Supplementary Materials

Supplementary Materials for:

Cancer-associated arginine-to-histidine mutations confer a gain in pH sensing to mutant proteins

Katharine A. White, Diego Garrido Ruiz, Zachary A. Szpiech, Nicolas B. Strauli, Ryan D. Hernandez, Matthew P. Jacobson, Diane L. Barber*

*Corresponding author. Email: diane.barber{at}ucsf.edu

This PDF file includes:

  • Fig. S1. EGFR-R776H activity is pH-sensitive in vitro and titrates with increasing pH.
  • Fig. S2. pHi control and pH-dependent EGFR-R776H activity in EGFR-null cells.
  • Fig. S3. EGFR-R776H activity is pH-sensitive at distinct autophosphorylation sites.
  • Fig. S4. Quantification of C helix flexibility and trajectory RMSD.
  • Fig. S5. EGFR MD simulations metrics for analysis.
  • Fig. S6. Full-well images of transformation assays.
  • Fig. S7. pHi control for p53 assays.
  • Table S1. pH-dependent transcriptional profiles.

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Citation: K. A. White, D. G. Ruiz, Z. A. Szpiech, N. B. Strauli, R. D. Hernandez, M. P. Jacobson, D. L. Barber, Cancer-associated arginine-to-histidine mutations confer a gain in pH sensing to mutant proteins. Sci. Signal. 10, eaam9931 (2017).

© 2017 American Association for the Advancement of Science