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

Unstable Polymerase-Nucleoprotein Interaction Is Not Responsible for Avian Influenza Virus Polymerase Restriction in Human Cells

1 Nov 2012

Abstract excerpt

Avian-origin influenza virus polymerase activity can be dramatically increased in human cells with the PB2 E627K mutation. Previously, others have proposed that this mutation increases the stability of the viral ribonucleoprotein complex (vRNP) measured by the interaction between PB2 and NP. However, we demonstrate here that a variety of PB2 adaptive mutations, including E627K, do not enhance the stability of the...

Read the complete abstract on PubMed

Topics

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

Share to Influenza Virus Research Studies
Share to interferon and immune responses
Share to Respiratory viral infections research

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 23115299
DOI: 10.1128/jvi.02597-12

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 22 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Unstable Polymerase-Nucleoprotein Interaction Is Not Responsible for Avian Influenza Virus Polymerase Restriction in Human CellsPMID 23115299Read ↗

Investigating the mechanisms of influenza polymerase host adaptationSemantic proximity Read ↗

Evidence for Avian and Human Host Cell Factors That Affect the Activity of Influenza Virus PolymeraseSemantic proximity Read ↗

The K526R substitution in viral protein PB2 enhances the effects of E627K on influenza virus replicationSemantic proximity Read ↗

Avian Influenza A Virus Polymerase Association with Nucleoprotein, but Not Polymerase Assembly, Is Impaired in Human Cells during the Course of InfectionSemantic proximity Read ↗

Novel Polymerase Gene Mutations for Human Adaptation in Clinical Isolates of Avian H5N1 Influenza Viruses.Semantic proximity Read ↗

Host-range determinants on the PB2 protein of influenza A viruses control the interaction between the viral polymerase and nucleoprotein in human cellsSemantic proximity Read ↗

The molecular basis of host range restriction of avian influenza virus polymerases in mammalian hostsSemantic proximity Read ↗

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

Replication and transcription activities of ribonucleoprotein complexes reconstituted from avian H5N1, H1N1pdm09 and H3N2 influenza A viruses.Semantic proximity Read ↗

Biochemical impact of the host adaptation-associated PB2 E627K mutation on the temperature-dependent RNA synthesis kinetics of influenza A virus polymerase complex.Semantic proximity Read ↗

Long-term evolution of human seasonal influenza virus A(H3N2) is associated with an increase in polymerase complex activitySemantic proximity Read ↗

Differential effect of nucleotide substitutions in the 3' arm of the influenza A virus vRNA promoter on transcription/replication by avian and human polymerase complexes is related to the nature of PB2 amino acid 627.Semantic proximity Read ↗

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