Evidence map›Paper›PMID 27026701›Full record

ArticleThe Journal of biological chemistry2016

Development of a μO-Conotoxin Analogue with Improved Lipid Membrane Interactions and Potency for the Analgesic Sodium Channel NaV1.8.

Jennifer R Deuis, Zoltan Dekan, Marco C Inserra, Tzong-Hsien Lee, Marie-Isabel Aguilar, David J Craik, Richard J Lewis, Paul F Alewood, Mehdi Mobli, Christina I Schroeder and 2 more

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
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. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. A novel proline-rich M-superfamily conotoxin that can simultaneously affect sodium, potassium and calcium currents.The journal of venomous animals and toxins including tropical diseases · 2021
    Article
  8. Article
  9. Mapping the Molecular Surface of the Analgesic NaACS pharmacology & translational science · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Sodium channels and pain: from toxins to therapies.British journal of pharmacology · 2018
    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

12 authors.

Jennifer R DeuisFrom the Institute for Molecular Bioscience and School of Pharmacy, The University of Queensland, Woolloongabba, Queensland 4102, Australia, and.
Zoltan DekanFrom the Institute for Molecular Bioscience and.
Marco C InserraFrom the Institute for Molecular Bioscience and School of Pharmacy, The University of Queensland, Woolloongabba, Queensland 4102, Australia, and.
Tzong-Hsien LeeDepartment of Biochemistry and Molecular Biology, Monash University, Wellington Road, Clayton, Victoria 3800, Australia.
Marie-Isabel AguilarDepartment of Biochemistry and Molecular Biology, Monash University, Wellington Road, Clayton, Victoria 3800, Australia.
David J CraikFrom the Institute for Molecular Bioscience and.
Richard J LewisFrom the Institute for Molecular Bioscience and.
Paul F AlewoodFrom the Institute for Molecular Bioscience and.
Mehdi MobliCentre for Advanced Imaging, The University of Queensland, St. Lucia, Queensland 4072, Australia.
Christina I SchroederFrom the Institute for Molecular Bioscience and c.schroeder@imb.uq.edu.au.
Sónia Troeira HenriquesFrom the Institute for Molecular Bioscience and s.henriques@imb.uq.edu.au.
Irina VetterFrom the Institute for Molecular Bioscience and School of Pharmacy, The University of Queensland, Woolloongabba, Queensland 4102, Australia, and i.vetter@uq.edu.au.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The μO-conotoxins MrVIA, MrVIB, and MfVIA inhibit the voltage-gated sodium channel NaV1.8, a well described target for the treatment of pain; however, little is known about the residues or structural elements that define this activity. In this study, we determined the three-dimensional structure of MfVIA, examined its membrane binding properties, performed alanine-scanning mutagenesis, and identified residues important for its activity at human NaV1.8. A second round of mutations resulted in (E5K,E8K)MfVIA, a double mutant with greater positive surface charge and greater affinity for lipid membranes compared with MfVIA. This analogue had increased potency at NaV1.8 and was analgesic in the mouse formalin assay.

Indexed as

Amino Acid SequenceAnalgesicsAnimalsBehavior, AnimalCell MembraneConotoxinsCrystallography, X-RayElectrophysiologyHEK293 CellsHumansLiposomesMagnetic Resonance SpectroscopyMaleMiceMice, Inbred C57BLMolecular Sequence DataAnalgesicsConotoxinsLiposomesmuO-conotoxin MrVIANAV1.8 Voltage-Gated Sodium Channellipid-protein interactionmutagenesisNaV1.8painpeptide chemical synthesissodium channelstructure-activity relationshipsμO-conotoxin MfVIA

Identifiers

PMID27026701
PMCPMC4882450

What OpenQuestion holds

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Registered trials

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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.