The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Protein Prenylation: Enzymes, Therapeutics, and Biotechnology Applications
Open accessAbstract
Protein prenylation is a ubiquitous covalent post-translational modification found in all eukaryotic cells, comprising attachment of either a farnesyl or a geranylgeranyl isoprenoid. It is essential for the proper cellular activity of numerous proteins, including Ras family GTPases and heterotrimeric G-proteins. Inhibition of prenylation has been extensively investigated to suppress the activity of oncogenic Ras proteins to achieve antitumor activity. Here, we review the biochemistry of the prenyltransferase enzymes and numerous isoprenoid analogs synthesized to investigate various aspects of prenylation and prenyltransferases. We also give an account of the current status of prenyltransferase inhibitors as potential therapeutics against several diseases including cancers, progeria, aging, parasitic diseases, and bacterial and viral infections. Finally, we discuss recent progress in utilizing protein prenylation for site-specific protein labeling for various biotechnology applications.
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Cites
Targeting protein prenylation for cancer therapy
Berndt, N., Hamilton, A. D., & Sebti, S. M. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3151 · Cited by 614
Trafficking and signaling by fatty-acylated and prenylated proteins
Resh, M. D. (2006) · Nature Chemical Biology · doi:10.1038/nchembio834 · Cited by 521
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Targeting Small GTPases and Their Prenylation in Diabetes Mellitus
Gendaszewska-Darmach, E., Garstka, M. A., & Błażewska, K. M. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00410 · Cited by 35
Metadata
- Authors
- Palsuledesai, C. C., & Distefano, M. D.
- Venue
- ACS Chemical Biology
- Publisher
- American Chemical Society (ACS)
- Published
- 2014-12-08
- Volume
- 10
- Issue
- 1
- Pages
- 51-62
- ISSN
- 1554-8929 (ISSN-L)
- 1554-8937
- OpenAlex
- W2324956847
- Cited by
- 259
- References
- 2
- FWCI
- 5.96
- Type
- journal article
- Language
- en
- Open access
- hybrid
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