Evidence map›Paper›PMID 35803948›Full record

ArticleNature communications2022

Mimicked synthetic ribosomal protein complex for benchmarking crosslinking mass spectrometry workflows.

Manuel Matzinger, Adrian Vasiu, Mathias Madalinski, Fränze Müller, Florian Stanek, Karl Mechtler

Abstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Structural proteomics reveals the functional docking interface of ferredoxin-NADPThe Plant journal : for cell and molecular biology · 2026
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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.

Manuel Matzinger *Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria. manuel.matzinger@imp.ac.at.ORCID 0000-0002-9765-7951
Adrian Vasiu *Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.
Mathias MadalinskiInstitute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.
Fränze MüllerInstitute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.ORCID 0000-0003-3764-3547
Florian StanekInstitute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.
Karl MechtlerInstitute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria. karl.mechtler@imp.ac.at.ORCID 0000-0002-3392-9946

Funding

Austrian Science Fund FWF I 3686Austrian Science Fund FWF P 35045
6 · The paper itself

Abstract

Cross-linking mass spectrometry has matured to a frequently used tool for the investigation of protein structures as well as interactome studies up to a system-wide level. The growing community generated a broad spectrum of applications, linker types, acquisition strategies and specialized data analysis tools, which makes it challenging to decide for an appropriate analysis workflow. Here, we report a large and flexible synthetic peptide library as reliable instrument to benchmark crosslink workflows. Additionally, we provide a tool, IMP-X-FDR, that calculates the real, experimentally validated, FDR, compares results across search engine platforms and analyses crosslink properties in an automated manner. We apply the library with 6 commonly used linker reagents and analyse the data with 6 established search engines. We thereby show that the correct algorithm and search setting choice is highly important to improve identification rate and reliability. We reach identification rates of up to ~70 % of the theoretical maximum (i.e. 700 unique lysine-lysine cross-links) while maintaining a real false-discovery-rate of <3 % at cross-link level with high reproducibility, representatively showing that our test system delivers valuable and statistically solid results.

Indexed as

Ribosomal ProteinsCross-Linking ReagentsLysineMass SpectrometryReproducibility of ResultsWorkflowCross-Linking ReagentsLysineRibosomal Proteins

Identifiers

PMID35803948
PMCPMC9270371

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.