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Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.
8 papers
Recent·Most cited
B. Kucukoglu, I. Mohammed, R. C. Guerrero-Ferreira, M. Kube, J. Radecke, S. Ribet, G. Varnavides, M. L. Leidl, K. Lau, S. Nazarov, A. Myasnikov, C. Sachse, K. Mueller-Caspary, C. Ophus, H. Stahlberg
This paper applies low-dose cryo-EM and 4D-STEM ptychography to achieve sub-nanometer resolution 3D reconstructions of frozen hydrated proteins.
bioRxiv · Feb 12, 2024Biophysics
T. Ni, Q. Jiang, P. C. Ng, J. Shen, H. Dou, Y. Zhu, J. Radecke, G. F. Dykes, F. Huang, L.-N. Liu, P. Zhang
The paper investigates the role of intrinsically disordered CsoS2 in α-carboxysome shell assembly using synthetic engineering and cryoEM structures, revealing its function as a molecular thread and identifying a conserved interaction motif.
bioRxiv · Jun 24, 2023Microbiology
P. Zhang, S. Gilbert, J. Radecke, T. Ni, L. Mendonca, Y. Zhu, A. Howe, P. M. Shah, Y. Sheng, A.-S. Krebs, H. M. E. Duyvesteyn, E. Allen, T. Lambe, C. Bissett, S. Morris, , D. I. Stuart
This study determines the native structure of ChAdOx1-vectored SARS-CoV-2 vaccines on cell surfaces, showing prefusion spikes in one-RBD-up conformation and improved RBD exposure in HexaPro-stabilized variants.
bioRxiv · May 22, 2023Microbiology
I. Bregy, R. B. Eberle, J. Radecke, A. Khosrozadeh, J. Llodra, A. Noga, H. van den Hoek, M. Kern, B. Haenni, B. D. Engel, P. Stettler, A. Schneider, C. A. Siebert, T. Ishikawa, B. Zuber, T. Ochsenreiter
This study uses cryo-electron tomography to analyze the tripartite attachment complex in Trypanosoma brucei, revealing the structural dynamics of the complex during kDNA segregation.
bioRxiv · Mar 6, 2023 · PreprintCell Biology
L. Mendonca, A. Howe, J. B. Gilchrist, D. Sun, M. Knight, L. C. Zanetti-Domingues, B. Bateman, A.-S. Krebs, L. Chen, J. Radecke, Y. Sheng, V. D. Li, T. Ni, I. Kounatidis, M. A. Koronfel, , P. Zhang
This study uses cryo-imaging to reveal SARS-CoV-2 replication, assembly, and egress pathways in infected cells.
bioRxiv · Nov 5, 2020 · PreprintMicrobiology
J. Huo, Y. Zhao, J. Ren, D. Zhou, H. M. E. Duyvesteyn, H. M. Ginn, L. Carrique, T. Malinauskas, R. R. Ruza, P. N. Shah, T. K. Tan, P. Rijal, N. Coombes, K. Bewley, J. Radecke, , D. I. Stuart
This paper identifies CR3022 as a monoclonal antibody that neutralizes SARS-CoV-2 by destroying its prefusion Spike conformation, suggesting therapeutic potential.
Cell Host & Microbe · Sep 1, 2020Peer-reviewedMicrobiology
L. Carrique, H. M. E. Duyvesteyn, T. Malinaukas, Y. Zhao, J. Ren, D. Zhou, T. S. Walter, J. Radecke, J. Huo, R. Ruza, P. N. Shah, E. E. Fry, D. I. Stuart
The paper identifies a lipid-binding pocket in the SARS-CoV-2 Spike that stabilizes the prefusion trimer and shields neutralizing epitopes, suggesting it as a potential drug target.
bioRxiv · Aug 13, 2020 · PreprintMicrobiology
D. Zhou, H. M. E. Duyvesteyn, C.-P. Chen, C.-G. Huang, T.-H. Chen, S.-R. Shih, Y.-C. Lin, C.-Y. Cheng, S.-H. Cheng, Y.-C. Huang, T.-Y. Lin, C. Ma, J. Huo, L. Carrique, T. Malinauskas, , K.-Y. A. Huang
This paper identifies an antibody, EY6A, from a convalescent patient that neutralizes SARS-CoV-2 and cross-reacts with SARS-CoV-1 by binding a conserved epitope on the Spike protein.
bioRxiv · Jun 12, 2020Microbiology