Evidence map›Paper›PMID 28346450›Full record

ArticleNature methods2017

Structural modeling of protein-RNA complexes using crosslinking of segmentally isotope-labeled RNA and MS/MS.

G Dorn, A Leitner, J Boudet, S Campagne, C von Schroetter, A Moursy, R Aebersold, F H-T Allain

Open access · greenAbstract read
In one paragraph

Article in Nature methods, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

25 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
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  4. The chloroplast RNA-binding protein CP29A supportsProceedings of the National Academy of Sciences of the United States of America · 2025
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  5. Article
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  7. FRET-guided modeling of nucleic acids.Nucleic acids research · 2024
    Article
  8. Article
  9. Article
  10. Journal of proteome research · 2023
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Sequence-specific RNA recognition by an RGG motif connects U1 and U2 snRNP for spliceosome assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  18. 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

8 authors at 2 institutions in 2 countries.

G Dorn *Department of Biology, Institute for Molecular Biology and Biophysics, ETH Zürich, 8093 Zürich, Switzerland.
A Leitner *Department of Biology, Institute of Molecular Systems Biology, ETH Zürich, 8093 Zürich, Switzerland.
J BoudetDepartment of Biology, Institute for Molecular Biology and Biophysics, ETH Zürich, 8093 Zürich, Switzerland.
S CampagneDepartment of Biology, Institute for Molecular Biology and Biophysics, ETH Zürich, 8093 Zürich, Switzerland.
C von SchroetterDepartment of Biology, Institute for Molecular Biology and Biophysics, ETH Zürich, 8093 Zürich, Switzerland.
A MoursyDepartment of Biology, Institute for Molecular Biology and Biophysics, ETH Zürich, 8093 Zürich, Switzerland.
R AebersoldDepartment of Biology, Institute of Molecular Systems Biology, ETH Zürich, 8093 Zürich, Switzerland.
F H-T AllainDepartment of Biology, Institute for Molecular Biology and Biophysics, ETH Zürich, 8093 Zürich, Switzerland.
ETH Zurich · CHUniversity of Zurich · CH

Funding

European Research Council 233226European Research Council 670821
6 · The paper itself

Abstract

Ribonucleoproteins (RNPs) are key regulators of cellular function. We established an efficient approach, crosslinking of segmentally isotope-labeled RNA and tandem mass spectrometry (CLIR-MS/MS), to localize protein-RNA interactions simultaneously at amino acid and nucleotide resolution. The approach was tested on polypyrimidine tract binding protein 1 and U1 small nuclear RNP. Our method provides distance restraints to support integrative atomic-scale structural modeling and to gain mechanistic insights into RNP-regulated processes.

Indexed as

Models, MolecularNucleic Acid ConformationBinding SitesCarbon IsotopesChromatography, High Pressure LiquidHeterogeneous-Nuclear RibonucleoproteinsNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularPolypyrimidine Tract-Binding ProteinProtein BindingRibonucleoprotein, U1 Small NuclearRNASoftwareTandem Mass SpectrometryUltraviolet RaysCarbon IsotopesHeterogeneous-Nuclear RibonucleoproteinsNitrogen IsotopesPolypyrimidine Tract-Binding ProteinPTBP1 protein, humanRibonucleoprotein, U1 Small NuclearRNA

Identifiers

PMID28346450
PMCPMC5505470
OpenAlexW2603316490

What OpenQuestion holds

Textmetadata
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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.