Evidence map›Paper›PMID 29936413›Full record

ArticleThe Journal of biological chemistry2018

Mechanical transduction of cytoplasmic-to-transmembrane-domain movements in a hyperpolarization-activated cyclic nucleotide-gated cation channel.

Christine Gross, Andrea Saponaro, Bina Santoro, Anna Moroni, Gerhard Thiel, Kay Hamacher

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Modular architecture of KEMBO reports · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review: HCN Channels in the Heart.Current cardiology reviews · 2022
    Review
  13. Article
  14. Article
  15. IProgress in biophysics and molecular biology · 2021
    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

6 authors at 3 institutions in 3 countries.

Christine GrossComputational Biology and Simulation Group, Technische Universität Darmstadt, 64287 Darmstadt, Germany.
Andrea SaponaroDepartment of Biosciences, University of Milan, 20133 Milan, Italy.
Bina SantoroDepartment of Neuroscience, Columbia University, New York, New York 10032.
Anna MoroniDepartment of Biosciences, University of Milan, 20133 Milan, Italy.
Gerhard ThielMembrane Biophysics, Department of Biology, Technische Universität Darmstadt, 64287 Darmstadt, Germany. Electronic address: thiel@bio.tu-darmstadt.de.
Kay HamacherComputational Biology and Simulation Group, Technische Universität Darmstadt, 64287 Darmstadt, Germany.
Technische Universität Darmstadt · DEUniversity of Milan · ITColumbia University · US

Funding

Regulation of HCN channel trafficking and function in the brain by TRIP8bR01NS036658 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI SIEGELBAUM, STEVEN A · 1998 to 2016
$4.5M
European Research Council 695078NINDS NIH HHS R01 NS036658
6 · The paper itself

Abstract

Hyperpolarization-activated cyclic nucleotide-gated cation (HCN) channels play a critical role in the control of pacemaking in the heart and repetitive firing in neurons. In HCN channels, the intracellular cyclic nucleotide-binding domain (CNBD) is connected to the transmembrane portion of the channel (TMPC) through a helical domain, the C-linker. Although this domain is critical for mechanical signal transduction, the conformational dynamics in the C-linker that transmit the nucleotide-binding signal to the HCN channel pore are unknown. Here, we use linear response theory to analyze conformational changes in the C-linker of the human HCN1 protein, which couple cAMP binding in the CNBD with gating in the TMPC. By applying a force to the tip of the so-called "elbow" of the C-linker, the coarse-grained calculations recapitulate the same conformational changes triggered by cAMP binding in experimental studies. Furthermore, in our simulations, a displacement of the C-linker parallel to the membrane plane (

Indexed as

Models, ChemicalCell MembraneCyclic AMPHumansHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsPotassium ChannelsProtein DomainsCyclic AMPHCN1 protein, humanHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsPotassium Channelsanisotropic network modelcAMP dependent gatingcomputational biologycyclic AMP (cAMP)HCN1 channellinear response theorypotassium channelprotein conformationprotein dynamic

Identifiers

PMID29936413
PMCPMC6102142
OpenAlexW2809334386

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.