Evidence map›Paper›PMID 25772504›Full record

ArticleBiochimica et biophysica acta2015

Genotype-specific differences in structural features of hepatitis C virus (HCV) p7 membrane protein.

Monoj Mon Kalita, Stephen Griffin, James J Chou, Wolfgang B Fischer

Open access · bronzeAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.7field-weighted citation impact, top 9% of its field
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

15 citing papers in PubMed, 25 citations in OpenAlex.

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  8. All-atom virus simulations.Current opinion in virology · 2018
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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

4 authors at 3 institutions in 4 countries.

Monoj Mon KalitaInstitute of Biophotonics, School of Biomedical Science and Engineering, Biophotonics & Molecular Imaging Research Center (BMIRC), National Yang-Ming University, Taipei, TW.
Stephen GriffinLeeds Institute of Cancer & Pathology, Faculty of Medicine and Health, St James' University Hospital, University of Leeds, Beckett St., Leeds, West Yorkshire LS9 7TF, UK.
James J ChouDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, USA.
Wolfgang B FischerInstitute of Biophotonics, School of Biomedical Science and Engineering, Biophotonics & Molecular Imaging Research Center (BMIRC), National Yang-Ming University, Taipei, TW. Electronic address: wfischer@ym.edu.tw.
National Yang Ming Chiao Tung University · TWHarvard University · USUniversity of Leeds · GB

Funding

Function and mechanism of the HCV p7 channel and its therapeutic potentialR56AI112960 · NIAID · HARVARD MEDICAL SCHOOL · PI CHOU, JAMES JEIWEN · 2014 to 2014
$508k
Medical Research Council G0700124NIAID NIH HHS R56 AI112960
6 · The paper itself

Abstract

The 63 amino acid polytopic membrane protein, p7, encoded by hepatitis C virus (HCV) is involved in the modulation of electrochemical gradients across membranes within infected cells. Structural information relating to p7 from multiple genotypes has been generated in silico (e.g. genotype (GT) 1a), as well as obtained from experiments in form of monomeric and hexameric structures (GTs 1b and 5a, respectively). However, sequence diversity and structural differences mean that comparison of their channel gating behaviour has not thus far been simulated. Here, a molecular model of the monomeric GT 1a protein is optimized and assembled into a hexameric bundle for comparison with both the 5a hexamer structure and another hexameric bundle generated using the GT 1b monomer structure. All bundles tend to turn into a compact structure during molecular dynamics (MD) simulations (Gromos96 (ffG45a3)) in hydrated lipid bilayers, as well as when simulated at 'low pH', which may trigger channel opening according to some functional studies. Both GT 1a and 1b channel models are gated via movement of the parallel aligned helices, yet the scenario for the GT 5a protein is more complex, with a short N-terminal helix being involved. However, all bundles display pulsatile dynamics identified by monitoring water dynamics within the pore.

Indexed as

Amino AcidsAmino Acid SequenceComputer SimulationGenotypeHepacivirusModels, MolecularMolecular Sequence DataPermeabilityProtein Structure, TertiaryProtonsSequence AlignmentViral ProteinsViroporin ProteinsWaterAmino Acidsp7 protein, Hepatitis C virusProtonsViral ProteinsViroporin ProteinsWaterChannel gatingGenotypesMolecular dynamics simulationNMR structurep7 of HCVViral channel protein

Identifiers

PMID25772504
PMCPMC7094707
OpenAlexW2143045059

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.