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Dana Rabara on Muck Rack

Dana Rabara

As seen in: Molecular Cancer Research, The Journal of Biological Chemistry
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Articles

How KRAS Mutations Impair Intrinsic GTP Hydrolysis: Experimental and Computational Investigations

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By Lin Song, Dana Rabara, Jun Pei
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Biophysical and structural analysis of KRAS switch-II pocket inhibitors reveals allele-specific binding constraints

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By Patrick Alexander, Leidos Biomedical Research, Albert Chan, Dana Rabara
| The Journal of Biological Chemistry Verified
Keywords KRAS covalent inhibitors switch-II pocket Surface plasmon resonance spectroscopy X-ray crystallography Microscale Thermophoresis Introduction RAS proteins function as molecular switches that cycle between an inactive, GDP-bound “off-state” and an active, GTP-bound “on-state” (1). Localized at the intracellular side of the plasma membrane, RAS proteins couple extracellular growth factor binding to intracellular signal transduction pathways.
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A Top-Down Proteomic Assay to Evaluate KRAS4B-Compound Engagement

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By Dana Rabara, Maria Blanco Verified, Robert A. D’Ippolito, Emily Alberico
| dx.doi.org
The RAS family of GTPases (HRAS, KRAS, and NRAS) behave as molecular switches through their association with GDP (inactive) or GTP (active) to activate multiple signaling cascades (e.g., MAPK and PI3K pathways) driving cell growth and differentiation, cell cycle regulation, and proliferation.
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