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 …

The epidermal growth factor receptor (EGFR) is a receptor tyrosine kinase (RTK) that links
extracellular signals to the control of cell survival, growth, proliferation and differentiation …

The protein K-Ras functions as a molecular switch in signaling pathways regulating cell
growth. In the human mitogen-activated protein kinase (MAPK) pathway, which is implicated …

KRAS homo‐dimerization has been implicated in the activation of RAF kinases, however,
the mechanism and structural basis remain elusive. We developed a system to study KRAS …

Proximally located in the membrane, oncogenic Ras dimers (or nanoclusters) can recruit
and promote Raf dimerization and MAPK (Raf/MEK/ERK) signaling. Among Ras isoforms …

Are the dimer structures of active Ras isoforms similar? This question is significant since Ras
can activate its effectors as a monomer; however, as a dimer, it promotes Raf's activation …

K-Ras4B preferentially activates Raf-1. The high-affinity interaction of Ras-binding domain
(RBD) of Raf with Ras was solved, but the relative position of Raf's cysteine-rich domain …

Ras is a membrane-anchored signaling protein that serves as a hub for many signaling
pathways and also plays a prominent role in cancer. The intrinsic behavior of Ras on the …

In Kessler et al.(1), the small molecule BI-2852 is shown to bind—at nanomolar affinity—to
KRAS between switch I and II, inhibiting interactions with effectors. Here, we identify an …

Membrane nanodomains have been implicated in Ras signaling, but what these domains
are and how they interact with Ras remain obscure. Here, using single particle tracking with …