@article{228c1fcc24434f91b64a445ad39068ee,
title = "Allosteric Activation of PI3Kα Results in Dynamic Access to Catalytically Competent Conformations",
abstract = "PI3Kα is a phospholipid kinase that phosphorylates PIP2 to generate PIP3, a scaffold for many important downstream signaling pathways. In this paper, Chakrabarti et al. demonstrate that dynamic allostery can increase the population of PI3Kα states compatible with catalysis, which has implications for the development of new PI3K therapeutics.",
keywords = "catalytic mechanism, dynamic allostery, enzyme activation, molecular dynamics, phosphoinositide (3,4,5)-trisphosphate, phosphoinositide (4,5)-bisphosphate, phosphoinositide kinase, population increase, signaling pathway",
author = "Mayukh Chakrabarti and Gabelli, {Sandra B.} and Amzel, {L. Mario}",
note = "Funding Information: We thank Dr. Yunlong Liu for helpful discussions. We acknowledge the use of the computational resources and scientific computing services at the Maryland Advanced Research Computing Center. This research was funded in part by the US Department of Defense, DOD CDMRP BC151831 (S.B.G.). M.C. Conceptualization, Methodology, Software, Validation, Formal Analysis, Investigation, Writing ? Original Draft, Visualization. S.B.G. Conceptualization, Writing ? Review & Editing. L.M.A. Conceptualization, Methodology, Validation, Resources, Writing ? Review & Editing, Visualization, Supervision, Project Administration, Funding Acquisition. The authors declare no competing interests. Funding Information: We thank Dr. Yunlong Liu for helpful discussions. We acknowledge the use of the computational resources and scientific computing services at the Maryland Advanced Research Computing Center. This research was funded in part by the US Department of Defense , DOD CDMRP BC151831 (S.B.G.). Publisher Copyright: {\textcopyright} 2020 Elsevier Ltd",
year = "2020",
month = apr,
day = "7",
doi = "10.1016/j.str.2020.01.010",
language = "English (US)",
volume = "28",
pages = "465--474.e5",
journal = "Structure with Folding & design",
issn = "0969-2126",
publisher = "Cell Press",
number = "4",
}