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Gilbert-Andre Keller

Researcher at Genentech

Publications -  22
Citations -  4259

Gilbert-Andre Keller is an academic researcher from Genentech. The author has contributed to research in topics: Vascular endothelial growth factor & Vascular endothelial growth factor A. The author has an hindex of 17, co-authored 22 publications receiving 4131 citations. Previous affiliations of Gilbert-Andre Keller include Howard Hughes Medical Institute.

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The vascular endothelial growth factor (VEGF) isoforms: differential deposition into the subepithelial extracellular matrix and bioactivity of extracellular matrix-bound VEGF.

TL;DR: VEGF associated with the ECM was bioactive, because endothelial cells cultured on ECM derived from cells expressing VEGF189 or V EGF206 were markedly stimulated to proliferate and can be released into a soluble and bioactive form by heparin or plasmin.
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VEGF is required for growth and survival in neonatal mice

TL;DR: Endothelial cells isolated from the liver of mFlt(1-3)-IgG-treated neonates demonstrated an increased apoptotic index, indicating that VEGF is required not only for proliferation but also for survival of endothelial cells.
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Identification of an angiogenic mitogen selective for endocrine gland endothelium

TL;DR: Endocrine-gland-derived vascular endothelial growth factor (EG-VEGF), induced proliferation, migration and fenestration in capillary endothelial cells derived from endocrine glands, but had little or no effect on a variety of other endothelial and non-endothelial cell types tested.
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In vitro megakaryocytopoietic and thrombopoietic activity of c-mpl ligand (TPO) on purified murine hematopoietic stem cells

TL;DR: The experiments show that the megakaryocytopoietic and thrombopoetic activities of TPO are initiated at the level of an early progenitor cell or upon the hematopoietIC stem cell.
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Cu,Zn superoxide dismutase is a peroxisomal enzyme in human fibroblasts and hepatoma cells.

TL;DR: The intracellular localization of Cu,Zn superoxide dismutase (superoxide:superoxide oxidoreductase, EC 1.15.1.1) has been examined by immunofluorescence and immunocryoelectron microscopy of yeast cells expressing human Cu, Znsuperoxide dismUTase showed that the enzyme is translocated to the peroxisomes.