Evidence map›Paper›PMID 27976756›Full record

ArticleWellcome open research2016

Quantitative cross-linking/mass spectrometry reveals subtle protein conformational changes.

Zhuo Chen, Lutz Fischer, Salman Tahir, Jimi-Carlo Bukowski-Wills, Paul Barlow, Juri Rappsilber

Abstract read
In one paragraph

Article in Wellcome open research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
  2. Article
  3. Kinetic principles of chemical cross-link formation for protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Crosslinking mass spectrometry: A link between structural biology and systems biology.Protein science : a publication of the Protein Society · 2021
    Review
  10. Review
  11. Review
  12. High-density chemical cross-linking for modeling protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Altered Domain Structure of the Prion Protein Caused by CuStructure (London, England : 1993) · 2019
    Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. 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

6 authors.

Zhuo ChenWellcome Trust Centre for Cell Biology, Institute of Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3BF, UK.
Lutz FischerWellcome Trust Centre for Cell Biology, Institute of Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3BF, UK.
Salman TahirWellcome Trust Centre for Cell Biology, Institute of Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3BF, UK.
Jimi-Carlo Bukowski-WillsWellcome Trust Centre for Cell Biology, Institute of Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3BF, UK.
Paul BarlowSchools of Chemistry and Biological Sciences, University of Edinburgh, Edinburgh, EH9 3JJ, UK.
Juri RappsilberWellcome Trust Centre for Cell Biology, Institute of Cell Biology, School of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3BF, UK.ORCID 0000-0001-5999-1310

Funding

Wellcome Trust 081179Wellcome Trust 092076Wellcome Trust 103139Wellcome Trust 103139/Z/13/ZWellcome Trust 108504
6 · The paper itself

Abstract

Quantitative cross-linking/mass spectrometry (QCLMS) probes protein structural dynamics in solution by quantitatively comparing the yields of cross-links between different conformational statuses. We have used QCLMS to understand the final maturation step of the proteasome lid and also to elucidate the structure of complement C3(H2O). Here we benchmark our workflow using a structurally well-described reference system, the human complement protein C3 and its activated cleavage product C3b. We found that small local conformational changes affect the yields of cross-linking residues that are near in space while larger conformational changes affect the detectability of cross-links. Distinguishing between minor and major changes required robust analysis based on replica analysis and a label-swapping procedure. By providing workflow, code of practice and a framework for semi-automated data processing, we lay the foundation for QCLMS as a tool to monitor the domain choreography that drives binary switching in many protein-protein interaction networks.

Indexed as

automated data processconformational changecross-linking/mass spectrometryisotope labeled cross-linkersquantitative protein structure

Identifiers

PMID27976756
PMCPMC5140025

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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.