C
Christine Ellis
Researcher at Mount Sinai Hospital
Publications - 6
Citations - 2992
Christine Ellis is an academic researcher from Mount Sinai Hospital. The author has contributed to research in topics: Receptor tyrosine kinase & Phosphorylation. The author has an hindex of 6, co-authored 6 publications receiving 2969 citations.
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Journal ArticleDOI
SH2 and SH3 Domains: Elements that Control Interactions of Cytoplasmic Signaling Proteins
TL;DR: Observations suggest that SH2 and SH3 domains participate in the control of intracellular responses to growth factor stimulation.
Journal ArticleDOI
Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases
TL;DR: It is shown that GAP, and two co-precipitating proteins of relative molecular masses 62,000 and 190,000 (p62 and p190) are phosphorylated on tyrosine in cells that have been transformed by cytoplasmic and receptor-like tyrosin kinases, which supports the idea that SH2 sequences direct the interactions of cytopLasmic proteins involved in signal transduction.
Journal ArticleDOI
Binding of GAP to activated PDGF receptors
TL;DR: The ras proto-oncogene products appear to relay intracellular signals via the Ras guanosine triphosphatase (GTPase) activator protein, GAP, in dog epithelial cells expressing human platelet-derived growth factor receptors.
Book ChapterDOI
Phospholipase C isozymes: structural and functional similarities.
Ronald W. Kriz,Lih-Ling Lin,Lisa A. Sultzman,Christine Ellis,Carl-Henrik Heldin,Tony Pawson,John L. Knopf +6 more
TL;DR: The overexpression of PLC Gamma 1 in Rat-2 cells results in increased phosphatidylinositol breakdown in response to PDGF treatment, demonstrating that PLC gamma 1 mediates this response.
Journal Article
Tyrosine phosphorylation of GAP and GAP-associated proteins in lymphoid and fibroblast cells expressing lck.
TL;DR: The results suggest that the tyrosine phosphorylation of GAP, and its interactions with SH2-binding proteins, may be involved in fibroblast transformation by activated lck, and may participate in signal transduction and cellular transformation in lymphoid cells.