Evidence map›Paper›PMID 27649375›Full record

ArticleAnalytical chemistry2016

Differential Tandem Mass Spectrometry-Based Cross-Linker: A New Approach for High Confidence in Identifying Protein Cross-Linking.

Jayanta K Chakrabarty, Aishwarya G Naik, Michael B Fessler, Gerhard R Munske, Saiful M Chowdhury

Abstract read
In one paragraph

Article in Analytical chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. ETD-Cleavable Linker for Confident Cross-linked Peptide Identifications.Journal of the American Society for Mass Spectrometry · 2019
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. 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

5 authors.

Jayanta K Chakrabarty
Aishwarya G Naik
Michael B FesslerImmunity, Inflammation and Disease Laboratory, National Institute of Environmental Health Sciences, NIH , Research Triangle Park, North Carolina 27709, United States.
Gerhard R MunskeLaboratory of Bioanalysis, Washington State University , Pullman, Washington 98195, United States.
Saiful M Chowdhury

Funding

Cell Signaling of Host DefenseZIAES102005 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI FESSLER, MICHAEL B · 2009 to 2025
$41.7M
Cell Signaling of Host DefenseZ01ES102005 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI FESSLER, MICHAEL B · 2006 to 2008
$3.3M
Identifying host-defense interactome caused by environmental and external agentsUA5GM113216 · NIGMS · UNIVERSITY OF TEXAS ARLINGTON · PI CHOWDHURY, SAIFUL M · 2015 to 2015
$355k
Intramural NIH HHS Z01 ES102005NIGMS NIH HHS UA5 GM113216
6 · The paper itself

Abstract

Chemical cross-linking and mass spectrometry are now widely used to analyze large-scale protein-protein interactions. The major challenge in cross-linking approaches is the complexity of the mass spectrometric data. New approaches are required that can identify cross-linked peptides with high-confidence and establish a user-friendly analysis protocol for the biomedical scientific community. Here, we introduce a novel cross-linker that can be selectively cleaved in the gas phase using two differential tandem mass-spectrometric fragmentation methods, such as collision-induced or electron transfer dissociation (CID and ETD). This technique produces two signature mass spectra of the same cross-linked peptide, thereby producing high confidence in identifying the sites of interaction. Further tandem mass spectrometry can also give additional confidence on the peptide sequences. We demonstrate a proof-of-concept for this method using standard peptides and proteins. Peptides and proteins were cross-linked and their fragmentation characteristics were analyzed using CID and ETD tandem mass spectrometry. Two sequential cleavages unambiguously identified cross-linked peptides. In addition, the labeling efficiency of the new cross-linker was evaluated in macrophage immune cells after stimulation with the microbial ligand lipopolysaccharide and subsequent pulldown experiments with biotin-avidin affinity chromatography. We believe this strategy will help advance insights into the structural biology and systems biology of cell signaling.

Indexed as

AnimalsCattleChromatography, LiquidCross-Linking ReagentsHydrazonesMiceNeurotensinPeptidesProteinsRAW 264.7 CellsSerum Albumin, BovineSuccinimidesTandem Mass SpectrometryUbiquitinCross-Linking ReagentsHydrazonesNeurotensinPeptidesProteinsSerum Albumin, BovineSuccinimidesUbiquitin

Identifiers

PMID27649375
PMCPMC5316473

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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.