Evidence map›Paper›PMID 19297321›Full record

ArticleThe Journal of biological chemistry2009

Hepatitis C virus NS5A protein is a substrate for the peptidyl-prolyl cis/trans isomerase activity of cyclophilins A and B.

Xavier Hanoulle, Aurélie Badillo, Jean-Michel Wieruszeski, Dries Verdegem, Isabelle Landrieu, Ralf Bartenschlager, François Penin, Guy Lippens

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

98 citing papers in PubMed, 162 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. PIN1 and PIN4 inhibitionFrontiers in microbiology · 2023
    Article
  10. Non-Immunosuppressive Cyclophilin Inhibitors.Angewandte Chemie (International ed. in English) · 2022
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. The Role of Cyclophilins in Inflammatory Bowel Disease and Colorectal Cancer.International journal of biological sciences · 2021
    Review
  18. Article
  19. Article
  20. Article

38 more citing papers are in PubMed but not listed here.

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

8 authors at 3 institutions in 2 countries.

Xavier HanoulleUnité de Glycobiologie Structurale et Fonctionnelle, UMR 8576 CNRS, IFR 147, Université des Sciences et Technologies de Lille, F-59655 Villeneuve d'Ascq, France.
Aurélie BadilloInstitut de Biologie et Chimie des Protéines, UMR 5086, CNRS, Université de Lyon, IFR 128, BioSciences Gerland-Lyon Sud, F-69397 Lyon, France.
Jean-Michel WieruszeskiUnité de Glycobiologie Structurale et Fonctionnelle, UMR 8576 CNRS, IFR 147, Université des Sciences et Technologies de Lille, F-59655 Villeneuve d'Ascq, France.
Dries VerdegemUnité de Glycobiologie Structurale et Fonctionnelle, UMR 8576 CNRS, IFR 147, Université des Sciences et Technologies de Lille, F-59655 Villeneuve d'Ascq, France.
Isabelle LandrieuUnité de Glycobiologie Structurale et Fonctionnelle, UMR 8576 CNRS, IFR 147, Université des Sciences et Technologies de Lille, F-59655 Villeneuve d'Ascq, France.
Ralf BartenschlagerDepartment of Molecular Virology, University of Heidelberg, Im Neuenheimer Feld 345, 69120 Heidelberg, Germany.
François PeninInstitut de Biologie et Chimie des Protéines, UMR 5086, CNRS, Université de Lyon, IFR 128, BioSciences Gerland-Lyon Sud, F-69397 Lyon, France.
Guy LippensUnité de Glycobiologie Structurale et Fonctionnelle, UMR 8576 CNRS, IFR 147, Université des Sciences et Technologies de Lille, F-59655 Villeneuve d'Ascq, France. Electronic address: guy.lippens@univ-lille1.fr.
Centre National de la Recherche Scientifique · FRUniversité Claude Bernard Lyon 1 · FRHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We report here a biochemical and structural characterization of domain 2 of the nonstructural 5A protein (NS5A) from the JFH1 Hepatitis C virus strain and its interactions with cyclophilins A and B (CypA and CypB). Gel filtration chromatography, circular dichroism spectroscopy, and finally NMR spectroscopy all indicate the natively unfolded nature of this NS5A-D2 domain. Because mutations in this domain have been linked to cyclosporin A resistance, we used NMR spectroscopy to investigate potential interactions between NS5A-D2 and cellular CypA and CypB. We observed a direct molecular interaction between NS5A-D2 and both cyclophilins. The interaction surface on the cyclophilins corresponds to their active site, whereas on NS5A-D2, it proved to be distributed over the many proline residues of the domain. NMR heteronuclear exchange spectroscopy yielded direct evidence that many proline residues in NS5A-D2 form a valid substrate for the enzymatic peptidyl-prolyl cis/trans isomerase (PPIase) activity of CypA and CypB.

Indexed as

Cyclophilin ACyclophilinsHepacivirusHumansMutationNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Structure, TertiaryRecombinant ProteinsRNA-Dependent RNA PolymeraseViral Nonstructural ProteinsCyclophilin Acyclophilin BCyclophilinsNS-5 protein, hepatitis C virusRecombinant ProteinsRNA-Dependent RNA PolymeraseViral Nonstructural Proteins

Identifiers

PMID19297321
PMCPMC2679460
OpenAlexW2095124892

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.