About (click to open/close)
I am a postdoctoral fellow in the Biomedical Sciences Division at the King Abdullah University of Science and Technology (KAUST), where I use cryo-electron microscopy to study the helicase-primase complexes of human cytomegalovirus and Epstein-Barr virus. I completed my PhD in Bioscience at KAUST in 2025 under Prof. Alfredo De Biasio, with a thesis on the structural basis of bidirectional replication-fork initiation by the SV40 Large Tumour Antigen helicase. Before that, I earned an MSc in Biotechnology at the Warsaw University of Technology and the University of Warsaw in the laboratory of Prof Maria Górna, studying the interactions between the human FAST and eIF4E proteins, with an Erasmus exchange at the University of Groningen. My training began with a BSc in Biochemistry at Ahmadu Bello University, Zaria.
My research combines single-particle cryo-electron microscopy and molecular dynamics simulation to understand conformationally dynamic nucleoprotein assemblies, in particular, the machinery of DNA replication. My main scientific contribution to date concerns the structural dynamics of DNA unwinding by a replicative helicase, published in Nature in 2025, alongside studies of the human replisome and clamp-loading machinery that appeared in eLife and Nucleic Acids Research. I retain a strong interest in African parasitic diseases, dating from my work in Nigeria on multi-epitope vaccine design and on drug targeting in Trypanosomes and Plasmodium.
My research has been supported by competitive fellowships and awards, including the KAUST PhD Fellowship, a Polish-Fulbright BioLAB Studentship, an EMBL EIPOD INSPIRES mentorship, an Erasmus+ scholarship, and the Ignacy Lukasiewicz scholarship of the Polish National Agency for Academic Exchange. In 2025, I received the Best Research Award of the Division of Bioscience at KAUST for my work on DNA unwinding by a replicative helicase.
Selected publications (click to open/close)
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1.
Briola GR, Tehseen M, Al-Amodi A, Young G, Danazumi AU, Nguyen PQ, et al. Structure of the human CTF18-RFC clamp loader bound to PCNA. Elife. 2026 Feb 23;13:RP103493. Cite
1.
Shahid T, Danazumi AU, Tehseen M, Alhudhali L, Clark AR, Savva CG, et al. Structural dynamics of DNA unwinding by a replicative helicase. Nature. 2025 May;641(8061):240–9. Cite
1.
Balogun EO, Joseph GI, Olabode SC, Dayaso NA, Danazumi AU, Bashford-Rogers R, et al. Computational Workflow to Design Novel Vaccine Candidates and Small-Molecule Therapeutics for Schistosomiasis. Pathogens. 2024 Sept 30;13(10):850. Cite
1.
Ouyang Y, Al-Amodi A, Tehseen M, Alhudhali L, Shirbini A, Takahashi M, et al. Single-molecule characterization of SV40 replisome and novel factors: human FPC and Mcm10. Nucleic Acids Res. 2024 Aug 27;52(15):8880–96. Cite
1.
Danazumi AU, Ishmam IT, Idris S, Izert MA, Balogun EO, Górna MW. Targeted protein degradation might present a novel therapeutic approach in the fight against African trypanosomiasis. Eur J Pharm Sci. 2023 July 1;186:106451. Cite