Mostafa Javaheri Moghadam

This study compares the unbinding pathways of two HTLV-1 protease inhibitors using molecular dynamics simulations to identify key residues affecting inhibitor binding.

This paper presents a method to perform unbiased molecular dynamics simulations on desktop computers to study ligand binding pathways, demonstrating dasatinib's binding to Src-kinase without biasing forces.

This study uses molecular dynamics simulations to reconstruct the unbinding pathway of dasatinib from c-Src kinase without applying biases, achieving complete unbinding in 392.6 ns.