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. 2021 Oct 15;10(10):1330. doi: 10.3390/pathogens10101330

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© 2021 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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A schematic representation of EBOV viral protein 24 (VP24). VP24 aa 169–173 facilitate interaction with NP, which is crucial for nucleocapsid (NC) formation, EBOV replication cycle and egress phase. Tyrosine-phosphorylated STAT1, hnRNP C1/C2 and VP24 interact with KPNA at the same position; therefore, upon VP24–KPNA interaction, transport of tyrosine-phosphorylated STAT1 to the nucleus is stopped as well as translocation of hnRNP C1/C2 from the cytoplasm to the nucleus is partially prevented.