Isabelle Huvent

The periplasmic binding protein of a tripartite tricarboxylate transporter is involved in signal transduction.

Crystal structure of Bordetella pertussis BugD solute receptor unveils the basis of ligand binding in a new family of periplasmic binding proteins.

Expression, purification, and structural prediction of the Ets transcription factor ERM.

Crystallization and preliminary X-ray diffraction analysis of two extracytoplasmic solute receptors of the DctP family from Bordetella pertussis.

Structural analysis of Bordetella pertussis BugE solute receptor in a bound conformation.

Crystal structures of two Bordetella pertussis periplasmic receptors contribute to defining a novel pyroglutamic acid binding DctP subfamily.

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.

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

Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor.

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.

SILAC-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-lactoferrin.

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

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.

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.

Modification by SUMOylation Controls Both the Transcriptional Activity and the Stability of Delta-Lactoferrin.

Proline Conformation in a Functional Tau Fragment.

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.