Patient-derived mutations within the N-terminal domains of p85α impact PTEN or Rab5 binding and regulation
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-018-25487-5.pdf
Reference53 articles.
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3. Cuevas, B. D. et al. Tyrosine phosphorylation of p85 relieves its inhibitory activity on phosphatidylinositol 3-kinase. J Biol Chem 276, 27455–27461 (2001).
4. Miled, N. et al. Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit. Science 317, 239–242 (2007).
5. Cantley, L. C. The phosphoinositide 3-kinase pathway. Science 296, 1655–1657 (2002).
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