Evidence map›Paper›PMID 24037665›Full record

ReviewMolecular & cellular proteomics : MCP2013

The coming of age of phosphoproteomics--from large data sets to inference of protein functions.

Philippe P Roux, Pierre Thibault

Abstract readReview
In one paragraph

Review in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Muscle Proteome Dynamics.Advances in experimental medicine and biology · 2025
    Review
  7. Review
  8. Review
  9. Network regulation meets substrate modification chemistry.Journal of the Royal Society, Interface · 2023
    Article
  10. Phosphoproteomics After Guanidinium Thiocyanate Extraction of Tissue Biopsies.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  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

2 authors.

Philippe P RouxInstitute for Research in Immunology and Cancer, Université de Montréal, P.O. Box 6128, Station. Centre-ville, Montréal, Québec H3C 3J7, Canada;
Pierre Thibault

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Protein phosphorylation is one of the most common post-translational modifications used in signal transduction to control cell growth, proliferation, and survival in response to both intracellular and extracellular stimuli. This modification is finely coordinated by a network of kinases and phosphatases that recognize unique sequence motifs and/or mediate their functions through scaffold and adaptor proteins. Detailed information on the nature of kinase substrates and site-specific phosphoregulation is required in order for one to better understand their pathophysiological roles. Recent advances in affinity chromatography and mass spectrometry (MS) sensitivity have enabled the large-scale identification and profiling of protein phosphorylation, but appropriate follow-up experiments are required in order to ascertain the functional significance of identified phosphorylation sites. In this review, we present meaningful technical details for MS-based phosphoproteomic analyses and describe important considerations for the selection of model systems and the functional characterization of identified phosphorylation sites.

Indexed as

Protein Processing, Post-TranslationalProteomicsAdaptor Proteins, Signal TransducingChromatography, LiquidEnzyme InhibitorsGene Expression RegulationHumansModels, BiologicalPhosphoproteinsPhosphoric Monoester HydrolasesPhosphorylationProtein KinasesSignal TransductionTandem Mass SpectrometryAdaptor Proteins, Signal TransducingEnzyme InhibitorsPhosphoproteinsPhosphoric Monoester HydrolasesProtein Kinases

Identifiers

PMID24037665
PMCPMC3861699

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.