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

Multiple mutations in hepatitis C virus NS5A domain II are required to confer a significant level of resistance to alisporivir.

Antimicrobial agents and chemotherapy - 1 Oct 2012

Garcia-Rivera Jose A, Bobardt Michael, Chatterji Udayan, Hopkins Sam, Gregory Matthew A, Wilkinson Barrie, Lin Kai, Gallay Philippe A

Abstract excerpt

Alisporivir is the most advanced host-targeting antiviral cyclophilin (Cyp) inhibitor in phase III studies and has demonstrated a great deal of promise in decreasing hepatitis C virus (HCV) viremia in infected patients. In an attempt to further elucidate the mechanism of action of alisporivir, HCV replicons resistant to the drug were selected. Interestingly, mutations constantly arose in domain II of NS5A. To...

Read the complete abstract on PubMed

Topics

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

Share to Antiviral Agents
Share to Cell Line, Tumor

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

Share to Cyclosporine

Share to Drug Resistance, Viral

Share to Hepacivirus

Share to Reverse Transcriptase Polymerase Chain Reaction

Share to Sequence Homology, Amino Acid

Share to Viral Nonstructural Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 22802259
DOI: 10.1128/AAC.00919-12
PMCID: PMC3457393

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

Multiple mutations in hepatitis C virus NS5A domain II are required to confer a significant level of resistance to alisporivir.PMID 22802259Read ↗

DEB025 (Alisporivir) Inhibits Hepatitis C Virus Replication by Preventing a Cyclophilin A Induced Cis-Trans Isomerisation in Domain II of NS5ASemantic proximity Read ↗

Profile of alisporivir and its potential in the treatment of hepatitis C.Semantic proximity Read ↗

The combination of alisporivir plus an NS5A inhibitor provides additive to synergistic anti-hepatitis C virus activity without detectable cross-resistance.Semantic proximity Read ↗

The combination of the NS5A and cyclophilin inhibitors results in an additive anti-HCV inhibition in humanized mice without development of resistance.Semantic proximity Read ↗

Mechanism of Resistance of Hepatitis C Virus Replicons to Structurally Distinct Cyclophilin InhibitorsSemantic proximity Read ↗

Identification of cellular and viral factors related to anti‐hepatitis C virus activity of cyclophilin inhibitorSemantic proximity Read ↗

Alisporivir inhibits MERS- and SARS-coronavirus replication in cell culture, but not SARS-coronavirus infection in a mouse modelSemantic proximity Read ↗

A conserved tandem cyclophilin-binding site in hepatitis C virus nonstructural protein 5A regulates Alisporivir susceptibility.Semantic proximity Read ↗

Viral resistance to specifically targeted antiviral therapies for hepatitis C (STAT-Cs)Semantic proximity Read ↗

Hepatocytes that express variants of cyclophilin A are resistant to HCV infection and replication.Semantic proximity Read ↗

The Cyclophilin Inhibitor SCY-635 Disrupts Hepatitis C Virus NS5A-Cyclophilin A ComplexesSemantic proximity Read ↗

A major determinant of cyclophilin dependence and cyclosporine susceptibility of hepatitis C virus identified by a genetic approach.Semantic proximity Read ↗

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