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How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assemblyInvestigation of Homeodomain Membrane Translocation Properties: Insights from the Structure Determination of Engrailed-2 Homeodomain in Aqueous and Membrane-Mimetic EnvironmentsCharacterization of ERM transactivation domain binding to the ACID/PTOV domain of the Mediator subunit MED25NMR Reveals the Interplay among the AMSH SH3 Binding Motif, STAM2, and Lys63-Linked Diubiquitin.Tau phosphorylation regulates the interaction between BIN1's SH3 domain and Tau's proline-rich domainIdentification of a Plasmodium falciparum inhibitor-2 motif involved in the binding and regulation activity of protein phosphatase type 1Cell-penetrating peptides with intracellular actin-remodeling activity in malignant fibroblasts.Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy.Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases.Structure, function, and evolution of the beta-thymosin/WH2 (WASP-Homology2) actin-binding module.Catalytic site inhibition of insulin-degrading enzyme by a small molecule induces glucose intolerance in miceCharacterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated KinaseMultifunctionality of the beta-thymosin/WH2 module: G-actin sequestration, actin filament growth, nucleation, and severing.Nuclear magnetic resonance spectroscopy characterization of interaction of Tau with DNA and its regulation by phosphorylation.Overall Structural Model of NS5A Protein from Hepatitis C Virus and Modulation by Mutations Confering Resistance of Virus Replication to Cyclosporin A.Metabolic phenotyping of human plasma by 1 H-NMR at high and medium magnetic field strengths: a case study for lung cancer.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.1H, 15N and 13C assignments of the N-terminal domain of the Mediator complex subunit MED26.NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.Proline Conformation in a Functional Tau Fragment.H/D exchange of a 15N labelled Tau fragment as measured by a simple Relax-EXSY experiment.Interaction study between HCV NS5A-D2 and NS5B using 19F NMR.Solution Structure of the N-Terminal Domain of Mediator Subunit MED26 and Molecular Characterization of Its Interaction with EAF1 and TAF7.Regulation of the interaction between the neuronal BIN1 isoform 1 and Tau proteins - role of the SH3 domain.A Phosphorylation-Induced Turn Defines the Alzheimer's Disease AT8 Antibody Epitope on the Tau Protein.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.A β-Turn Motif in the Steroid Hormone Receptor's Ligand-Binding Domains Interacts with the Peptidyl-prolyl Isomerase (PPIase) Catalytic Site of the Immunophilin FKBP52.A functional fragment of Tau forms fibers without the need for an intermolecular cysteine bridgeStudying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR SpectroscopyNuclear Magnetic Resonance Analysis of the Acetylation Pattern of the Neuronal Tau ProteinBackbone chemical shift assignments of human 14-3-3σDirect Crosstalk Between -GlcNAcylation and Phosphorylation of Tau Protein Investigated by NMR SpectroscopyStructural Basis of Tau Interaction With BIN1 and Regulation by Tau PhosphorylationKinetically Controlled Chemoselective Cyclization Simplifies the Access to Cyclic and Branched Peptides
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P50
description
onderzoeker
@nl
researcher, ORCID id # 0000-0002-3413-5443
@en
name
François-Xavier Cantrelle
@ast
François-Xavier Cantrelle
@en
François-Xavier Cantrelle
@es
François-Xavier Cantrelle
@nl
François-Xavier Cantrelle
@sl
type
label
François-Xavier Cantrelle
@ast
François-Xavier Cantrelle
@en
François-Xavier Cantrelle
@es
François-Xavier Cantrelle
@nl
François-Xavier Cantrelle
@sl
altLabel
Francois-Xavier Cantrelle
@ast
Francois-Xavier Cantrelle
@en
Francois-Xavier Cantrelle
@es
Francois-Xavier Cantrelle
@nl
prefLabel
François-Xavier Cantrelle
@ast
François-Xavier Cantrelle
@en
François-Xavier Cantrelle
@es
François-Xavier Cantrelle
@nl
François-Xavier Cantrelle
@sl
P106
P1153
22933909400
P21
P2381
P31
P496
0000-0002-3413-5443
P569
2000-01-01T00:00:00Z