Evidence map›Paper›PMID 15454416›Full record

ArticleBiophysical journal2004

Models of the structure and voltage-gating mechanism of the shaker K+ channel.

Stewart R Durell, Indira H Shrivastava, H Robert Guy

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In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.2field-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

28 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Review
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  9. Article
  10. Article
  11. Architecture and gating of Hv1 proton channels.The Journal of physiology · 2009
    Review
  12. Potassium channel opening: a subtle two-step.The Journal of physiology · 2009
    Article
  13. Article
  14. Article
  15. Article
  16. S0, where is it?The Journal of general physiology · 2008
    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

3 authors at 1 institution in 1 country.

Stewart R DurellLaboratory of Experimental and Computational Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-5567, USA.
Indira H Shrivastava
H Robert Guy
Center for Cancer Research · US

Funding

MEMBRANE PROTEIN MODELINGZ01BC008363 · BC · BASIC SCIENCES · PI GUY, HOMER ROBERT · 1996 to 2005
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6 · The paper itself

Abstract

In the preceding, accompanying article, we present models of the structure and voltage-dependent gating mechanism of the KvAP bacterial K+ channel that are based on three types of evidence: crystal structures of portions of the KvAP protein, theoretical modeling criteria for membrane proteins, and biophysical studies of the properties of native and mutated voltage-gated channels. Most of the latter experiments were performed on the Shaker K+ channel. Some of these data are difficult to relate directly to models of the KvAP channel's structure due to differences in the Shaker and KvAP sequences. We have dealt with this problem by developing new models of the structure and gating mechanism of the transmembrane and extracellular portions of the Shaker channel. These models are consistent with almost all of the biophysical data. In contrast, much of the experimental data are incompatible with the "paddle" model of gating that was proposed when the KvAP crystal structures were first published. The general folding pattern and gating mechanisms of our current models are similar to some of our earlier models of the Shaker channel.

Indexed as

Models, BiologicalModels, ChemicalModels, MolecularAnimalsBinding SitesComputer SimulationHumansIon Channel GatingPotassium ChannelsPotassium Channels, Voltage-GatedProtein BindingProtein ConformationProtein Structure, TertiaryShaker Superfamily of Potassium ChannelsStructure-Activity RelationshipPotassium ChannelsPotassium Channels, Voltage-GatedShaker Superfamily of Potassium Channels

Identifiers

PMID15454416
PMCPMC1304639
OpenAlexW2120570952

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.