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

Conserved GXXXG- and S/T-like motifs in the transmembrane domains of NS4B protein are required for hepatitis C virus replication.

Journal of virology - 1 Jul 2011

Han Qingxia, Aligo Jason, Manna David, Belton Kerry, Chintapalli Sree V, Hong Yoojin, Patterson Randen L, van Rossum Damian B, Konan Kouacou V

Abstract excerpt

Hepatitis C virus (HCV) nonstructural protein 4B (NS4B) is an integral membrane protein, which plays an important role in the organization and function of the HCV replication complex (RC). Although much is understood about its amphipathic N-terminal and C-terminal domains, we know very little about the role of the transmembrane domains (TMDs) in NS4B function. We hypothesized that in addition to anchoring NS4B...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Cell Membrane

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Consensus Sequence

Share to Hepacivirus

Share to Protein Multimerization

Share to Structure-Activity Relationship

Share to Viral Nonstructural Proteins

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 21507970
DOI: 10.1128/JVI.02298-10
PMCID: PMC3126491

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conserved GXXXG- and S/T-like motifs in the transmembrane domains of NS4B protein are required for hepatitis C virus replication.PMID 21507970Read ↗

Modulation of hepatitis C virus genome encapsidation by nonstructural protein 4B.Semantic proximity Read ↗

A genetic interaction between the core and NS3 proteins of hepatitis C virus is essential for production of infectious virus.Semantic proximity Read ↗

Charged residues in hepatitis C virus NS4B are critical for multiple NS4B functions in RNA replication.Semantic proximity Read ↗

Interaction networks of hepatitis C virus NS4B: implications for antiviral therapySemantic proximity Read ↗

The Replacement of 10 Non-Conserved Residues in the Core Protein of JFH-1 Hepatitis C Virus Improves Its Assembly and Secretion.Semantic proximity Read ↗

Hepatitis C Virus Envelope Glycoproteins: A Balancing Act of Order and DisorderSemantic proximity Read ↗

NS4B self-interaction through conserved C-terminal elements is required for the establishment of functional hepatitis C virus replication complexes.Semantic proximity Read ↗

A Nucleotide Binding Motif in Hepatitis C Virus (HCV) NS4B Mediates HCV RNA ReplicationSemantic proximity Read ↗

High-Resolution Functional Profiling of Hepatitis C Virus GenomeSemantic proximity Read ↗

Identification of a class of HCV inhibitors directed against the nonstructural protein NS4B.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 ↗

The hepatitis C virus NS4B protein can trans-complement viral RNA replication and modulates production of infectious virus.Semantic proximity Read ↗

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