User profiles for Isabelle Krimm
Isabelle KrimmCentre de Recheche en Cancérologie de Lyon Verified email at univ-lyon1.fr Cited by 2500 |
[PDF][PDF] The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy
I Krimm, C Östlund, B Gilquin, J Couprie, P Hossenlopp… - Structure, 2002 - cell.com
Lamins are nuclear intermediate filaments that, together with lamin-associated proteins,
maintain nuclear shape and provide a structural support for chromosomes and replicating DNA. …
maintain nuclear shape and provide a structural support for chromosomes and replicating DNA. …
The carboxyl-terminal region common to lamins A and C contains a DNA binding domain
V Stierlé, J Couprie, C Östlund, I Krimm… - Biochemistry, 2003 - ACS Publications
Lamins A and C are intermediate filament proteins which polymerize into the nucleus to
form the nuclear lamina network. The lamina is apposed to the inner nuclear membrane and …
form the nuclear lamina network. The lamina is apposed to the inner nuclear membrane and …
NMR-based analysis of protein–ligand interactions
Physiological processes are mainly controlled by intermolecular recognition mechanisms
involving protein–protein and protein–ligand (low molecular weight molecules) interactions. …
involving protein–protein and protein–ligand (low molecular weight molecules) interactions. …
Fragment linking strategies for structure-based drug design
…, M Le Borgne, JF Guichou, I Krimm - Journal of Medicinal …, 2020 - ACS Publications
Fragment-based drug discovery is a strategy widely used in both academia and pharmaceutical
companies to generate small-molecule protein inhibitors and drug candidates. Among …
companies to generate small-molecule protein inhibitors and drug candidates. Among …
[HTML][HTML] Fragment-based discovery of a new family of non-peptidic small-molecule cyclophilin inhibitors with potent antiviral activities
Cyclophilins are peptidyl-prolyl cis/trans isomerases (PPIase) that catalyse the interconversion
of the peptide bond at proline residues. Several cyclophilins play a pivotal role in the life …
of the peptide bond at proline residues. Several cyclophilins play a pivotal role in the life …
[HTML][HTML] Enabling STD-NMR fragment screening using stabilized native GPCR: A case study of adenosine receptor
Structural studies of integral membrane proteins have been limited by the intrinsic
conformational flexibility and the need to stabilize the proteins in solution. Stabilization by …
conformational flexibility and the need to stabilize the proteins in solution. Stabilization by …
Fragment-Based Deconstruction of Bcl-xL Inhibitors
…, O Marcillat, JM Lancelin, I Krimm - Journal of medicinal …, 2010 - ACS Publications
Fragment-based drug design consists of screening low-molecular-weight compounds in order
to identify low-affinity ligands that are then modified or linked to yield potent inhibitors. The …
to identify low-affinity ligands that are then modified or linked to yield potent inhibitors. The …
Ligand-orientation based fragment selection in STD NMR screening
While saturation transfer difference (STD) is a widely used NMR method for ligand screening,
the selection of specific binders requires the validation of the hits through competition …
the selection of specific binders requires the validation of the hits through competition …
1D NMR WaterLOGSY as an efficient method for fragment-based lead discovery
WaterLOGSY is a sensitive ligand-observed NMR experiment for detection of interaction
between a ligand and a protein and is now well-established as a screening technique for …
between a ligand and a protein and is now well-established as a screening technique for …
Linkers in fragment-based drug design: an overview of the literature
Introduction In fragment-based drug design, fragment linking is a popular strategy where
two fragments binding to different sub-pockets of a target are linked together. This attractive …
two fragments binding to different sub-pockets of a target are linked together. This attractive …