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

Cleavage between replicase proteins p28 and p65 of mouse hepatitis virus is not required for virus replication.

Journal of virology - 1 Jun 2004

Denison Mark R, Yount Boyd, Brockway Sarah M, Graham Rachel L, Sims Amy C, Lu XiaoTao, Baric Ralph S

Abstract excerpt

The p28 and p65 proteins of mouse hepatitis virus (MHV) are the most amino-terminal protein domains of the replicase polyprotein. Cleavage between p28 and p65 has been shown to occur in vitro at cleavage site 1 (CS1), (247)Gly downward arrow Val(248), in the polyprotein. Although critical residues for CS1 cleavage have been mapped in vitro, the requirements for cleavage have not been studied in infected cells. To...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Murine hepatitis virus

Share to Mutation

Share to RNA-Dependent RNA Polymerase

Share to RNA, Viral

Share to Viral Proteins

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 15140993
DOI: 10.1128/JVI.78.11.5957-5965.2004
PMCID: PMC415798

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

Cleavage between replicase proteins p28 and p65 of mouse hepatitis virus is not required for virus replication.PMID 15140993Read ↗

Processing of open reading frame 1a replicase proteins nsp7 to nsp10 in murine hepatitis virus strain A59 replication.Semantic proximity Read ↗

Identification of mouse hepatitis virus papain-like proteinase 2 activity.Semantic proximity Read ↗

Murine hepatitis virus replicase protein nsp10 is a critical regulator of viral RNA synthesis.Semantic proximity Read ↗

Proteolytic Processing of the Coronavirus Replicase Nonstructural Protein 14 Exonuclease Is Not Required for Virus Replication but Alters RNA Synthesis and Viral Fitness.Semantic proximity Read ↗

A novel mutation in murine hepatitis virus nsp5, the viral 3C-like proteinase, causes temperature-sensitive defects in viral growth and protein processing.Semantic proximity Read ↗

Biochemical and genetic analyses of murine hepatitis virus Nsp15 endoribonuclease.Semantic proximity Read ↗

The nsp2 Replicase Proteins of Murine Hepatitis Virus and Severe Acute Respiratory Syndrome Coronavirus Are Dispensable for Viral ReplicationSemantic proximity Read ↗

Mutagenesis of the murine hepatitis virus nsp1-coding region identifies residues important for protein processing, viral RNA synthesis, and viral replicationSemantic proximity Read ↗

The Small Envelope Protein E Is Not Essential for Murine Coronavirus ReplicationSemantic proximity Read ↗

Processing of the hepatitis E virus polyprotein can be mediated by a cellular proteaseSemantic proximity Read ↗

Genetic analysis of Murine hepatitis virus nsp4 in virus replication.Semantic proximity Read ↗

Folding and particle assembly are disrupted by single-point mutations near the autocatalytic cleavage site of Nudaurelia capensis omega virus capsid protein.Semantic proximity Read ↗

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