Evidence map›Paper›PMID 22806145›Full record

ArticleMolecular systems biology2012

Deciphering a global network of functionally associated post-translational modifications.

Pablo Minguez, Luca Parca, Francesca Diella, Daniel R Mende, Runjun Kumar, Manuela Helmer-Citterich, Anne-Claude Gavin, Vera van Noort, Peer Bork

Abstract read
In one paragraph

Article in Molecular systems biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 129 papers.

0numbers the graph read from it
0cells of the map it votes in
129citing 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

129 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. CLASPP: A unified model for predicting post-translational modifications.bioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Article
  8. Dynamic expression of lamin B1 during adult neurogenesis in the vertebrate brain.Developmental dynamics : an official publication of the American Association of Anatomists · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Protein lysine acetylation regulates oral microorganisms.Frontiers in cellular and infection microbiology · 2025
    Review
  15. Posttranslational Modifications ofPharmacological reviews · 2024
    Review
  16. Article
  17. Article
  18. Review
  19. Production of Plant Proteins and Peptides with Pharmacological Potential.Advances in biochemical engineering/biotechnology · 2024
    Review
  20. Metabolites · 2023
    Article

69 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Pablo MinguezStructural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
Luca Parca
Francesca Diella
Daniel R Mende
Runjun Kumar
Manuela Helmer-Citterich
Anne-Claude Gavin
Vera van Noort
Peer Bork

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Various post-translational modifications (PTMs) fine-tune the functions of almost all eukaryotic proteins, and co-regulation of different types of PTMs has been shown within and between a number of proteins. Aiming at a more global view of the interplay between PTM types, we collected modifications for 13 frequent PTM types in 8 eukaryotes, compared their speed of evolution and developed a method for measuring PTM co-evolution within proteins based on the co-occurrence of sites across eukaryotes. As many sites are still to be discovered, this is a considerable underestimate, yet, assuming that most co-evolving PTMs are functionally associated, we found that PTM types are vastly interconnected, forming a global network that comprise in human alone >50,000 residues in about 6000 proteins. We predict substantial PTM type interplay in secreted and membrane-associated proteins and in the context of particular protein domains and short-linear motifs. The global network of co-evolving PTM types implies a complex and intertwined post-translational regulation landscape that is likely to regulate multiple functional states of many if not all eukaryotic proteins.

Indexed as

AnimalsCattleChickensEvolution, MolecularHumansMacaca mulattaMicePhylogenyProtein Processing, Post-TranslationalProteinsProteomicsRatsSystems BiologyProteins

Identifiers

PMID22806145
PMCPMC3421446

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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.