Author

N. Drinkwater

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 3 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:plant (other)· 3 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Organism:mouse· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

S. McGowan· 4 shared T. R. Malcolm· 4 shared B. K. Hayes· 2 shared N. A. Borg· 2 shared S. C. Atkinson· 2 shared A. M. Buckle· 1 shared B. T. Riley· 1 shared C. D. Suraweera· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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4 shared papersBiochemistry

S. McGowan

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

On-target, dual aminopeptidase inhibition provides cross-species antimalarial activity.

R. C. Edgar, G. Siddiqui, T. R. Malcolm, S. Duffy, M. Chowdhury, J. Marfurt, G. Wirjanata, R. Noviyanti, K. Daware, M. Dans, C. D. Suraweera, N. A. Counihan, R. N. Price, S. Whittlin, V. M. Avery, , S. McGowan

This paper identifies MMV1557817 as a dual aminopeptidase inhibitor effective against multiple Plasmodium species and highlights its potential as a multi-target antimalarial drug.

bioRxiv · Oct 1, 2023Microbiology

Mapping the substrate sequence and length of the Plasmodium M1 and M17 aminopeptidases

T. R. Malcolm, K. W. Swiderska, B. K. Hayes, M. Drag, N. Drinkwater, S. McGowan

This study profiles the substrate specificity and kinetic behavior of M1 and M17 aminopeptidases from Plasmodium species, revealing differences in substrate preference and catalytic responses across species.

bioRxiv · Oct 13, 2020 · PreprintBiochemistry

Metal Dependent Dynamic Equilibrium: A Regulatory Mechanism for M17 Aminopeptidases from Plasmodium falciparum and Plasmodium vivax

T. R. Malcolm, M. J. Belousoff, H. Venugopal, N. A. Borg, N. Drinkwater, S. C. Atkinson, S. McGowan

This study identifies a metal-dependent dynamic equilibrium in M17 aminopeptidases from Plasmodium species that regulates hexamer formation and catalytic activity.

bioRxiv · Oct 8, 2020 · PreprintBiochemistry

A metal-dependent switch moderates activity of the hexameric M17 aminopeptidases.

N. Drinkwater, W. Yang, B. T. Riley, B. K. Hayes, K. Kannan Sivaraman, T. R. Malcolm, S. C. Atkinson, N. A. Borg, I. Kass, A. M. Buckle, S. McGowan

This study identifies a metal-dependent regulatory mechanism in PfA-M17 aminopeptidase, showing how oligomerization and metal center re-modelling control proteolytic activity.

bioRxiv · Feb 21, 2019 · PreprintBiochemistry