Evidence map›Paper›PMID 27267252›Full record

ArticleACS chemical biology2016

N-Myristoyltransferase Inhibition Induces ER-Stress, Cell Cycle Arrest, and Apoptosis in Cancer Cells.

Emmanuelle Thinon, Julia Morales-Sanfrutos, David J Mann, Edward W Tate

Open access · hybridAbstract read
In one paragraph

Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.2field-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

46 citing papers in PubMed, 78 citations in OpenAlex.

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  15. Impact of Protein NLife (Basel, Switzerland) · 2023
    Review
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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

4 authors at 1 institution in 1 country.

Emmanuelle ThinonDepartment of Chemistry, Imperial College London , Exhibition Road, London SW72AZ, United Kingdom.
Julia Morales-SanfrutosDepartment of Chemistry, Imperial College London , Exhibition Road, London SW72AZ, United Kingdom.
David J MannDepartment of Life Sciences, Imperial College London , Exhibition Road, London SW72AZ, United Kingdom.
Edward W TateDepartment of Chemistry, Imperial College London , Exhibition Road, London SW72AZ, United Kingdom.
Imperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D02014X/1Cancer Research UK 20183Cancer Research UK C29637/A10711Cancer Research UK C29637/A20183Cancer Research UK C29637/A9913Medical Research Council MC_PC_13064
6 · The paper itself

Abstract

N-Myristoyltransferase (NMT) covalently attaches a C14 fatty acid to the N-terminal glycine of proteins and has been proposed as a therapeutic target in cancer. We have recently shown that selective NMT inhibition leads to dose-responsive loss of N-myristoylation on more than 100 protein targets in cells, and cytotoxicity in cancer cells. N-myristoylation lies upstream of multiple pro-proliferative and oncogenic pathways, but to date the complex substrate specificity of NMT has limited determination of which diseases are most likely to respond to a selective NMT inhibitor. We describe here the phenotype of NMT inhibition in HeLa cells and show that cells die through apoptosis following or concurrent with accumulation in the G1 phase. We used quantitative proteomics to map protein expression changes for more than 2700 proteins in response to treatment with an NMT inhibitor in HeLa cells and observed down-regulation of proteins involved in cell cycle regulation and up-regulation of proteins involved in the endoplasmic reticulum stress and unfolded protein response, with similar results in breast (MCF-7, MDA-MB-231) and colon (HCT116) cancer cell lines. This study describes the cellular response to NMT inhibition at the proteome level and provides a starting point for selective targeting of specific diseases with NMT inhibitors, potentially in combination with other targeted agents.

Indexed as

ApoptosisCell Cycle CheckpointsEndoplasmic Reticulum StressAcyltransferasesCell Line, TumorEnzyme InhibitorsHumansProteomeAcyltransferasesEnzyme Inhibitorsglycylpeptide N-tetradecanoyltransferaseProteome

Identifiers

PMID27267252
PMCPMC5077176
OpenAlexW2419320951

What OpenQuestion holds

Textmetadata
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.