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

Structure and function of the membrane anchor domain of hepatitis C virus nonstructural protein 5A.

The Journal of biological chemistry - 24 Sept 2004

Penin François, Brass Volker, Appel Nicole, Ramboarina Stephanie, Montserret Roland, Ficheux Damien, Blum Hubert E, Bartenschlager Ralf, Moradpour Darius

Abstract excerpt

Hepatitis C virus (HCV) nonstructural protein 5A (NS5A) is a membrane-associated, essential component of the viral replication complex. Here, we report the three-dimensional structure of the membrane anchor domain of NS5A as determined by NMR spectroscopy. An alpha-helix extending from amino acid residue 5 to 25 was observed in the presence of different membrane mimetic media. This helix exhibited a hydrophobic,...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies, Monoclonal
Share to Cytosol

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

Share to Lipid Bilayers

Share to Magnetic Resonance Spectroscopy

Share to Micelles

Share to Microscopy, Confocal

Share to Protein Structure, Secondary

Share to Viral Nonstructural Proteins

Source

Identifiers

PMID: 15247283
DOI: 10.1074/jbc.M404761200

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

Structure and function of the membrane anchor domain of hepatitis C virus nonstructural protein 5A.PMID 15247283Read ↗

An amino-terminal amphipathic alpha-helix mediates membrane association of the hepatitis C virus nonstructural protein 5A.Semantic proximity Read ↗

Amphipathic α-Helix AH2 Is a Major Determinant for the Oligomerization of Hepatitis C Virus Nonstructural Protein 4BSemantic proximity Read ↗

Aminoterminal amphipathic α-helix AH1 of hepatitis C virus nonstructural protein 4B possesses a dual role in RNA replication and virus production.Semantic proximity Read ↗

Interaction between Nonstructural Proteins NS4B and NS5A Is Essential for Proper NS5A Localization and Hepatitis C Virus RNA Replication.Semantic proximity Read ↗

ACIDIC BICELLES ARE A SUITABLE MEMBRANE MIMIC FOR STRUCTURAL STUDIES OF THE LASSA VIRUS FUSION DOMAINSemantic proximity Read ↗

The N-terminal helix α(0) of hepatitis C virus NS3 protein dictates the subcellular localization and stability of NS3/NS4A complex.Semantic proximity Read ↗

Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A.Semantic proximity Read ↗

Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a "fuzzy complex" with VAPB-MSP domain which carries ALS-causing mutations.Semantic proximity Read ↗

Membrane association of hepatitis C virus nonstructural proteins and identification of the membrane alteration that harbors the viral replication complexSemantic proximity Read ↗

Dengue virus NS4A cytoplasmic domain binding to liposomes is sensitive to membrane curvature.Semantic proximity Read ↗

Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly.Semantic proximity Read ↗

Characterization of nonstructural protein membrane anchor deletion mutants expressed in the context of the hepatitis C virus polyprotein.Semantic proximity Read ↗

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