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

Further requirements for cleavage by the murine coronavirus 3C-like proteinase: identification of a cleavage site within ORF1b.

Virology - 25 Oct 1999

Piñón J D, Teng H, Weiss S R

Abstract excerpt

The coronavirus mouse hepatitis virus strain A59 (MHV-A59) encodes a 3C-like proteinase (3CLpro) that is proposed to be responsible for the majority of the processing events that take place within the replicase polyproteins pp1a and pp1ab. In this study we demonstrate that the Q939/S940 peptide bond, located between the polymerase and Zn-finger regions of pp1ab (the POL/Zn site), is processed by the 3CLpro,...

Read the complete abstract on PubMed

Topics

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

Share to Consensus Sequence
Share to Coronavirus
Share to Coronavirus 3C Proteases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cysteine Endopeptidases

Share to DNA-Directed DNA Polymerase

Share to Molecular Weight

Share to Protein Processing, Post-Translational

Share to Zinc Fingers

Source

Open in PubMed Open full text

Identifiers

PMID: 10544119
DOI: 10.1006/viro.1999.9954
PMCID: PMC7131300

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Further requirements for cleavage by the murine coronavirus 3C-like proteinase: identification of a cleavage site within ORF1b.PMID 10544119Read ↗

Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases.Semantic proximity Read ↗

Mutational analysis of the putative substrate-binding site of 3C proteinase of coxsackievirus B3.Semantic proximity Read ↗

Mutational analysis of the active centre of coronavirus 3C-like proteases.Semantic proximity Read ↗

Further Characterization of the Coronavirus Infectious Bronchitis Virus 3C-like Proteinase and Determination of a New Cleavage SiteSemantic proximity Read ↗

Analysis of putative active site residues of the poliovirus 3C protease.Semantic proximity Read ↗

Critical residues for proteolysis activity of maize chlorotic dwarf virus (MCDV) 3C-like protease and comparison of activity of orthologous waikavirus proteases.Semantic proximity Read ↗

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

Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinaseSemantic proximity Read ↗

Identification of the active-site residues of the 3C proteinase of foot-and-mouth disease virus.Semantic proximity Read ↗

Engineering a novel endopeptidase based on SARS 3CL(pro).Semantic proximity Read ↗

Human Coronavirus 229E Papain-Like Proteases Have Overlapping Specificities but Distinct Functions in Viral ReplicationSemantic proximity Read ↗

Structural and mutagenic analysis of foot-and-mouth disease virus 3C protease reveals the role of the beta-ribbon in proteolysis.Semantic proximity Read ↗

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