Evidence map›Paper›PMID 39251624›Full record

ArticleNature communications2024

Modelling protein complexes with crosslinking mass spectrometry and deep learning.

Kolja Stahl, Robert Warneke, Lorenz Demann, Rica Bremenkamp, Björn Hormes, Oliver Brock, Jörg Stülke, Juri Rappsilber

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing 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

57 citing papers in PubMed.

  1. Article
  2. The phenotypic landscape of the model firmicuteProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Evaluation of methods for AlphaFold-based integrative modeling.bioRxiv : the preprint server for 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

8 authors.

Kolja StahlTechnische Universität Berlin, Chair of Bioanalytics, Berlin, Germany.ORCID 0000-0002-9990-7643
Robert WarnekeGeorg-August-Universität Göttingen, Department of General Microbiology, Institute for Microbiology & Genetics, GZMB, Göttingen, Germany.
Lorenz DemannGeorg-August-Universität Göttingen, Department of General Microbiology, Institute for Microbiology & Genetics, GZMB, Göttingen, Germany.
Rica BremenkampGeorg-August-Universität Göttingen, Department of General Microbiology, Institute for Microbiology & Genetics, GZMB, Göttingen, Germany.
Björn HormesGeorg-August-Universität Göttingen, Department of General Microbiology, Institute for Microbiology & Genetics, GZMB, Göttingen, Germany.
Oliver BrockTechnische Universität Berlin, Robotics and Biology Laboratory, Berlin, Germany.ORCID 0000-0001-5881-5390
Jörg StülkeGeorg-August-Universität Göttingen, Department of General Microbiology, Institute for Microbiology & Genetics, GZMB, Göttingen, Germany. jstuelk@gwdg.de.ORCID 0000-0002-3719-7754
Juri RappsilberTechnische Universität Berlin, Chair of Bioanalytics, Berlin, Germany. juri.rappsilber@tu-berlin.de.ORCID 0000-0001-5999-1310

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) 390523135Deutsche Forschungsgemeinschaft (German Research Foundation) 390540038Wellcome TrustWellcome Trust 203149Wellcome Trust 227166
6 · The paper itself

Abstract

Scarcity of structural and evolutionary information on protein complexes poses a challenge to deep learning-based structure modelling. We integrate experimental distance restraints obtained by crosslinking mass spectrometry (MS) into AlphaFold-Multimer, by extending AlphaLink to protein complexes. Integrating crosslinking MS data substantially improves modelling performance on challenging targets, by helping to identify interfaces, focusing sampling, and improving model selection. This extends to single crosslinks from whole-cell crosslinking MS, opening the possibility of whole-cell structural investigations driven by experimental data. We demonstrate this by revealing the molecular basis of iron homoeostasis in Bacillus subtilis.

Indexed as

Bacillus subtilisBacterial ProteinsDeep LearningMass SpectrometryCross-Linking ReagentsIronModels, MolecularProtein ConformationBacterial ProteinsCross-Linking ReagentsIron

Identifiers

PMID39251624
PMCPMC11383924

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.