Evidence map›Paper›PMID 28864772›Full record

ArticleThe Journal of biological chemistry2017

Mechanism for the inhibition of the cAMP dependence of HCN ion channels by the auxiliary subunit TRIP8b.

John R Bankston, Hannah A DeBerg, Stefan Stoll, William N Zagotta

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  9. IProgress in biophysics and molecular biology · 2021
    Review
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  12. Pulse Dipolar EPR Reveals Double-Histidine Motif CuThe journal of physical chemistry letters · 2021
    Article
  13. Review
  14. Article
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  16. Isoform-specific regulation of HCN4 channels by a family of endoplasmic reticulum proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Review
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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

4 authors at 2 institutions in 2 countries.

John R BankstonFrom the Departments of Physiology and Biophysics and.
Hannah A DeBergFrom the Departments of Physiology and Biophysics and.
Stefan StollChemistry, University of Washington, Seattle, Washington 98195.
William N ZagottaFrom the Departments of Physiology and Biophysics and zagotta@uw.edu.
University of Washington · USInstitute of Molecular Biology and Biophysics · RU

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
GATING MECHANISMS OF RETINAL ROD CGMP-ACTIVATED CHANNELSR01EY010329 · NEI · UNIVERSITY OF WASHINGTON · PI ZAGOTTA, WILLIAM N · 1994 to 2023
$7.7M
Function and regulation of acid-sensing ion channels in corneal neuronsR00EY024267 · NEI · UNIVERSITY OF COLORADO DENVER · PI BANKSTON, JOHN · 2017 to 2019
$747k
Molecular mechanisms for regulation of HCN channels by TRIP8b subunitsR21NS074053 · NINDS · UNIVERSITY OF WASHINGTON · PI ZAGOTTA, WILLIAM N · 2011 to 2012
$429k
Function and regulation of acid-sensing ion channels in corneal neuronsK99EY024267 · NEI · UNIVERSITY OF WASHINGTON · PI BANKSTON, JOHN · 2014 to 2015
$181k
NEI NIH HHS K99 EY024267NEI NIH HHS R00 EY024267NEI NIH HHS R01 EY010329NIGMS NIH HHS P41 GM103311NINDS NIH HHS R21 NS074053
6 · The paper itself

Abstract

TRIP8b, an accessory subunit of hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channels, alters both the cell surface expression and cyclic nucleotide dependence of these channels. However, the mechanism by which TRIP8b exerts these dual effects is still poorly understood. In addition to binding to the carboxyl-terminal tripeptide of HCN channels, TRIP8b also binds directly to the cyclic nucleotide-binding domain (CNBD). That interaction, which requires a small central portion of TRIP8b termed TRIP8b

Indexed as

Cyclic AMPHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsPotassium ChannelsReceptors, Cytoplasmic and NuclearAnimalsBinding SitesHumansProtein DomainsXenopus laevisCyclic AMPHCN2 protein, humanHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsPEX5L protein, humanPotassium ChannelsReceptors, Cytoplasmic and Nuclearcyclic nucleotideelectron paramagnetic resonance (EPR)fluorescence anisotropyinhibition mechanismion channelprotein-protein interaction

Identifiers

PMID28864772
PMCPMC5663879
OpenAlexW2750707643

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.