Caroline Smet-Nocca

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

The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding.

Structure and plasticity of the peptidyl-prolyl isomerase Par27 of Bordetella pertussis revealed by X-ray diffraction and small-angle X-ray scattering.

SUMO-1 possesses DNA binding activity.

NMR-based detection of acetylation sites in peptides.

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

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 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.

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

50nm-scale localization of single unmodified, isotopically enriched, proteins in cells.

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

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

A TDG/CBP/RARα ternary complex mediates the retinoic acid-dependent expression of DNA methylation-sensitive genes.

A functional fragment of Tau forms fibers without the need for an intermolecular cysteine bridge.

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

Traceless purification and desulfurization of tau protein ligation products.

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

Interplay between troponin T phosphorylation and O-N-acetylglucosaminylation in ischaemic heart failure.

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

Semi-synthesis of a tag-free O-GlcNAcylated tau protein by sequential chemoselective ligation.

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.

Tag-Free Semi-Synthesis of the Tau Protein.