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Publication : Structure of the erythropoietin receptor.

First Author  Mayeux P Year  1994
Journal  Proc Soc Exp Biol Med Volume  206
Issue  3 Pages  200-4
PubMed ID  8016154 Mgi Jnum  J:18954
Mgi Id  MGI:67186 Doi  10.3181/00379727-206-43742
Citation  Mayeux P, et al. (1994) Structure of the erythropoietin receptor. Proc Soc Exp Biol Med 206(3):200-4
abstractText  Despite extensive studies, the structure of the erythropoietin receptor remains little understood. cDNAs encoding the human and murine erythropoietin receptors have been cloned and the structure of these proteins is discussed. Although the proteins encoded by these cDNAs play key roles in erythropoietin binding and in erythropoietin signal transduction, increasing evidence strongly suggests that the erythropoietin receptor is a multimeric complex. The murine erythropoietin receptor has been solubilized under mild conditions and the molecular mass of the native receptor has been shown to be significantly higher than the molecular mass of the cloned chain. Cross-linking experiments have revealed the presence of three proteins covalently bound to erythropoietin by the cross-linking reagents; however, only one of them seems to derive from the cloned chain. Moreover, functional evidence also suggests the presence of other erythropoietin receptor subunits.
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