Evidence map›Paper›PMID 18641075›Full record

ArticleBiophysical journal2008

Models of the structure and gating mechanisms of the pore domain of the NaChBac ion channel.

Yinon Shafrir, Stewart R Durell, H Robert Guy

Abstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
  2. Structures of closed and open states of a voltage-gated sodium channel.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
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  12. Article
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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

3 authors.

Yinon ShafrirLaboratory of Cell Biology, CCR, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-5567, USA.
Stewart R Durell
H Robert Guy

Funding

Modeling of the structure and functional mechanisms of voltage-gated channelsZIABC010721 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI GUY, HOMER ROBERT · 2009 to 2010
$642k
Modeling of the structure and functional mechanisms of voltage-gated channelsZ01BC010721 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI GUY, HOMER ROBERT · 2006 to 2008
$604k
Molecular Modeling of Ion Channel and Other Membrane ProteinsZICBC011071 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI DURELL, STEWART · 2009 to 2010
$133k
Molecular Modeling of Ion Channel and Other Membrane ProteinsZ01BC011071 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI DURELL, STEWART · 2008 to 2008
$64k
Intramural NIH HHS
6 · The paper itself

Abstract

The NaChBac prokaryotic sodium channel appears to be a descendent of an evolutionary link between voltage-gated K(V) and Ca(V) channels. Like K(V) channels, four identical six-transmembrane subunits comprise the NaChBac channel, but its selectivity filter possesses a signature sequence of eukaryotic Ca(V) channels. We developed structural models of the NaChBac channel in closed and open conformations, using K(+)-channel crystal structures as initial templates. Our models were also consistent with numerous experimental results and modeling criteria. This study concerns the pore domain. The major differences between our models and K(+) crystal structures involve the latter portion of the selectivity filter and the bend region in S6 of the open conformation. These NaChBac models may serve as a stepping stone between K(+) channels of known structure and Na(V), Ca(V), and TRP channels of unknown structure.

Indexed as

Ion Channel GatingModels, MolecularAmino Acid SequenceAmino Acid SubstitutionBacillusBacterial ProteinsComputer SimulationConserved SequenceMolecular Sequence DataMutant ProteinsMutationProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsSequence AlignmentSodium ChannelsBacterial ProteinsMutant ProteinsNaChBac protein, bacteriaProtein SubunitsSodium Channels

Identifiers

PMID18641075
PMCPMC2553130

What OpenQuestion holds

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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.