The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Acylation of Proteins with Myristic Acid Occurs Cotranslationally
Abstract
Several proteins of viral and cellular origin are acylated with myristic acid early during their biogenesis. To investigate the possibility that myristylation occurred cotranslationally, the BC 3 H1 muscle cell line, which contains a broad array of myristylated proteins, was pulse-labeled with [ 3 H]myristic acid. Nascent polypeptide chains covalently associated with transfer RNA were isolated subsequently by ion-exchange chromatography. [ 3 H]Myristate was attached to nascent chains through an amide linkage and was identified by thin-layer chromatography after its release from nascent chains by acid methanolysis. Inhibition of cellular protein synthesis with puromycin resulted in cessation of [ 3 H]myristate-labeling of nascent chains, in agreement with the dependence of this modification on protein synthesis in vivo. These data represent a direct demonstration that myristylation of proteins is a cotranslational modification.
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Identification of the NH2‐terminal blocking group of calcineurin B as myristic acid
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Metadata
- Authors
- Wilcox, C., Hu, J.-S., & Olson, E. N.
- Venue
- Science
- Published
- 1987-11-27
- Volume
- 238
- Issue
- 4831
- Pages
- 1275-1278
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2030202169
- Cited by
- 273
- References
- 14
- FWCI
- 7.53
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
