Evidence map›Paper›PMID 24557493›Full record

ReviewImmunologic research2014

HCV core protein and virus assembly: what we know without structures.

Katarzyna Gawlik, Philippe A Gallay

Open access · greenAbstract readReview
In one paragraph

Review in Immunologic research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

26 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Prediction of Intrinsically Disordered Regions That Bind RNA with DisoRDPbind.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Roles of X-box binding protein 1 in liver pathogenesis.Clinical and molecular hepatology · 2025
    Review
  6. Review
  7. Can iron chelators ameliorate viral infections?Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Activation of the CaViruses · 2022
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article
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

2 authors at 1 institution in 1 country.

Katarzyna GawlikDepartment of Immunology and Microbial Science, IMM-9, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA, 92037, USA.
Philippe A Gallay
Scripps Research Institute · US

Funding

Cyclophilins, Cyclophilin Inhibitors and Hepatitis CR01AI087746 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI GALLAY, PHILIPPE ANDRE · 2010 to 2014
$2.3M
Cyclophilins and the IFN ResponseR01AI105007 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI GALLAY, PHILIPPE ANDRE · 2014 to 2017
$1.6M
NIAID NIH HHS AI087746NIAID NIH HHS R01 AI087746NIAID NIH HHS R01 AI105007
6 · The paper itself

Abstract

Chronic hepatitis C virus (HCV) infection results in a progressive disease that may end in cirrhosis and, eventually, in hepatocellular carcinoma. In the last several years, tremendous progress has been made in understanding the HCV life cycle and in the development of small molecule compounds for the treatment of chronic hepatitis C. Nevertheless, the complete understanding of HCV assembly and particle release as well as the detailed characterization and structure of HCV particles is still missing. One of the most important events in the HCV assembly is the nucleocapsid formation which is driven by the core protein, that can oligomerize upon interaction with viral RNA, and is orchestrated by viral and host proteins. Despite a growing number of new factors involved in HCV assembly process, we do not know the three-dimensional structure of the core protein or its topology in the nucleocapsid. Since the core protein contains a hydrophobic C-terminal domain responsible for the binding to cellular membranes, the assembly pathway of HCV virions might proceed via coassembly at endoplasmic reticulum membranes. Recently, new mechanisms involving viral proteins and host factors in HCV particle formation and egress have been described. The present review aims to summarize the advances in our understanding of HCV assembly with an emphasis on the core protein as a structural component of virus particles that possesses the ability to interact with a variety of cellular components and is potentially an attractive target for the development of a novel class of anti-HCV agents.

Indexed as

Viral Core ProteinsAntiviral AgentsHepacivirusHumansVirus AssemblyAntiviral Agentsnucleocapsid protein, Hepatitis C virusViral Core Proteins

Identifiers

PMID24557493
PMCPMC6659715
OpenAlexW1996826591

What OpenQuestion holds

Textmetadata
LicenceTDM
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.