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

Mapping of the VP40-binding regions of the nucleoprotein of Ebola virus.

Journal of virology - 1 Apr 2007

Noda Takeshi, Watanabe Shinji, Sagara Hiroshi, Kawaoka Yoshihiro

Abstract excerpt

Expression of Ebola virus nucleoprotein (NP) in mammalian cells leads to the formation of helical structures, which serve as a scaffold for the nucleocapsid. We recently found that NP binding with the matrix protein VP40 is important for nucleocapsid incorporation into virions (T. Noda, H. Ebihar...

Read the complete abstract on PubMed

Topics

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

Share to Capsid Proteins
Share to Ebolavirus
Share to Microscopy, Electron, Transmission

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microscopy, Immunoelectron

Share to Nucleoproteins

Share to Peptide Hydrolases

Share to Viral Matrix Proteins

Share to Virion

Source

Open in PubMed Open full text

Identifiers

PMID: 17229682
DOI: 10.1128/JVI.02183-06
PMCID: PMC1866061

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17229682-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mapping of the VP40-binding regions of the nucleoprotein of Ebola virus.PMID 17229682Read ↗

Functional Mapping of the Nucleoprotein of Ebola VirusSemantic proximity Read ↗

Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and genome packaging.Semantic proximity Read ↗

Subcellular Characterization of the Molecular Determinants of Ebola VP40 Trafficking and AssemblySemantic proximity Read ↗

Structural basis of Ebola virus nucleocapsid assembly and functionsSemantic proximity Read ↗

Insight into the Ebola virus nucleocapsid assembly mechanism: crystal structure of Ebola virus nucleoprotein core domain at 1.8 Å resolutionSemantic proximity Read ↗

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

Structural dissection of Ebola virus and its assembly determinants using cryo-electron tomographySemantic proximity Read ↗

Structure and assembly of the Ebola virus nucleocapsidSemantic proximity Read ↗

A cationic, C-terminal patch and structural rearrangements in Ebola virus matrix VP40 protein control its interactions with phosphatidylserine.Semantic proximity Read ↗

A loop region in the N-terminal domain of Ebola virus VP40 is important in viral assembly, budding, and egress.Semantic proximity Read ↗

Identification of RUVBL1 and RUVBL2 as Novel Cellular Interactors of the Ebola Virus NucleoproteinSemantic proximity Read ↗

Mutation of Hydrophobic Residues in the C-Terminal Domain of the Marburg Virus Matrix Protein VP40 Disrupts Trafficking to the Plasma Membrane.Semantic proximity Read ↗

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