KRAS is the most frequently mutated oncogene in human cancer. In addition to holding this
distinction, unsuccessful attempts to target this protein have led to the characterization of …

Ras proteins are classical members of small GTPases that function as molecular switches by
alternating between inactive GDP-bound and active GTP-bound states. Ras activation is …

Mutations yield significant effect on the structural flexibility of two switch domains, SW1 and
SW2, in K-Ras, which is considered as an important target of anticancer drug design. To …

The aberrant activity of Ras homologous (Rho) family small GTPases (20 human members)
has been implicated in cancer and other human diseases. However, in contrast to the direct …

Ras oncoproteins play pivotal roles in both the development and maintenance of many
tumor types. Unfortunately, these proteins are difficult to directly target using traditional …

Allosteric modulators bound to structurally diverse allosteric sites can achieve better
pharmacological advantages than orthosteric ligands. The discovery of allosteric …

The Ras superfamily of small GTPases are guanine‐nucleotide‐dependent switches
essential for numerous cellular processes. Mutations or dysregulation of these proteins are …

Despite intense efforts in pharmaceutical industry and academia, a therapeutic grip on
oncogenic Ras proteins has remained elusive. Mutated Ras is associated with∼ 20− 30% of …

Drug action is inherently multiscale: it connects molecular interactions to emergent
properties at cellular and larger scales. Simulation techniques at each of these different …

Ras proteins are small GTPases, cycling between inactive GDP-bound and active GTP-
bound states. Through these switches they regulate signaling that controls cell growth and …