Uma Murthy
University of Pennsylvania
8 Papers
447 Citations
Uma Murthy is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Receptor & Growth factor. The author has an hindex of 7, co-authored 8 publications.
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Papers
Binding of an antagonistic monoclonal antibody to an intact and fragmented EGF-receptor polypeptide☆
TL;DR: The results of antibody binding studies indicate that the epitope is closely linked to the EGF binding active site, and is common to both high- and low-affinity EGF-receptors.
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Perinuclear location and recycling of epidermal growth factor receptor kinase: immunofluorescent visualization using antibodies directed to kinase and extracellular domains.
TL;DR: The results demonstrate the following: the receptor kinase domain migrates to the perinuclear region upon challenge with EGF; both extracellular and cytoplasmic domains of the receptor are involved in migration as a unit; withdrawal of EGF results in rapid recycling of the perInuclear receptors to the plasma membrane; this return to the cell surface is inhibited by methylamine, chloroquine, and monensin.
•Journal Article
Presence of Tumor-associated Antigens in Epidermal Growth Factor Receptors from Different Human Carcinomas
TL;DR: The results of cell-binding, immunoprecipitation, and Western blot analyses of the antigen-positive carcinomas indicate that sialylated Lea/Y type of antigenicity is intrinsic to the EGF receptors of these cells, and that the antigen is present in receptors from both over-expressing and normal- expressing carcinomas.
Regulation of Kinase and Intermolecular Bonding in Intact and Truncated Epidermal Growth Factor Receptor
TL;DR: Results suggest that both intra- and extracellular domains of the receptor act to stabilize the kinase-regulatory dimer, indicating that nucleotide binding rather than autophosphorylation is responsible for stabilizing the monomeric receptor form.
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A new trophoblast-derived growth factor from human placenta: purification and receptor identification.
TL;DR: The results demonstrate that the preparation is homogeneous and show that growth factor activity is intrinsic to the 34-kDa polypeptide and interacts with target cells through highly specific surface receptors.
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