ArticleMolecular and cellular biochemistry
Mammalian myristoyl CoA: protein N-myristoyltransferase.
Article in Molecular and cellular biochemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 34 citations in OpenAlex.
- Protein lipidation in cardiovascular homeostasis, development, and disease.Clinical science (London, England : 1979) · 2026Review
- The role of N-myristoyltransferase 1 in tumour development.Annals of medicine · 2023Review
- Protein N-myristoylation: functions and mechanisms in control of innate immunity.Cellular & molecular immunology · 2021Review
- Myristoylation of EV71 VP4 is Essential for Infectivity and Interaction with Membrane Structure.Virologica Sinica · 2020Article
- The myristoylated amino-terminus of an Arabidopsis calcium-dependent protein kinase mediates plasma membrane localization.Plant molecular biology · 2013Article
- Protein myristoylation in health and disease.Journal of chemical biology · 2010Article
- Biochemical characterization of bovine brain myristoyl-CoA:protein N-myristoyltransferase type 2.Journal of biomedicine & biotechnology · 2009Article
- Biological significance of phosphorylation and myristoylation in the regulation of cardiac muscle proteins.Molecular and cellular biochemistry · 1997Review
- Coenzyme A dependent myristoylation and demyristoylation in the regulation of bovine spleen N-myristoyltransferase.Molecular and cellular biochemistry · 1996Article
- Expression of human N-myristoyltransferase in Escherichia coli. Comparison with N-myristoyltransferases expressed in different tissues.Molecular and cellular biochemistry · 1996Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myristoyl CoA:Protein N-myristoyltransferase (NMT) is the enzyme which catalyses the covalent transfer of myristate from myristoyl CoA to the amino-terminal glycine residue of protein substrates. Although NMT is ubiquitous in eukaryotic cells, the enzyme levels and cellular distribution vary among tissues. In this article, we describe the properties of mammalian NMT(s) with reference to subcellular distribution, molecular weights, substrate specificity and the possible involvement of NMT in pathological processes. The cytosolic fraction of bovine brain contains majority of NMT activity. In contrast, rabbit colon and rat liver NMT activity was predominantly particulate. Regional differences in NMT activity have been observed in both rabbit intestine and bovine brain. Results from our laboratory along with the existing knowledge, provide evidence for the existence of tissue specific isozymes of NMT.
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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.