One of the most common drivers in human cancer is the mutant KRAS protein. Not so long
ago KRAS was considered as an undruggable oncoprotein. After a long struggle, however …

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 …

Despite the prominent role of the K-Ras protein in many different types of human cancer,
major gaps in atomic-level information severely limit our understanding of its functions in …

Intrinsically disordered proteins (IDPs) are proteins that lack rigid 3D structure. Hence, they
are often misconceived to present a challenge to Anfinsen's dogma. However, IDPs exist as …

H-Ras, K-Ras, and N-Ras are small GTPases that are important in the control of cell
proliferation, differentiation, and survival, and their mutants occur frequently in human …

Mutations in K-Ras are involved in a large number of all human cancers, thus, K-Ras is
regarded as a promising target for anticancer drug design. Understanding the target roles of …

Approximately 15% of all human tumors harbor mutant KRAS, a membrane-associated
small GTPase and notorious oncogene. Mutations that render KRAS constitutively active will …

Ras GTPases are mutated at codons 12, 13, and 61, with different frequencies in KRas,
HRas, and NRas and in a cancer-specific manner. The G13D mutant appears in 25% of …

Understanding the molecular mechanism of the GTP-KRAS binding is significant for
improving the target roles of KRAS in cancer treatment. In this work, multiple replica …

A mutated KRAS protein is frequently observed in human cancers. Traditionally, the
oncogenic properties of KRAS missense mutants at position 12 (G12X) have been …