ITCH E3 Ubiquitin Ligase Interacts with Ebola Virus VP40 To Regulate Budding. - Wikidata - awgldk - TriplyDB

ITCH E3 Ubiquitin Ligase Interacts with Ebola Virus VP40 To Regulate Budding.

ITCH E3 Ubiquitin Ligase Interacts with Ebola Virus VP40 To Regulate Budding.

http://www.wikidata.org/entity/Q37300449

about

Chaperone-Mediated Autophagy Protein BAG3 Negatively Regulates Ebola and Marburg VP40-Mediated Egress.Regulation of Ebola virus VP40 matrix protein by SUMO.Ubiquitin Ligase WWP1 Interacts with Ebola Virus VP40 to Regulate Egress.Forty Years of Ebolavirus Molecular Biology: Understanding a Novel Disease Agent Through the Development and Application of New Technologies.Host Factors Involved in Ebola Virus Replication.

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ITCH E3 Ubiquitin Ligase Interacts with Ebola Virus VP40 To Regulate Budding.

http://www.wikidata.org/entity/Q37300449

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 03 August 2016

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

ITCH E3 Ubiquitin Ligase Interacts with Ebola Virus VP40 To Regulate Budding.

@en

ITCH E3 Ubiquitin Ligase Interacts with Ebola Virus VP40 To Regulate Budding.

@nl

type

label

ITCH E3 Ubiquitin Ligase Interacts with Ebola Virus VP40 To Regulate Budding.

@en

ITCH E3 Ubiquitin Ligase Interacts with Ebola Virus VP40 To Regulate Budding.

@nl

prefLabel

ITCH E3 Ubiquitin Ligase Interacts with Ebola Virus VP40 To Regulate Budding.

@en

ITCH E3 Ubiquitin Ligase Interacts with Ebola Virus VP40 To Regulate Budding.

@nl

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Journal of Virology

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ITCH E3 Ubiquitin Ligase Interacts with Ebola Virus VP40 To Regulate Budding.

@en

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Cari A Sagum

http://www.w3.org/2001/XMLSchema#string

Marius Sudol

http://www.w3.org/2001/XMLSchema#string

Mark T Bedford

http://www.w3.org/2001/XMLSchema#string

Ronald N Harty

http://www.w3.org/2001/XMLSchema#string

Sachdev S Sidhu

http://www.w3.org/2001/XMLSchema#string

Ziying Han

http://www.w3.org/2001/XMLSchema#string

P2860

ISG15 inhibits Ebola VP40 VLP budding in an L-domain-dependent manner by blocking Nedd4 ligase activity

The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules

Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding

Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: involvement of host proteins TSG101 and VPS-4.

Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cells

The ESCRT-associated protein Alix recruits the ubiquitin ligase Nedd4-1 to facilitate HIV-1 release through the LYPXnL L domain motif

ISG15 inhibits Nedd4 ubiquitin E3 activity and enhances the innate antiviral response

A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: implications for filovirus budding

Characterization of a novel protein-binding module--the WW domain

The WW domain: a signalling site in dystrophin?

P304

9163-9171

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scholarly article

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10.1128/JVI.01078-16

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20

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90

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2016-08-03T00:00:00Z

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27489272

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5044852

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