Evidence map›Paper›PMID 31006618›Full record

ArticleCell chemical biology2019

Validation and Invalidation of Chemical Probes for the Human N-myristoyltransferases.

Wouter W Kallemeijn, Gregor A Lueg, Monica Faronato, Kate Hadavizadeh, Andrea Goya Grocin, Ok-Ryul Song, Michael Howell, Dinis P Calado, Edward W Tate

Open access · hybridAbstract read
In one paragraph

Article in Cell chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

34 citing papers in PubMed, 51 citations in OpenAlex.

  1. Review
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  3. ACS medicinal chemistry letters · 2026
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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

9 authors at 3 institutions in 1 country.

Wouter W KallemeijnDepartment of Chemistry, Imperial College London, Molecular Research Science Hub, 80 Wood Lane, London W12 0BZ, UK.
Gregor A LuegDepartment of Chemistry, Imperial College London, Molecular Research Science Hub, 80 Wood Lane, London W12 0BZ, UK; The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Monica FaronatoDepartment of Chemistry, Imperial College London, Molecular Research Science Hub, 80 Wood Lane, London W12 0BZ, UK; The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Kate HadavizadehDepartment of Chemistry, Imperial College London, Molecular Research Science Hub, 80 Wood Lane, London W12 0BZ, UK.
Andrea Goya GrocinDepartment of Chemistry, Imperial College London, Molecular Research Science Hub, 80 Wood Lane, London W12 0BZ, UK.
Ok-Ryul SongThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Michael HowellThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Dinis P CaladoThe Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK; Peter Gorer Department of Immunobiology, School of Immunology & Microbial Sciences, King's College London, London SE1 9RT, UK.
Edward W TateDepartment of Chemistry, Imperial College London, Molecular Research Science Hub, 80 Wood Lane, London W12 0BZ, UK; The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK. Electronic address: e.tate@imperial.ac.uk.
The Francis Crick Institute · GBImperial College London · GBKing's College London · GB

Funding

Cancer Research UK 20183Cancer Research UK C29637/A20183Cancer Research UK C29637/A21451Cancer Research UK FC001057Cancer Research UK FC001097Medical Research Council FC001057Medical Research Council FC001097Medical Research Council MR/J008060/1Wellcome Trust FC001057Wellcome Trust FC001097
6 · The paper itself

Abstract

On-target, cell-active chemical probes are of fundamental importance in chemical and cell biology, whereas poorly characterized probes often lead to invalid conclusions. Human N-myristoyltransferase (NMT) has attracted increasing interest as target in cancer and infectious diseases. Here we report an in-depth comparison of five compounds widely applied as human NMT inhibitors, using a combination of quantitative whole-proteome N-myristoylation profiling, biochemical enzyme assays, cytotoxicity, in-cell protein synthesis, and cell-cycle assays. We find that N-myristoylation is unaffected by 2-hydroxymyristic acid (100 μM), D-NMAPPD (30 μM), or Tris-DBA palladium (10 μM), with the latter compounds causing cytotoxicity through mechanisms unrelated to NMT. In contrast, drug-like inhibitors IMP-366 (DDD85646) and IMP-1088 delivered complete and specific inhibition of N-myristoylation in a range of cell lines at 1 μM and 100 nM, respectively. This study enables the selection of appropriate on-target probes for future studies and suggests the need for reassessment of previous studies that used off-target compounds.

Indexed as

AcyltransferasesAntineoplastic AgentsApoptosisCell CycleCell Line, TumorCell ProliferationCell SurvivalDose-Response Relationship, DrugDrug Screening Assays, AntitumorEnzyme InhibitorsHumansMolecular StructureMyristic AcidsStructure-Activity RelationshipAcyltransferasesalpha-hydroxymyristic acidAntineoplastic AgentsEnzyme Inhibitorsglycylpeptide N-tetradecanoyltransferaseMyristic Acids2-hydroxymyristic acidchemical proteomicsD-NMAPPD (B13)IMP-1088IMP-366 (DDD85646)metabolic taggingN-myristoylationN-myristoyltransferases (NMT)sortase A ligationTris-DBA palladium

Identifiers

PMID31006618
PMCPMC6593224
OpenAlexW2936149497

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.