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

Ribonucleocapsid Formation of Severe Acute Respiratory Syndrome Coronavirus through Molecular Action of the N-Terminal Domain of N Protein

18 Jan 2007

Abstract excerpt

Conserved among all coronaviruses are four structural proteins: the matrix (M), small envelope (E), and spike (S) proteins that are embedded in the viral membrane and the nucleocapsid phosphoprotein (N), which exists in a ribonucleoprotein complex in the lumen. The N-terminal domain of coronaviral N proteins (N-NTD) provides a scaffold for RNA binding, while the C-terminal domain (N-CTD) mainly acts as...

Read the complete abstract on PubMed

Topics

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

Share to Animal Virus Infections Studies
Share to SARS-CoV-2 and COVID-19 Research
Share to Viral gastroenteritis research and epidemiology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 17229691
DOI: 10.1128/jvi.02236-06

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Ribonucleocapsid Formation of Severe Acute Respiratory Syndrome Coronavirus through Molecular Action of the N-Terminal Domain of N ProteinPMID 17229691Read ↗

X-Ray Structures of the N- and C-Terminal Domains of a Coronavirus Nucleocapsid Protein: Implications for Nucleocapsid FormationSemantic proximity Read ↗

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

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

Interactions between the Nucleoprotein and the Phosphoprotein of Pneumoviruses: Structural Insight for Rational Design of AntiviralsSemantic proximity Read ↗

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

The Coronavirus Nucleocapsid Is a Multifunctional ProteinSemantic proximity Read ↗

Nucleocapsid assembly in pneumoviruses is regulated by conformational switching of the N proteinSemantic proximity Read ↗

Characterization of the Interaction Domains between the Phosphoprotein and the Nucleoprotein of Human Metapneumovirus.Semantic proximity Read ↗

Structural Characterization of Human Coronavirus NL63 N ProteinSemantic proximity Read ↗

Affinity tag free purification of SARS-Cov-2 N protein and its crystal structure in complex with ssDNASemantic proximity Read ↗

Reconstitution of the SARS-CoV-2 ribonucleosome provides insights into genomic RNA packaging and regulation by phosphorylationSemantic proximity Read ↗

Crystal Structure of the Core Region of Hantavirus Nucleocapsid Protein Reveals the Mechanism for Ribonucleoprotein Complex FormationSemantic proximity Read ↗

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