Evidence map›Paper›PMID 25173706›Full record

ArticleNature methods2014

Photo-cross-linking and high-resolution mass spectrometry for assignment of RNA-binding sites in RNA-binding proteins.

Katharina Kramer, Timo Sachsenberg, Benedikt M Beckmann, Saadia Qamar, Kum-Loong Boon, Matthias W Hentze, Oliver Kohlbacher, Henning Urlaub

Open access · bronzeAbstract read
In one paragraph

Article in Nature methods, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.

0numbers the graph read from it
0cells of the map it votes in
150citing papers in PubMed
10.8field-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

150 citing papers in PubMed, 270 citations in OpenAlex.

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  17. Malonate promotes CD8Cellular & molecular immunology · 2025
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90 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

8 authors at 3 institutions in 1 country.

Katharina Kramer1] Bioanalytical Mass Spectrometry Group, Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany. [2].
Timo Sachsenberg1] Center for Bioinformatics, University of Tübingen, Tübingen, Germany. [2] Department of Computer Science, University of Tübingen, Tübingen, Germany. [3].ORCID 0000000228336070
Benedikt M Beckmann1] European Molecular Biology Laboratory, Heidelberg, Germany. [2].
Saadia QamarBioanalytical Mass Spectrometry Group, Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Kum-Loong BoonDepartment of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Matthias W HentzeEuropean Molecular Biology Laboratory, Heidelberg, Germany.
Oliver Kohlbacher1] Center for Bioinformatics, University of Tübingen, Tübingen, Germany. [2] Department of Computer Science, University of Tübingen, Tübingen, Germany. [3] Quantitative Biology Center, University of Tübingen, Tübingen, Germany. [4] Faculty of Medicine, University of Tübingen, Tübingen, Germany.ORCID 0000000317394598
Henning Urlaub1] Bioanalytical Mass Spectrometry Group, Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany. [2] Bioanalytics Research Group, Department of Clinical Chemistry, University Medical Center, Göttingen, Germany.
Max Planck Institute for Biophysical Chemistry · DEBernstein Center for Computational Neuroscience Tübingen · DEEuropean Molecular Biology Laboratory · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA-protein complexes play pivotal roles in many central biological processes. Although methods based on high-throughput sequencing have advanced our ability to identify the specific RNAs bound by a particular protein, there is a need for precise and systematic ways to identify RNA interaction sites on proteins. We have developed an experimental and computational workflow combining photo-induced cross-linking, high-resolution mass spectrometry and automated analysis of the resulting mass spectra for the identification of cross-linked peptides, cross-linking sites and the cross-linked RNA oligonucleotide moieties of such RNA-binding proteins. The workflow can be applied to any RNA-protein complex of interest or to whole proteomes. We applied the approach to human and yeast mRNA-protein complexes in vitro and in vivo, demonstrating its powerful utility by identifying 257 cross-linking sites on 124 distinct RNA-binding proteins. The open-source software pipeline developed for this purpose, RNP(xl), is available as part of the OpenMS project.

Indexed as

Amino AcidsAutomationBinding SitesComputer SimulationCross-Linking ReagentsFungal ProteinsHumansMass SpectrometryOligonucleotidesPeptidesProteomeProteomicsRNARNA-Binding ProteinsSoftwareAmino AcidsCross-Linking ReagentsFungal ProteinsOligonucleotidesPeptidesProteomeRNARNA-Binding Proteins

Identifiers

PMID25173706
PMCPMC6485471
OpenAlexW2077527436

What OpenQuestion holds

Textmetadata
LicenceTDM
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.