Evidence map›Paper›PMID 30076228›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Insights into the molecular mechanism for hyperpolarization-dependent activation of HCN channels.

Galen E Flynn, William N Zagotta

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

41 citing papers in PubMed, 68 citations in OpenAlex.

  1. Review
  2. Article
  3. Roles of funny HCN.Comparative biochemistry and physiology. Toxicology & pharmacology : CBP · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
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  10. Review
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  13. Review
  14. Article
  15. Fifty years of gating currents and channel gating.The Journal of general physiology · 2023
    Review
  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

2 authors at 1 institution in 1 country.

Galen E FlynnDepartment of Physiology and Biophysics, University of Washington, Seattle, WA 98195 galen@uw.edu.ORCID 0000-0001-7813-578X
William N ZagottaDepartment of Physiology and Biophysics, University of Washington, Seattle, WA 98195.ORCID 0000-0002-7631-8168
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
Regulation of KCNH ion channelsR01MH102378 · NIMH · UNIVERSITY OF WASHINGTON · PI ZAGOTTA, WILLIAM N · 2014 to 2018
$1.9M
NEI NIH HHS R01 EY010329NIMH NIH HHS R01 MH102378
6 · The paper itself

Abstract

Hyperpolarization-activated, cyclic nucleotide-gated (HCN) ion channels are both voltage- and ligand-activated membrane proteins that contribute to electrical excitability and pace-making activity in cardiac and neuronal cells. These channels are members of the voltage-gated Kv channel superfamily and cyclic nucleotide-binding domain subfamily of ion channels. HCN channels have a unique feature that distinguishes them from other voltage-gated channels: the HCN channel pore opens in response to hyperpolarizing voltages instead of depolarizing voltages. In the canonical model of electromechanical coupling, based on Kv channels, a change in membrane voltage activates the voltage-sensing domains (VSD) and the activation energy passes to the pore domain (PD) through a covalent linker that connects the VSD to the PD. In this investigation, the covalent linkage between the VSD and PD, the S4-S5 linker, and nearby regions of spHCN channels were mutated to determine the functional role each plays in hyperpolarization-dependent activation. The results show that: (

Indexed as

Ion Channel GatingAnimalsCyclic Nucleotide-Gated Cation ChannelsProtein DomainsSea UrchinsStructure-Activity RelationshipCyclic Nucleotide-Gated Cation Channelsallosterycyclic nucleotide-gatedpatch-clampSpIHvoltage-dependent gating

Identifiers

PMID30076228
PMCPMC6112743
OpenAlexW2887526852

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.