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

The NTPase/helicase domain of hepatitis C virus nonstructural protein 3 inhibits protein kinase C independently of its NTPase activity.

Cellular & molecular biology letters - 1 Sept 2013

Hartjen Philip, Höchst Bastian, Heim Denise, von der Kammer Henning, Lucke Judith, Reinholz Michael, Baier Andrea, Smeets Ralf, Wege Henning, Borowski Peter, Schulze Zur Wiesch Julian

Abstract excerpt

Helicase motif VI is a short arginine-rich motif within the NTPase/helicase domain of the non-structural protein 3 (NS3) of the hepatitis C virus (HCV). We previously demonstrated that it reduces the catalytic activity and intracellular shuttling of protein kinase C (PKC). Thus, NS3-mediated PKC...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Biocatalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electrophoresis, Polyacrylamide Gel

Share to Hepacivirus

Share to Hydrolysis

Share to Protein Kinase C

Share to RNA Helicases

Share to Viral Nonstructural Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 23893289
DOI: 10.2478/s11658-013-0099-7
PMCID: PMC6275940

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-23893289-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The NTPase/helicase domain of hepatitis C virus nonstructural protein 3 inhibits protein kinase C independently of its NTPase activity.PMID 23893289Read ↗

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

The inhibition of cAMP-dependent protein kinase by full-length hepatitis C virus NS3/4A complex is due to ATP hydrolysis.Semantic proximity Read ↗

Hepatitis C virus NS3 protease is activated by low concentrations of protease inhibitors.Semantic proximity Read ↗

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

Involvement of Creatine Kinase B in Hepatitis C Virus Genome Replication through Interaction with the Viral NS4A ProteinSemantic proximity Read ↗

Regulation of interferon regulatory factor-3 by the hepatitis C virus serine protease.Semantic proximity Read ↗

Motif V is an allosteric couple between the SARS-CoV-2 nsp13 nucleotide triphosphatase and helicase active sites.Semantic proximity Read ↗

Mutational analysis of hepatitis C virus NS3-associated helicase.Semantic proximity Read ↗

Functional interactions between conserved motifs of the hepatitis C virus RNA helicase protein NS3.Semantic proximity Read ↗

Single-point mutations of hepatitis C virus NS3 that impair p53 interaction and anti-apoptotic activity of NS3.Semantic proximity Read ↗

An ELISA for RNA helicase activity: application as an assay of the NS3 helicase of hepatitis C virus.Semantic proximity Read ↗

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