Ritzefeld, M, Wright, MH orcid.org/0000-0003-2731-4707 and Tate, EW (2018) New developments in probing and targeting protein acylation in malaria, leishmaniasis and African sleeping sickness. Parasitology, 145 (2). pp. 157-174. ISSN 0031-1820
Abstract
Infections by protozoan parasites, such as Plasmodium falciparum or Leishmania donovani, have a significant health, social and economic impact and threaten billions of people living in tropical and sub-tropical regions of developing countries worldwide. The increasing range of parasite strains resistant to frontline therapeutics makes the identification of novel drug targets and the development of corresponding inhibitors vital. Post-translational modifications (PTMs) are important modulators of biology and inhibition of protein lipidation has emerged as a promising therapeutic strategy for treatment of parasitic diseases. In this review we summarize the latest insights into protein lipidation in protozoan parasites. We discuss how recent chemical proteomic approaches have delivered the first global overviews of protein lipidation in these organisms, contributing to our understanding of the role of this PTM in critical metabolic and cellular functions. Additionally, we highlight the development of new small molecule inhibitors to target parasite acyl transferases.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © 2017, Cambridge University Press. This article has been published in a revised form in Parasitology https:// doi.org/10.1017/S0031182017000282. This version is free to view and download for private research and study only. Not for re-distribution, re-sale or use in derivative works. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | acyl transferase; palmitoylation; post-translational modification; protozoan parasites; protein lipidation; small molecule inhibitor; proteomics; NMT; N-myristoyl transferase |
Dates: |
|
Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) > Organic Chemistry (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 15 Mar 2017 16:04 |
Last Modified: | 19 Mar 2018 15:38 |
Status: | Published |
Publisher: | Cambridge University Press |
Identification Number: | 10.1017/S0031182017000282 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:113585 |