Cellular function of phosphoinositide 3-kinases: Implications for development, immunity, homeostasis, and cancer

By R. Katso, K. Okkenhaug, K. Ahmadi, S. White, J. Timms, M. Waterfield. 2001

1,090 citations recorded by the source corpus.

Subfields: Genetics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/a9d867433808f06fabedeca8d77273c2813e802b

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Genetics

1. David M. Sabatini
2. J. Engelman
3. P. Pandolfi
4. Arkaitz Carracedo

In Molecular Biology

1. David M. Sabatini
2. P. Pandolfi
3. Arkaitz Carracedo
4. Lewis C. Cantley
5. J. Engelman
6. M. Laplante
7. Siraj M. Ali
8. Dos D. Sarbassov

Citations in the corpus

• Targeting the phosphoinositide 3-kinase (PI3K) pathway in cancer (2009, background): “Pathway background PI3Ks are divided into three classes according to their structural characteristics and substrate specificit”
• A Pharmacological Map of the PI3-K Family Defines a Role for p110α in Insulin Signaling (2006, neutral): “In the appropriate cellular context, these three lipids control diverse physiological processes including cell growth, survival, differentiation, and chemotaxis (Katso et al., 2001).”
• Activation of the PI3K/Akt pathway and chemotherapeutic resistance. (2002, background): “This results in the production of D3 phosphorylated phosphoinositides, most importantly phosphatidylinositol-4,5-bisphosphate (PIP2) and phosphatidylinositol-3,4,5-trisphosphate (PIP3), which serve as second messengers by binding to and regulating the function of a diverse set of signaling proteins ”
• Regulation and role of autophagy in mammalian cells. (2004, background): “Class I PI3K enzymes phosphorylate PtdIns4P and PtdIns(4,5)P2 to produce PtdIns(3,4)P2 and PtdIns(3,4,5)P3, which, via Pleckstrin Homology (PH) domains bind to protein kinase B (Akt/PKB) and its activator phosphoinositide-dependent kinase-1 (PDK1) (Brazil & Hemmings, 2001; Katso et al., 2001).”
• mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. (2002, background): “…led us and diabetes (reviewed by Dixon and Fordham-Skelton, to hypothesize that in vivo mTOR exists as a complex 1998; Johnston and Gallant, 2002; Katso et al., 2001; with one or more proteins that are lost during isolation Kozma and Thomas, 2002; Schmelzle and Hall, 2000). of mTOR for in vitro…”
• Negative regulation of Toll-like receptor-mediated immune responses (2005, background): “It is constitutively expressed by most cells and functions as an early signal in many cellular event”