Andrew G. Stephen

Dragging ras back in the ring.

Biochemical assays for the discovery of TDP1 inhibitors.

Farnesylated and methylated KRAS4b: high yield production of protein suitable for biophysical studies of prenylated protein-lipid interactions.

Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ.

Inhibition of Ras/Raf/MEK/ERK Pathway Signaling by a Stress-Induced Phospho-Regulatory Circuit.

K-Ras4B Remains Monomeric on Membranes over a Wide Range of Surface Densities and Lipid Compositions.

New weapons to penetrate the armor: Novel reagents and assays developed at the NCI RAS Initiative to enable discovery of RAS therapeutics.

Molecular recognition of RAS/RAF complex at the membrane: Role of RAF cysteine-rich domain.

The bacterial Ras/Rap1 site-specific endopeptidase RRSP cleaves Ras through an atypical mechanism to disrupt Ras-ERK signaling.

Quantitative biophysical analysis defines key components modulating recruitment of the GTPase KRAS to the plasma membrane.

KRAS Prenylation Is Required for Bivalent Binding with Calmodulin in a Nucleotide-Independent Manner.

Structures of N-terminally processed KRAS provide insight into the role of N-acetylation.

Organization of Farnesylated, Carboxymethylated KRAS4B on Membranes.

PIP2 Influences the Conformational Dynamics of Membrane-Bound KRAS4b.

Second harmonic generation detection of Ras conformational changes and discovery of a small molecule binder.