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NMR Meets Tau: Insights into Its Function and PathologyCrystal structures of two Bordetella pertussis periplasmic receptors contribute to defining a novel pyroglutamic acid binding DctP subfamilyStructure-based mechanism of ligand binding for periplasmic solute-binding protein of the Bug familySILAC-based proteomic profiling of the human MDA-MB-231 metastatic breast cancer cell line in response to the two antitumoral lactoferrin isoforms: the secreted lactoferrin and the intracellular delta-lactoferrinStudying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy.Tau monoclonal antibody generation based on humanized yeast models: impact on Tau oligomerization and diagnosticsModification by SUMOylation Controls Both the Transcriptional Activity and the Stability of Delta-Lactoferrin.A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA ReplicationCrystallization and preliminary X-ray diffraction analysis of two extracytoplasmic solute receptors of the DctP family from Bordetella pertussis.NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease.The FK506-binding protein FKBP52 in vitro induces aggregation of truncated Tau forms with prion-like behavior.Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins.Isomerization and Oligomerization of Truncated and Mutated Tau Forms by FKBP52 are Independent Processes.Proline Conformation in a Functional Tau Fragment.H/D exchange of a 15N labelled Tau fragment as measured by a simple Relax-EXSY experiment.Spectroscopic studies of GSK3{beta} phosphorylation of the neuronal tau protein and its interaction with the N-terminal domain of apolipoprotein E.The periplasmic binding protein of a tripartite tricarboxylate transporter is involved in signal transduction.Identification of the Tau phosphorylation pattern that drives its aggregation.Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline-rich region of the disordered Tau protein.A functional fragment of Tau forms fibers without the need for an intermolecular cysteine bridgeMechanism of Tau-Promoted Microtubule Assembly As Probed by NMR SpectroscopyNuclear Magnetic Resonance Analysis of the Acetylation Pattern of the Neuronal Tau ProteinComparison between E1A gene from oncogenic and non-oncogenic adenoviruses in cellular transformation (Ad E1A conserved region)Structural analysis of Bordetella pertussis BugE solute receptor in a bound conformation
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0000-0002-7241-0290