Evidence map›Paper›PMID 19692468›Full record

ArticleJournal of virology2009

An amphipathic alpha-helix at the C terminus of hepatitis C virus nonstructural protein 4B mediates membrane association.

Jérôme Gouttenoire, Roland Montserret, Audrey Kennel, François Penin, Darius Moradpour

Abstract read
In one paragraph

Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Jérôme GouttenoireDivision of Gastroenterology and Hepatology, Centre Hospitalier Universitaire Vaudois, BU44/07/2421, Rue du Bugnon 44, CH-1011 Lausanne, Switzerland.
Roland Montserret
Audrey Kennel
François Penin
Darius Moradpour

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nonstructural protein 4B (NS4B) plays an essential role in the formation of the hepatitis C virus (HCV) replication complex. It is an integral membrane protein that has been only poorly characterized to date. It is believed to comprise a cytosolic N-terminal part, a central part harboring four transmembrane passages, and a cytosolic C-terminal part. Here, we describe an amphipathic alpha-helix at the C terminus of NS4B (amino acid residues 229 to 253) that mediates membrane association and is involved in the formation of a functional HCV replication complex.

Indexed as

Protein Structure, SecondaryVirus InternalizationAmino Acid SequenceCell LineHepacivirusHumansModels, MolecularMolecular Sequence DataProtein Structure, TertiaryRecombinant Fusion ProteinsSequence AlignmentViral Nonstructural ProteinsVirus ReplicationRecombinant Fusion ProteinsViral Nonstructural Proteins

Identifiers

PMID19692468
PMCPMC2772773

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.