Evidence map›Paper›PMID 30266825›Full record

ArticleThe EMBO journal2018

Phosphoproteomic screening identifies physiological substrates of the CDKL5 kinase.

Ivan M Muñoz, Michael E Morgan, Julien Peltier, Florian Weiland, Mateusz Gregorczyk, Fiona Cm Brown, Thomas Macartney, Rachel Toth, Matthias Trost, John Rouse

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

54 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
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  4. CDKL5 modulates the plasticity of excitatory synapses via liquid-liquid phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  11. Transcriptomic Profiling of Zebrafish Mutant forInternational journal of molecular sciences · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Novel CDKL5 targets identified in human iPSC-derived neurons.Cellular and molecular life sciences : CMLS · 2024
    Article
  18. Article
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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

10 authors at 1 institution in 1 country.

Ivan M MuñozMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK.
Michael E MorganMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK.
Julien PeltierMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK.
Florian WeilandMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK.
Mateusz GregorczykMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK.
Fiona Cm BrownMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK.
Thomas MacartneyMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK.
Rachel TothMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK.
Matthias TrostMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK matthias.trost@ncl.ac.uk j.rouse@dundee.ac.uk.ORCID 0000-0002-5732-700X
John RouseMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK matthias.trost@ncl.ac.uk j.rouse@dundee.ac.uk.ORCID 0000-0003-1183-8303
University of Dundee · GB

Funding

Medical Research Council MC_UP_A500_1020Medical Research Council MC_UU_00018/5Medical Research Council MC_UU_12016/1Medical Research Council MC_UU_12016/5
6 · The paper itself

Abstract

Mutations in the gene encoding the protein kinase CDKL5 cause a debilitating neurodevelopmental disease termed CDKL5 disorder. The impact of these mutations on CDKL5 function is poorly understood because the substrates and cellular processes controlled by CDKL5 are unclear. Here, we describe a quantitative phosphoproteomic screening which identified MAP1S, CEP131 and DLG5-regulators of microtubule and centrosome function-as cellular substrates of CDKL5. Antibodies against MAP1S phospho-Ser

Indexed as

Amino Acid MotifsCell Cycle ProteinsCell Line, TumorCentrosomeCytoskeletal ProteinsEpileptic SyndromesHEK293 CellsHumansMembrane ProteinsMicrotubule-Associated ProteinsMicrotubule ProteinsMicrotubulesMutationProtein Serine-Threonine KinasesProteomicsSpasms, InfantileCDKL5 protein, humanCell Cycle ProteinsCEP131 protein, humanCytoskeletal ProteinsDLG5 protein, humanMAP1S protein, humanMembrane ProteinsMicrotubule-Associated ProteinsMicrotubule ProteinsProtein Serine-Threonine KinasesTumor Suppressor ProteinsCDKL5 disordercentrosomeciliakinasemicrotubule

Identifiers

PMID30266825
PMCPMC6293279
OpenAlexW2892383969

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.