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Article

In vitro phosphorylation of the erythropoietin receptor and an associated protein, pp130.

Molecular and cellular biology - 1 Feb 1992

Yoshimura A, Lodish H F

Abstract excerpt

The cytoplasmic domain of the cloned erythropoietin (EPO) receptor (EPOR) contains no protein kinase motif, yet addition of EPO to EPO-responsive cells causes an increase in protein-tyrosine phosphorylation. Here we show that addition of EPO or interleukin-3 (IL-3) to an IL-3-dependent cell line expressing the wild-type EPOR causes a small fraction (less than 5%) of total cellular EPOR to shift in gel mobility...

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Source

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Identifiers

PMID: 1310150
DOI: 10.1128/mcb.12.2.706-715.1992
PMCID: PMC364272

Genes

EPOR
EPO

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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In vitro phosphorylation of the erythropoietin receptor and an associated protein, pp130.PMID 1310150Read ↗

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