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

Functional analysis of the influenza virus H5N1 nucleoprotein tail loop reveals amino acids that are crucial for oligomerization and ribonucleoprotein activities.

Journal of virology - 1 Jul 2010

Chan Wai-Hon, Ng Andy Ka-Leung, Robb Nicole C, Lam Mandy Ka-Han, Chan Paul Kay-Sheung, Au Shannon Wing-Ngor, Wang Jia-Huai, Fodor Ervin, Shaw Pang-Chui

Abstract excerpt

Homo-oligomerization of the nucleoprotein (NP) of influenza A virus is crucial for providing a major structural framework for the assembly of viral ribonucleoprotein (RNP) particles. The nucleoprotein is also essential for transcription and replication during the virus life cycle. In the H5N1 NP structure, the tail loop region is important for NP to form oligomers. Here, by an RNP reconstitution assay, we...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Influenza A Virus, H5N1 Subtype

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Nucleocapsid Proteins

Share to Protein Conformation

Share to Protein Multimerization

Share to RNA-Binding Proteins

Share to Viral Core Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 20463064
DOI: 10.1128/JVI.02474-09
PMCID: PMC2898228

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional analysis of the influenza virus H5N1 nucleoprotein tail loop reveals amino acids that are crucial for oligomerization and ribonucleoprotein activities.PMID 20463064Read ↗

Biochemical characterization of the respiratory syncytial virus N0-P complex in solutionSemantic proximity Read ↗

Structure and oligomerization state of the C-terminal region of the Middle East respiratory syndrome coronavirus nucleoproteinSemantic proximity Read ↗

Structure and assembly of the influenza A virus ribonucleoprotein complexSemantic proximity Read ↗

Molecular dynamics studies of the nucleoprotein of influenza A virus: role of the protein flexibility in RNA binding.Semantic proximity Read ↗

Ribonucleocapsid Formation of Severe Acute Respiratory Syndrome Coronavirus through Molecular Action of the N-Terminal Domain of N ProteinSemantic proximity Read ↗

The Structure of Native Influenza Virion RibonucleoproteinsSemantic proximity Read ↗

Recombinant severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein forms a dimer through its C-terminal domain.Semantic proximity Read ↗

Importance of RNA length for in vitro encapsidation by the nucleoprotein of human respiratory syncytial virusSemantic proximity Read ↗

Identification of influenza A nucleoprotein body domain residues essential for viral RNA expression expose antiviral target.Semantic proximity Read ↗

Full-length three-dimensional structure of the influenza A virus M1 protein and its organization into a matrix layer.Semantic proximity Read ↗

Structural basis for dimerization and RNA binding of avian infectious bronchitis virus nsp9Semantic proximity Read ↗

VP40 octamers are essential for Ebola virus replication.Semantic proximity Read ↗

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