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

Potent and selective inhibition of pathogenic viruses by engineered ubiquitin variants

18 May 2017

Abstract excerpt

The recent Middle East respiratory syndrome coronavirus (MERS-CoV), Ebola and Zika virus outbreaks exemplify the continued threat of (re-)emerging viruses to human health, and our inability to rapidly develop effective therapeutic countermeasures. Many viruses, including MERS-CoV and the Crimean-Congo hemorrhagic fever virus (CCHFV) encode deubiquitinating (DUB) enzymes that are critical for viral replication and...

Read the complete abstract on PubMed

Topics

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

Share to interferon and immune responses
Share to Ubiquitin and proteasome pathways
Share to Viral Infections and Outbreaks Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 28542609
DOI: 10.1371/journal.ppat.1006372

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Potent and selective inhibition of pathogenic viruses by engineered ubiquitin variantsPMID 28542609Read ↗

Ubiquitin variants potently inhibit SARS-CoV-2 PLpro and viral replication via a novel site distal to the protease active siteSemantic proximity Read ↗

Crystal structure of the Middle East respiratory syndrome coronavirus (MERS-CoV) papain-like protease bound to ubiquitin facilitates targeted disruption of deubiquitinating activity to demonstrate its role in innate immune suppression.Semantic proximity Read ↗

The deubiquitinating activity of Middle East respiratory syndrome coronavirus papain-like protease delays the innate immune response and enhances virulence in a mouse modelSemantic proximity Read ↗

Ebola Virus VP35 Interacts Non-Covalently with Ubiquitin Chains to Promote Viral Replication Creating New Therapeutic OpportunitiesSemantic proximity Read ↗

The Role of the Host Ubiquitin System in Promoting Replication of Emergent VirusesSemantic proximity Read ↗

Ebola virus VP35 interacts non-covalently with ubiquitin chains to promote viral replicationSemantic proximity Read ↗

Crimean-Congo Hemorrhagic Fever Virus Suppresses Innate Immune Responses via a Ubiquitin and ISG15 Specific ProteaseSemantic proximity Read ↗

E3 Ubiquitin Ligases in Gammaherpesviruses and HIV: A Review of Virus Adaptation and ExploitationSemantic proximity Read ↗

The Role of Deubiquitinases in Virus Replication and Host Innate Immune ResponseSemantic proximity Read ↗

Probing the impact of nairovirus genomic diversity on viral ovarian tumor domain protease (vOTU) structure and deubiquitinase activitySemantic proximity Read ↗

Deubiquitinase function of arterivirus papain-like protease 2 suppresses the innate immune response in infected host cells.Semantic proximity Read ↗

Structurally Guided Removal of DeISGylase Biochemical Activity from Papain-Like Protease Originating from Middle East Respiratory Syndrome Coronavirus.Semantic proximity Read ↗

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