176 related articles for article (PubMed ID: 22194938)
1. NMR studies of the C-terminus of alpha4 reveal possible mechanism of its interaction with MID1 and protein phosphatase 2A.
Du H; Massiah MA
PLoS One; 2011; 6(12):e28877. PubMed ID: 22194938
[TBL] [Abstract][Full Text] [Related]
2. 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]
3. 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]
4. The E3 ubiquitin ligase- and protein phosphatase 2A (PP2A)-binding domains of the Alpha4 protein are both required for Alpha4 to inhibit PP2A degradation.
LeNoue-Newton M; Watkins GR; Zou P; Germane KL; McCorvey LR; Wadzinski BE; Spiller BW
J Biol Chem; 2011 May; 286(20):17665-71. PubMed ID: 21454489
[TBL] [Abstract][Full Text] [Related]
5. Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination.
McConnell JL; Watkins GR; Soss SE; Franz HS; McCorvey LR; Spiller BW; Chazin WJ; Wadzinski BE
Biochemistry; 2010 Mar; 49(8):1713-8. PubMed ID: 20092282
[TBL] [Abstract][Full Text] [Related]
6. Detection and characterization of the in vitro e3 ligase activity of the human MID1 protein.
Han X; Du H; Massiah MA
J Mol Biol; 2011 Apr; 407(4):505-20. PubMed ID: 21296087
[TBL] [Abstract][Full Text] [Related]
7. 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]
8. 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]
9. Molecular dynamics simulation reveals insights into the mechanism of unfolding by the A130T/V mutations within the MID1 zinc-binding Bbox1 domain.
Zhao Y; Zeng C; Massiah MA
PLoS One; 2015; 10(4):e0124377. PubMed ID: 25874572
[TBL] [Abstract][Full Text] [Related]
10. 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]
11. The structure of Tap42/alpha4 reveals a tetratricopeptide repeat-like fold and provides insights into PP2A regulation.
Yang J; Roe SM; Prickett TD; Brautigan DL; Barford D
Biochemistry; 2007 Jul; 46(30):8807-15. PubMed ID: 17616149
[TBL] [Abstract][Full Text] [Related]
12. Interaction analysis of the heterotrimer formed by the phosphatase 2A catalytic subunit, alpha4 and the mammalian ortholog of yeast Tip41 (TIPRL).
Smetana JH; Zanchin NI
FEBS J; 2007 Nov; 274(22):5891-904. PubMed ID: 17944932
[TBL] [Abstract][Full Text] [Related]
13. 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]
14. Progestin-inducible EDD E3 ubiquitin ligase binds to α4 phosphoprotein to regulate ubiquitination and degradation of protein phosphatase PP2Ac.
McDonald WJ; Thomas LN; Koirala S; Too CKL
Mol Cell Endocrinol; 2014 Jan; 382(1):254-261. PubMed ID: 24145130
[TBL] [Abstract][Full Text] [Related]
15. Solution structure of the MID1 B-box2 CHC(D/C)C(2)H(2) zinc-binding domain: insights into an evolutionarily conserved RING fold.
Massiah MA; Matts JA; Short KM; Simmons BN; Singireddy S; Yi Z; Cox TC
J Mol Biol; 2007 May; 369(1):1-10. PubMed ID: 17428496
[TBL] [Abstract][Full Text] [Related]
16. Solution structure of the RBCC/TRIM B-box1 domain of human MID1: B-box with a RING.
Massiah MA; Simmons BN; Short KM; Cox TC
J Mol Biol; 2006 Apr; 358(2):532-45. PubMed ID: 16529770
[TBL] [Abstract][Full Text] [Related]
17. Structure of the MID1 tandem B-boxes reveals an interaction reminiscent of intermolecular ring heterodimers.
Tao H; Simmons BN; Singireddy S; Jakkidi M; Short KM; Cox TC; Massiah MA
Biochemistry; 2008 Feb; 47(8):2450-7. PubMed ID: 18220417
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. 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]
20. B-box1 Domain of MID1 Interacts with the Ube2D1 E2 Enzyme Differently Than RING E3 Ligases.
Kaur A; Gladu EM; Wright KM; Webb JA; Massiah MA
Biochemistry; 2023 Mar; 62(5):1012-1025. PubMed ID: 36820504
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]