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

Topics Community

Article

Role of influenza A virus NP acetylation on viral growth and replication.

Nature communications - 2 Nov 2017

Giese Sebastian, Ciminski Kevin, Bolte Hardin, Moreira Étori Aguiar, Lakdawala Seema, Hu Zehan, David Quinnlan, Kolesnikova Larissa, Götz Veronika, Zhao Yongxu, Dengjel Jörn, Chin Y Eugene, Xu Ke, Schwemmle Martin

Abstract excerpt

Lysine acetylation is a post-translational modification known to regulate protein functions. Here we identify several acetylation sites of the influenza A virus nucleoprotein (NP), including the lysine residues K77, K113 and K229. Viral growth of mutant virus encoding K229R, mimicking a non-acetylated NP lysine residue, is severely impaired compared to wildtype or the mutant viruses encoding K77R or K113R. This...

Topics

Acetylation
Animals
Dogs
HEK293 Cells
Humans
Influenza A virus
Lysine
Madin Darby Canine Kidney Cells
Mutation
Nucleocapsid Proteins
RNA-Binding Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Viral Core Proteins

Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 29097654
DOI: 10.1038/s41467-017-01112-3
PMCID: PMC5668263

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of influenza A virus NP acetylation on viral growth and replication.PMID 29097654Read ↗

Influenza A Virus and Acetylation: The Picture Is Becoming ClearerSemantic proximity Read ↗

Orchestration of protein acetylation as a toggle for cellular defense and virus replicationSemantic proximity Read ↗

The ubiquitination landscape of the Influenza A Virus polymeraseSemantic proximity Read ↗

Sumoylation of Influenza A Virus Nucleoprotein Is Essential for Intracellular Trafficking and Virus GrowthSemantic proximity Read ↗

Acetylation at K108 of the NS1 protein is important for the replication and virulence of influenza virusSemantic proximity Read ↗

Role of Post-translational Modifications in Influenza A Virus Life Cycle and Host Innate Immune ResponseSemantic proximity Read ↗

Quantitative Analysis of Lysine Acetylation in Vero Cells Infected With Peste Des Petits Ruminants VirusSemantic proximity Read ↗

Role of the PB2 627 Domain in Influenza A Virus Polymerase FunctionSemantic proximity Read ↗

Acetylation, Methylation and Allysine Modification Profile of Viral and Host Proteins during Influenza A Virus InfectionSemantic proximity Read ↗

N-terminal acetylation controls multiple functional aspects of the influenza A virus ribonuclease PA-XSemantic proximity Read ↗

Histone Deacetylases in Herpesvirus Replication and Virus-Stimulated Host DefenseSemantic proximity Read ↗

RNA-Free and Ribonucleoprotein-Associated Influenza Virus Polymerases Directly Bind the Serine-5-Phosphorylated Carboxyl-Terminal Domain of Host RNA Polymerase IISemantic proximity Read ↗

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