Evidence map›Paper›PMID 29804821›Full record

ArticleStructure (London, England : 1993)2018

Modeling Protein Complexes Using Restraints from Crosslinking Mass Spectrometry.

Joshua Matthew Allen Bullock, Neeladri Sen, Konstantinos Thalassinos, Maya Topf

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Evaluation of methods for AlphaFold-based integrative modeling.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
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  5. Article
  6. Mapping the interaction surface between CaNature communications · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Shape shifting: The multiple conformational substates of the PTEN N-terminal PIPProtein science : a publication of the Protein Society · 2022
    Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Automated Modeling and Validation of Protein Complexes in Cryo-EM Maps.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  18. Article
  19. Article
  20. Article
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

4 authors.

Joshua Matthew Allen BullockInstitute of Structural and Molecular Biology, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK.
Neeladri SenIndian Institute of Science Education and Research Pune, Pashan, Pune 411 008, India.
Konstantinos ThalassinosInstitute of Structural and Molecular Biology, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK; Institute of Structural and Molecular Biology, Division of Biosciences, University College London, London WC1E 6BT, UK.
Maya TopfInstitute of Structural and Molecular Biology, Birkbeck College, University of London, Malet Street, London WC1E 7HX, UK. Electronic address: m.topf@cryst.bbk.ac.uk.

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council MR/M019292/1Medical Research Council MR/N009614/1Wellcome Trust 209250/Z/17/Z
6 · The paper itself

Abstract

Modeling macromolecular assemblies with restraints from crosslinking mass spectrometry (XL-MS) tends to focus solely on distance violation. Recently, we identified three different modeling features inherent in crosslink data: (1) expected distance between crosslinked residues; (2) violation of the crosslinker's maximum bound; and (3) solvent accessibility of crosslinked residues. Here, we implement these features in a scoring function. cMNXL, and demonstrate that it outperforms the commonlyused crosslink distance violation. We compare the different methods of calculating the distance between crosslinked residues, which shows no significant change in performance when using Euclidean distance compared with the solvent-accessible surface distance. Finally, we create a combined score that incorporates information from 3D electron microscopy maps as well as crosslinking. This achieves, on average, better results than either information type alone and demonstrates the potential of integrative modeling with XL-MS and low-resolution cryoelectron microscopy.

Indexed as

Cross-Linking ReagentsCryoelectron MicroscopyMacromolecular SubstancesMass SpectrometryModels, MolecularProtein ConformationCross-Linking ReagentsMacromolecular Substances3D electron microscopycrosslinkingcrosslinking mass spectrometrycryo-EMintegrative modelingprotein structure modellingscoring function

Identifiers

PMID29804821
PMCPMC6039719

What OpenQuestion holds

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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.