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From disorder to order: cryo-EM reveals RNA-dependent remodeling of Nipah virus polymerase
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).
2025 (English)In: Trends in Biochemical Sciences (TIBS), ISSN 0968-0004, E-ISSN 1362-4326, Vol. 50, no 8, p. 639-641Article in journal, Editorial material (Refereed) Published
Abstract [en]

A flurry of recent structural studies have focused on the polymerase complex of the deadly zoonotic pathogen Nipah virus (NiV). These include a report by Sala et al. describing an RNA duplex-bound state. This structure constitutes a snapshot of the complex in an early elongation step of the RNA synthesis cycle.

Place, publisher, year, edition, pages
Elsevier, 2025. Vol. 50, no 8, p. 639-641
Keywords [en]
cryo-EM, L-P, Nipah virus, nsNSV, RdRP, viral polymerase, viral replication
National Category
Biochemistry Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-239814DOI: 10.1016/j.tibs.2025.05.003PubMedID: 40450410Scopus ID: 2-s2.0-105006948362OAI: oai:DiVA.org:umu-239814DiVA, id: diva2:1974861
Available from: 2025-06-23 Created: 2025-06-23 Last updated: 2025-09-24Bibliographically approved

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Jayachandran, Rupesh BalajiRenner, Max

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