Evidence map›Paper›PMID 23525108›Full record

ArticleThe Journal of biological chemistry2013

A secondary structural transition in the C-helix promotes gating of cyclic nucleotide-regulated ion channels.

Michael C Puljung, William N Zagotta

Open access · hybridAbstract 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 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021
    Review
  3. Article
  4. Allosteric conformational change of a cyclic nucleotide-gated ion channel revealed by DEER spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Transition metal ion FRET uncovers KNature communications · 2016
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Dynamic measurements for funny channels.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

2 authors at 1 institution in 1 country.

Michael C PuljungDepartment of Physiology and Biophysics, University of Washington, Seattle, Washington 98195-7290, USA.
William N Zagotta
University 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
CNG Channel Gating Movements Monitored via Fluorescene QuenchingF32EY018981 · NEI · UNIVERSITY OF WASHINGTON · PI PULJUNG, MICHAEL C · 2008 to 2009
$105k
NEI NIH HHS F32 EY018981NEI NIH HHS F32EY018981NEI NIH HHS R01 EY010329
6 · The paper itself

Abstract

Cyclic nucleotide-regulated ion channels bind second messengers like cAMP to a C-terminal domain, consisting of a β-roll, followed by two α-helices (B- and C-helices). We monitored the cAMP-dependent changes in the structure of the C-helix of a C-terminal fragment of HCN2 channels using transition metal ion FRET between fluorophores on the C-helix and metal ions bound between histidine pairs on the same helix. cAMP induced a change in the dimensions of the C-helix and an increase in the metal binding affinity of the histidine pair. cAMP also caused an increase in the distance between a fluorophore on the C-helix and metal ions bound to the B-helix. Stabilizing the C-helix of intact CNGA1 channels by metal binding to a pair of histidines promoted channel opening. These data suggest that ordering of the C-helix is part of the gating conformational change in cyclic nucleotide-regulated channels.

Indexed as

AnimalsCattleCyclic AMPCyclic Nucleotide-Gated Cation ChannelsHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsIon Channel GatingIon ChannelsIon TransportMetalsMicePotassium ChannelsProtein StabilityProtein Structure, SecondaryCnga1 protein, mouseCyclic AMPCyclic Nucleotide-Gated Cation ChannelsHcn2 protein, mouseHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsIon ChannelsMetalsPotassium ChannelsAllosteric RegulationCyclic AMP (cAMP)FluorescenceFluorescence Resonance Energy Transfer (FRET)Ion Channels

Identifiers

PMID23525108
PMCPMC3642337
OpenAlexW2167946665

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.