Aminopeptidases of malaria parasites: New targets for chemotherapy.
- Bentham Science Publishers Ltd
- Publication Type:
- Journal Article
- Infectious Disorders Drug Targets, 2010, 10 (3), pp. 217 - 225
- Issue Date:
|dc.identifier.citation||Infectious Disorders Drug Targets, 2010, 10 (3), pp. 217 - 225||en_US|
|dc.description.abstract||Novel targets for new drug development are urgently required to combat malaria, a disease that puts half of the world's population at risk. One group of enzymes identified within the genome of the most lethal of the causative agents of malaria, Plasmodium falciparum, that may have the potential to become new targets for antimalarial drug development are the aminopeptidases. These enzymes catalyse the cleavage of the N-terminal amino acids from proteins and peptides. P. falciparum appears to encode for at least nine aminopeptidases, two neutral aminopeptidases, one aspartyl aminopeptidase, one aminopeptidase P, one prolyl aminopeptidase and four methionine aminopeptidases. Recent advances in our understanding of these genes and their protein products are outlined in this review, including their potential for antimalarial drug development||en_US|
|dc.publisher||Bentham Science Publishers Ltd||en_US|
|dc.relation.ispartof||Infectious Disorders Drug Targets||en_US|
|dc.title||Aminopeptidases of malaria parasites: New targets for chemotherapy.||en_US|
|pubs.organisational-group||/University of Technology Sydney|
|pubs.organisational-group||/University of Technology Sydney/Faculty of Science|
|pubs.organisational-group||/University of Technology Sydney/Faculty of Science/School of Life Sciences|
OPUS (Open Publications of UTS Scholars) is the UTS institutional repository. It showcases the research of UTS staff and postgraduate students to a global audience. For you, as a researcher, OPUS increases the visibility and accessibility of your research by making it openly available regardless of where you choose to publish.
Items in OPUS are enhanced with high quality metadata and seeded to search engines such as Google Scholar as well as being linked to your UTS research profile, increasing discoverability and opportunities for citation of your work and collaboration. In addition, works in OPUS are preserved for long-term access and discovery.
The UTS Open Access Policy requires UTS research outputs to be openly available via OPUS. Depositing your work in OPUS also assists you in complying with ARC, NHMRC and other funder Open Access policies. Providing Open Access to your research outputs through OPUS not only ensures you comply with these important policies, but increases opportunities for other researchers to cite and build upon your work.
OPUS archives UTS research submitted for Higher Education Research Data Collection (HERDC) and Excellence in Research for Australia (ERA). It also stores digital theses and forms of scholarship that do not usually see formal publication.
When you claim (or enter) your research in Symplectic Elements, simply upload a copy of your work which can be made openly available. Symplectic provides information on which version of your work to upload. If you are unsure, please supply a copy of the Accepted Manuscript version. Ensure you check the box to "agree to the OPUS license terms".
Once uploaded, your works are automatically sent to OPUS and placed temporarily in Closed Access until reviewed by UTS Library staff.
Once items are cleared of copyright constraints and/or publisher embargoes, your work is moved to Open Access and made accessible to the public.
Instructions are available from the Symplectic User Guide or contact firstname.lastname@example.org for further information.