ReviewACS chemical biology2020
N-Myristoyltransferase as a Glycine and Lysine Myristoyltransferase in Cancer, Immunity, and Infections.
Review in ACS chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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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.
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.
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Who cites it
14 citing papers in PubMed, 33 citations in OpenAlex.
- Post-translational modifications at the crossroads of cancer metabolism and immune regulation: therapeutic opportunities and challenges.International journal of surgery (London, England) · 2026Review
- Review
- Inhibition of human N myristoyltransferase 1 as a strategy to suppress cancer progression driven by myristoylation.Scientific reports · 2025Article
- Lysine myristoylation mediates long-term potentiation via membrane enrichment of synaptic plasticity effectors.The EMBO journal · 2025Article
- GC/MS Fatty Acid Profile of Marine-Derived Actinomycetes from Extreme Environments: Chemotaxonomic Insights and Biotechnological Potential.Marine drugs · 2024Article
- Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023Review
- Impact of Protein NLife (Basel, Switzerland) · 2023Review
- Shedding Light on Bacterial Physiology with Click Chemistry.Israel journal of chemistry · 2023Article
- Lipids and Secretory Vesicle Exocytosis.Advances in neurobiology · 2023Article
- Reversible lysine fatty acylation of an anchoring protein mediates adipocyte adrenergic signaling.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Binding Affinity Determines Substrate Specificity and Enables Discovery of Substrates for N-Myristoyltransferases.ACS catalysis · 2021Article
- A Not-So-Ancient Grease History: Click Chemistry and Protein Lipid Modifications.Chemical reviews · 2021Review
- Myristic Acid Serum Levels and Their Significance for Diagnosis of Systemic Inflammatory Response, Sepsis, and Bacteraemia.Journal of personalized medicine · 2021Article
- Lysine Fatty Acylation: Regulatory Enzymes, Research Tools, and Biological Function.Frontiers in cell and developmental biology · 2021Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Protein myristoylation, the addition of a 14-carbon saturated acyl group, is an abundant modification implicated in biological events as diverse as development, immunity, oncogenesis, and infections. N-Myristoyltransferase (NMT) is the enzyme that catalyzes this modification. Many elegant studies have established the rules guiding the catalysis including substrate amino acid sequence requirements with the indispensable N-terminal glycine, and a co-translational mode of action. Recent advances in technology such as the development of fatty acid analogs, small molecule inhibitors, and new proteomic strategies, allowed a deeper insight into the NMT activity and function. Here we focus on discussing recent work demonstrating that NMT is also a lysine myristoyltransferase, the enzyme's regulation by a previously unnoticed solvent channel, and the mechanism of NMT regulation by protein-protein interactions. We also summarize recent findings on NMT's role in cancer, immunity, and infections and the advances in pharmacological targeting of myristoylation. Our analyses highlight opportunities for further understanding and discoveries.
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Registered trials
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.