Evidence map›Paper›PMID 18931410›Full record

ArticleActa crystallographica. Section D, Biological crystallography2008

Structures of pseudechetoxin and pseudecin, two snake-venom cysteine-rich secretory proteins that target cyclic nucleotide-gated ion channels: implications for movement of the C-terminal cysteine-rich domain.

Nobuhiro Suzuki, Yasuo Yamazaki, R Lane Brown, Zui Fujimoto, Takashi Morita, Hiroshi Mizuno

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

28 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Toxins · 2019
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Positive Selection in the Evolution of Mammalian CRISPs.Journal of molecular evolution · 2018
    Article
  13. Article
  14. Article
  15. Actiflagelin, a new sperm activator isolated fromThe journal of venomous animals and toxins including tropical diseases · 2018
    Article
  16. Article
  17. Article
  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

6 authors at 5 institutions in 2 countries.

Nobuhiro SuzukiDepartment of Applied Biochemistry, University of Tsukuba, Tsukuba, Ibaraki 305-8572, Japan.
Yasuo Yamazaki
R Lane Brown
Zui Fujimoto
Takashi Morita
Hiroshi Mizuno
Meiji Pharmaceutical University · JPInstitute of Agrobiological Sciences · JPNational Institute of Advanced Industrial Science and Technology · JPOregon Health & Science University · USUniversity of Tsukuba · JP

Funding

Generation of Retinal Signals for Circadian EntrainmentR01MH067094 · NIMH · WASHINGTON STATE UNIVERSITY · PI BROWN, RONALD LANE · 2003 to 2007
$1.6M
NIMH NIH HHS MH67094NIMH NIH HHS R01 MH067094
6 · The paper itself

Abstract

Cyclic nucleotide-gated (CNG) ion channels play pivotal roles in sensory transduction by retinal photoreceptors and olfactory neurons. The elapid snake toxins pseudechetoxin (PsTx) and pseudecin (Pdc) are the only known protein blockers of CNG channels. These toxins belong to a cysteine-rich secretory protein (CRISP) family containing an N-terminal pathogenesis-related proteins of group 1 (PR-1) domain and a C-terminal cysteine-rich domain (CRD). PsTx and Pdc are highly homologous proteins, but their blocking affinities on CNG channels are different: PsTx blocks both the olfactory and retinal channels with approximately 15-30-fold higher affinity than Pdc. To gain further insights into their structure and function, the crystal structures of PsTx, Pdc and Zn2+-bound Pdc were determined. The structures revealed that most of the amino-acid-residue differences between PsTx and Pdc are located around the concave surface formed between the PR-1 domain and the CRD, suggesting that the concave surface is functionally important for CNG-channel binding and inhibition. A structural comparison in the presence and absence of Zn2+ ion demonstrated that the concave surface can open and close owing to movement of the CRD upon Zn2+ binding. The data suggest that PsTx and Pdc occlude the pore entrance and that the dynamic motion of the concave surface facilitates interaction with the CNG channels.

Indexed as

Ion Channel GatingAmino Acid SequenceCell LineCrystallography, X-RayCysteineHumansIon ChannelsModels, MolecularMolecular Sequence DataProtein ConformationSequence Homology, Amino AcidSnake VenomsCysteineIon Channelspseudechetoxin, Pseudechis australisSnake Venoms

Identifiers

PMID18931410
PMCPMC2725782
OpenAlexW1980835782

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.