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

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.

Journal of virology - 1 Jul 1995

Lin C, Thomson J A, Rice C M

Abstract excerpt

A virus-encoded serine proteinase mediates four site-specific cleavages in the hepatitis C virus polyprotein. In addition to the catalytic domain, which is located in the N-terminal one-third of nonstructural protein NS3, the 54-residue NS4A protein is required for cleavage at some but not all sites. Here, we provide evidence for a non-ionic detergent-stable interaction between NS4A and the NS3 serine proteinase...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Molecular Sequence Data

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

Share to Mutation

Share to Octoxynol

Share to Serine Endopeptidases

Share to Viral Nonstructural Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 7769699
DOI: 10.1128/JVI.69.7.4373-4380.1995
PMCID: PMC189178

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

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.PMID 7769699Read ↗

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

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

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

Structural and functional insights into alphavirus polyprotein processing and pathogenesis.Semantic proximity Read ↗

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

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

Autocatalytic Cleavage within Classical Swine Fever Virus NS3 Leads to a Functional Separation of Protease and HelicaseSemantic proximity Read ↗

Hepatitis G virus encodes protease activities which can effect processing of the virus putative nonstructural proteins.Semantic 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 ↗

Mutagenesis of the NS2B-NS3-mediated cleavage site in the flavivirus capsid protein demonstrates a requirement for coordinated processing.Semantic proximity Read ↗

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

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