Evidence map›Paper›PMID 17676784›Full record

ArticleJournal of proteome research2007

Informatics strategies for large-scale novel cross-linking analysis.

Gordon A Anderson, Nikola Tolic, Xiaoting Tang, Chunxiang Zheng, James E Bruce

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

33 citing papers in PubMed, 51 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. The First MS-Cleavable, Photo-Thiol-Reactive Cross-Linker for Protein Structural Studies.Journal of the American Society for Mass Spectrometry · 2019
    Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Protein Structural Analysis via Mass Spectrometry-Based Proteomics.Advances in experimental medicine and biology · 2016
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  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

5 authors at 3 institutions in 1 country.

Gordon A AndersonEnvironmental Molecular Sciences Laboratory (EMSL), Pacific Northwest National Laboratory (PNNL), Richland, Washington 99352, USA.
Nikola Tolic
Xiaoting Tang
Chunxiang Zheng
James E Bruce
Pacific Northwest National Laboratory · USEnvironmental Molecular Sciences Laboratory · USWashington State University · US

Funding

New Technology for Protein Interaction Network and Topology AnalysisR01RR023334 · NCRR · WASHINGTON STATE UNIVERSITY · PI BRUCE, JAMES EDWARD · 2007 to 2009
$750k
MALDI TOF/TOF MASS SPECTROMETER SYSTEM FOR PROTEOMICSS10RR022538 · NCRR · WASHINGTON STATE UNIVERSITY · PI BRUCE, JAMES EDWARD · 2006 to 2006
$378k
NCRR NIH HHS R01 RR023334NCRR NIH HHS S10 RR022538
6 · The paper itself

Abstract

The detection of protein interactions in biological systems represents a significant challenge for today's technology. Chemical cross-linking provides the potential to impart new chemical bonds in a complex system that result in mass changes in a set of tryptic peptides detected by mass spectrometry. However, system complexity and cross-linking product heterogeneity have precluded widespread chemical cross-linking use for large-scale identification of protein-protein interactions. The development of mass spectrometry identifiable cross-linkers called protein interaction reporters (PIRs) has enabled on-cell chemical cross-linking experiments with product type differentiation. However, the complex datasets resultant from PIR experiments demand new informatics capabilities to allow interpretation. This manuscript details our efforts to develop such capabilities and describes the program X-links, which allows PIR product type differentiation. Furthermore, we also present the results from Monte Carlo simulation of PIR-type experiments to provide false discovery rate estimates for the PIR product type identification through observed precursor and released peptide masses. Our simulations also provide peptide identification calculations based on accurate masses and database complexity that can provide an estimation of false discovery rates for peptide identification. Overall, the calculations show a low rate of false discovery of PIR product types due to random mass matching of approximately 12% with 10 ppm mass measurement accuracy and spectral complexity resulting from 100 peptides. In addition, consideration of a reduced database resulting from stage 1 analysis of Shewanella oneidensis MR-1 containing 367 proteins resulted in a significant reduction of expected identification false discovery rate estimation compared to that from the entire Shewanella oneidensis MR-1 proteome.

Indexed as

Bacterial ProteinsComputational BiologyCross-Linking ReagentsDatabases, ProteinData Interpretation, StatisticalHumansMass SpectrometryMonte Carlo MethodPeptidesProteinsProteomicsReproducibility of ResultsShewanellaSoftwareTrypsinBacterial ProteinsCross-Linking ReagentsPeptidesProteinsTrypsin

Identifiers

PMID17676784
PMCPMC2475505
OpenAlexW2092040511

What OpenQuestion holds

Textmetadata
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.