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NMR Meets Tau: Insights into Its Function and PathologyInvolvement of 14-3-3 in tubulin instability and impaired axon development is mediated by TauInterplay between troponin T phosphorylation and O-N-acetylglucosaminylation in ischaemic heart failureIncreasing brain protein O-GlcNAc-ylation mitigates breathing defects and mortality of Tau.P301L miceCell signaling, post-translational protein modifications and NMR spectroscopyThe thymine-DNA glycosylase regulatory domain: residual structure and DNA bindingA TDG/CBP/RARα ternary complex mediates the retinoic acid-dependent expression of DNA methylation-sensitive genesMolecular basis for an ancient partnership between prolyl isomerase Pin1 and phosphatase inhibitor-2SUMO-1 possesses DNA binding activity.SUMO-1 regulates the conformational dynamics of thymine-DNA Glycosylase regulatory domain and competes with its DNA binding activity.Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.Molecular implication of PP2A and Pin1 in the Alzheimer's disease specific hyperphosphorylation of Tau.Neurofibrillary degeneration of the Alzheimer-type: an alternate pathway to neuronal apoptosis?50nm-scale localization of single unmodified, isotopically enriched, proteins in cells.Studying the natively unfolded neuronal Tau protein by solution NMR spectroscopy.Exploring the molecular function of PIN1 by nuclear magnetic resonance.Molecular mechanisms of the phospho-dependent prolyl cis/trans isomerase Pin1.NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease.Nuclear magnetic resonance spectroscopy characterization of interaction of Tau with DNA and its regulation by phosphorylation.Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins.Tau pathology modulates Pin1 post-translational modifications and may be relevant as biomarker.Proline Conformation in a Functional Tau Fragment.Control of protein-protein interactions: structure-based discovery of low molecular weight inhibitors of the interactions between Pin1 WW domain and phosphopeptides.Pin1: a therapeutic target in Alzheimer neurodegeneration.NMR-based detection of acetylation sites in peptides.Structure and plasticity of the peptidyl-prolyl isomerase Par27 of Bordetella pertussis revealed by X-ray diffraction and small-angle X-ray scattering.Proline-directed random-coil chemical shift values as a tool for the NMR assignment of the tau phosphorylation sites.The peptidyl prolyl cis/trans-isomerase Pin1 recognizes the phospho-Thr212-Pro213 site on Tau.The Study of Posttranslational Modifications of Tau Protein by Nuclear Magnetic Resonance Spectroscopy: Phosphorylation of Tau Protein by ERK2 Recombinant Kinase and Rat Brain Extract, and Acetylation by Recombinant Creb-Binding Protein.The O-β-linked N-acetylglucosaminylation of the Lamin B receptor and its impact on DNA binding and phosphorylation.Identification of the Tau phosphorylation pattern that drives its aggregation.Traceless purification and desulfurization of tau protein ligation products.Tag-Free Semi-Synthesis of the Tau Protein.Semi-synthesis of a tag-free O-GlcNAcylated tau protein by sequential chemoselective ligation.Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.A functional fragment of Tau forms fibers without the need for an intermolecular cysteine bridgeRegulation of Pin1 peptidyl-prolylcis/transisomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau proteinNuclear Magnetic Resonance Analysis of the Acetylation Pattern of the Neuronal Tau ProteinAccepting its Random Coil Nature Allows a Partial NMR Assignment of the Neuronal Tau ProteinFrom Epigenomic to Morphogenetic Emergence
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