about
An 'open' structure of the RecOR complex supports ssDNA binding within the core of the complexConformational polymorphism or structural invariance in DNA photoinduced lesions: implications for repair rates.Correlation of bistranded clustered abasic DNA lesion processing with structural and dynamic DNA helix distortion.High-chloride concentrations abolish the binding of adenine nucleotides in the mitochondrial ADP/ATP carrier family.Structural and energetic study of cation-π-cation interactions in proteins.Effects of Phospholipid Composition on the Transfer of a Small Cationic Peptide Across a Model Biological Membrane.Assessing the physiological relevance of alternate architectures of the p7 protein of hepatitis C virus in different environments.Solubilities inferred from the combination of experiment and simulation. Case study of quercetin in a variety of solvents.The substrate specificity of the human ADP/ATP carrier AAC1.Mitochondrial ADP/ATP Carrier in Dodecylphosphocholine Binds Cardiolipins with Non-native Affinity.Effect of Meso vs Macro Size of Hierarchical Porous Silica on the Adsorption and Activity of Immobilized β-Galactosidase.Accurate Estimation of the Standard Binding Free Energy of Netropsin with DNA.Deciphering the photosensitization mechanisms of hypericin towards biological membranes.How Detergent Impacts Membrane Proteins: Atomic-Level Views of Mitochondrial Carriers in Dodecylphosphocholine.Thermodynamics of DNA: sensitizer recognition. Characterizing binding motifs with all-atom simulations.Repair Rate of Clustered Abasic DNA Lesions by Human Endonuclease: Molecular Bases of Sequence Specificity.AlaScan: A Graphical User Interface for Alanine Scanning Free-Energy Calculations.Long-range electrostatic interactions in hybrid quantum and molecular mechanical dynamics using a lattice summation approach.Dangerous liaisons between detergents and membrane proteins. The case of mitochondrial uncoupling protein 2.OPEP: a tool for the optimal partitioning of electric properties.Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Entropy-Driven Translational Isomerism: A Tristable Molecular ShuttleRemarkable Positional Discrimination in Bistable Light- and Heat-Switchable Hydrogen-Bonded Molecular ShuttlesUnidirectional rotation in a mechanically interlocked molecular rotorDynamics and interactions of AAC3 in DPC are not functionally relevantModeling Membranes under a Transmembrane PotentialImpaired Transport of Nucleotides in a Mitochondrial Carrier Explains Severe Human Genetic DiseasesDerivation of Distributed Models of Atomic Polarizability for Molecular SimulationsModeling Induction Phenomena in Intermolecular Interactions with an Ab Initio Force FieldEnergetics of ion transport in a peptide nanotubeA Toolkit for the Analysis of Free-Energy Perturbation CalculationsEffects of hydration on the protonation state of a lysine analog crossing a phospholipid bilayer - insights from molecular dynamics and free-energy calculationsMechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitorsConformational changes of DNA induced by a trans-azobenzene derivative via non-covalent interactionsEnthalpy-Entropy Interplay in π-Stacking Interaction of Benzene Dimer in WaterChanges in Microenvironment Modulate the B- to A-DNA TransitionBinding properties of the quaternary assembly protein SPAG1The three Endonuclease III variants of Deinococcus radiodurans possess distinct and complementary DNA repair activitiesCharge Transfer and Chemo-Mechanical Coupling in Respiratory Complex I
P50
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
François Dehez
@ast
François Dehez
@en
François Dehez
@es
François Dehez
@nl
François Dehez
@sl
type
label
François Dehez
@ast
François Dehez
@en
François Dehez
@es
François Dehez
@nl
François Dehez
@sl
prefLabel
François Dehez
@ast
François Dehez
@en
François Dehez
@es
François Dehez
@nl
François Dehez
@sl
P106
P21
P31
P496
0000-0001-8076-6222