Evidence map›Paper›PMID 33067342›Full record

ArticleMolecular & cellular proteomics : MCP2020

OpenPepXL: An Open-Source Tool for Sensitive Identification of Cross-Linked Peptides in XL-MS.

Eugen Netz, Tjeerd M H Dijkstra, Timo Sachsenberg, Lukas Zimmermann, Mathias Walzer, Thomas Monecke, Ralf Ficner, Olexandr Dybkov, Henning Urlaub, Oliver Kohlbacher

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

6 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. All-in-One Pseudo-MSJournal of the American Society for Mass Spectrometry · 2023
    Article
  4. Article
  5. Article
  6. Review
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

10 authors at 7 institutions in 3 countries.

Eugen NetzBiomolecular Interactions, Max Planck Institute for Developmental Biology, Tübingen, Germany; Institute for Bioinformatics and Medical Informatics, University of Tübingen, Tübingen, Germany; Applied Bioinformatics, Dept. of Computer Science, University of Tübingen, Tübingen, Germany. Electronic address: eugen.netz@tuebingen.mpg.de.
Tjeerd M H DijkstraBiomolecular Interactions, Max Planck Institute for Developmental Biology, Tübingen, Germany; Institute for Bioinformatics and Medical Informatics, University of Tübingen, Tübingen, Germany; Applied Bioinformatics, Dept. of Computer Science, University of Tübingen, Tübingen, Germany; Center for Women's Health, University Clinic Tübingen, Tübingen, Germany.
Timo SachsenbergInstitute for Bioinformatics and Medical Informatics, University of Tübingen, Tübingen, Germany; Applied Bioinformatics, Dept. of Computer Science, University of Tübingen, Tübingen, Germany.
Lukas ZimmermannBiomolecular Interactions, Max Planck Institute for Developmental Biology, Tübingen, Germany; Institute for Bioinformatics and Medical Informatics, University of Tübingen, Tübingen, Germany; Institute for Translational Bioinformatics, University Hospital Tübingen, Tübingen, Germany.
Mathias WalzerInstitute for Translational Bioinformatics, University Hospital Tübingen, Tübingen, Germany; European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Wellcome Trust Genome Campus, Hinxton, Cambridge, UK.
Thomas MoneckeX-Ray Crystallography Facility, Institute of Pharmaceutical Biotechnology, University of Ulm, Ulm, Germany; Department of Molecular Structural BiologyInstitute for Microbiology and GeneticsGZMB, Georg-August-University Göttingen, Göttingen, Germany.
Ralf FicnerDepartment of Molecular Structural BiologyInstitute for Microbiology and GeneticsGZMB, Georg-August-University Göttingen, Göttingen, Germany.
Olexandr DybkovDepartment for Cellular BiochemistryMax Planck Institute for Biophysical Chemistry, Göttingen, Germany.
Henning UrlaubBioanalytical Mass SpectrometryMax Planck Institute for Biophysical Chemistry, Göttingen, Germany; BioanalyticsInstitute for Clinical Chemistry, University Medical Center, Göttingen, Germany.
Oliver KohlbacherBiomolecular Interactions, Max Planck Institute for Developmental Biology, Tübingen, Germany; Institute for Bioinformatics and Medical Informatics, University of Tübingen, Tübingen, Germany; Applied Bioinformatics, Dept. of Computer Science, University of Tübingen, Tübingen, Germany; Institute for Translational Bioinformatics, University Hospital Tübingen, Tübingen, Germany; Quantitative Biology Center, University of Tübingen, Tübingen, Germany. Electronic address: oliver.kohlbacher@uni-tuebingen.de.
Max Planck Institute for Developmental Biology · DEBernstein Center for Computational Neuroscience Tübingen · DEEuropean Bioinformatics Institute · GBMax Planck Institute for Biophysical Chemistry · DEUniversitätsmedizin Göttingen · DEUniversität Ulm · DEUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cross-linking MS (XL-MS) has been recognized as an effective source of information about protein structures and interactions. In contrast to regular peptide identification, XL-MS has to deal with a quadratic search space, where peptides from every protein could potentially be cross-linked to any other protein. To cope with this search space, most tools apply different heuristics for search space reduction. We introduce a new open-source XL-MS database search algorithm, OpenPepXL, which offers increased sensitivity compared with other tools. OpenPepXL searches the full search space of an XL-MS experiment without using heuristics to reduce it. Because of efficient data structures and built-in parallelization OpenPepXL achieves excellent runtimes and can also be deployed on large compute clusters and cloud services while maintaining a slim memory footprint. We compared OpenPepXL to several other commonly used tools for identification of noncleavable labeled and label-free cross-linkers on a diverse set of XL-MS experiments. In our first comparison, we used a data set from a fraction of a cell lysate with a protein database of 128 targets and 128 decoys. At 5% FDR, OpenPepXL finds from 7% to over 50% more unique residue pairs (URPs) than other tools. On data sets with available high-resolution structures for cross-link validation OpenPepXL reports from 7% to over 40% more structurally validated URPs than other tools. Additionally, we used a synthetic peptide data set that allows objective validation of cross-links without relying on structural information and found that OpenPepXL reports at least 12% more validated URPs than other tools. It has been built as part of the OpenMS suite of tools and supports Windows, macOS, and Linux operating systems. OpenPepXL also supports the MzIdentML 1.2 format for XL-MS identification results. It is freely available under a three-clause BSD license at https://openms.org/openpepxl.

Indexed as

SoftwareAlgorithmsAmino Acid SequenceCross-Linking ReagentsDatabases, ProteinHEK293 CellsHumansMass SpectrometryModels, MolecularPeptidesRibosomesCross-Linking ReagentsPeptidescrosslinkingProtein cross-linkingprotein structurestructural biologytandem mass spectrometryXL-MS

Identifiers

PMID33067342
PMCPMC7710140
OpenAlexW3093023670

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.