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Joan C. Egrie

Researcher at Amgen

Publications -  45
Citations -  9638

Joan C. Egrie is an academic researcher from Amgen. The author has contributed to research in topics: Erythropoietin & Hematocrit. The author has an hindex of 25, co-authored 45 publications receiving 9493 citations.

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Correction of the anemia of end-stage renal disease with recombinant human erythropoietin. Results of a combined phase I and II clinical trial.

TL;DR: It is demonstrated that recombinant human erythropoietin is effective, can eliminate the need for transfusions with their risks of immunologic sensitization, infection, and iron overload, and can restore the hematocrit to normal in many patients with the anemia of end-stage renal disease.
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The effects of normal as compared with low hematocrit values in patients with cardiac disease who are receiving hemodialysis and epoetin.

TL;DR: In patients with clinically evident congestive heart failure or ischemic heart disease who are receiving hemodialysis, administration of epoetin to raise their hematocrit to 42 percent is not recommended.
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Cloning and expression of the human erythropoietin gene.

TL;DR: The human erythropoietin gene has been isolated from a genomic phage library by using mixed 20-mer and 17-mer oligonucleotide probes and encodes a 27-amino acid signal peptide and a 166-AMino acid mature protein with a calculated Mr of 18,399.
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Development and characterization of novel erythropoiesis stimulating protein (NESP)

TL;DR: Darbepoetin alfa (novel erythropoiesis stimulating protein, NESP, ARANESPTM, Amgen Inc, Thousand Oaks, CA), which was engineered to contain 5 N-linked carbohydrate chains, is currently being evaluated in human clinical trials for treatment of anaemia and reduction in its incidence.
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Efficiency of signalling through cytokine receptors depends critically on receptor orientation

TL;DR: The crystal structure of erythropoietin complexed to the extracellular ligand-binding domains of the erymorphic receptor, determined at 1.9 Å from two crystal forms, shows that erythrooiet in imposes a unique 120° angular relationship and orientation that is responsible for optimal signalling through intracellular kinase pathways.