Evidence map›Paper›PMID 10445881›Full record

ArticleRNA (New York, N.Y.)1999

Finding the right RNA: identification of cellular mRNA substrates for RNA-binding proteins.

P Trifillis, N Day, M Kiledjian

Abstract read
In one paragraph

Article in RNA (New York, N.Y.), 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

  1. Role of the RNA-binding protein family in gynecologic cancers.American journal of cancer research · 2023
    Review
  2. The iron chaperone and nucleic acid-binding activities of poly(rC)-binding protein 1 are separable and independently essential.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  3. Trans-acting translational regulatory RNA binding proteins.Wiley interdisciplinary reviews. RNA · 2018
    Review
  4. Article
  5. Advances in the characterization of RNA-binding proteins.Wiley interdisciplinary reviews. RNA · 2016
    Review
  6. Article
  7. Review
  8. Article
  9. Computational Methods for CLIP-seq Data Processing.Bioinformatics and biology insights · 2014
    Review
  10. Article
  11. Review
  12. Article
  13. The FHA domain proteins DAWDLE in Arabidopsis and SNIP1 in humans act in small RNA biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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.

P TrifillisDepartment of Cell Biology and Neuroscience, Rutgers University, Piscataway, New Jersey 08855, USA.
N Day
M Kiledjian

Funding

RNA/PROTEIN INTERACTIONS REGULATING MRNA STABILITYR01DK051611 · NIDDK · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI KILEDJIAN, MEGERDITCH · 1997 to 2006
$1.8M
NIDDK NIH HHS DK51611
6 · The paper itself

Abstract

Defects in RNA-binding proteins have been implicated in human genetic disorders. However, efforts in understanding the functions of these proteins have been hampered by the inability to obtain their mRNA substrates. To identify cognate cellular mRNAs associated with an RNA-binding protein, we devised a strategy termed isolation of specific nucleic acids associated with proteins (SNAAP). The SNAAP technique allows isolation and subsequent identification of these mRNAs. To assess the validity of this approach, we utilized cellular mRNA and protein from K562 cells and alphaCP1, a protein implicated in a-globin mRNA stability, as a model system. Immobilization of an RNA-binding protein with the glutathione-S-transferase (GST) domain enables isolation of mRNA within an mRNP context and the identity of the bound mRNAs is determined by the differential display assay. The specificity of protein-RNA interactions was considerably enhanced when the interactions were carried out in the presence of cellular extract rather than purified components. Two of the mRNAs specifically bound by alphaCP1 were mRNAs encoding the transmembrane receptor protein, TAPA-1, and the mitochondrial cytochrome c oxidase subunit II enzyme, coxII. A specific poly(C)-sensitive complex formed on the TAPA-1 and coxII 3' UTRs consistent with the binding of aCP1. Furthermore, direct binding of purified alphaCP proteins to these 3' UTRs was demonstrated and the binding sites determined. These results support the feasibility of the SNAAP technique and suggest a broad applicability for the approach in identifying mRNA targets for clinically relevant RNA-binding proteins that will provide insights into their possible functions.

Indexed as

Genetic TechniquesHeterogeneous-Nuclear RibonucleoproteinsMembrane Proteins3' Untranslated RegionsAntigens, CDBase SequenceBlotting, NorthernDNA-Binding ProteinsElectron Transport Complex IVGlutathione TransferaseHemoglobinsHumansK562 CellsModels, GeneticMolecular Sequence DataPeptide Fragments3' Untranslated Regionsalpha(A) globinAntigens, CDCD81 protein, humanDNA-Binding ProteinsElectron Transport Complex IVGlutathione TransferaseHemoglobinsHeterogeneous-Nuclear RibonucleoproteinsMembrane ProteinsPCBP1 protein, humanPeptide FragmentsRNA-Binding ProteinsRNA, MessengerTetraspanin 28

Identifiers

PMID10445881
PMCPMC1369830

What OpenQuestion holds

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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.