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Michael D. Waterfield

Researcher at Ludwig Institute for Cancer Research

Publications -  152
Citations -  30785

Michael D. Waterfield is an academic researcher from Ludwig Institute for Cancer Research. The author has contributed to research in topics: Kinase & Proto-oncogene tyrosine-protein kinase Src. The author has an hindex of 76, co-authored 151 publications receiving 30122 citations. Previous affiliations of Michael D. Waterfield include University of Fribourg & University College London.

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Phosphatidylinositol-3-oh kinase as a direct target of ras

TL;DR: In vivo, dominant negative Ras mutant N17 inhibits growth factor induced production of 3′ hosphorylated phosphoinositides in PC12 cells, and transfection of Ras, but not Raf, into COS cells results in a large elevation in the level of these lipids.
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Synthesis and Function of 3-Phosphorylated Inositol Lipids

TL;DR: This review is focused on the 3-phosphoinositide lipids, the synthesis of which is acutely triggered by extracellular stimuli, the enzymes responsible for their synthesis and metabolism, and their cell biological roles.
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Platelet-derived growth factor is structurally related to the putative transforming protein p28sis of simian sarcoma virus.

TL;DR: A partial amino acid sequence of human platelet-derived growth factor, the major mitogen in serum for cells of mesenchymal origin, shows virtual identity with the predicted sequence of p28sis, the putative transforming protein of simian sarcoma virus (SSV).
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Cellular function of phosphoinositide 3-kinases: Implications for development, immunity, homeostasis, and cancer

TL;DR: This review uses transgenic and knockout mouse studies where either PI3K or its signaling components are deregulated as a framework to build a profile of PI3k function within both the cell and the organism and focuses, in particular, on the role ofPI3K in cell regulation, immunity, and development.
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Role of Phosphoinositide 3-OH Kinase in Cell Transformation and Control of the Actin Cytoskeleton by Ras

TL;DR: The pathways by which mammalian Ras proteins induce cortical actin rearrangement and cause cellular transformation are investigated using partial loss of function mutants of Ras and activated and inhibitory forms of various postulated target enzymes for Ras.