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

Disruption of Stress Granule Formation by the Multifunctional Cricket Paralysis Virus 1A Protein

22 Dec 2016

Abstract excerpt

ABSTRACT Stress granules (SGs) are cytosolic ribonucleoprotein aggregates that are induced during cellular stress. Several viruses modulate SG formation, suggesting that SGs have an impact on virus infection. However, the mechanisms and impact of modulating SG assembly in infected cells are not completely understood. In this study, we identify the dicistrovirus cricket paralysis virus 1A (CrPV-1A) protein that...

Read the complete abstract on PubMed

Topics

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

Share to Plant Virus Research Studies
Share to Viral Infections and Immunology Research
Share to Viral Infectious Diseases and Gene Expression in Insects

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 28003491
DOI: 10.1128/jvi.01779-16

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Disruption of Stress Granule Formation by the Multifunctional Cricket Paralysis Virus 1A ProteinPMID 28003491Read ↗

Japanese Encephalitis Virus Core Protein Inhibits Stress Granule Formation through an Interaction with Caprin-1 and Facilitates Viral PropagationSemantic proximity Read ↗

Cytoplasmic RNA Granules and Viral InfectionSemantic proximity Read ↗

Antagonism of stress granules key for SARS-CoV-2 infection and pathogenesisSemantic proximity Read ↗

Feline Calicivirus Infection Disrupts Assembly of Cytoplasmic Stress Granules and Induces G3BP1 CleavageSemantic proximity Read ↗

SARS-CoV-2 nucleocapsid protein impairs stress granule formation to promote viral replicationSemantic proximity Read ↗

Pro-Viral and Anti-Viral Roles of the RNA-Binding Protein G3BP1Semantic proximity Read ↗

A little less aggregation a little more replication: Viral manipulation of stress granulesSemantic proximity Read ↗

Stress Granule Components G3BP1 and G3BP2 Play a Proviral Role Early in Chikungunya Virus ReplicationSemantic proximity Read ↗

Viral Regulation of RNA Granules in Infected CellsSemantic proximity Read ↗

SARS-CoV-2 nucleocapsid protein inhibits the PKR-mediated integrated stress response through RNA-binding domain N2bSemantic proximity Read ↗

Chandipura Virus Forms Cytoplasmic Inclusion Bodies through Phase Separation and Proviral Association of Cellular Protein Kinase R and Stress Granule Protein TIA-1Semantic proximity Read ↗

Stress Granules in the Viral Replication CycleSemantic proximity Read ↗

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