Evidence map›Paper›PMID 30862673›Full record

ArticleThe Journal of biological chemistry2019

Identification and characterization of potent and selective aquaporin-3 and aquaporin-7 inhibitors.

Yonathan Sonntag, Patrizia Gena, Anna Maggio, Tania Singh, Isabella Artner, Michal K Oklinski, Urban Johanson, Per Kjellbom, John Dirk Nieland, Søren Nielsen and 2 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

39 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. MOMASTAntioxidants (Basel, Switzerland) · 2024
    Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Molecular basis for human aquaporin inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

12 authors at 3 institutions in 3 countries.

Yonathan SonntagFrom the Division of Biochemistry and Structural Biology, Department of Chemistry, Lund University, 22100 Lund, Sweden.
Patrizia Genathe Department of Biosciences, Biotechnologies, and Biopharmaceutics, University of Bari "Aldo Moro," 70125 Bari, Italy.
Anna Maggiothe Department of Biosciences, Biotechnologies, and Biopharmaceutics, University of Bari "Aldo Moro," 70125 Bari, Italy.
Tania Singhthe Stem Cell Center, Lund University, 22184 Lund, Sweden, and.
Isabella Artnerthe Stem Cell Center, Lund University, 22184 Lund, Sweden, and.
Michal K Oklinskithe Department of Health Science and Technology, Aalborg University, 9220 Aalborg, Denmark.
Urban JohansonFrom the Division of Biochemistry and Structural Biology, Department of Chemistry, Lund University, 22100 Lund, Sweden.ORCID 0000-0001-8862-128X
Per KjellbomFrom the Division of Biochemistry and Structural Biology, Department of Chemistry, Lund University, 22100 Lund, Sweden.
John Dirk Nielandthe Department of Health Science and Technology, Aalborg University, 9220 Aalborg, Denmark.
Søren Nielsenthe Department of Health Science and Technology, Aalborg University, 9220 Aalborg, Denmark.
Giuseppe Calamitathe Department of Biosciences, Biotechnologies, and Biopharmaceutics, University of Bari "Aldo Moro," 70125 Bari, Italy.
Michael Rützlerthe Department of Health Science and Technology, Aalborg University, 9220 Aalborg, Denmark miru@hst.aau.dk.ORCID 0000-0001-5597-8880
Lund University · SEAalborg University · DKUniversity of Bari Aldo Moro · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The aquaglyceroporins are a subfamily of aquaporins that conduct both water and glycerol. Aquaporin-3 (AQP3) has an important physiological function in renal water reabsorption, and AQP3-mediated hydrogen peroxide (H

Indexed as

AnimalsAquaporin 3AquaporinsCell Membrane PermeabilityCHO CellsCricetulusErythrocytesGlycerolHumansMiceMolecular Docking SimulationStructure-Activity RelationshipThiophenesWaterAQP3 protein, humanAqp3 protein, mouseAQP7 protein, humanAqp7 protein, mouseAquaporin 3AquaporinsGlycerolThiophenesWateraquaporinaquaporin inhibitorcalceinCHO cell assayglycerolhydrogen peroxideHyPerinhibitormolecular dockingresidual pore

Identifiers

PMID30862673
PMCPMC6509502
OpenAlexW2922259588

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.