Evidence map›Paper›PMID 28446610›Full record

ArticleThe Journal of biological chemistry2017

Conformational changes at cytoplasmic intersubunit interactions control Kir channel gating.

Shizhen Wang, William F Borschel, Sarah Heyman, Phillip Hsu, Colin G Nichols

Open access · hybridAbstract readComparative Study
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 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.2field-weighted citation impact, top 45% 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

8 citing papers in PubMed, 7 citations in OpenAlex.

  1. Molecular mechanisms of Kir channel gating.Biochemical Society transactions · 2026
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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

5 authors at 1 institution in 1 country.

Shizhen WangFrom the Department of Cell Biology and Physiology and the Center for the Investigation of Membrane Excitability Diseases, Washington University School of Medicine, St. Louis, Missouri 63110.
William F BorschelFrom the Department of Cell Biology and Physiology and the Center for the Investigation of Membrane Excitability Diseases, Washington University School of Medicine, St. Louis, Missouri 63110.
Sarah HeymanFrom the Department of Cell Biology and Physiology and the Center for the Investigation of Membrane Excitability Diseases, Washington University School of Medicine, St. Louis, Missouri 63110.
Phillip HsuFrom the Department of Cell Biology and Physiology and the Center for the Investigation of Membrane Excitability Diseases, Washington University School of Medicine, St. Louis, Missouri 63110.
Colin G NicholsFrom the Department of Cell Biology and Physiology and the Center for the Investigation of Membrane Excitability Diseases, Washington University School of Medicine, St. Louis, Missouri 63110 cnichols@wustl.edu.
Washington University in St. Louis · US

Funding

Rectification &Block of Ion Channel CurrentsR01HL054171 · NHLBI · WASHINGTON UNIVERSITY · PI NICHOLS, COLIN G · 1995 to 2017
$4.5M
Pediatric Cardiovascular and Pulmonary Research Training Program.T32HL125241 · NHLBI · WASHINGTON UNIVERSITY · PI Juliane Bubeck Wardenburg, Kory J. Lavine · 2015 to 2026
$4.1M
NHLBI NIH HHS R01 HL054171
6 · The paper itself

Abstract

The defining structural feature of inward-rectifier potassium (Kir) channels is the unique Kir cytoplasmic domain. Recently we showed that salt bridges located at the cytoplasmic domain subunit interfaces (CD-Is) of eukaryotic Kir channels control channel gating via stability of a novel inactivated closed state. The cytoplasmic domains of prokaryotic and eukaryotic Kir channels show similar conformational rearrangements to the common gating ligand, phosphatidylinositol bisphosphate (PIP

Indexed as

Models, MolecularAmino Acid SubstitutionBacterial ProteinsBinding SitesBurkholderia pseudomalleiDimerizationKineticsLigandsLipid BilayersLiposomesMutationPhosphatidylinositol 4,5-DiphosphatePotassium Channels, Inwardly RectifyingProtein ConformationProtein Conformation, beta-StrandProtein Interaction Domains and MotifsBacterial ProteinsKCNJ2 protein, humanLigandsLipid BilayersLiposomesPhosphatidylinositol 4,5-DiphosphatePotassium Channels, Inwardly RectifyingRecombinant Fusion ProteinsRecombinant Proteinsfluorescence resonance energy transfer (FRET)gatingmembrane transporter reconstitutionphosphatidylinositolpotassium channel

Identifiers

PMID28446610
PMCPMC5473215
OpenAlexW2609662130

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.