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

10.1128/JVI.01078-16

Saved in:

Bibliographic Details
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
Tags:	Add Tag No Tags, Be the first to tag this record!
Institution:	National University of Singapore

id	sg-nus-scholar.10635-175267
record_format	dspace
spelling	sg-nus-scholar.10635-1752672024-04-04T01:09:47Z ITCH E3 ubiquitin ligase interacts with Ebola virus VP40 to regulate budding Han, Z Sagum, C.A Bedford, M.T Sidhu, S.S Sudol, M Harty, R.N PHYSIOLOGY 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 ubiquitin protein ligase 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 Ebolavirus host pathogen interaction metabolism physiology protein analysis Animals Cell Line Ebolavirus Host-Pathogen Interactions Humans Nucleoproteins Protein Interaction Mapping Repressor Proteins Ubiquitin-Protein Ligases Viral Core Proteins Virus Release 10.1128/JVI.01078-16 Journal of Virology 90 20 9163-9171 2020-09-09T06:42:19Z 2020-09-09T06:42:19Z 2016 Article Han, Z, Sagum, C.A, Bedford, M.T, Sidhu, S.S, Sudol, M, Harty, R.N (2016). ITCH E3 ubiquitin ligase interacts with Ebola virus VP40 to regulate budding. Journal of Virology 90 (20) : 9163-9171. ScholarBank@NUS Repository. https://doi.org/10.1128/JVI.01078-16 0022-538X https://scholarbank.nus.edu.sg/handle/10635/175267 American Society for Microbiology Unpaywall 20200831
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	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 ubiquitin protein ligase 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 Ebolavirus host pathogen interaction metabolism physiology protein analysis Animals Cell Line Ebolavirus Host-Pathogen Interactions Humans Nucleoproteins Protein Interaction Mapping Repressor Proteins Ubiquitin-Protein Ligases Viral Core Proteins Virus Release
spellingShingle	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 ubiquitin protein ligase 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 Ebolavirus host pathogen interaction metabolism physiology protein analysis Animals Cell Line Ebolavirus Host-Pathogen Interactions Humans Nucleoproteins Protein Interaction Mapping Repressor Proteins Ubiquitin-Protein Ligases Viral Core Proteins Virus Release Han, Z Sagum, C.A Bedford, M.T Sidhu, S.S Sudol, M Harty, R.N ITCH E3 ubiquitin ligase interacts with Ebola virus VP40 to regulate budding
description	10.1128/JVI.01078-16
author2	PHYSIOLOGY
author_facet	PHYSIOLOGY Han, Z Sagum, C.A Bedford, M.T Sidhu, S.S Sudol, M Harty, R.N
format	Article
author	Han, Z Sagum, C.A Bedford, M.T Sidhu, S.S Sudol, M Harty, R.N
author_sort	Han, Z
title	ITCH E3 ubiquitin ligase interacts with Ebola virus VP40 to regulate budding
title_short	ITCH E3 ubiquitin ligase interacts with Ebola virus VP40 to regulate budding
title_full	ITCH E3 ubiquitin ligase interacts with Ebola virus VP40 to regulate budding
title_fullStr	ITCH E3 ubiquitin ligase interacts with Ebola virus VP40 to regulate budding
title_full_unstemmed	ITCH E3 ubiquitin ligase interacts with Ebola virus VP40 to regulate budding
title_sort	itch e3 ubiquitin ligase interacts with ebola virus vp40 to regulate budding
publisher	American Society for Microbiology
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/175267
_version_	1795374374057934848

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

Similar Items