Author

A. S. Nasamu

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· 3

Signature Assays, Organisms & Methods

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Organism:plant (other)· 3 Approach:experimental assay· 2 Research Focus:cell signaling & trafficking· 1 Assay:DNA methylation· 1 Research Focus:drug response / drug discovery· 1 Research Focus:gene regulatory network inference· 1 Approach:genetic perturbation / CRISPR· 1 Research Focus:genome assembly· 1

Frequent Co-Authors

A. Falla· 1 shared A. J. Polino· 1 shared B. A. Wall· 1 shared C. F. A. Pasaje· 1 shared D. E. Goldberg· 1 shared D. Goldberg· 1 shared J. C. Niles· 1 shared J. C. Wagner· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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1 shared paperMicrobiology

A. Falla

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Activation of the Plasmodium egress effector subtilisin-like protease 1 is achieved by plasmepsin X destruction of the propiece.

S. Mukherjee, A. S. Nasamu, K. Rubiano, D. Goldberg

This paper identifies that plasmepsin X (PM X) activates Plasmodium subtilisin-like protease 1 (SUB1) by cleaving its inhibitory propiece, enabling SUB1 to function without requiring conversion to its p47 form.

bioRxiv · Jan 13, 2023 · PreprintMicrobiology

An integrated platform for genome engineering and gene expression perturbation in Plasmodium falciparum

A. S. Nasamu, A. Falla, C. F. A. Pasaje, B. A. Wall, J. C. Wagner, S. M. Ganesan, S. J. Goldfless, J. C. Niles

This paper develops a DNA assembly framework to overcome challenges in genome engineering for Plasmodium falciparum by using linear plasmids for high AT-content DNA constructs.

bioRxiv · Oct 24, 2019Microbiology

Assessment of biological role and insight into druggability of the Plasmodium falciparum protease plasmepsin V

D. E. Goldberg, J. Niles, A. J. Polino, A. S. Nasamu

This paper validates plasmepsin V as an essential malaria parasite protein by showing its depletion arrests parasite growth and reveals an unexpected role in early development.

bioRxiv · Sep 26, 2018Microbiology