Evidence map›Paper›PMID 40775003›Full record

ArticleScientific reports2025

Inhibition of human N myristoyltransferase 1 as a strategy to suppress cancer progression driven by myristoylation.

Mohammed Merae Alshahrani

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Article
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

1 author.

Mohammed Merae AlshahraniDepartment of Clinical Laboratory Sciences, Faculty of Applied Medical Sciences, Najran University, 1988, Najran, 61441, Saudi Arabia. mmalshahrani@nu.edu.sa.ORCID http://orcid.org/0000-0002-9387-5492

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-myristoyltransferase 1 (NMT-1) catalyzes the co-translational addition of myristic acid to the N-terminal glycine of substrate proteins, regulating membrane localization and protein-protein interactions essential for oncogenic signaling. Its overexpression in diverse malignancies has rendered NMT-1 a valuable target for anticancer drug discovery. The study identified four promising inhibitors (Diverse-lib ID: 17506136, 103050917, 24289547, and 24314423) with docking scores ranging from - 11.5 to - 11.2 kcal/mol. DFT analysis revealed favorable frontier orbital characteristics, particularly in 24,289,547, which exhibited the lowest HOMO-LUMO ΔE

Indexed as

AcyltransferasesAntineoplastic AgentsEnzyme InhibitorsMyristic AcidNeoplasmsCatalytic DomainDisease ProgressionHumansMolecular Docking SimulationMolecular Dynamics SimulationProtein BindingAcyltransferasesAntineoplastic AgentsEnzyme Inhibitorsglycylpeptide N-tetradecanoyltransferaseMyristic AcidCancerDensity functional theoryDiverse-libMolecular dynamicsN-myristoyltransferase 1

Identifiers

PMID40775003
PMCPMC12331916

What Socratic holds

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LicenceCC BY-NC-ND
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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 Socratic graph.