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 evolution balances conflicting roles of N protein phosphorylation.

PLoS pathogens - 1 Nov 2024

Syed Abdullah M, Ciling Alison, Chen Irene P, Carlson Christopher R, Adly Armin N, Martin Hannah S, Taha Taha Y, Khalid Mir M, Price Nathan, Bouhaddou Mehdi, Ummadi Manisha R, Moen Jack M, Krogan Nevan J, Morgan David O, Ott Melanie, Doudna Jennifer A

Abstract excerpt

All lineages of SARS-CoV-2, the coronavirus responsible for the COVID-19 pandemic, contain mutations between amino acids 199 and 205 in the nucleocapsid (N) protein that are associated with increased infectivity. The effects of these mutations have been difficult to determine because N protein contributes to both viral replication and viral particle assembly during infection. Here, we used single-cycle infection...

Read the complete abstract on PubMed

Topics

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

Share to Virus Assembly
Share to Chlorocebus aethiops

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Coronavirus Nucleocapsid Proteins

Share to COVID-19

Share to Phosphoproteins

Share to SARS-CoV-2

Share to Vero Cells

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 39571001
DOI: 10.1371/journal.ppat.1012741
PMCID: PMC11620656

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

SARS-CoV-2 evolution balances conflicting roles of N protein phosphorylation.PMID 39571001Read ↗

Epistasis between SARS-CoV-2 M and N Proteins Balances Particle Assembly and Immune EvasionSemantic proximity Read ↗

Convergent evolution in nucleocapsid facilitated SARS-CoV-2 adaptation for human infection.Semantic proximity Read ↗

Nucleocapsid mutations in SARS-CoV-2 augment replication and pathogenesis.Semantic proximity Read ↗

Saudi Arabian SARS-CoV-2 genomes implicate a mutant Nucleocapsid protein in modulating host interactions and increased viral load in COVID-19 patientsSemantic proximity Read ↗

Nucleocapsid mutations R203K/G204R increase the infectivity, fitness, and virulence of SARS-CoV-2.Semantic proximity Read ↗

A truncated SARS-CoV-2 nucleocapsid protein enhances virus fitness by evading antiviral responsesSemantic proximity Read ↗

Nucleocapsid Mutations R203K/G204R Increase the Infectivity, Fitness and Virulence of SARS-CoV-2Semantic proximity Read ↗

SARS-CoV-2 N protein coordinates viral particle assembly through multiple domainsSemantic proximity Read ↗

SARS-CoV-2 genomes from Saudi Arabia implicate nucleocapsid mutations in host response and increased viral loadSemantic proximity Read ↗

The R203M and D377Y mutations of the nucleocapsid protein promote SARS-CoV-2 infectivity by impairing RIG-I-mediated antiviral signalingSemantic proximity Read ↗

Unique RNA replication characteristics and nucleocapsid protein expression may explain differences in the replication capacity of SARS-COV-2 lineagesSemantic proximity Read ↗

Mechanism of SARS-CoV-2 Nucleocapsid Protein Phosphorylation-induced Functional SwitchSemantic proximity Read ↗

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