Evidence map›Paper›PMID 2172968›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1990

Cloning of the cDNA encoding an RNA regulatory protein--the human iron-responsive element-binding protein.

T A Rouault, C K Tang, S Kaptain, W H Burgess, D J Haile, F Samaniego, O W McBride, J B Harford, R D Klausner

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
9.6field-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

73 citing papers in PubMed, 207 citations in OpenAlex.

  1. Review
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  14. The indispensable role of mammalian iron sulfur proteins in function and regulation of multiple diverse metabolic pathways.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2019
    Review
  15. Article
  16. Article
  17. Review
  18. Conditional Müller Cell Ablation Leads to Retinal Iron Accumulation.Investigative ophthalmology & visual science · 2017
    Article
  19. Article
  20. Metabolic Enzymes Enjoying New Partnerships as RNA-Binding Proteins.Trends in endocrinology and metabolism: TEM · 2015
    Review

13 more citing papers are in PubMed but not listed here.

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

9 authors at 1 institution in 1 country.

T A RouaultCell Biology and Metabolism Branch, National Institute of Child Health, Bethesda, MD 20892.
C K Tang
S Kaptain
W H Burgess
D J Haile
F Samaniego
O W McBride
J B Harford
R D Klausner
Lymphoma Research Foundation · US

Funding

STRUCTURAL BASIS FOR VASCULAR HOMEOSTASIS IN VITROR01HL035762 · NHLBI · AMERICAN NATIONAL RED CROSS · PI BURGESS, WILSON H · 1987 to 1994
–
NHLBI NIH HHS HL35762
6 · The paper itself

Abstract

Iron-responsive elements (IREs) are stemloop structures found in the mRNAs encoding ferritin and the transferrin receptor. These elements participate in the iron-induced regulation of the translation of ferritin and the stability of the transferrin receptor mRNA. Regulation in both instances is mediated by binding of a cytosolic protein to the IREs. High-affinity binding is seen when cells are starved of iron and results in repression of ferritin translation and inhibition of transferrin receptor mRNA degradation. The IRE-binding protein (IRE-BP) has been identified as an approximately 90-kDa protein that has been purified by both affinity and conventional chromatography. In this report we use RNA affinity chromatography and two-dimensional gel electrophoresis to isolate the IRE-BP for protein sequencing. A degenerate oligonucleotide probe derived from a single peptide sequence was used to isolate a cDNA clone that encodes a protein containing 13 other sequenced peptides obtained from the IRE-BP. Consistent with previous characterization of the IRE-BP, the cDNA encodes a protein of 87 kDa with a slightly acidic pI, and the corresponding mRNA of approximately 3.6 kilobases is found in a variety of cell types. The encoded protein contains a nucleotide-binding consensus sequence and regions of cysteine and histidine clusters. This mRNA is encoded by a single gene on human chromosome 9, a finding consistent with previous localization by functional mapping. The protein contains no previously defined consensus motifs for either RNA or DNA binding. The simultaneous cloning of a different, but highly homologous, cDNA suggests that the IRE-BP is a member of a distinct gene family.

Indexed as

Chromosomes, Human, Pair 9Iron-Binding ProteinsAmino Acid SequenceAnimalsBase SequenceCarrier ProteinsChromosome MappingCloning, MolecularCricetinaeDNAFerritinsGene LibraryHumansIronIron-Regulatory ProteinsMolecular Sequence DataCarrier ProteinsDNAferritin receptorFerritinsIronIron-Binding ProteinsIron-Regulatory ProteinsReceptors, Cell SurfaceReceptors, TransferrinRNA, Messenger

Identifiers

PMID2172968
PMCPMC54871
OpenAlexW2055667111

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.