Evidence map›Paper›PMID 7892223›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

AUH, a gene encoding an AU-specific RNA binding protein with intrinsic enoyl-CoA hydratase activity.

J Nakagawa, H Waldner, S Meyer-Monard, J Hofsteenge, P Jenö, C Moroni

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

42 citing papers in PubMed, 130 citations in OpenAlex.

  1. Article
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  4. The Physiological and Pathological Role of Acyl-CoA Oxidation.International journal of molecular sciences · 2023
    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

6 authors at 1 institution in 1 country.

J NakagawaInstitute for Medical Microbiology, University of Basel, Switzerland.
H Waldner
S Meyer-Monard
J Hofsteenge
P Jenö
C Moroni
University of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AU-rich elements within the 3' untranslated region of transcripts of lymphokines and some protooncogenes serve as signal for rapid mRNA degradation. By using an AUUUA matrix, we have affinity-purified a 32-kDa protein, microsequenced it, and cloned the corresponding cDNA. In vitro, the recombinant protein bound specifically to AU-rich transcripts, including those for interleukin 3, granulocyte/macrophage colony-stimulating factor, c-fos, and c-myc. Sequence analysis revealed an unexpected homology to enoyl-CoA hydratase (EC 4.2.1.17), and the recombinant protein showed a low degree of the enzymatic activity. Thus, this gene, designated AUH, encodes an RNA binding protein with intrinsic enzymatic activity. Protein immobilized on an AUUUA matrix was enzymatically active, suggesting that hydratase and AU-binding functions are located on distinct domains within a single polypeptide.

Indexed as

Amino Acid SequenceAnimalsBase SequenceBlotting, WesternBrainChromatography, AffinityCloning, MolecularDNA PrimersEnoyl-CoA HydrataseGene LibraryGenes, fosGenes, mycGranulocyte-Macrophage Colony-Stimulating FactorHumansImmunoblottingInterleukin-3AUH protein, humanDNA PrimersEnoyl-CoA HydrataseGranulocyte-Macrophage Colony-Stimulating FactorInterleukin-3OligodeoxyribonucleotidesPeptide FragmentsPeptidesRecombinant ProteinsRNA-Binding Proteins

Identifiers

PMID7892223
PMCPMC42421
OpenAlexW2050444660

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.