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 C viral NS3-4A protease activity is enhanced by the NS3 helicase.

The Journal of biological chemistry - 31 Oct 2008

Beran Rudolf K F, Pyle Anna Marie

Abstract excerpt

Non-structural protein 3 (NS3) is a multifunctional enzyme possessing serine protease, NTPase, and RNA unwinding activities that are required for hepatitis C viral (HCV) replication. HCV non-structural protein 4A (NS4A) binds to the N-terminal NS3 protease domain to stimulate NS3 serine protease activity. In addition, the NS3 protease domain enhances the RNA binding, ATPase, and RNA unwinding activities of the...

Read the complete abstract on PubMed

Topics

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

Share to Hepacivirus
Share to Hepatitis C
Share to Hydrogen-Ion Concentration

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

Share to Peptide Hydrolases

Share to RNA Helicases

Share to Serine

Share to Viral Nonstructural Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 18723512
DOI: 10.1074/jbc.M804065200
PMCID: PMC2573085

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

Hepatitis C viral NS3-4A protease activity is enhanced by the NS3 helicase.PMID 18723512Read ↗

Nonstructural protein 3-4A: the Swiss army knife of hepatitis C virus.Semantic proximity Read ↗

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

Structural and biological identification of residues on the surface of NS3 helicase required for optimal replication of the hepatitis C virus.Semantic proximity Read ↗

Protease and helicase activities of hepatitis C virus genotype 4, 5, and 6 NS3-NS4A proteins.Semantic proximity Read ↗

Conserved motifs in the flavivirus NS3 RNA helicase enzymeSemantic 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 ↗

Helicase Inhibitors as Specifically Targeted Antiviral Therapy for Hepatitis cSemantic proximity Read ↗

Crystal Structure of the NS3 Protease-Helicase from Dengue VirusSemantic proximity Read ↗

NS3 from Hepatitis C Virus Strain JFH-1 Is an Unusually Robust Helicase That Is Primed To Bind and Unwind Viral RNA.Semantic proximity Read ↗

Cross-genotypic interaction between hepatitis C virus NS3 protease domains and NS4A cofactors.Semantic proximity Read ↗

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

The N-terminal region of hepatitis C virus nonstructural protein 3 (NS3) is essential for stable complex formation with NS4A.Semantic proximity Read ↗

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