Separate functional domains of the herpes simplex virus type 1 protease: evidence for cleavage inside capsids.

doi:10.1128/JVI.70.7.4317-4328.1996

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

Back to search

Article

Separate functional domains of the herpes simplex virus type 1 protease: evidence for cleavage inside capsids.

Journal of virology - 1 Jul 1996

Robertson B J, McCann P J, Matusick-Kumar L, Newcomb W W, Brown J C, Colonno R J, Gao M

Abstract excerpt

The herpes simplex virus type 1 (HSV-1) protease (Pra) and related proteins are involved in the assembly of viral capsids and virion maturation. Pra is a serine protease, and the active-site residue has been mapped to amino acid (aa) 129 (Ser). This 635-aa protease, encoded by the UL26 gene, is a...

Topics

Animals
Base Sequence
Binding Sites
Capsid
Cell Line
Chlorocebus aethiops
DNA Primers
Genetic Complementation Test
Herpesvirus 1, Human
Humans
Molecular Sequence Data
Mutation
Serine Endopeptidases
Vero Cells
Viral Proteins
Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 8676454
DOI: 10.1128/JVI.70.7.4317-4328.1996
PMCID: PMC190364

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8676454-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics