Evidence map›Paper›PMID 19481093›Full record

ArticleJournal of molecular biology2009

A gating model for the archeal voltage-dependent K(+) channel KvAP in DPhPC and POPE:POPG decane lipid bilayers.

Daniel Schmidt, Samuel R Cross, Roderick MacKinnon

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

46 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Comparison of KHandbook of experimental pharmacology · 2021
    Article
  5. Peptide Toxins Targeting KV Channels.Handbook of experimental pharmacology · 2021
    Review
  6. Review
  7. Article
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  11. Review
  12. Article
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  15. Article
  16. Much more than a leak: structure and function of K₂p-channels.Pflugers Archiv : European journal of physiology · 2015
    Review
  17. Article
  18. Article
  19. Lipid bilayer modules as determinants of K+ channel gating.The Journal of biological chemistry · 2014
    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

3 authors at 2 institutions in 1 country.

Daniel SchmidtHoward Hughes Medical Institute, Rockefeller University, New York, NY 10065, USA.
Samuel R Cross
Roderick MacKinnon
Howard Hughes Medical Institute · USRockefeller University · US

Funding

Voltage-Dependent Ion Channel GatingR01GM043949 · NIGMS · ROCKEFELLER UNIVERSITY · PI MACKINNON, RODERICK · 1990 to 2024
$10.1M
NIGMS NIH HHS GM43949NIGMS NIH HHS R01 GM043949
6 · The paper itself

Abstract

Voltage-dependent K(+) (Kv) channels form the basis of the excitability of nerves and muscles. KvAP is a well-characterized archeal Kv channel that has been widely used to investigate many aspects of Kv channel biochemistry, biophysics, and structure. In this study, a minimal kinetic gating model for KvAP function in two different phospholipid decane bilayers is developed. In most aspects, KvAP gating is similar to the well-studied eukaryotic Shaker Kv channel: conformational changes occur within four voltage sensors, followed by pore opening. Unlike the Shaker Kv channel, KvAP possesses an inactivated state that is accessible from the pre-open state of the channel. Changing the lipid composition of the membrane influences multiple gating transitions in the model, but, most dramatically, the rate of recovery from inactivation. Inhibition by the voltage sensor toxin VSTx1 is most easily explained if VSTx1 binds only to the depolarized conformation of the voltage sensor. By delaying the voltage sensor's return to the hyperpolarized conformation, VSTx1 favors the inactivated state of KvAP.

Indexed as

Ion Channel GatingAlkanesArchaeaKineticsLipid BilayersPeptidesPhosphatidylcholinesPhosphatidylethanolaminesPhosphatidylglycerolsPotassium Channels, Voltage-GatedShaker Superfamily of Potassium ChannelsSpider Venoms1,2-diphytanoylphosphatidylcholine1-palmitoyl-2-oleoylglycero-3-phosphoglycerol1-palmitoyl-2-oleoylphosphatidylethanolamineAlkanesdecaneLipid BilayersPeptidesPhosphatidylcholinesPhosphatidylethanolaminesPhosphatidylglycerolsPotassium Channels, Voltage-GatedShaker Superfamily of Potassium ChannelsSpider VenomsVSTX1 protein, Grammostola spatulata

Identifiers

PMID19481093
PMCPMC2778279
OpenAlexW2070504376

What OpenQuestion holds

Textmetadata
LicenceTDM
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.