Evidence map›Paper›PMID 25823605›Full record

ArticleOrganic & biomolecular chemistry2015

Synthesis of two new enrichable and MS-cleavable cross-linkers to define protein-protein interactions by mass spectrometry.

Anthony M Burke, Wynne Kandur, Eric J Novitsky, Robyn M Kaake, Clinton Yu, Athit Kao, Danielle Vellucci, Lan Huang, Scott D Rychnovsky

Abstract read
In one paragraph

Article in Organic & biomolecular chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
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  5. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Protein interaction landscapes revealed by advanced in vivo cross-linking-mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Review
  17. 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

9 authors.

Anthony M BurkeDepartment of Chemistry, University of California, Irvine, CA 92697, USA. srychnov@uci.edu.
Wynne Kandur
Eric J Novitsky
Robyn M Kaake
Clinton Yu
Athit Kao
Danielle Vellucci
Lan Huang
Scott D Rychnovsky

Funding

Biomedical Informatics Training ProgramT15LM007443 · NLM · UNIVERSITY OF CALIFORNIA-IRVINE · PI BALDI, PIERRE · 2002 to 2012
$9.3M
Proteomics of the Proteasome Interacting NetworksR01GM074830 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI HUANG, LAN · 2005 to 2022
$6.1M
Function and Regulation of the CSN in the NF-kB Activation PathwayR21CA161807 · NCI · UNIVERSITY OF CALIFORNIA-IRVINE · PI HUANG, LAN · 2012 to 2013
$358k
NCI NIH HHS R21 CA161807NCI NIH HHS R21CA161807NIGMS NIH HHS R01 GM074830NIGMS NIH HHS R01GM074830-06A1NIGMS NIH HHS T32-GM10856NLM NIH HHS 5T15LM007443-10NLM NIH HHS T15 LM007443
6 · The paper itself

Abstract

The cross-linking Mass Spectrometry (XL-MS) technique extracts structural information from protein complexes without requiring highly purified samples, crystallinity, or large amounts of material. However, there are challenges to applying the technique to protein complexes in vitro, and those challenges become more daunting with in vivo experiments. Issues include effective detection and identification of cross-linked peptides from complex mixtures. While MS-cleavable cross-linkers facilitate the sequencing and identification of cross-linked peptides, enrichable cross-linkers increase their detectability by allowing their separation from non-cross-linked peptides prior to MS analysis. Although a number of cross-linkers with single functionality have been developed in recent years, an ideal reagent would incorporate both capabilities for XL-MS studies. Therefore, two new cross-linkers have been designed and prepared that incorporate an azide (azide-A-DSBSO) or alkyne (alkyne-A-DSBSO) to enable affinity purification strategies based on click chemistry. The integration of an acid cleavage site next to the enrichment handle allows easy recovery of cross-linked products during affinity purification. In addition, these sulfoxide containing cross-linking reagents possess robust MS-cleavable bonds to facilitate fast and easy identification of cross-linked peptides using MS analysis. Optimized, gram-scale syntheses of these cross-linkers have been developed and the azide-A-DSBSO cross-linker has been evaluated with peptides and proteins to demonstrate its utility in XL-MS analysis.

Indexed as

AlkynesAzidesClick ChemistryCross-Linking ReagentsMass SpectrometryMolecular StructureProtein BindingProteinsSulfoxidesAlkynesAzidesCross-Linking ReagentsProteinsSulfoxides

Identifiers

PMID25823605
PMCPMC4420144

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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.