Evidence map›Paper›PMID 23801332›Full record

ArticleThe Journal of biological chemistry2013

Sea anemone peptide with uncommon β-hairpin structure inhibits acid-sensing ion channel 3 (ASIC3) and reveals analgesic activity.

Dmitry I Osmakov, Sergey A Kozlov, Yaroslav A Andreev, Sergey G Koshelev, Nadezhda P Sanamyan, Karen E Sanamyan, Igor A Dyachenko, Dmitry A Bondarenko, Arkadii N Murashev, Konstantin S Mineev and 2 more

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Cnidarian toxins: omics approaches and recombinant proteins.The journal of venomous animals and toxins including tropical diseases · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Isolation and cDNA cloning of four peptide toxins from the sea anemoneThe journal of venomous animals and toxins including tropical diseases · 2024
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
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.

Dmitry I OsmakovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, 117997 Moscow.
Sergey A Kozlov
Yaroslav A Andreev
Sergey G Koshelev
Nadezhda P Sanamyan
Karen E Sanamyan
Igor A Dyachenko
Dmitry A Bondarenko
Arkadii N Murashev
Konstantin S Mineev
Alexander S Arseniev
Eugene V Grishin

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Three novel peptides were isolated from the venom of the sea anemone Urticina grebelnyi. All of them are 29 amino acid peptides cross-linked by two disulfide bridges, with a primary structure similar to other sea anemone peptides belonging to structural group 9a. The structure of the gene encoding the shared precursor protein of the identified peptides was determined. One peptide, π-AnmTX Ugr 9a-1 (short name Ugr 9-1), produced a reversible inhibition effect on both the transient and the sustained current of human ASIC3 channels expressed in Xenopus laevis oocytes. It completely blocked the transient component (IC50 10 ± 0.6 μM) and partially (48 ± 2%) inhibited the amplitude of the sustained component (IC50 1.44 ± 0.19 μM). Using in vivo tests in mice, Ugr 9-1 significantly reversed inflammatory and acid-induced pain. The other two novel peptides, AnmTX Ugr 9a-2 (Ugr 9-2) and AnmTX Ugr 9a-3 (Ugr 9-3), did not inhibit the ASIC3 current. NMR spectroscopy revealed that Ugr 9-1 has an uncommon spatial structure, stabilized by two S-S bridges, with three classical β-turns and twisted β-hairpin without interstrand disulfide bonds. This is a novel peptide spatial structure that we propose to name boundless β-hairpin.

Indexed as

AnalgesicsPeptidesSea AnemonesAcid Sensing Ion ChannelsAmino Acid SequenceAnimalsHumansMaleMiceMolecular Sequence DataPainProtein Structure, SecondaryXenopus laevisAcid Sensing Ion ChannelsAnalgesicsASIC3 protein, humanASIC3 protein, mousePeptidesAcid Sensing Ion Channels (ASIC)Gene StructureNuclear Magnetic ResonancePeptidesProtein ChemistryProtein PurificationProtein SequenceProtein Structure

Identifiers

PMID23801332
PMCPMC3743484

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.