Evidence map›Paper›PMID 30643114›Full record

ArticleNature communications2019

Rapid determination of quaternary protein structures in complex biological samples.

Simon Hauri, Hamed Khakzad, Lotta Happonen, Johan Teleman, Johan Malmström, Lars Malmström

Abstract readEvaluation Study
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Article
  2. Article
  3. Rapid Proteome-Wide Discovery of Protein-Protein Interactions With ppIRIS.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Article
  5. Article
  6. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  7. Article
  8. Article
  9. Epitope Mapping with Sidewinder: An XL-MS and Structural Modeling Approach.International journal of molecular sciences · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  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

6 authors.

Simon HauriDivision of Infection Medicine, Department of Clinical Sciences Lund, Faculty of Medicine, Lund University, Klinikgatan 32, SE-22184, Lund, Sweden.ORCID http://orcid.org/0000-0002-7249-2011
Hamed KhakzadS3IT, University of Zurich, Winterthurerstrasse 190, CH-8057, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-8556-0650
Lotta HapponenDivision of Infection Medicine, Department of Clinical Sciences Lund, Faculty of Medicine, Lund University, Klinikgatan 32, SE-22184, Lund, Sweden.
Johan TelemanDivision of Infection Medicine, Department of Clinical Sciences Lund, Faculty of Medicine, Lund University, Klinikgatan 32, SE-22184, Lund, Sweden.
Johan MalmströmDivision of Infection Medicine, Department of Clinical Sciences Lund, Faculty of Medicine, Lund University, Klinikgatan 32, SE-22184, Lund, Sweden. johan.malmstrom@med.lu.se.ORCID http://orcid.org/0000-0002-2889-7169
Lars MalmströmDivision of Infection Medicine, Department of Clinical Sciences Lund, Faculty of Medicine, Lund University, Klinikgatan 32, SE-22184, Lund, Sweden. lars.malmstroem@uzh.ch.ORCID http://orcid.org/0000-0001-9885-9312

Funding

European Research Council 309831
6 · The paper itself

Abstract

The understanding of complex biological systems is still hampered by limited knowledge of biologically relevant quaternary protein structures. Here, we demonstrate quaternary structure determination in biological samples using a combination of chemical cross-linking, high-resolution mass spectrometry and high-accuracy protein structure modeling. This approach, termed targeted cross-linking mass spectrometry (TX-MS), relies on computational structural models to score sets of targeted cross-linked peptide signals acquired using a combination of mass spectrometry acquisition techniques. We demonstrate the utility of TX-MS by creating a high-resolution quaternary model of a 1.8 MDa protein complex composed of a pathogen surface protein and ten human plasma proteins. The model is based on a dense network of cross-link distance constraints obtained directly in a mixture of human plasma and live bacteria. These results demonstrate that TX-MS can increase the applicability of flexible backbone docking algorithms to large protein complexes by providing rich cross-link distance information from complex biological samples.

Indexed as

Protein Structure, QuaternaryAlgorithmsBlood ProteinsChromatography, Reverse-PhaseCross-Linking ReagentsHealthy VolunteersHumansMolecular Docking SimulationMultiprotein ComplexesRecombinant ProteinsSoftwareTandem Mass SpectrometryBlood ProteinsCross-Linking ReagentsMultiprotein ComplexesRecombinant Proteins

Identifiers

PMID30643114
PMCPMC6331586

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.