Evidence map›Paper›PMID 1656216›Full record

ArticleMolecular and cellular biology1991

Induction of tyrosine phosphorylation by the erythropoietin receptor correlates with mitogenesis.

O Miura, A D'Andrea, D Kabat, J N Ihle

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
19.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

52 citing papers in PubMed, 226 citations in OpenAlex.

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  11. The erythropoietin receptor: molecular structure and hematopoietic signaling pathways.Journal of investigative medicine : the official publication of the American Federation for Clinical Research · 2011
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

O MiuraDepartment of Biochemistry, St. Jude Children's Research Hospital, Memphis, Tennessee 38105.
A D'Andrea
D Kabat
J N Ihle
St. Jude Children's Research Hospital · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
INTERLEUKIN-3 REGULATED GROWTH OF HEMATOPOIETIC CELLSR01DK042932 · NIDDK · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI IHLE, JAMES N · 1990 to 2007
$2.5M
LEUKEMOGENIC RETROVIRAL GLYCOPROTEIN: GP55-GP70SR01CA025810 · NCI · OREGON HEALTH AND SCIENCE UNIVERSITY · PI KABAT, DAVID · 1985 to 2001
$414k
NCI NIH HHS CA25810NCI NIH HHS P30 CA21765NIDDK NIH HHS R01 DK42932
6 · The paper itself

Abstract

A role for tyrosine phosphorylation in the signal-transducing mechanisms of several hematopoietic growth factors has been hypothesized. To extend these observations, we have examined the effects of erythropoietin (Epo) on tyrosine phosphorylation in an Epo-responsive cell that was obtained by transfecting the murine erythropoietin receptor (EpoR) into an interleukin-3 (IL-3)-dependent cell line. By two-dimensional analysis of phosphotyrosine-containing proteins isolated with a monoclonal antibody (1G2) against phosphotyrosine, Epo and IL-3 were found to rapidly induce tyrosine phosphorylation of comparable substrates of 92, 70, and 56 kDa. In addition, Epo uniquely induced phosphorylation of a 72-kDa substrate while IL-3 uniquely induced phosphorylation of a 140-kDa substrate. Immunoprecipitation and mixing experiments indicated that the 72-kDa substrate may represent a small fraction of the EpoR. To explore the significance of tyrosine phosphorylation, we generated two mutants of the EpoR that lacked 108 or 146 amino acids at their carboxyl termini. In addition we constructed an internally deleted mutant that lacked 20 amino acids in a region of sequence homology with the IL-2 receptor beta chain. Although all mutants were expressed at comparable levels and had comparable binding affinities for Epo, only the mutant lacking 108 amino acids at the carboxyl terminus retained significant mitogenic activity or the ability to induce tyrosine phosphorylation.

Indexed as

Cell DivisionAmino Acid SequenceBase SequenceCell LineEnzyme InductionErythropoietinGene Expression RegulationImmunoblottingInterleukin-3Molecular Sequence DataMutationPhosphorylationReceptors, Cell SurfaceReceptors, ErythropoietinReceptors, Interleukin-2Sequence Homology, Nucleic AcidErythropoietinInterleukin-3Receptors, Cell SurfaceReceptors, ErythropoietinReceptors, Interleukin-2Tyrosine

Identifiers

PMID1656216
PMCPMC361458
OpenAlexW1751978888

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.