MX2 forms nucleoporin-comprising cytoplasmic biomolecular condensates that lure viral capsids
Authors:
Open Access
- 9 October 2024
- journal article
- research article
- Published by Elsevier in Cell Host & Microbe
- Vol. 32 (10) , 1705-1724.e14
Abstract
No abstract availableKeywords
Funding Information
- Fonds Wetenschappelijk Onderzoek (1S54021N)
- HORIZON EUROPE European Research Council
- Vlaams Instituut voor Biotechnologie
- University of Glasgow
- Universiteit Gent
- European Resuscitation Council (101098331 \u2014 GlycoCAR \u2014 ERC-2022-ADG)
- Deutsche Forschungsgemeinschaft (EXC2155 RESIST 390874280)
- Deutsche Forschungsgemeinschaft (443889136)
- Deutsche Forschungsgemeinschaft (G091522N)
This publication has 115 references indexed in Scilit:
- Formation, function, and pathology of RNP granulesCell, 2023
- Cone-shaped HIV-1 capsids are transported through intact nuclear poresCell, 2021
- GTPase Activity of MxB Contributes to Its Nuclear Location, Interaction with Nucleoporins and Anti-HIV-1 ActivityVirologica Sinica, 2020
- The GTPase Domain of MX2 Interacts with the HIV-1 Capsid, Enabling Its Short Isoform to Moderate Antiviral RestrictionCell Reports, 2019
- Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like DomainsCell, 2018
- FUS Phase Separation Is Modulated by a Molecular Chaperone and Methylation of Arginine Cation-π InteractionsCell, 2018
- Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple SitesCell, 2018
- Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine MethylationCell, 2018
- Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned ResponseCell, 2017
- BioID: A Screen for Protein‐Protein InteractionsCurrent Protocols in Protein Science, 2013