We study protein folding, amyloid aggregation, ligand docking, and complex networks.
Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases.
Carnosine Inhibits Aβ(42) Aggregation by Perturbing the H-Bond Network in and around the Central Hydrophobic Cluster.
Optimization of Inhibitors of the Tyrosine Kinase EphB4. 2. Cellular Potency Improvement and Binding Mode Validation by X-ray Crystallography.
Distribution of Reciprocal of Interatomic Distances: A Fast Structural Metric
Methylations of Tryptophan Modified Naphtoquinone Affect Its Inhibitory Potential Towards Aβ Aggregation.
Discovery of a novel chemotype of tyrosine kinase inhibitors by fragment-based docking and molecular dynamics
Peptide binding to the PDZ3 domain by conformational selection.
Discovery of Tyrosine Kinase Inhibitors by Docking into an Inactive Kinase Conformation Generated by Molecular Dynamics.
Free Energy Guided Sampling
How Does Darunavir Prevent HIV-1 Protease Dimerization?
Mechanisms and kinetics of amyloid aggregation investigated by a phenomenological coarse-grained model
Ultrametricity in Protein Folding Dynamics
Efficient Construction of Mesostate Networks from Molecular Dynamics Trajectories
Complexity in Protein Folding: Simulation Meets Experiment
50 Years of Lifson–Roig Models: Application to Molecular Simulation Data
Hydrogen bonding penalty upon ligand binding.
Surfactant Effects on Amyloid Aggregation Kinetics.
Disordered binding of small molecules to A{beta}12-28.
Delineation of Folding Pathways of a β-Sheet Mini-Protein.
Dynamics in the active site of β-secretase: A network analysis of atomistic simulations.
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