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

Hepatitis A virus proteinase 3C binding to viral RNA: correlation with substrate binding and enzyme dimerization.

The Biochemical journal - 15 Jan 2005

Peters Hannelore, Kusov Yuri Y, Meyer Sonja, Benie Andrew J, Bäuml Englbert, Wolff Maike, Rademacher Christoph, Peters Thomas, Gauss-Müller Verena

Abstract excerpt

Proteinase 3C of hepatitis A virus (HAV) plays a key role in the viral life cycle by generating mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, 3C binds to viral RNA, and thus influences viral genome replication. In order to investigate the interplay between proteolytic activity and RNA binding at the molecular level, we subjected HAV 3C and three variants carrying...

Read the complete abstract on PubMed

Topics

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

Share to Carcinoma, Hepatocellular
Share to Cysteine Endopeptidases

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

Share to Dimerization

Share to Hepatitis A virus

Share to Hydrolysis

Share to Liver Neoplasms

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Peptide Fragments

Source

Open in PubMed Open full text

Identifiers

PMID: 15361063
DOI: 10.1042/BJ20041153
PMCID: PMC1134706

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Hepatitis A virus proteinase 3C binding to viral RNA: correlation with substrate binding and enzyme dimerization.PMID 15361063Read ↗

New details of HCV NS3/4A proteinase functionality revealed by a high-throughput cleavage assay.Semantic proximity Read ↗

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

3-Chymotrypsin-like Protease (3CLpro): Validation as a Molecular Target, Proposal of a Novel Catalytic Mechanism, and Inhibitors in Preclinical and Clinical TrialsSemantic proximity Read ↗

A central region in the hepatitis C virus NS4A protein allows formation of an active NS3-NS4A serine proteinase complex in vivo and in vitro.Semantic proximity Read ↗

Mutation of Asn28 disrupts the dimerization and enzymatic activity of SARS 3CL(pro) .Semantic proximity Read ↗

Insights into the enzyme-substrate interaction in the norovirus 3C-like protease.Semantic proximity Read ↗

A naturally occurring G11S mutation in the 3C-like protease from the SARS-CoV-2 virus dramatically weakens the dimer interface.Semantic proximity Read ↗

Structure of Senecavirus A 3C Protease Revealed the Cleavage Pattern of 3C Protease in PicornavirusesSemantic proximity Read ↗

Mutation of the proteolytic cleavage site enhances stability and yield of recombinant hepatitis C virus core protein in bacterial cells.Semantic proximity Read ↗

A comparative biochemical analysis of the NS2B(H)-NS3pro protease complex from four dengue virus serotypes.Semantic proximity Read ↗

Identification of amino acid variants in the hepatitis C virus non-structural protein 4A.Semantic proximity Read ↗

Cooperativity and communication between the active sites of the dimeric SARS-CoV-2 main protease.Semantic proximity Read ↗

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