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

Identification of in vivo-interacting domains of the murine coronavirus nucleocapsid protein.

Journal of virology - 1 Jul 2009

Hurst Kelley R, Koetzner Cheri A, Masters Paul S

Abstract excerpt

The coronavirus nucleocapsid protein (N), together with the large, positive-strand RNA viral genome, forms a helically symmetric nucleocapsid. This ribonucleoprotein structure becomes packaged into virions through association with the carboxy-terminal endodomain of the membrane protein (M), which is the principal constituent of the virion envelope. Previous work with the prototype coronavirus mouse hepatitis...

Read the complete abstract on PubMed

Topics

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

Share to Cell Membrane
Share to Coronavirus Infections
Share to Coronavirus Nucleocapsid Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Murine hepatitis virus

Share to Nucleocapsid Proteins

Share to Protein Structure, Tertiary

Share to Rodent Diseases

Share to Virus Assembly

Source

Open in PubMed Open full text

Identifiers

PMID: 19420077
DOI: 10.1128/JVI.00440-09
PMCID: PMC2704785

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

Identification of in vivo-interacting domains of the murine coronavirus nucleocapsid protein.PMID 19420077Read ↗

A major determinant for membrane protein interaction localizes to the carboxy-terminal domain of the mouse coronavirus nucleocapsid protein.Semantic proximity Read ↗

Recognition of the Murine Coronavirus Genomic RNA Packaging Signal Depends on the Second RNA-Binding Domain of the Nucleocapsid ProteinSemantic proximity Read ↗

Analyses of Coronavirus Assembly Interactions with Interspecies Membrane and Nucleocapsid Protein Chimeras.Semantic proximity Read ↗

Characterization of a Critical Interaction between the Coronavirus Nucleocapsid Protein and Nonstructural Protein 3 of the Viral Replicase-Transcriptase ComplexSemantic proximity Read ↗

Identification of functionally important negatively charged residues in the carboxy end of mouse hepatitis coronavirus A59 nucleocapsid protein.Semantic proximity Read ↗

An interaction between the nucleocapsid protein and a component of the replicase-transcriptase complex is crucial for the infectivity of coronavirus genomic RNA.Semantic proximity Read ↗

The Coronavirus Nucleocapsid Is a Multifunctional ProteinSemantic proximity Read ↗

Definition of the components required for selective packaging of coronavirus genomic RNASemantic proximity Read ↗

Coronavirus membrane protein with a fluorescent protein tag enables tracking of virus particles in live cellsSemantic proximity Read ↗

Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomersSemantic proximity Read ↗

The Cellular Interactome of the Coronavirus Infectious Bronchitis Virus Nucleocapsid Protein and Functional Implications for Virus BiologySemantic proximity Read ↗

Structures of the N- and C-terminal domains of MHV-A59 nucleocapsid protein corroborate a conserved RNA-protein binding mechanism in coronavirusSemantic proximity Read ↗

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