Evidence map›Paper›PMID 12432397›Full record

ArticleNature2002

The heteromeric cyclic nucleotide-gated channel adopts a 3A:1B stoichiometry.

Haining Zhong, Laurie L Molday, Robert S Molday, King-Wai Yau

Open access · greenAbstract read
In one paragraph

Article in Nature, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

122 citing papers in PubMed, 251 citations in OpenAlex.

  1. Article
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  6. Article
  7. Review
  8. Review
  9. Article
  10. Development of a translatable gene augmentation therapy for CNGB1-retinitis pigmentosa.Molecular therapy : the journal of the American Society of Gene Therapy · 2023
    Article
  11. Structural basis of calmodulin modulation of the rod cyclic nucleotide-gated channel.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Review
  13. Photoreceptor Ion Channels in Signaling and Disease.Advances in experimental medicine and biology · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

62 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

4 authors at 3 institutions in 2 countries.

Haining ZhongDepartment of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Laurie L Molday
Robert S Molday
King-Wai Yau
University of British Columbia · CAHoward Hughes Medical Institute · USJohns Hopkins Medicine · US

Funding

VISUAL TRANSDUCTION IN RETINAL PHOTORECEPTORSR37EY006837 · NEI · JOHNS HOPKINS UNIVERSITY · PI YAU, KING-WAI · 1992 to 2002
$822k
NEI NIH HHS R37 EY006837
6 · The paper itself

Abstract

Cyclic nucleotide-gated (CNG) channels are crucial for visual and olfactory transductions. These channels are tetramers and in their native forms are composed of A and B subunits, with a stoichiometry thought to be 2A:2B (refs 6, 7). Here we report the identification of a leucine-zipper-homology domain named CLZ (for carboxy-terminal leucine zipper). This domain is present in the distal C terminus of CNG channel A subunits but is absent from B subunits, and mediates an inter-subunit interaction. With cross-linking, non-denaturing gel electrophoresis and analytical centrifugation, this CLZ domain was found to mediate a trimeric interaction. In addition, a mutant cone CNG channel A subunit with its CLZ domain replaced by a generic trimeric leucine zipper produced channels that behaved much like the wild type, but less so if replaced by a dimeric or tetrameric leucine zipper. This A-subunit-only, trimeric interaction suggests that heteromeric CNG channels actually adopt a 3A:1B stoichiometry. Biochemical analysis of the purified bovine rod CNG channel confirmed this conclusion. This revised stoichiometry provides a new foundation for understanding the structure and function of the CNG channel family.

Indexed as

Amino Acid SequenceAnimalsCattleCell LineCentrifugationChromatography, GelCross-Linking ReagentsCyclic Nucleotide-Gated Cation ChannelsHumansIon ChannelsLeucine ZippersMiceMolecular Sequence DataMutationPrecipitin TestsProtein BindingCross-Linking ReagentsCyclic Nucleotide-Gated Cation ChannelsIon ChannelsProtein Subunits

Identifiers

PMID12432397
PMCPMC2877395
OpenAlexW2006307429

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.