Evidence map›Paper›PMID 25255805›Full record

ArticleNature communications2014

Global profiling of co- and post-translationally N-myristoylated proteomes in human cells.

Emmanuelle Thinon, Remigiusz A Serwa, Malgorzata Broncel, James A Brannigan, Ute Brassat, Megan H Wright, William P Heal, Anthony J Wilkinson, David J Mann, Edward W Tate

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 149 papers.

0numbers the graph read from it
0cells of the map it votes in
149citing papers in PubMed
9.1field-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

149 citing papers in PubMed, 241 citations in OpenAlex.

  1. Review
  2. Molecular insights into NLRP1 Gly/N-degron recognition by CRL2Acta crystallographica. Section F, Structural biology communications · 2026
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89 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

10 authors at 4 institutions in 3 countries.

Emmanuelle Thinon1] Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, UK [2] Department of Life Sciences, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Remigiusz A SerwaDepartment of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Malgorzata BroncelDepartment of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
James A BranniganYork Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, UK.
Ute Brassat1] Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, UK [2] Department of Life Sciences, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Megan H Wright1] Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, UK [2] Department of Chemistry, Institute of Chemical Biology, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
William P HealDepartment of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Anthony J WilkinsonYork Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5DD, UK.
David J Mann1] Department of Life Sciences, Imperial College London, Exhibition Road, London SW7 2AZ, UK [2] Department of Chemistry, Institute of Chemical Biology, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Edward W Tate1] Department of Chemistry, Imperial College London, Exhibition Road, London SW7 2AZ, UK [2] Department of Chemistry, Institute of Chemical Biology, Imperial College London, Exhibition Road, London SW7 2AZ, UK.
Imperial College London · GBUniversity of York · GBKing's College London · GBTechnical University of Munich · DE

Funding

Biotechnology and Biological Sciences Research Council BB/D02014X/1Cancer Research UK C29637/A10711Cancer Research UK C29637/A9913Medical Research Council 0900278Medical Research Council G0900278
6 · The paper itself

Abstract

Protein N-myristoylation is a ubiquitous co- and post-translational modification that has been implicated in the development and progression of a range of human diseases. Here, we report the global N-myristoylated proteome in human cells determined using quantitative chemical proteomics combined with potent and specific human N-myristoyltransferase (NMT) inhibition. Global quantification of N-myristoylation during normal growth or apoptosis allowed the identification of >100 N-myristoylated proteins, >95% of which are identified for the first time at endogenous levels. Furthermore, quantitative dose response for inhibition of N-myristoylation is determined for >70 substrates simultaneously across the proteome. Small-molecule inhibition through a conserved substrate-binding pocket is also demonstrated by solving the crystal structures of inhibitor-bound NMT1 and NMT2. The presented data substantially expand the known repertoire of co- and post-translational N-myristoylation in addition to validating tools for the pharmacological inhibition of NMT in living cells.

Indexed as

AcyltransferasesCrystallography, X-RayHeLa CellsHumansMyristic AcidProtein Processing, Post-TranslationalProteomeAcyltransferasesglycylpeptide N-tetradecanoyltransferaseMyristic AcidProteome

Identifiers

PMID25255805
PMCPMC4200515
OpenAlexW2062491810

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Registered trials

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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.