These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

162 related articles for article (PubMed ID: 31284641)

  • 1. PEA-15 C-Terminal Tail Allosterically Modulates Death-Effector Domain Conformation and Facilitates Protein-Protein Interactions.
    Crespo-Flores SL; Cabezas A; Hassan S; Wei Y
    Int J Mol Sci; 2019 Jul; 20(13):. PubMed ID: 31284641
    [TBL] [Abstract][Full Text] [Related]  

  • 2. PEA-15 engages in allosteric interactions using a common scaffold in a phosphorylation-dependent manner.
    Ikedife J; He J; Wei Y
    Sci Rep; 2022 Jan; 12(1):116. PubMed ID: 34997083
    [TBL] [Abstract][Full Text] [Related]  

  • 3. The anti-apoptotic protein PEA-15 is a tight binding inhibitor of ERK1 and ERK2, which blocks docking interactions at the D-recruitment site.
    Callaway K; Abramczyk O; Martin L; Dalby KN
    Biochemistry; 2007 Aug; 46(32):9187-98. PubMed ID: 17658892
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Substantial conformational change mediated by charge-triad residues of the death effector domain in protein-protein interactions.
    Twomey EC; Cordasco DF; Kozuch SD; Wei Y
    PLoS One; 2013; 8(12):e83421. PubMed ID: 24391764
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain.
    Hill JM; Vaidyanathan H; Ramos JW; Ginsberg MH; Werner MH
    EMBO J; 2002 Dec; 21(23):6494-504. PubMed ID: 12456656
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Profound conformational changes of PED/PEA-15 in ERK2 complex revealed by NMR backbone dynamics.
    Twomey EC; Cordasco DF; Wei Y
    Biochim Biophys Acta; 2012 Dec; 1824(12):1382-93. PubMed ID: 22820249
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Phosphorylation of PEA-15 switches its binding specificity from ERK/MAPK to FADD.
    Renganathan H; Vaidyanathan H; Knapinska A; Ramos JW
    Biochem J; 2005 Sep; 390(Pt 3):729-35. PubMed ID: 15916534
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Phosphoprotein enriched in astrocytes (PEA)-15: a potential therapeutic target in multiple disease states.
    Greig FH; Nixon GF
    Pharmacol Ther; 2014 Sep; 143(3):265-74. PubMed ID: 24657708
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Structure of ERK2 bound to PEA-15 reveals a mechanism for rapid release of activated MAPK.
    Mace PD; Wallez Y; Egger MF; Dobaczewska MK; Robinson H; Pasquale EB; Riedl SJ
    Nat Commun; 2013; 4():1681. PubMed ID: 23575685
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Quantifying ERK2-protein interactions by fluorescence anisotropy: PEA-15 inhibits ERK2 by blocking the binding of DEJL domains.
    Callaway K; Rainey MA; Dalby KN
    Biochim Biophys Acta; 2005 Dec; 1754(1-2):316-23. PubMed ID: 16324895
    [TBL] [Abstract][Full Text] [Related]  

  • 11. FADD adaptor and PEA-15/ERK1/2 partners in major depression and schizophrenia postmortem brains: basal contents and effects of psychotropic treatments.
    García-Fuster MJ; Díez-Alarcia R; Ferrer-Alcón M; La Harpe R; Meana JJ; García-Sevilla JA
    Neuroscience; 2014 Sep; 277():541-51. PubMed ID: 25075716
    [TBL] [Abstract][Full Text] [Related]  

  • 12. The death effector domain protein PEA-15 prevents nuclear entry of ERK2 by inhibiting required interactions.
    Whitehurst AW; Robinson FL; Moore MS; Cobb MH
    J Biol Chem; 2004 Mar; 279(13):12840-7. PubMed ID: 14707138
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Structural Studies of ERK2 Protein Complexes.
    Weijman JF; Riedl SJ; Mace PD
    Methods Mol Biol; 2017; 1487():53-63. PubMed ID: 27924558
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Molecular basis of death effector domain chain assembly and its role in caspase-8 activation.
    Singh N; Hassan A; Bose K
    FASEB J; 2016 Jan; 30(1):186-200. PubMed ID: 26370846
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Phosphorylation of phosphoprotein enriched in astrocytes (PEA-15) regulates extracellular signal-regulated kinase-dependent transcription and cell proliferation.
    Krueger J; Chou FL; Glading A; Schaefer E; Ginsberg MH
    Mol Biol Cell; 2005 Aug; 16(8):3552-61. PubMed ID: 15917297
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Human astrocytes are resistant to Fas ligand and tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis.
    Song JH; Bellail A; Tse MC; Yong VW; Hao C
    J Neurosci; 2006 Mar; 26(12):3299-308. PubMed ID: 16554480
    [TBL] [Abstract][Full Text] [Related]  

  • 17. RSK2 activity is regulated by its interaction with PEA-15.
    Vaidyanathan H; Ramos JW
    J Biol Chem; 2003 Aug; 278(34):32367-72. PubMed ID: 12796492
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Quantitative analysis of ERK2 interactions with substrate proteins: roles for kinase docking domains and activity in determining binding affinity.
    Burkhard KA; Chen F; Shapiro P
    J Biol Chem; 2011 Jan; 286(4):2477-85. PubMed ID: 21098038
    [TBL] [Abstract][Full Text] [Related]  

  • 19. PEA-15 modulates TNFalpha intracellular signaling in astrocytes.
    Sharif A; Canton B; Junier MP; Chneiweiss H
    Ann N Y Acad Sci; 2003 Dec; 1010():43-50. PubMed ID: 15033692
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Biochemical and biological functions of the N-terminal, noncatalytic domain of extracellular signal-regulated kinase 2.
    Eblen ST; Catling AD; Assanah MC; Weber MJ
    Mol Cell Biol; 2001 Jan; 21(1):249-59. PubMed ID: 11113199
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 9.