Guy Lippens

Solid-phase enolate chemistry investigated using HR-MAS NMR spectroscopy.

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

Osmoregulated periplasmic glucans of the free-living photosynthetic bacterium Rhodobacter sphaeroides.

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.

Resin dynamics contributes to the NMR line broadening of organic molecules grafted onto a polystyrene resin.

Fine-tuned characterization at the solid/solution interface of organotin compounds grafted onto cross-linked polystyrene by using high-resolution MAS NMR spectroscopy.

Pin1: a therapeutic target in Alzheimer neurodegeneration.

HRMAS NMR observation of beta-sheet secondary structure on a water swollen solid support.

Restricted linear least square treatment processing of heteronuclear spectra of biomolecules using the ANAFOR strategy.

Cobatoxin 1 from Centruroides noxius scorpion venom: chemical synthesis, three-dimensional structure in solution, pharmacology and docking on K+ channels.

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.

Practical aspects of shimming a high resolution magic angle spinning probe.

Development of a high-resolution magic-angle spinning nuclear magnetic resonance identity assay of the capsular polysaccharide from Haemophilus influenzae type b present in cetavlon precipitate.

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.

Pin1 allows for differential Tau dephosphorylation in neuronal cells.

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

ELISE NMR: experimental liquid sealing of NMR samples.

New DEFT sequences for the acquisition of one-dimensional carbon NMR spectra of small unlabelled molecules.

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.

Contribution of rotational diffusion to pulsed field gradient diffusion measurements.

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

Measurement of amyloid fibril length distributions by inclusion of rotational motion in solution NMR diffusion measurements.

NMR observation of Tau in Xenopus oocytes.

Sandwich-ELISE NMR: reducing the sample volume of NMR samples.

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

Graphical interpretation of Boolean operators for protein NMR assignments.

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?

Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded.

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.

Fluorescent BODIPY-based Zn(II) complex as a molecular probe for selective detection of neurofibrillary tangles in the brains of Alzheimer's disease patients.

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

The domain 2 of the HCV NS5A protein is intrinsically unstructured.

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.

DEB025 (Alisporivir) inhibits hepatitis C virus replication by preventing a cyclophilin A induced cis-trans isomerisation in domain II of NS5A.

Intermolecular interaction studies using small volumes.

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

Oleuropein and derivatives from olives as Tau aggregation inhibitors.

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.

Substrate recognition by the POTRA domains of TpsB transporter FhaC.

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.

Glycerol and glycerol carbonate as ultraviscous solvents for mixture analysis by NMR.

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.

Structural activation of the transcriptional repressor EthR from Mycobacterium tuberculosis by single amino acid change mimicking natural and synthetic ligands.

Differential contribution of the repeats to heparin binding of HBHA, a major adhesin of Mycobacterium tuberculosis.

Towards understanding the phosphorylation code of tau.

Post-translational modification: nature's escape from genetic imprisonment and the basis for dynamic information encoding.

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

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

Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A.

Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.

A new strategy for sequential assignment of intrinsically unstructured proteins based on 15N single isotope labelling.

Dissociation kinetics of a binary complex in solution by protein displacement.

Increasing brain protein O-GlcNAc-ylation mitigates breathing defects and mortality of Tau.P301L mice.

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.

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.

Tau monoclonal antibody generation based on humanized yeast models: impact on Tau oligomerization and diagnostics.

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

A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication.

Catalytic site inhibition of insulin-degrading enzyme by a small molecule induces glucose intolerance in mice.

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

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

Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy.

NMR Meets Tau: Insights into Its Function and Pathology.

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.

Molecular Dynamics Simulation of Tau Peptides for the Investigation of Conformational Changes Induced by Specific Phosphorylation Patterns.

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.