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356 related items for PubMed ID: 26800003

  • 1. Epitope mapping and structural basis for the recognition of phosphorylated tau by the anti-tau antibody AT8.
    Malia TJ, Teplyakov A, Ernst R, Wu SJ, Lacy ER, Liu X, Vandermeeren M, Mercken M, Luo J, Sweet RW, Gilliland GL.
    Proteins; 2016 Apr; 84(4):427-34. PubMed ID: 26800003
    [Abstract] [Full Text] [Related]

  • 2. Uncovering the Effect of pS202/pT205/pS208 Triple Phosphorylations on the Conformational Features of the Key Fragment G192-T212 of Tau Protein.
    Liu H, Li Q, Xiong C, Zhong H, Zhang Q, Liu H, Yao X.
    ACS Chem Neurosci; 2021 Mar 17; 12(6):1039-1048. PubMed ID: 33663205
    [Abstract] [Full Text] [Related]

  • 3. Monoclonal antibody PHF-9 recognizes phosphorylated serine 404 of tau protein and labels paired helical filaments.
    Zemlan FP, Dean GE.
    J Neurosci Res; 1996 Oct 01; 46(1):90-7. PubMed ID: 8892109
    [Abstract] [Full Text] [Related]

  • 4. Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation.
    Zheng-Fischhöfer Q, Biernat J, Mandelkow EM, Illenberger S, Godemann R, Mandelkow E.
    Eur J Biochem; 1998 Mar 15; 252(3):542-52. PubMed ID: 9546672
    [Abstract] [Full Text] [Related]

  • 5. Molecular implication of PP2A and Pin1 in the Alzheimer's disease specific hyperphosphorylation of Tau.
    Landrieu I, Smet-Nocca C, Amniai L, Louis JV, Wieruszeski JM, Goris J, Janssens V, Lippens G.
    PLoS One; 2011 Mar 15; 6(6):e21521. PubMed ID: 21731772
    [Abstract] [Full Text] [Related]

  • 6. Epitope mapping of mAbs AT8 and Tau5 directed against hyperphosphorylated regions of the human tau protein.
    Porzig R, Singer D, Hoffmann R.
    Biochem Biophys Res Commun; 2007 Jun 29; 358(2):644-9. PubMed ID: 17499212
    [Abstract] [Full Text] [Related]

  • 7. A Phosphorylation-Induced Turn Defines the Alzheimer's Disease AT8 Antibody Epitope on the Tau Protein.
    Gandhi NS, Landrieu I, Byrne C, Kukic P, Amniai L, Cantrelle FX, Wieruszeski JM, Mancera RL, Jacquot Y, Lippens G.
    Angew Chem Int Ed Engl; 2015 Jun 01; 54(23):6819-23. PubMed ID: 25881502
    [Abstract] [Full Text] [Related]

  • 8. Recognition of the minimal epitope of monoclonal antibody Tau-1 depends upon the presence of a phosphate group but not its location.
    Szendrei GI, Lee VM, Otvos L.
    J Neurosci Res; 1993 Feb 01; 34(2):243-9. PubMed ID: 7680727
    [Abstract] [Full Text] [Related]

  • 9. Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein.
    Goedert M, Jakes R, Crowther RA, Cohen P, Vanmechelen E, Vandermeeren M, Cras P.
    Biochem J; 1994 Aug 01; 301 ( Pt 3)(Pt 3):871-7. PubMed ID: 7519852
    [Abstract] [Full Text] [Related]

  • 10. Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205.
    Goedert M, Jakes R, Vanmechelen E.
    Neurosci Lett; 1995 Apr 21; 189(3):167-9. PubMed ID: 7624036
    [Abstract] [Full Text] [Related]

  • 11. Unique Alzheimer's disease paired helical filament specific epitopes involve double phosphorylation at specific sites.
    Hoffmann R, Lee VM, Leight S, Varga I, Otvos L.
    Biochemistry; 1997 Jul 01; 36(26):8114-24. PubMed ID: 9201960
    [Abstract] [Full Text] [Related]

  • 12. X-ray structure of the PHF core C-terminus: insight into the folding of the intrinsically disordered protein tau in Alzheimer's disease.
    Sevcik J, Skrabana R, Dvorsky R, Csokova N, Iqbal K, Novak M.
    FEBS Lett; 2007 Dec 22; 581(30):5872-8. PubMed ID: 18061582
    [Abstract] [Full Text] [Related]

  • 13. Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404.
    Otvos L, Feiner L, Lang E, Szendrei GI, Goedert M, Lee VM.
    J Neurosci Res; 1994 Dec 15; 39(6):669-73. PubMed ID: 7534834
    [Abstract] [Full Text] [Related]

  • 14. Preparation, crystallization and preliminary X-ray analysis of the Fab fragment of monoclonal antibody MN423, revealing the structural aspects of Alzheimer's paired helical filaments.
    Csóková N, Skrabana R, Urbániková L, Kovácech B, Popov A, Sevcík J, Novák M.
    Protein Pept Lett; 2006 Dec 15; 13(9):941-4. PubMed ID: 17100650
    [Abstract] [Full Text] [Related]

  • 15. Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease.
    Augustinack JC, Schneider A, Mandelkow EM, Hyman BT.
    Acta Neuropathol; 2002 Jan 15; 103(1):26-35. PubMed ID: 11837744
    [Abstract] [Full Text] [Related]

  • 16. Oxidized and phosphorylated synthetic peptides corresponding to the second and third tubulin-binding repeats of the tau protein reveal structural features of paired helical filament assembly.
    Hoffmann R, Dawson NF, Wade JD, Otvös L.
    J Pept Res; 1997 Aug 15; 50(2):132-42. PubMed ID: 9273897
    [Abstract] [Full Text] [Related]

  • 17. Proline-directed pseudo-phosphorylation at AT8 and PHF1 epitopes induces a compaction of the paperclip folding of Tau and generates a pathological (MC-1) conformation.
    Jeganathan S, Hascher A, Chinnathambi S, Biernat J, Mandelkow EM, Mandelkow E.
    J Biol Chem; 2008 Nov 14; 283(46):32066-76. PubMed ID: 18725412
    [Abstract] [Full Text] [Related]

  • 18. The pattern of human tau phosphorylation is the result of priming and feedback events in primary hippocampal neurons.
    Bertrand J, Plouffe V, Sénéchal P, Leclerc N.
    Neuroscience; 2010 Jun 30; 168(2):323-34. PubMed ID: 20394726
    [Abstract] [Full Text] [Related]

  • 19. Tau Antibody Structure Reveals a Molecular Switch Defining a Pathological Conformation of the Tau Protein.
    Chukwu JE, Pedersen JT, Pedersen LØ, Volbracht C, Sigurdsson EM, Kong XP.
    Sci Rep; 2018 Apr 18; 8(1):6209. PubMed ID: 29670132
    [Abstract] [Full Text] [Related]

  • 20. Crystallization and preliminary X-ray diffraction analysis of two peptides from Alzheimer PHF in complex with the MN423 antibody Fab fragment.
    Skrabana R, Cehlar O, Flachbartova Z, Kovac A, Sevcik J, Novak M.
    Acta Crystallogr Sect F Struct Biol Cryst Commun; 2012 Oct 01; 68(Pt 10):1186-90. PubMed ID: 23027744
    [Abstract] [Full Text] [Related]

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