Tess R Malcolm
Overview
Explore the profile of Tess R Malcolm including associated specialties, affiliations and a list of published articles.
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Articles
14
Citations
102
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0
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Recent Articles
11.
Malcolm T, Swiderska K, Hayes B, Webb C, Drag M, Drinkwater N, et al.
Biochem J
. 2021 Jun;
478(13):2697-2713.
PMID: 34133730
During malarial infection, Plasmodium parasites digest human hemoglobin to obtain free amino acids for protein production and maintenance of osmotic pressure. The Plasmodium M1 and M17 aminopeptidases are both postulated...
12.
Malcolm T, Belousoff M, Venugopal H, Borg N, Drinkwater N, Atkinson S, et al.
J Biol Chem
. 2020 Dec;
296:100173.
PMID: 33303633
M17 leucyl aminopeptidases are metal-dependent exopeptidases that rely on oligomerization to diversify their functional roles. The M17 aminopeptidases from Plasmodium falciparum (PfA-M17) and Plasmodium vivax (Pv-M17) function as catalytically active...
13.
Drinkwater N, Malcolm T, McGowan S
Biochimie
. 2019 Jan;
166:38-51.
PMID: 30654132
The family of M17 aminopeptidases (alias 'leucine aminopeptidases', M17-LAPs) utilize a highly conserved hexameric structure and a binuclear metal center to selectively remove N-terminal amino acids from short peptides. However,...
14.
Hydroxamic Acid Inhibitors Provide Cross-Species Inhibition of Plasmodium M1 and M17 Aminopeptidases
Vinh N, Drinkwater N, Malcolm T, Kassiou M, Lucantoni L, Grin P, et al.
J Med Chem
. 2018 Dec;
62(2):622-640.
PMID: 30537832
There is an urgent clinical need for antimalarial compounds that target malaria caused by both Plasmodium falciparum and Plasmodium vivax. The M1 and M17 metalloexopeptidases play key roles in Plasmodium...
15.
Drinkwater N, Lee J, Yang W, Malcolm T, McGowan S
FEBS J
. 2017 Jan;
284(10):1473-1488.
PMID: 28075056
M1 aminopeptidase enzymes are a diverse family of metalloenzymes characterized by conserved structure and reaction specificity. Excluding viruses, M1 aminopeptidases are distributed throughout all phyla, and have been implicated in...