Evidence map›Paper›PMID 26445091›Full record

ArticleBritish journal of pharmacology2016

Identification of a resveratrol tetramer as a potent inhibitor of hepatitis C virus helicase.

Sungjin Lee, Kee Dong Yoon, Myungeun Lee, Yoojin Cho, Gahee Choi, Hongje Jang, BeomSeok Kim, Da-Hee Jung, Jin-Gyo Oh, Geon-Woo Kim and 8 more

Open access · bronzeAbstract read
In one paragraph

Article in British journal of pharmacology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 13% 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

20 citing papers in PubMed, 1 synthesis or guideline pooled it, 47 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Fighting coronaviruses with natural polyphenols.Biocatalysis and agricultural biotechnology · 2021
    Article
  7. Article
  8. Review
  9. Grapevine as a Rich Source of Polyphenolic Compounds.Molecules (Basel, Switzerland) · 2020
    Review
  10. Review
  11. Natural and nature-inspired stilbenoids as antiviral agents.European journal of medicinal chemistry · 2020
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Resveratrol: How Much Wine Do You Have to Drink to Stay Healthy?Advances in nutrition (Bethesda, Md.) · 2016
    Review
  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

18 authors at 7 institutions in 1 country.

Sungjin LeeCollege of Pharmacy, Dongguk University, Goyang, Korea.
Kee Dong YoonCollege of Pharmacy and Integrated Research Institute of Pharmaceutical Sciences, The Catholic University of Korea, Bucheon, Korea.
Myungeun LeeHepatitis Research Laboratory, Institut Pasteur Korea, Seongnam, Korea.
Yoojin ChoHepatitis Research Laboratory, Institut Pasteur Korea, Seongnam, Korea.
Gahee ChoiHepatitis Research Laboratory, Institut Pasteur Korea, Seongnam, Korea.
Hongje JangDepartment of Chemistry, Seoul National University, Seoul, Korea.
BeomSeok KimTranslational Research Center for Protein Function Control, Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul, Korea.
Da-Hee JungDepartment of Bio and Nano Chemistry, Kookmin University, Seoul, Korea.
Jin-Gyo OhCollege of Pharmacy and Integrated Research Institute of Pharmaceutical Sciences, The Catholic University of Korea, Bucheon, Korea.
Geon-Woo KimDepartment of Biotechnology, Yonsei University, Seoul, Korea.
Jong-Won OhDepartment of Biotechnology, Yonsei University, Seoul, Korea.
Yong-Joo JeongDepartment of Bio and Nano Chemistry, Kookmin University, Seoul, Korea.
Ho Jeong KwonTranslational Research Center for Protein Function Control, Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul, Korea.
Soo Kyung BaeCollege of Pharmacy and Integrated Research Institute of Pharmaceutical Sciences, The Catholic University of Korea, Bucheon, Korea.
Dal-Hee MinDepartment of Chemistry, Seoul National University, Seoul, Korea.
Marc P WindischHepatitis Research Laboratory, Institut Pasteur Korea, Seongnam, Korea.
Tae-Hwe HeoCollege of Pharmacy and Integrated Research Institute of Pharmaceutical Sciences, The Catholic University of Korea, Bucheon, Korea.
Choongho LeeCollege of Pharmacy, Dongguk University, Goyang, Korea.
Catholic University of Korea · KRInstitut Pasteur Korea · KRDongguk University · KRKookmin University · KRSeoul National University · KRYonsei Proteome Research Center · KRYonsei University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

background and purposeHepatitis C virus (HCV) infection is responsible for various chronic inflammatory liver diseases. Here, we have identified a naturally occurring compound with anti-HCV activity and have elucidated its mode of antiviral action. EXPERIMENTAL APPROACH: Luciferase reporter and real-time RT-PCR assays were used to measure HCV replication. Western blot, fluorescence-labelled HCV replicons and infectious clones were employed to quantitate expression levels of viral proteins. Resistant HCV mutant mapping, in vitro NS3 protease, helicase, NS5B polymerase and drug affinity responsive target stability assays were also used to study the antiviral mechanism. KEY

resultsA resveratrol tetramer, vitisin B from grapevine root extract showed high potency against HCV replication (EC50 = 6 nM) with relatively low cytotoxicity (EC50 >10 μM). Combined treatment of vitisin B with an NS5B polymerase inhibitor (sofosbuvir) exhibited a synergistic or at least additive antiviral activity. Analysis of a number of vitisin B-resistant HCV variants suggested an NS3 helicase as its potential target. We confirmed a direct binding between vitisin B and a purified NS3 helicase in vitro. Vitisin B was a potent inhibitor of a HCV NS3 helicase (IC50 = 3 nM). In vivo, Finally, we observed a preferred tissue distribution of vitisin B in the liver after i.p. injection in rats, at clinically attainable concentrations. Conclusion and Implications Vitisin B is one of the most potent HCV helicase inhibitors identified so far. Vitisin B is thus a prime candidate to be developed as the first HCV drug derived from natural products.

Indexed as

AnimalsBenzofuransBiological ProductsCell LineCell SurvivalDEAD-box RNA HelicasesDose-Response Relationship, DrugDrug SynergismFlavonoidsHepacivirusHumansNucleoside-TriphosphatasePhenolsProtein BindingRatsResveratrolampelopsinBenzofuransBiological ProductsDEAD-box RNA Helicasesepsilon-viniferinFlavonoidsmalvidin-3-O-glucoside-4 vinylNS3 protein, hepatitis C virusNS-5 protein, hepatitis C virusNucleoside-TriphosphatasePhenolsResveratrolRNA-Dependent RNA PolymeraseRNA HelicasesSerine EndopeptidasesSofosbuvirStilbenesViral Nonstructural ProteinsViral Proteasesvitisin Awilsonol C

Identifiers

PMID26445091
PMCPMC4813382
OpenAlexW1811003528

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.