ITCH E3 ubiquitin ligase interacts with Ebola virus VP40 to regulate budding

• Main Authors: Han, Z, Sagum, C.A, Bedford, M.T, Sidhu, S.S, Sudol, M, Harty, R.N
• Other Authors: PHYSIOLOGY
• Format: Article
• Published: American Society for Microbiology 2020
• Subjects: protein VP40; ubiquitin protein ligase; ubiquitin protein ligase ITCH E3; ubiquitin protein ligase NEDD4; unclassified drug; core protein; ITCH protein, human; nucleoprotein; nucleoprotein VP40, Ebola virus; repressor protein; Article; controlled study; Ebolavirus; enzyme activation; enzyme activity; human; human cell; nonhuman; priority journal; protein binding; protein domain; protein expression; protein function; protein interaction; regulatory mechanism; virion; virus particle; virus release; animal; cell line; host pathogen interaction; metabolism; physiology; protein analysis; Animals; Cell Line; Host-Pathogen Interactions; Humans; Nucleoproteins; Protein Interaction Mapping; Repressor Proteins; Ubiquitin-Protein Ligases; Viral Core Proteins; Virus Release
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/175267
• Institution: National University of Singapore

10.1128/JVI.01078-16