Author

E. Pietsch

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· 4 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell type annotation· 3 Organism:human· 3 Research Focus:host-pathogen & immune response· 2 Assay:proteomics· 2 Assay:cryo-EM· 1 Approach:microscopy & imaging analysis· 1 Organism:mouse· 1

Frequent Co-Authors

P.-C. Burda· 3 shared T.-W. Gilberger· 3 shared A. Ramaprasad· 2 shared F. Frischknecht· 2 shared M. J. Blackman· 2 shared A. P. Snijders· 1 shared A. Sait· 1 shared C. Söhnchen· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 26 mutual co-author links

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3 shared papersMicrobiology

P.-C. Burda

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Disruption of a Plasmodium falciparum patatin-like phospholipase delays male gametocyte exflagellation

E. Pietsch, K. Niedermueller, T.-W. Gilberger, P.-C. Burda

This study identifies a patatin-like phospholipase in Plasmodium falciparum that delays male gametocyte exflagellation when disrupted, suggesting a non-essential but important role in gametogenesis.

bioRxiv · Apr 28, 2023 · PreprintMicrobiology

A malaria parasite phospholipase facilitates efficient asexual blood stage egress

A. Ramaprasad, P.-C. Burda, K. Koussis, J. A. Thomas, E. Pietsch, E. Calvani, S. A. Howell, J. I. MacRae, A. P. Snijders, T. W. Gilberger, M. J. Blackman

This study identifies LCAT as a key enzyme required for efficient egress of malaria parasites from red blood cells during the asexual blood stage.

bioRxiv · Mar 13, 2023Microbiology

Form follows function: Variable microtubule architecture in the malaria parasite

J. L. Ferreira, V. Prazak, D. Vasishtan, M. Siggel, F. Hentzschel, E. Pietsch, J. Kosinski, F. Frischknecht, T.-W. Gilberger, K. Grünewald

The paper uses electron cryo-tomography to study microtubule architecture in malaria parasites across their life cycle, revealing structural diversity not seen in other organisms.

bioRxiv · Apr 13, 2022Microbiology

Global analysis of putative phospholipases in the malaria parasite Plasmodium falciparum reveals critical factors for parasite proliferation

P.-C. Burda, A. Ramaprasad, E. Pietsch, S. Bielfeld, C. Söhnchen, L. Wilcke, J. Strauss, D. Schwudke, A. Sait, L. M. Collinson, M. J. Blackman, T.-W. Gilberger

The paper identifies essential phospholipases in Plasmodium falciparum, showing PF3D7_1013500 is critical for parasite maturation and PF3D7_1358000 is vital for mitochondrial function and growth.

bioRxiv · Jun 28, 2021 · PreprintMicrobiology

APEX-based proximity labeling in Plasmodium identifies a membrane protein with dual functions during mosquito infection

J. Kehrer, D. Ricken, L. Strauss, E. Pietsch, J. M. Heinze, F. Frischknecht

The paper uses APEX2-mediated proximity labeling to identify novel proteins in Plasmodium ookinetes, uncovering a membrane protein with dual roles in gamete egress and ookinete migration.

bioRxiv · Sep 29, 2020 · PreprintCell Biology