Manickam Yogavel
Overview
Explore the profile of Manickam Yogavel including associated specialties, affiliations and a list of published articles.
Author names and details appear as published. Due to indexing inconsistencies, multiple individuals may share a name, and a single author may have variations. MedLuna displays this data as publicly available, without modification or verification
Snapshot
Snapshot
Articles
40
Citations
692
Followers
0
Related Specialties
Related Specialties
Top 10 Co-Authors
Top 10 Co-Authors
Published In
Published In
Affiliations
Affiliations
Soon will be listed here.
Recent Articles
1.
Mishra S, Malhotra N, Laleu B, Chakraborti S, Yogavel M, Sharma A
iScience
. 2024 Aug;
27(7):110049.
PMID: 39104570
The prolyl-tRNA synthetase (PRS) is an essential enzyme for protein translation and a validated target against malaria parasite. We describe five ATP mimetics (L95, L96, L97, L35, and L36) against...
2.
Yogavel M, Bougdour A, Mishra S, Malhotra N, Chhibber-Goel J, Bellini V, et al.
PLoS Pathog
. 2023 Feb;
19(2):e1011124.
PMID: 36854028
The prolyl-tRNA synthetase (PRS) is a validated drug target for febrifugine and its synthetic analog halofuginone (HFG) against multiple apicomplexan parasites including Plasmodium falciparum and Toxoplasma gondii. Here, a novel...
3.
Sharma V, Chhibber-Goel J, Yogavel M, Sharma A
Mol Biochem Parasitol
. 2022 Nov;
253:111530.
PMID: 36370911
Aminoacyl-tRNA synthetases (aaRSs) are essential enzymes in protein translation machinery that provide the charged tRNAs needed for protein synthesis. Over the past decades, aaRSs have been studied as anti-parasitic, anti-bacterial,...
4.
Sharma V, Gupta S, Chhibber-Goel J, Yogavel M, Sharma A
Mol Biochem Parasitol
. 2022 Jun;
250:111488.
PMID: 35644266
The specificity of each aminoacyl-tRNA synthetase (aaRS) for its cognate amino acid ensures correct tRNA esterification and allows fidelity in protein synthesis. The aaRSs discriminate based on the chemical properties...
5.
Chhibber-Goel J, Yogavel M, Sharma A
Protein Sci
. 2021 Jun;
30(9):1793-1803.
PMID: 34184352
Malaria is a parasitic illness caused by the genus Plasmodium from the apicomplexan phylum. Five plasmodial species of P. falciparum (Pf), P. knowlesi, P. malariae, P. ovale, and P. vivax...
6.
Structural basis of malaria parasite phenylalanine tRNA-synthetase inhibition by bicyclic azetidines
Sharma M, Malhotra N, Yogavel M, Harlos K, Melillo B, Comer E, et al.
Nat Commun
. 2021 Jan;
12(1):343.
PMID: 33436639
The inhibition of Plasmodium cytosolic phenylalanine tRNA-synthetase (cFRS) by a novel series of bicyclic azetidines has shown the potential to prevent malaria transmission, provide prophylaxis, and offer single-dose cure in...
7.
Gupta S, Chhibber-Goel J, Sharma M, Parvez S, Harlos K, Sharma A, et al.
Acta Crystallogr D Struct Biol
. 2020 Feb;
76(Pt 2):135-146.
PMID: 32038044
Scaffold modules known as aminoacyl-tRNA synthetase (aaRS)-interacting multifunctional proteins (AIMPs), such as AIMP1/p43, AIMP2/p38 and AIMP3/p18, are important in driving the assembly of multi-aaRS (MARS) complexes in eukaryotes. Often, AIMPs...
8.
Mishra S, Malhotra N, Kumari S, Sato M, Kikuchi H, Yogavel M, et al.
Acta Crystallogr F Struct Biol Commun
. 2019 Nov;
75(Pt 11):714-724.
PMID: 31702585
Prolyl-tRNA synthetase (PRS) is a member of the aminoacyl-tRNA synthetase family that drives protein translation in cells. The apicomplexan PRSs are validated targets of febrifugine (FF) and its halogenated derivative...
9.
Baragana B, Forte B, Choi R, Hewitt S, Bueren-Calabuig J, Pisco J, et al.
Proc Natl Acad Sci U S A
. 2019 Mar;
116(14):7015-7020.
PMID: 30894487
Malaria and cryptosporidiosis, caused by apicomplexan parasites, remain major drivers of global child mortality. New drugs for the treatment of malaria and cryptosporidiosis, in particular, are of high priority; however,...
10.
Nachiappan M, Jain V, Sharma A, Yogavel M, Jeyakanthan J
Int J Biol Macromol
. 2018 Sep;
120(Pt B):1379-1386.
PMID: 30248426
Aminoacyl-tRNA synthetases (AaRSs) are vital enzymes for translation of proteins in cells. AaRSs catalyse the esterification of a specific amino acid to corresponding tRNAs to form an aminoacyl-tRNA that is...