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Gary Britton

Researcher at University College London

Publications -  9
Citations -  504

Gary Britton is an academic researcher from University College London. The author has contributed to research in topics: Vascular endothelial growth factor A & Angiogenesis. The author has an hindex of 7, co-authored 8 publications receiving 461 citations.

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VEGF binding to NRP1 is essential for VEGF stimulation of endothelial cell migration, complex formation between NRP1 and VEGFR2, and signaling via FAK Tyr407 phosphorylation.

TL;DR: It is shown for the first time that binding of vascular endothelial growth factor to the neuropilin-1 b1 domain is essential for VEGF complex formation with VEGFR2/KDR and is important for endothelial cell migration and tubulogenesis.
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Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells.

TL;DR: It is reported that p130Cas tyrosine phosphorylation is stimulated by hepatocyte growth factor and platelet-derived growth factor in U87MG glioma cells and VEGF in endothelial cells and is dependent on NRP1 via its intracellular domain and identified a critical role for a novel N RP1-p130Cas pathway in the regulation of chemotaxis.
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Vascular endothelial growth factor induces heat shock protein (HSP) 27 serine 82 phosphorylation and endothelial tubulogenesis via protein kinase D and independent of p38 kinase.

TL;DR: Findings identify a novel pathway for VEGF-induced HSP27 serine 82 phosphorylation via PKC-mediated PKD activation and direct phosphorylated of HSP 27 by PKD, and show that PKDs and HSP26 play major roles in the angiogenic response to VEGf.
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The zinc-finger transcription factor, early growth response 3, mediates VEGF-induced angiogenesis.

TL;DR: Findings indicate that Egr3 has an essential downstream role in VEGF-mediated endothelial functions leading to angiogenesis and may have particular relevance for adult angiogenic processes involved in vascular repair and neovascular disease.
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Vascular Endothelial Growth Factor (VEGF) Promotes Assembly of the p130Cas Interactome to Drive Endothelial Chemotactic Signaling and Angiogenesis

TL;DR: Findings indicate a cardinal role for assembly of the p130Cas interactome in mediating the cell migratory response to VEGF in angiogenesis, and provide a basis for further studies of p130 Cas in cell movement.