Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Ubiquitin Ligase WWP1 Interacts with Ebola Virus VP40 To Regulate Egress

3 Aug 2017

Abstract excerpt

ABSTRACT Ebola virus (EBOV) is a member of the Filoviridae family and the cause of hemorrhagic fever outbreaks. The EBOV VP40 (eVP40) matrix protein is the main driving force for virion assembly and budding. Indeed, expression of eVP40 alone in mammalian cells results in the formation and budding of virus-like particles (VLPs) which mimic the budding process and morphology of authentic, infectious EBOV. To...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Hepatitis B Virus Studies
Share to Viral Infections and Outbreaks Research
Share to Viral Infections and Vectors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 28768865
DOI: 10.1128/jvi.00812-17

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Ubiquitin Ligase WWP1 Interacts with Ebola Virus VP40 To Regulate EgressPMID 28768865Read ↗

ITCH E3 Ubiquitin Ligase Interacts with Ebola Virus VP40 To Regulate BuddingSemantic proximity Read ↗

Regulation of Ebola virus VP40 matrix protein by SUMO.Semantic proximity Read ↗

Chaperone-Mediated Autophagy Protein BAG3 Negatively Regulates Ebola and Marburg VP40-Mediated EgressSemantic proximity Read ↗

ALIX Rescues Budding of a Double PTAP/PPEY L-Domain Deletion Mutant of Ebola VP40: A Role for ALIX in Ebola Virus EgressSemantic proximity Read ↗

Host and Viral Proteins Modulating Ebola and Marburg Virus EgressSemantic proximity Read ↗

Nedd4 Regulates Egress of Ebola Virus-Like Particles from Host CellsSemantic proximity Read ↗

Regulation of Marburg virus (MARV) budding by Nedd4.1: a different WW domain of Nedd4.1 is critical for binding to MARV and Ebola virus VP40Semantic proximity Read ↗

The Host E3-Ubiquitin Ligase TRIM6 Ubiquitinates the Ebola Virus VP35 Protein and Promotes Virus ReplicationSemantic proximity Read ↗

Overlapping Motifs (PTAP and PPEY) within the Ebola Virus VP40 Protein Function Independently as Late Budding Domains: Involvement of Host Proteins TSG101 and VPS-4Semantic proximity Read ↗

Cullin E3 Ligases and Their Rewiring by Viral FactorsSemantic proximity Read ↗

Functional Replacement of a Retroviral Late Domain by Ubiquitin FusionSemantic proximity Read ↗

Conserved Motifs within Ebola and Marburg Virus VP40 Proteins Are Important for Stability, Localization, and Subsequent Budding of Virus-Like ParticlesSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.