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

Regions of the herpes simplex virus scaffolding protein that are important for intermolecular self-interaction.

Journal of virology - 1 Jan 2002

Preston Valerie G, McDougall Iris M

Abstract excerpt

The herpes simplex virus type 1 (HSV-1) scaffolding protein encoded by gene UL26.5 promotes the formation of the icosahedral capsid shell through its association with the major capsid protein VP5 and through intermolecular interactions with itself. Inside the capsid shell, the UL26.5 product together with the maturational protease, a minor protein, form a spherical structure which is broken down and released from...

Read the complete abstract on PubMed

Topics

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

Share to Baculoviridae
Share to Capsid
Share to Centrifugation, Density Gradient

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Herpesvirus 1, Human

Share to Herpesvirus 3, Human

Share to Microscopy, Immunoelectron

Share to Vero Cells

Share to Virus Assembly

Source

Open in PubMed Open full text

Identifiers

PMID: 11752158
DOI: 10.1128/jvi.76.2.673-687.2002
PMCID: PMC136825

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

Regions of the herpes simplex virus scaffolding protein that are important for intermolecular self-interaction.PMID 11752158Read ↗

Evidence for controlled incorporation of herpes simplex virus type 1 UL26 protease into capsids.Semantic proximity Read ↗

The 25 amino acid residues at the carboxy terminus of the herpes simplex virus type 1 UL26.5 protein are required for the formation of the capsid shell around the scaffold.Semantic proximity Read ↗

Second site mutations in the N-terminus of the major capsid protein (VP5) overcome a block at the maturation cleavage site of the capsid scaffold proteins of herpes simplex virus type 1.Semantic proximity Read ↗

Second-site mutations encoding residues 34 and 78 of the major capsid protein (VP5) of herpes simplex virus type 1 are important for overcoming a blocked maturation cleavage site of the capsid scaffold proteins.Semantic proximity Read ↗

Mechanical Capsid Maturation Facilitates the Resolution of Conflicting Requirements for Herpesvirus Assembly.Semantic proximity Read ↗

Unraveling the role of the C-terminal helix turn helix of the coat-binding domain of bacteriophage P22 scaffolding protein.Semantic proximity Read ↗

Subassemblies and Asymmetry in Assembly of Herpes Simplex Virus ProcapsidSemantic proximity Read ↗

Scaffolding mutants identifying domains required for P22 procapsid assembly and maturation.Semantic proximity Read ↗

Major capsid reinforcement by a minor protein in herpesviruses and phageSemantic proximity Read ↗

Amino acids 143 to 150 of the herpes simplex virus type 1 scaffold protein are required for the formation of portal-containing capsids.Semantic proximity Read ↗

Different functional sensitivity to mutation at intersubunit interfaces involved in consecutive stages of foot-and-mouth disease virus assembly.Semantic proximity Read ↗

Functional Solubilization of Aggregation-prone HIV Envelope Proteins by Covalent Fusion with Chaperone ModulesSemantic proximity Read ↗

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