about
Measuring residual dipolar couplings at high hydrostatic pressure: robustness of alignment media to high pressure.p15PAF is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins.Tau aggregation in Alzheimer's disease: what role for phosphorylation?NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease.Structural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS.Reactivity, secondary structure, and molecular topology of the Escherichia coli sulfite reductase flavodoxin-like domain.Structural and functional characterization of the interaction between cyclophilin B and a heparin-derived oligosaccharide.Small-angle scattering studies of intrinsically disordered proteins and their complexes.Structural basis for the non-immunosuppressive character of the cyclosporin A analogue Debio 025.Comparative NMR study on the impact of point mutations on protein stability of Pseudomonas mendocina lipase.1H, 13C and 15N assignment of the flavodoxin-like domain of the Escherichia coli sulfite reductase.Side chain orientation from methyl 1H-1H residual dipolar couplings measured in highly deuterated proteins.Selective backbone labelling of ILV methyl labelled proteins.NMR analysis of a Tau phosphorylation pattern.Structural Characterization of Highly Flexible Proteins by Small-Angle Scattering.A General Strategy to Access Structural Information at Atomic Resolution in Polyglutamine Homorepeats.Oleuropein and derivatives from olives as Tau aggregation inhibitors.Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline-rich region of the disordered Tau protein.Solution structure of the sulfite reductase flavodoxin-like domain from Escherichia coli.Structural impact of heparin binding to full-length Tau as studied by NMR spectroscopyLow concentration of a Gd-chelate increases the signal-to-noise ratio in fast pulsing BEST experimentsRealistic Ensemble Models of Intrinsically Disordered Proteins Using a Structure-Encoding Coil DatabaseSite-Specific Isotopic Labeling (SSIL): Access to High-Resolution Structural and Dynamic Information in Low-Complexity ProteinsInterplay of Protein Disorder in Retinoic Acid Receptor Heterodimer and Its Corepressor Regulates Gene Expression
P50
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P50
description
researcher ORCID ID = 0000-0001-8145-6795
@en
wetenschapper
@nl
name
Nathalie Sibille
@ast
Nathalie Sibille
@en
Nathalie Sibille
@es
Nathalie Sibille
@nl
type
label
Nathalie Sibille
@ast
Nathalie Sibille
@en
Nathalie Sibille
@es
Nathalie Sibille
@nl
prefLabel
Nathalie Sibille
@ast
Nathalie Sibille
@en
Nathalie Sibille
@es
Nathalie Sibille
@nl
P108
P106
P108
P1153
6506501072
P21
P31
P496
0000-0001-8145-6795