Author

E. Deu

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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Microbiology· 2 Biochemistry· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:plant (other)· 3 Research Focus:host-pathogen & immune response· 2 Research Focus:cell type annotation· 1 Research Focus:clustering· 1 Research Focus:drug response / drug discovery· 1 Assay:flow cytometry· 1 Assay:fluorescence / live-cell microscopy· 1

Frequent Co-Authors

C. Lehmann· 3 shared A. P. Patel· 2 shared L. E. de Vries· 2 shared M. I. Sanchez· 2 shared S. Ridewood· 2 shared A. Snijder· 1 shared A. Weston· 1 shared B. Dirac-Svejstrup· 1 shared

Activity by Year

2017-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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3 shared papersCell Biology

C. Lehmann

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

The Aspartyl Protease Ddi1 Is Essential for Erythrocyte Invasion by the Malaria Parasite

S. Ridewood, B. Dirac-Svejstrup, S. A. Howell, A. Weston, C. Lehmann, A. P. Patel, L. Collinson, R. Bingham, D. Powell, A. Snijder, J. Q. Svejstrup, E. Deu

This study shows that PfDdi1 proteolytic activity is essential for Plasmodium falciparum erythrocyte invasion and identifies it as a potential antimalarial target.

bioRxiv · May 11, 2021 · PreprintCell Biology

High Content and High Throughout Phenotypic Assay for the Hourly Resolution of the Malaria Parasite Erythrocytic Cycle

D. Bell, S. Ridewood, A. P. Patel, S. H. Lee, Y.-T. Chang, E. Deu

This paper introduces a high-content, high-throughput phenotypic assay for studying the erythrocytic cycle of malaria parasites with hourly resolution.

bioRxiv · Mar 15, 2021 · PreprintMicrobiology

Characterization of P. falciparum dipeptidyl aminopeptidase 3 specificity reveals structural factors responsible for differences in amino acid preferences between peptide-based substrates and covalent inhibitors.

L. E. de Vries, M. I. Sanchez, K. Groborz, L. Kuppens, M. Poreba, C. Lehmann, F. Yuan, S. Arastu-Kapur, M. Horn, M. Mares, M. Bogyo, M. Drag, E. Deu

The paper characterizes P. falciparum DPAP3 specificity and identifies structural factors causing differences in amino acid preferences between peptide substrates and covalent inhibitors.

bioRxiv · Aug 10, 2018 · PreprintBiochemistry

Plasmodium falciparum dipeptidyl aminopeptidase 3 activity is important for efficient erythrocyte invasion by the malaria parasite

C. Lehmann, M. S. Y. Tan, L. E. de Vries, I. Russo, M. I. Sanchez, D. E. Goldberg, E. Deu

This study shows that DPAP3 protease activity is crucial for Plasmodium falciparum erythrocyte invasion but not egress.

bioRxiv · Nov 8, 2017Microbiology