Evidence map›Paper›PMID 7479756›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

Subunit interactions in coordination of Ni2+ in cyclic nucleotide-gated channels.

S E Gordon, W N Zagotta

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

51 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
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  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Insulin receptor regulates photoreceptor CNG channel activity.American journal of physiology. Endocrinology and metabolism · 2012
    Article
  11. Gating in CNGA1 channels.Pflugers Archiv : European journal of physiology · 2010
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  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

2 authors at 1 institution in 1 country.

S E GordonDepartment of Physiology and Biophysics, Howard Hughes Medical Institute, University of Washington School of Medicine, Seattle 98195-7290, USA.
W N Zagotta
Howard Hughes Medical Institute · US

Funding

GATING MECHANISMS OF RETINAL ROD CGMP-ACTIVATED CHANNELSR01EY010329 · NEI · UNIVERSITY OF WASHINGTON · PI ZAGOTTA, WILLIAM N · 1994 to 2023
$7.7M
NEI NIH HHS EY10329NEI NIH HHS R01 EY010329
6 · The paper itself

Abstract

Cyclic nucleotide-gated (CNG) channels present a unique model for studying the molecular mechanisms of channel gating. We have studied the mechanism of potentiation of expressed rod CNG channels by Ni2+ as a first step toward understanding the channel gating process. Here we report that coordination of Ni2+ between histidine residues (H420) on adjacent channel subunits occurs when the channels are open. Mutation of H420 to lysine completely eliminated the potentiation by Ni2+ but did not markedly alter the apparent cGMP affinity of the channel, indicating that the introduction of positive charge at the Ni(2+)-binding site was not sufficient to produce potentiation. Deletion or mutation of most of the other histidines present in the channel did not diminish potentiation by Ni2+. We studied the role of subunit interactions in Ni2+ potentiation by generating heteromultimeric channels using tandem dimers of the rod CNG channel sequence. Injection of single heterodimers in which one subunit contained H420 and the other did not (wt/H420Q or H420Q/wt) resulted in channels that were not potentiated by Ni2+. However, coinjection of both heterodimers into Xenopus oocytes resulted in channels that exhibited potentiation. The H420 residues probably occurred predominantly in nonadjacent subunits when each heterodimer was injected individually, but, when the two heterodimers were coinjected, the H420 residues could occur in adjacent subunits as well. These results suggest that the mechanism of Ni2+ potentiation involves intersubunit coordination of Ni2+ by H420. Based on the preferential binding of Ni2+ to open channels, we suggest that alignment of H420 residues of neighboring subunits into the Ni(2+)-coordinating position may be associated with channel opening.

Indexed as

Amino Acid SequenceAnimalsCattleCyclic Nucleotide-Gated Cation ChannelsEye ProteinsFemaleIon ChannelsMacromolecular SubstancesMembrane PotentialsModels, StructuralMolecular Sequence DataNickelOocytesPolymerase Chain ReactionProtein Structure, SecondaryRecombinant ProteinsCyclic Nucleotide-Gated Cation ChannelsEye ProteinsIon ChannelsMacromolecular SubstancesNickelRecombinant Proteins

Identifiers

PMID7479756
PMCPMC40768
OpenAlexW1990657957

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.