Author

B. Vojtesek

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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Cancer Biology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 3 Assay:bulk RNA-seq· 1 Research Focus:cancer & tumor microenvironment· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1 Organism:E. coli· 1

Frequent Co-Authors

D. P. Lane· 2 shared S. Sedimbi· 2 shared A. Lerma Clavero· 1 shared A. Rising· 1 shared A. S. Ng· 1 shared C. Bosdotter· 1 shared C. Sahin· 1 shared D. Lama· 1 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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2 shared papersCancer Biology

D. P. Lane

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

MDM2 inhibitors, nutlin-3a and navtemadelin, retain efficacy in human and mouse cancer cells cultured in hypoxia

A. Lerma Clavero, P. Lafqvist Boqvist, K. Ingelshed, C. Bosdotter, S. Sedimbi, L. Jiang, F. Wermeling, B. Vojtesek, D. P. Lane, P. Kannan

This study shows that MDM2 inhibitors nutlin-3a and navtemadelin remain effective in hypoxic conditions in human and mouse cancer cells with wild-type p53, but not in mutant or null p53 cells.

bioRxiv · Oct 20, 2022Cancer Biology

SRSF1 as a novel interacting partner for IFITM1/3 unravels the emergent role of IFITM1/3 mediating protein expression

S. Kote, M. Gomez-Herranz, J. Faktor, M. Yebenes Mayordomo, M. Pilch, L. Hernychova, K. L. Ball, B. Vojtesek, T. Hupp

This study identifies SRSF1 as an interacting partner of IFITM1/3, revealing their role in regulating protein synthesis by interacting with HLA-B mRNA and affecting ribosomal function.

bioRxiv · Feb 2, 2022 · PreprintCancer Biology

A spindle and thread-mechanism unblocks translation of N-terminally disordered proteins

M. Kaldmae, T. Vosselman, X. Zhong, D. Lama, G. Chen, M. Saluri, N. Kronqvist, J. W. Siau, A. S. Ng, F. J. Ghadessy, P. Sabatier, B. Vojtesek, M. Sarr, C. Sahin, N. Osterlund, , M. Landreh

This study shows that fusing disordered proteins to an engineered spider silk domain improves their translation efficiency and activity in cells.

bioRxiv · Feb 22, 2021 · PreprintBiochemistry