Evidence map›Paper›PMID 22168182›Full record

ArticleJournal of proteome research2012

In vivo application of photocleavable protein interaction reporter technology.

Li Yang, Chunxiang Zheng, Chad R Weisbrod, Xiaoting Tang, Gerhard R Munske, Michael R Hoopmann, Jimmy K Eng, James E Bruce

Abstract read
In one paragraph

Article in Journal of proteome research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. The First MS-Cleavable, Photo-Thiol-Reactive Cross-Linker for Protein Structural Studies.Journal of the American Society for Mass Spectrometry · 2019
    Article
  7. Review
  8. Novel Concepts of MS-Cleavable Cross-linkers for Improved Peptide Structure Analysis.Journal of the American Society for Mass Spectrometry · 2017
    Article
  9. Article
  10. Review
  11. Mitochondrial protein interactome elucidated by chemical cross-linking mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
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

8 authors.

Li YangDepartment of Chemistry, Washington State University, Pullman, Washington, 99164, USA.
Chunxiang Zheng
Chad R Weisbrod
Xiaoting Tang
Gerhard R Munske
Michael R Hoopmann
Jimmy K Eng
James E Bruce

Funding

Quantitation of protein interactions in cancer cellsR01GM086688 · NIGMS · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD · 2009 to 2019
$4.2M
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 5R01GM086688NIGMS NIH HHS R01 GM086688
6 · The paper itself

Abstract

In vivo protein structures and protein-protein interactions are critical to the function of proteins in biological systems. As a complementary approach to traditional protein interaction identification methods, cross-linking strategies are beginning to provide additional data on protein and protein complex topological features. Previously, photocleavable protein interaction reporter (pcPIR) technology was demonstrated by cross-linking pure proteins and protein complexes and the use of ultraviolet light to cleave or release cross-linked peptides to enable identification. In the present report, the pcPIR strategy is applied to Escherichia coli cells, and in vivo protein interactions and topologies are measured. More than 1600 labeled peptides from E. coli were identified, indicating that many protein sites react with pcPIR in vivo. From those labeled sites, 53 in vivo intercross-linked peptide pairs were identified and manually validated. Approximately half of the interactions have been reported using other techniques, although detailed structures exist for very few. Three proteins or protein complexes with detailed crystallography structures are compared to the cross-linking results obtained from in vivo application of pcPIR technology.

Indexed as

PhotolysisAmino Acid SequenceBinding SitesCross-Linking ReagentsEscherichia coliEscherichia coli ProteinsMass SpectrometryModels, MolecularMolecular Sequence DataMultiprotein ComplexesPeptide FragmentsPhotochemistryProtein Interaction MappingReproducibility of ResultsSequence AlignmentUltraviolet RaysCross-Linking ReagentsEscherichia coli ProteinsMultiprotein ComplexesPeptide Fragments

Identifiers

PMID22168182
PMCPMC3319076

What OpenQuestion holds

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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.