Isabelle Landrieu

Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.

Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana.

Assignment of the 1H, 13C and 15N resonances and secondary structure of the monomeric p13suc1 protein of Saccharomyces pombe.

Pin1: a therapeutic target in Alzheimer neurodegeneration.

Neurofibrillary degeneration of the Alzheimer-type: an alternate pathway to neuronal apoptosis?

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.

Structural analysis of Escherichia coli OpgG, a protein required for the biosynthesis of osmoregulated periplasmic glucans.

A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana.

Characterization of the Arabidopsis thaliana Arath;CDC25 dual-specificity tyrosine phosphatase.

Accepting its random coil nature allows a partial NMR assignment of the neuronal Tau protein.

Monitoring of the ethionamide pro-drug activation in mycobacteria by (1)H high resolution magic angle spinning NMR.

Regulation of Pin1 peptidyl-prolyl cis/trans isomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau protein.

High-resolution magic angle spinning NMR of the neuronal tau protein integrated in Alzheimer's-like paired helical fragments.

Control of protein-protein interactions: structure-based discovery of low molecular weight inhibitors of the interactions between Pin1 WW domain and phosphopeptides.

Regions of tau implicated in the paired helical fragment core as defined by NMR.

Studying the natively unfolded neuronal Tau protein by solution NMR spectroscopy.

NMR analysis of a Tau phosphorylation pattern.

Arabidopsis PASTICCINO2 is an antiphosphatase involved in regulation of cyclin-dependent kinase A.

ELISE NMR: experimental liquid sealing of NMR samples.

Exploring the molecular function of PIN1 by nuclear magnetic resonance.

Selective intracellular accumulation of the major metabolite issued from the activation of the prodrug ethionamide in mycobacteria.

Structural impact of heparin binding to full-length Tau as studied by NMR spectroscopy.

NMR investigation of the interaction between the neuronal protein tau and the microtubules.

Structural and functional characterization of the interaction between cyclophilin B and a heparin-derived oligosaccharide.

The peptidyl-prolyl isomerase and chaperone Par27 of Bordetella pertussis as the prototype for a new group of parvulins.

Microinjection of recombinant O-GlcNAc transferase potentiates Xenopus oocytes M-phase entry.

NMR observation of Tau in Xenopus oocytes.

The talin rod IBS2 alpha-helix interacts with the beta3 integrin cytoplasmic tail membrane-proximal helix by establishing charge complementary salt bridges.

Alzheimer disease specific phosphoepitopes of Tau interfere with assembly of tubulin but not binding to microtubules.

Tau aggregation in Alzheimer's disease: what role for phosphorylation?

Selective backbone labelling of ILV methyl labelled proteins.

Hepatitis C virus NS5A protein is a substrate for the peptidyl-prolyl cis/trans isomerase activity of cyclophilins A and B.

Structural basis for the non-immunosuppressive character of the cyclosporin A analogue Debio 025.

Microtubule and MAPs: thermodynamics of complex formation by AUC, ITC, fluorescence, and NMR.

NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease.

Spectroscopic studies of GSK3{beta} phosphorylation of the neuronal tau protein and its interaction with the N-terminal domain of apolipoprotein E.

Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.

Mice lacking phosphatase PP2A subunit PR61/B'delta (Ppp2r5d) develop spatially restricted tauopathy by deregulation of CDK5 and GSK3beta.

Comparative analysis of Erk phosphorylation suggests a mixed strategy for measuring phospho-form distributions.

Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A.

Molecular basis for an ancient partnership between prolyl isomerase Pin1 and phosphatase inhibitor-2.

Molecular implication of PP2A and Pin1 in the Alzheimer's disease specific hyperphosphorylation of Tau.

Systematic identification of tubulin-interacting fragments of the microtubule-associated protein Tau leads to a highly efficient promoter of microtubule assembly.

Characterization of the AT180 epitope of phosphorylated Tau protein by a combined nuclear magnetic resonance and fluorescence spectroscopy approach.

Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline-rich region of the disordered Tau protein.

Plasmodium falciparum inhibitor-3 homolog increases protein phosphatase type 1 activity and is essential for parasitic survival.

Towards understanding the phosphorylation code of tau.

Tau pathology modulates Pin1 post-translational modifications and may be relevant as biomarker.

Cell signaling, post-translational protein modifications and NMR spectroscopy.

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 bridge.

Immunophilin FKBP52 induces Tau-P301L filamentous assembly in vitro and modulates its activity in a model of tauopathy.

Nuclear magnetic resonance analysis of the acetylation pattern of the neuronal Tau protein.

Ranking high affinity ligands of low solubility by NMR spectroscopy.

Identification of a Plasmodium falciparum inhibitor-2 motif involved in the binding and regulation activity of protein phosphatase type 1.

Mechanism of Tau-promoted microtubule assembly as probed by NMR spectroscopy.

Phosphorylation in intrinsically disordered regions regulates the activity of Neurogenin2.

H/D exchange of a (15)N labelled Tau fragment as measured by a simple Relax-EXSY experiment.

Nuclear magnetic resonance spectroscopy characterization of interaction of Tau with DNA and its regulation by phosphorylation.

Tamoxifen inhibits CDK5 kinase activity by interacting with p35/p25 and modulates the pattern of tau phosphorylation.

A Phosphorylation-Induced Turn Defines the Alzheimer's Disease AT8 Antibody Epitope on the Tau Protein.

The FK506-binding protein FKBP52 in vitro induces aggregation of truncated Tau forms with prion-like behavior.

Involvement of 14-3-3 in tubulin instability and impaired axon development is mediated by Tau.

Characterization of ERM transactivation domain binding to the ACID/PTOV domain of the Mediator subunit MED25.

Tau phosphorylation regulates the interaction between BIN1's SH3 domain and Tau's proline-rich domain.

Stabilizer-Guided Inhibition of Protein-Protein Interactions.

Proline Conformation in a Functional Tau Fragment.

Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated Kinase.

1H, 15N and 13C assignments of the N-terminal domain of the Mediator complex subunit MED26.

NMR Meets Tau: Insights into Its Function and Pathology.

Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases.

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.

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.