Title : The influence of domain structures on the signal transduction of chimeric receptors derived from the erythropoietin receptor.

Pub. Date : 2009 May

PMID : 19155265






2 Functional Relationships(s)
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1 In this study, we designed a series of chimeric erythropoietin receptor (EpoR) variants encoding a haemagglutinin epitope-tagged anti-fluorescein single-chain Fv and different combinations of extracellular D1/D2 domain(s) of EpoR as the extracellular domain to allow the receptor to be activated by multiple ligands. Fluorescein erythropoietin receptor Mus musculus
2 In this study, we designed a series of chimeric erythropoietin receptor (EpoR) variants encoding a haemagglutinin epitope-tagged anti-fluorescein single-chain Fv and different combinations of extracellular D1/D2 domain(s) of EpoR as the extracellular domain to allow the receptor to be activated by multiple ligands. Fluorescein erythropoietin receptor Mus musculus