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

SARS-CoV-2 nucleocapsid protein impairs stress granule formation to promote viral replication

25 May 2021

Abstract excerpt

The newly emerging coronavirus SARS-CoV-2 causes severe lung disease and substantial mortality. How the virus evades host defense for efficient replication is not fully understood. In this report, we found that the SARS-CoV-2 nucleocapsid protein (NP) impaired stress granule (SG) formation induced by viral RNA. SARS-CoV-2 NP associated with the protein kinase PKR after dsRNA stimulation. SARS-CoV-2 NP did not...

Read the complete abstract on PubMed

Topics

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

Share to RNA regulation and disease
Share to Viral gastroenteritis research and epidemiology
Share to Viral Infections and Immunology Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 34035218
DOI: 10.1038/s41421-021-00275-0

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

SARS-CoV-2 nucleocapsid protein impairs stress granule formation to promote viral replicationPMID 34035218Read ↗

SARS-CoV-2 N Protein Antagonizes Stress Granule Assembly and IFN Production by Interacting with G3BPs to Facilitate Viral ReplicationSemantic proximity Read ↗

Beyond Stress Granules: G3BP1 and G3BP2 Redundantly Suppress SARS-CoV-2 InfectionSemantic proximity Read ↗

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

SARS-CoV-2 Nucleocapsid protein attenuates stress granule formation and alters gene expression via direct interaction with host mRNAsSemantic proximity Read ↗

SARS-CoV-2 nucleocapsid protein binds host mRNAs and attenuates stress granules to impair host stress responseSemantic proximity Read ↗

The Stress Granule Protein G3BP1 Recruits Protein Kinase R To Promote Multiple Innate Immune Antiviral ResponsesSemantic proximity Read ↗

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

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

Disruption of molecular interactions between G3BP1 stress granule host protein and nucleocapsid (NTD-N) protein impedes SARS-CoV-2 virus replicationSemantic proximity Read ↗

Middle East Respiratory Coronavirus Accessory Protein 4a Inhibits PKR-Mediated Antiviral Stress ResponsesSemantic proximity Read ↗

Interaction between host G3BP and viral nucleocapsid protein regulates SARS-CoV-2 replicationSemantic proximity Read ↗

Stress Granules in the Viral Replication CycleSemantic proximity Read ↗

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