-activated protein kinase and apoptosis is opposed by alpha-4 targeting of protein phosphatase 2A for site-specific dephosphorylation of MEK3.
    Prickett TD; Brautigan DL
    Mol Cell Biol; 2007 Jun; 27(12):4217-27. PubMed ID: 17438131
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Control of mTORC1 signaling by the Opitz syndrome protein MID1.
    Liu E; Knutzen CA; Krauss S; Schweiger S; Chiang GG
    Proc Natl Acad Sci U S A; 2011 May; 108(21):8680-5. PubMed ID: 21555591
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Mechanism of midline defect-causing mutation P151L in MID1 revealed.
    Nicholson LK
    FEBS J; 2017 Jul; 284(14):2167-2169. PubMed ID: 28714291
    [TBL] [Abstract][Full Text] [Related]  

  • 17. FXY2/MID2, a gene related to the X-linked Opitz syndrome gene FXY/MID1, maps to Xq22 and encodes a FNIII domain-containing protein that associates with microtubules.
    Perry J; Short KM; Romer JT; Swift S; Cox TC; Ashworth A
    Genomics; 1999 Dec; 62(3):385-94. PubMed ID: 10644436
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit α4, altering PP2A stability and microtubule-associated protein phosphorylation.
    Watkins GR; Wang N; Mazalouskas MD; Gomez RJ; Guthrie CR; Kraemer BC; Schweiger S; Spiller BW; Wadzinski BE
    J Biol Chem; 2012 Jul; 287(29):24207-15. PubMed ID: 22613722
    [TBL] [Abstract][Full Text] [Related]  

  • 19. The MID1/PP2A complex: a key to the pathogenesis of Opitz BBB/G syndrome.
    Schweiger S; Schneider R
    Bioessays; 2003 Apr; 25(4):356-66. PubMed ID: 12655643
    [TBL] [Abstract][Full Text] [Related]  

  • 20. XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.
    Wright KM; Wu K; Babatunde O; Du H; Massiah MA
    PLoS One; 2014; 9(9):e107537. PubMed ID: 25216264
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 9.