ArticleHepatitis monthly2014
HEV-ORF3 Encoding Phosphoprotein Interacts With Hepsin.
Article in Hepatitis monthly, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
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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.
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Who cites it
5 citing papers in PubMed.
- Structural aspects of hepatitis E virus.Archives of virology · 2022Review
- Hepatitis E virus: advances and challenges.Nature reviews. Gastroenterology & hepatology · 2018Review
- Article
- Article
- Therapeutic targets for the treatment of hepatitis E virus infection.Expert opinion on therapeutic targets · 2015Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundHepatitis E virus (HEV) is a major causative agent of acute clinical hepatitis in adults through much of Asia, the Middle East and Africa. Open reading frame 3 (ORF3) encodes around 120 amino acids of phosphorylation protein that associates with the cytoskeleton, while its precise biological function is still unknown.
objectivesIn order to understand the function of ORF3 protein (pORF3) in depth, HEV ORF3 interacting proteins were screened in human hepatocytes cDNA library using two-hybrid system techniques and further verification of the interactions were carried out through co-immunoprecipitation (Co-IP). MATERIALS AND
methodsThe Cyto-Trap two-hybrid system technology, a classical method for analyzing protein interactions, was used to screen the pORF3 interacting proteins from human hepatocytes cDNA library.
resultsThrough the Cyto-Trap two-hybrid system, eight proteins interacting with pORF3 were winnowed. The Co-IP results confirmed that hepsin which is reported to function as the inhibitor of several tumors reacted with pORF3.
conclusionsOut of eight screened proteins interacting with pORF3, hepsin was confirmed to have specific interactions with pORF3.
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