Evidence map›Paper›PMID 30374081›Full record

ReviewNature structural & molecular biology2018

Cross-linking mass spectrometry: methods and applications in structural, molecular and systems biology.

Francis J O'Reilly, Juri Rappsilber

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 183 papers.

0numbers the graph read from it
0cells of the map it votes in
183citing 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

183 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Article
  20. Article

123 more citing papers are in PubMed but not listed here.

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

2 authors.

Francis J O'ReillyBioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany.
Juri RappsilberBioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany. juri.rappsilber@tu-berlin.de.ORCID http://orcid.org/0000-0001-5999-1310

Funding

Wellcome Trust 103139/Z/13/ZWellcome Trust 203149
6 · The paper itself

Abstract

Over the past decade, cross-linking mass spectrometry (CLMS) has developed into a robust and flexible tool that provides medium-resolution structural information. CLMS data provide a measure of the proximity of amino acid residues and thus offer information on the folds of proteins and the topology of their complexes. Here, we highlight notable successes of this technique as well as common pipelines. Novel CLMS applications, such as in-cell cross-linking, probing conformational changes and tertiary-structure determination, are now beginning to make contributions to molecular biology and the emerging fields of structural systems biology and interactomics.

Indexed as

AnimalsComputational BiologyCross-Linking ReagentsHumansMass SpectrometryModels, MolecularMultiprotein ComplexesProtein ConformationProtein Interaction MapsProteinsProtein Structure, TertiaryProteomeSystems BiologyCross-Linking ReagentsMultiprotein ComplexesProteinsProteome

Identifiers

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.