Evidence map›Paper›PMID 23413883›Full record

ArticleJournal of proteome research2013

In vivo protein interaction network identified with a novel real-time cross-linked peptide identification strategy.

Chad R Weisbrod, Juan D Chavez, Jimmy K Eng, Li Yang, Chunxiang Zheng, James E Bruce

Abstract read
In one paragraph

Article in Journal of proteome research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing 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

85 citing papers in PubMed.

  1. Article
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  9. Review
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  11. Review
  12. An optimized protocol forSTAR protocols · 2022
    Article
  13. Review
  14. 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
  15. Article
  16. Review
  17. Crosslinking mass spectrometry: A link between structural biology and systems biology.Protein science : a publication of the Protein Society · 2021
    Review
  18. Review
  19. Review
  20. Article

25 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

6 authors.

Chad R WeisbrodDepartment of Genome Sciences, University of Washington , Seattle, Washington 98109, United States.
Juan D Chavez
Jimmy K Eng
Li Yang
Chunxiang Zheng
James E Bruce

Funding

Quantitation of protein interactions in cancer cellsR01GM086688 · NIGMS · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD · 2009 to 2019
$4.2M
Instrumentation Development: MS Array for Quantitative ProteomicsR01GM097112 · NIGMS · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD · 2011 to 2020
$2.9M
An LC-FTICR Mass Spectrometer for Proteomics and Metabolomics ResearchS10RR025107 · NCRR · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD · 2008 to 2008
$990k
New Technology for Protein Interaction Network and Topology AnalysisR01RR023334 · NCRR · WASHINGTON STATE UNIVERSITY · PI BRUCE, JAMES EDWARD · 2007 to 2009
$750k
NCRR NIH HHS 5R01RR023334NCRR NIH HHS 7S10RR025107NCRR NIH HHS R01 RR023334NCRR NIH HHS S10 RR025107NIGMS NIH HHS 1R01GM097112NIGMS NIH HHS 2R01GM086688NIGMS NIH HHS R01 GM086688NIGMS NIH HHS R01 GM097112
6 · The paper itself

Abstract

Protein interaction topologies are critical determinants of biological function. Large-scale or proteome-wide measurements of protein interaction topologies in cells currently pose an unmet challenge that could dramatically improve understanding of complex biological systems. A primary impediment includes direct protein topology and interaction measurements from living systems since interactions that lack biological significance may be introduced during cell lysis. Furthermore, many biologically relevant protein interactions will likely not survive the lysis/sample preparation and may only be measured with in vivo methods. As a step toward meeting this challenge, a new mass spectrometry method called Real-time Analysis for Cross-linked peptide Technology (ReACT) has been developed that enables assignment of cross-linked peptides "on-the-fly". Using ReACT, 708 unique cross-linked (<5% FDR) peptide pairs were identified from cross-linked E. coli cells. These data allow assembly of the first protein interaction network that also contains topological features of every interaction, as it existed in cells during cross-linker application. Of the identified interprotein cross-linked peptide pairs, 40% are derived from known interactions and provide new topological data that can help visualize how these interactions exist in cells. Other identified cross-linked peptide pairs are from proteins known to be involved within the same complex, but yield newly discovered direct physical interactors. ReACT enables the first view of these interactions inside cells, and the results acquired with this method suggest cross-linking can play a major role in future efforts to map the interactome in cells.

Indexed as

AlgorithmsAmino Acid SequenceCross-Linking ReagentsEscherichia coliMass SpectrometryMolecular Sequence DataPeptidesProtein Interaction MappingCross-Linking ReagentsPeptides

Identifiers

PMID23413883
PMCPMC3925062

What OpenQuestion holds

Textmetadata
LicenceTDM
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.