Evidence map›Paper›PMID 8382775›Full record

ArticleMolecular and cellular biology1993

Inactivation of erythropoietin receptor function by point mutations in a region having homology with other cytokine receptors.

O Miura, J L Cleveland, J N Ihle

Open access · hybridAbstract read
In one paragraph

Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
12.5field-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

53 citing papers in PubMed, 170 citations in OpenAlex.

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  17. Erythropoietin in thyroid cancer.Journal of endocrinological investigation · 2006
    Article
  18. Expression of a homodimeric type I cytokine receptor is required for JAK2V617F-mediated transformation.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  19. Article
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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

3 authors at 1 institution in 1 country.

O MiuraDepartment of Biochemistry, St. Jude Children's Research Hospital, Memphis, Tennessee 31051.
J L Cleveland
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
NCI NIH HHS P30 CA21765NIDDK NIH HHS DK42932NIDDK NIH HHS DK44159
6 · The paper itself

Abstract

The cytoplasmic domain of the erythropoietin receptor (EpoR) contains a region, proximal to the transmembrane domain, that is essential for function and has homology with other members of the cytokine receptor family. To explore the functional significance of this region and to identify critical residues, we introduced several amino acid substitutions and examined their effects on erythropoietin-induced mitogenesis, tyrosine phosphorylation, and expression of immediate-early (c-fos, c-myc, and egr-1) and early (ornithine decarboxylase and T-cell receptor gamma) genes in interleukin-3-dependent cell lines. Amino acid substitution of W-282, which is strictly conserved at the middle portion of the homology region, completely abolished all the functions of the EpoR. Point mutation at L-306 or E-307, both of which are in a conserved LEVL motif, drastically impaired the function of the receptor in all assays. Other point mutations, introduced into less conserved amino acid residues, did not significantly impair the function of the receptor. These results demonstrate that conserved amino acid residues in this domain of the EpoR are required for mitogenesis, stimulation of tyrosine phosphorylation, and induction of immediate-early and early genes.

Indexed as

Amino Acid SequenceAnimalsCell DivisionCell Line, TransformedCytokinesEnzyme InductionErythropoietinInterleukin-3Leukemia, MyeloidMolecular Sequence DataMutagenesis, Site-DirectedPhosphorylationPoint MutationProtein-Tyrosine KinasesReceptors, Cell SurfaceReceptors, ErythropoietinCytokinesErythropoietinInterleukin-3Protein-Tyrosine KinasesReceptors, Cell SurfaceReceptors, Erythropoietin

Identifiers

PMID8382775
PMCPMC359491
OpenAlexW1836713718

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.