Evidence map›Paper›PMID 15167810›Full record

ReviewThe Biochemical journal2004

Dynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes.

Carol Mackintosh

Open access · greenAbstract readReview
In one paragraph

Review in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 218 papers.

0numbers the graph read from it
0cells of the map it votes in
218citing papers in PubMed
14.2field-weighted citation impact, top 1% 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

218 citing papers in PubMed, 535 citations in OpenAlex.

  1. TheBiomolecules · 2025
    Review
  2. Article
  3. Deciphering opening mechanisms of 14-3-3 proteins.Protein science : a publication of the Protein Society · 2025
    Article
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  6. Review
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  9. The role of the adenylate kinase 5 gene in various diseases and cancer.Journal of clinical and translational science · 2024
    Review
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  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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  19. Article
  20. Review

158 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

1 author at 1 institution in 1 country.

Carol MackintoshMRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK. c.mackintosh@dundee.ac.uk
MRC Protein Phosphorylation and Ubiquitylation Unit · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

14-3-3 proteins exert an extraordinarily widespread influence on cellular processes in all eukaryotes. They operate by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. In these ways, 14-3-3s 'finish the job' when phosphorylation alone lacks the power to drive changes in the activities of intracellular proteins. By interacting dynamically with phosphorylated proteins, 14-3-3s often trigger events that promote cell survival--in situations from preventing metabolic imbalances caused by sudden darkness in leaves to mammalian cell-survival responses to growth factors. Recent work linking specific 14-3-3 isoforms to genetic disorders and cancers, and the cellular effects of 14-3-3 agonists and antagonists, indicate that the cellular complement of 14-3-3 proteins may integrate the specificity and strength of signalling through to different cellular responses.

Indexed as

Cell Physiological Phenomena14-3-3 ProteinsAnimalsHumansPhosphoproteinsProtein Interaction MappingProtein Structure, Quaternary14-3-3 ProteinsPhosphoproteins

Identifiers

PMID15167810
PMCPMC1133837
OpenAlexW2042054309

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.