Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/164792
Title: Structural insights into Plasmodium PPIases
Authors: Rajan, Sreekanth
Yoon, Ho Sup
Keywords: Science::Biological sciences
Issue Date: 2022
Source: Rajan, S. & Yoon, H. S. (2022). Structural insights into Plasmodium PPIases. Frontiers in Cellular and Infection Microbiology, 12, 931635-. https://dx.doi.org/10.3389/fcimb.2022.931635
Journal: Frontiers in Cellular and Infection Microbiology
Abstract: Malaria is one of the most prevalent infectious diseases posing a serious challenge over the years, mainly owing to the emergence of drug-resistant strains, sparking a need to explore and identify novel protein targets. It is a well-known practice to adopt a chemo-genomics approach towards identifying targets for known drugs, which can unravel a novel mechanism of action to aid in better drug targeting proficiency. Immunosuppressive drugs cyclosporin A, FK506 and rapamycin, were demonstrated to inhibit the growth of the malarial parasite, Plasmodium falciparum. Peptidyl prolyl cis/trans isomerases (PPIases), comprising cylcophilins and FK506-binding proteins (FKBPs), the specific target of these drugs, were identified in the Plasmodium parasite and proposed as an antimalarial drug target. We previously attempted to decipher the structure of these proteins and target them with non-immunosuppressive drugs, predominantly on FKBP35. This review summarizes the structural insights on Plasmodium PPIases, their inhibitor complexes and perspectives on drug discovery.
URI: https://hdl.handle.net/10356/164792
ISSN: 2235-2988
DOI: 10.3389/fcimb.2022.931635
Schools: School of Biological Sciences 
Rights: © 2022 Rajan and Yoon. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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