Evidence map›Paper›PMID 22286754›Full record

ArticleMolecular & cellular proteomics : MCP2012

Expanding the chemical cross-linking toolbox by the use of multiple proteases and enrichment by size exclusion chromatography.

Alexander Leitner, Roland Reischl, Thomas Walzthoeni, Franz Herzog, Stefan Bohn, Friedrich Förster, Ruedi Aebersold

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 161 papers.

0numbers the graph read from it
0cells of the map it votes in
161citing papers in PubMed
13.4field-weighted citation impact, top 1% of its field
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

161 citing papers in PubMed, 318 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure of cytoplasmic RNA polymerase II.Nature communications · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Structure of the human 20S U5 snRNP.Nature structural & molecular biology · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

101 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

7 authors at 4 institutions in 3 countries.

Alexander LeitnerInstitute of Molecular Systems Biology, Eidgenössische Technische Hochschule Zurich, Wolfgang-Pauli-Strasse 16, 8093 Zurich, Switzerland.
Roland Reischl
Thomas Walzthoeni
Franz Herzog
Stefan Bohn
Friedrich Förster
Ruedi Aebersold
ETH Zurich · CHMax Planck Institute of Biochemistry · DECenter for Pediatric Endocrinology Zurich · CHUniversity of Vienna · AT

Funding

European Research Council 233226
6 · The paper itself

Abstract

Chemical cross-linking in combination with mass spectrometric analysis offers the potential to obtain low-resolution structural information from proteins and protein complexes. Identification of peptides connected by a cross-link provides direct evidence for the physical interaction of amino acid side chains, information that can be used for computational modeling purposes. Despite impressive advances that were made in recent years, the number of experimentally observed cross-links still falls below the number of possible contacts of cross-linkable side chains within the span of the cross-linker. Here, we propose two complementary experimental strategies to expand cross-linking data sets. First, enrichment of cross-linked peptides by size exclusion chromatography selects cross-linked peptides based on their higher molecular mass, thereby depleting the majority of unmodified peptides present in proteolytic digests of cross-linked samples. Second, we demonstrate that the use of proteases in addition to trypsin, such as Asp-N, can additionally boost the number of observable cross-linking sites. The benefits of both SEC enrichment and multiprotease digests are demonstrated on a set of model proteins and the improved workflow is applied to the characterization of the 20S proteasome from rabbit and Schizosaccharomyces pombe.

Indexed as

Chromatography, GelAnimalsCattleChromatography, LiquidCross-Linking ReagentsPeptide FragmentsPeptide HydrolasesProteasome Endopeptidase ComplexProtein ConformationProteinsRabbitsSchizosaccharomycesTandem Mass SpectrometryTrypsinCross-Linking ReagentsPeptide FragmentsPeptide HydrolasesProteasome Endopeptidase ComplexProteinsTrypsin

Identifiers

PMID22286754
PMCPMC3316732
OpenAlexW2168248023

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.