Evidence map›Paper›PMID 19671703›Full record

ArticleThe Journal of biological chemistry2009

Absence of direct cyclic nucleotide modulation of mEAG1 and hERG1 channels revealed with fluorescence and electrophysiological methods.

Tinatin I Brelidze, Anne E Carlson, William N Zagotta

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

74 citing papers in PubMed, 99 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. A Historical Outline of Fluorescence Spectroscopy in Ion Channel Research.Advances in experimental medicine and biology · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. The ERG1 KFrontiers in molecular neuroscience · 2022
    Review
  11. Conformation-sensitive antibody reveals an altered cytosolic PAS/CNBh assembly during hERG channel gating.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. hERG Function in Light of Structure.Biophysical journal · 2020
    Review
  18. Article
  19. Article
  20. Article

14 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

3 authors at 2 institutions in 1 country.

Tinatin I BrelidzeDepartment of Physiology and Biophysics, University of Washington School of Medicine, Seattle, Washington 98195; Howard Hughes Medical Institute, University of Washington, Seattle, Washington 98195.
Anne E CarlsonDepartment of Physiology and Biophysics, University of Washington School of Medicine, Seattle, Washington 98195.
William N ZagottaDepartment of Physiology and Biophysics, University of Washington School of Medicine, Seattle, Washington 98195; Howard Hughes Medical Institute, University of Washington, Seattle, Washington 98195. Electronic address: zagotta@u.washington.edu.
Howard Hughes Medical Institute · USUniversity of Washington · US

Funding

GATING MECHANISMS OF RETINAL ROD CGMP-ACTIVATED CHANNELSR01EY010329 · NEI · UNIVERSITY OF WASHINGTON · PI ZAGOTTA, WILLIAM N · 1994 to 2023
$7.7M
A Regulator for Eag Family ChannelsF32HL095241 · NHLBI · UNIVERSITY OF WASHINGTON · PI CARLSON, ANNE E · 2009 to 2011
$156k
Howard Hughes Medical InstituteNEI NIH HHS 2R01EY010329-16NEI NIH HHS R01 EY010329NHLBI NIH HHS F32 HL095241
6 · The paper itself

Abstract

Similar to CNG and HCN channels, EAG and ERG channels contain a cyclic nucleotide binding domain (CNBD) in their C terminus. While cyclic nucleotides have been shown to facilitate opening of CNG and HCN channels, their effect on EAG and ERG channels is less clear. Here we explored cyclic nucleotide binding and modulation of mEAG1 and hERG1 channels with fluorescence and electrophysiology. Binding of cyclic nucleotides to the isolated CNBD of mEAG1 and hERG1 channels was examined with two independent fluorescence-based methods: changes in tryptophan fluorescence and fluorescence of an analog of cAMP, 8-NBD-cAMP. As a positive control for cyclic nucleotide binding we used changes in the fluorescence of the isolated CNBD of mHCN2 channels. Our results indicated that cyclic nucleotides do not bind to the isolated CNBD domain of mEAG1 channels and bind with low affinity (K(d) > or = 51 microm) to the isolated CNBD of hERG1 channels. Consistent with the results on the isolated CNBD, application of cyclic nucleotides to inside-out patches did not affect currents recorded from mEAG1 channels. Surprisingly, despite its low affinity binding to the isolated CNBD, cAMP also had no effect on currents from hERG1 channels even at high concentrations. Our results indicate that cyclic nucleotides do not directly modulate mEAG1 and hERG1 channels. Further studies are necessary to determine if the CNBD in the EAG family of K(+) channels might harbor a binding site for a ligand yet to be uncovered.

Indexed as

Amino Acid SequenceAnimalsCyclic AMPCyclic GMPERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsHumansIon Channel GatingMiceModels, MolecularMolecular Sequence DataPatch-Clamp TechniquesProtein BindingProtein IsoformsProtein Structure, SecondaryProtein Structure, TertiaryCyclic AMPCyclic GMPERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsKcnh1 protein, mouseKcnh2 protein, mouseProtein Isoforms

Identifiers

PMID19671703
PMCPMC2788851
OpenAlexW2041958683

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.