Evidence map›Paper›PMID 21725060›Full record

ArticleMolecular & cellular proteomics : MCP2011

Visualization and biochemical analyses of the emerging mammalian 14-3-3-phosphoproteome.

Catherine Johnson, Michele Tinti, Nicola T Wood, David G Campbell, Rachel Toth, Fanny Dubois, Kathryn M Geraghty, Barry H C Wong, Laura J Brown, Jennifer Tyler and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

43 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Molecular Analysis ofInternational journal of molecular sciences · 2021
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  8. Review
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  10. Modular bioengineered kinase sensorsChemical science · 2020
    Article
  11. Article
  12. Article
  13. Small heat shock proteins: Simplicity meets complexity.The Journal of biological chemistry · 2019
    Review
  14. Review
  15. Article
  16. Modulators of 14-3-3 Protein-Protein Interactions.Journal of medicinal chemistry · 2018
    Review
  17. Article
  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

14 authors at 2 institutions in 1 country.

Catherine JohnsonMRC Protein Phosphorylation Unit, College of Life Sciences, University of Dundee, James Black Centre, Dow Street, Dundee DD1 5EH, Scotland, UK.
Michele Tinti
Nicola T Wood
David G Campbell
Rachel Toth
Fanny Dubois
Kathryn M Geraghty
Barry H C Wong
Laura J Brown
Jennifer Tyler
Aurélie Gernez
Shuai Chen
Silvia Synowsky
Carol MacKintosh
University of Dundee · GBMRC Protein Phosphorylation and Ubiquitylation Unit · GB

Funding

Medical Research Council
6 · The paper itself

Abstract

Hundreds of candidate 14-3-3-binding (phospho)proteins have been reported in publications that describe one interaction at a time, as well as high-throughput 14-3-3-affinity and mass spectrometry-based studies. Here, we transcribed these data into a common format, deposited the collated data from low-throughput studies in MINT (http://mint.bio.uniroma2.it/mint), and compared the low- and high-throughput data in VisANT graphs that are easy to analyze and extend. Exploring the graphs prompted questions about technical and biological specificity, which were addressed experimentally, resulting in identification of phosphorylated 14-3-3-binding sites in the mitochondrial import sequence of the iron-sulfur cluster assembly enzyme (ISCU), cytoplasmic domains of the mitochondrial fission factor (MFF), and endoplasmic reticulum-tethered receptor expression-enhancing protein 4 (REEP4), RNA regulator SMAUG2, and cytoskeletal regulatory proteins, namely debrin-like protein (DBNL) and kinesin light chain (KLC) isoforms. Therefore, 14-3-3s undergo physiological interactions with proteins that are destined for diverse subcellular locations. Graphing and validating interactions underpins efforts to use 14-3-3-phosphoproteomics to identify mechanisms and biomarkers for signaling pathways in health and disease.

Indexed as

14-3-3 ProteinsAnimalsBinding SitesBiomarkersDatabases, ProteinHEK293 CellsHumansMass SpectrometryMiceMitochondriaPhosphoproteinsProtein BindingProtein Structure, TertiaryRecombinant ProteinsSignal Transduction14-3-3 ProteinsBiomarkersPhosphoproteinsRecombinant Proteins

Identifiers

PMID21725060
PMCPMC3205853
OpenAlexW2166227754

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.