Hydrophobic residues outside the active site of HIV-1 protease frequently mutate in patients
undergoing protease inhibitor therapy; however, the mechanism by which these mutations …

HIV-1 protease remains an important anti-AIDS drug target. Although it has been known that
ligand binding induces large conformational changes in the protease, the dynamic aspects …

The protease from type 1 human immunodeficiency virus (HIV‐1) is a critical drug target
against which many therapeutically useful inhibitors have been developed; however, the set …

Background: The human immunodeficiency virus type 1 (HIV-1) protease is an essential
viral protein that is a major drug target in the fight against Acquired Immune Deficiency …

HIV-1 protease variants resist drugs by active and non-active-site mutations. The active-site
mutations, which are the primary or first set of mutations, hamper the stability of the enzyme …

The emergence of compensatory drug-resistant mutations in HIV-1 protease challenges the
common view of the reaction mechanism of this enzyme. Here, we address this issue by …

Human immunodeficiency virus Type-1 (HIV-1) protease is crucial for viral maturation and
infectivity. Studies of protease dynamics suggest that the rearrangement of the hydrophobic …

Background Protease inhibitors designed to bind to protease have become major anti-AIDS
drugs. Unfortunately, the emergence of viral mutations severely limits the long-term …

We report unrestrained, all-atom molecular dynamics simulations of HIV-1 protease that
sample large conformational changes of the active site flaps. In particular, the unliganded …

The PR20 HIV-1 protease, a variant with 20 mutations, exhibits high levels of multi-drug
resistance; however, to date, there has been no report detailing the impact of these 20 …