Ras proteins play a major role in human cancers but have not yielded to therapeutic attack.
Ras-driven cancers are among the most difficult to treat and often excluded from therapies …

The initial discovery that ras genes endowed retroviruses with potent carcinogenic
properties and the subsequent determination that mutated ras genes were present in a wide …

Absolute binding free energy calculations and free energy decompositions are presented for
the protein–protein complexes H-Ras/C-Raf1 and H-Ras/RalGDS. Ras is a central switch in …

Estimating protein–protein interaction energies is a very challenging task for current
simulation protocols. Here, absolute binding free energies are reported for the complex H …

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 …

It is useful to consider seven transmembrane receptors (7TMRs) as disordered proteins able
to allosterically respond to a number of binding partners. Considering 7TMRs as allosteric …

Whereas previously we have successfully utilized the folding funnels concept to rationalize
binding mechanisms (Ma B, Kumar S, Tsai CJ, Nussinov R, 1999, Protein Eng 12: 713–720) …

We report the identification of three cyclic peptide ligands of K-Ras (G12D) using an
integrated in vitro translation–mRNA display selection platform. These cyclic peptides show …

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 …

We have investigated the dynamic properties of the switch I region of the GTP-binding
protein Ras by using mutants of Thr-35, an invariant residue necessary for the switch …