Evidence map›Paper›PMID 25735772›Full record

ArticleBioinformatics (Oxford, England)2015

14-3-3-Pred: improved methods to predict 14-3-3-binding phosphopeptides.

Fábio Madeira, Michele Tinti, Gavuthami Murugesan, Emily Berrett, Margaret Stafford, Rachel Toth, Christian Cole, Carol MacKintosh, Geoffrey J Barton

Open access · hybridAbstract read
In one paragraph

Article in Bioinformatics (Oxford, England), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

117 citing papers in PubMed, 223 citations in OpenAlex.

  1. Article
  2. A complex of MAST1 and 14-3-3η regulates Tau phosphorylation in the developing cortex.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Identification of 14-3-3 Proteins as Binding Partners of TRP Channels.Journal of chemical information and modeling · 2026
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  12. microPublication biology · 2026
    Article
  13. Potential 14-3-3 binding sites in sirtuins reveal extended phosphosite-recognition modes.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
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57 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

9 authors at 2 institutions in 1 country.

Fábio MadeiraDivision of Computational Biology.
Michele TintiDivision of Cell and Developmental Biology.
Gavuthami MurugesanDivision of Computational Biology.
Emily BerrettDivision of Computational Biology.
Margaret StaffordMRC Protein Phosphorylation Unit.
Rachel TothDivision of Signal Transduction Therapy.
Christian ColeDivision of Computational Biology.
Carol MacKintoshDivision of Cell and Developmental Biology.
Geoffrey J BartonDivision of Computational Biology, Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK.
MRC Protein Phosphorylation and Ubiquitylation Unit · GBUniversity of Dundee · GB

Funding

Diabetes UK 12/0004557Medical Research Council G0801767Wellcome Trust 097945Wellcome Trust 100150/Z/12/Z
6 · The paper itself

Abstract

motivationThe 14-3-3 family of phosphoprotein-binding proteins regulates many cellular processes by docking onto pairs of phosphorylated Ser and Thr residues in a constellation of intracellular targets. Therefore, there is a pressing need to develop new prediction methods that use an updated set of 14-3-3-binding motifs for the identification of new 14-3-3 targets and to prioritize the downstream analysis of >2000 potential interactors identified in high-throughput experiments.

resultsHere, a comprehensive set of 14-3-3-binding targets from the literature was used to develop 14-3-3-binding phosphosite predictors. Position-specific scoring matrix, support vector machines (SVM) and artificial neural network (ANN) classification methods were trained to discriminate experimentally determined 14-3-3-binding motifs from non-binding phosphopeptides. ANN, position-specific scoring matrix and SVM methods showed best performance for a motif window spanning from -6 to +4 around the binding phosphosite, achieving Matthews correlation coefficient of up to 0.60. Blind prediction showed that all three methods outperform two popular 14-3-3-binding site predictors, Scansite and ELM. The new methods were used for prediction of 14-3-3-binding phosphosites in the human proteome. Experimental analysis of high-scoring predictions in the FAM122A and FAM122B proteins confirms the predictions and suggests the new 14-3-3-predictors will be generally useful. AVAILABILITY AND IMPLEMENTATION: A standalone prediction web server is available at http://www.compbio.dundee.ac.uk/1433pred. Human candidate 14-3-3-binding phosphosites were integrated in ANIA: ANnotation and Integrated Analysis of the 14-3-3 interactome database.

Indexed as

14-3-3 ProteinsAmino Acid MotifsBinding SitesHEK293 CellsHumansNeural Networks, ComputerPhosphopeptidesPhosphoproteinsPosition-Specific Scoring MatricesProteomeProteomicsSoftwareSupport Vector Machine14-3-3 ProteinsPhosphopeptidesPhosphoproteinsProteome

Identifiers

PMID25735772
PMCPMC4495292
OpenAlexW2110844810

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.