Evidence map›Paper›PMID 16735758›Full record

ArticleThe Journal of general physiology2006

Statistical limits to the identification of ion channel domains by sequence similarity.

Anthony A Fodor, Richard W Aldrich

Abstract readComparative Study
In one paragraph

Article in The Journal of general physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Calcium-Activated KHandbook of experimental pharmacology · 2021
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. The RCK2 domain of the human BKCa channel is a calcium sensor.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  15. Article
  16. Mg2+ mediates interaction between the voltage sensor and cytosolic domain to activate BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  17. Gating rings formed by RCK domains: keys to gate opening.The Journal of general physiology · 2007
    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

2 authors.

Anthony A FodorDepartment of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University School of Medicine, CA 94305, USA. anthony.fodor@gmail.com
Richard W Aldrich

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The study of ion channel function is constrained by the availability of structures for only a small number of channels. A commonly used bioinformatics technique is to assert, based on sequence similarity, that a domain within a channel of interest has the same structure as a reference domain for which the structure is known. This technique, while useful, is often employed when there is only a slight similarity between the channel of interest and the domain of known structure. In this study, we exploit recent advances in structural genomics to calculate the sequence-based probability of the presence of putative domains in a number of ion channels. We find strong support for the presence of many domains that have been proposed in the literature. For example, eukaryotic and prokaryotic CLC proteins almost certainly share a common structure. A number of proposed domains, however, are not as well supported. In particular, for the COOH terminus of the BK channel we find a number of literature proposed domains for which the assertion of common structure based on common sequence has a nontrivial probability of error.

Indexed as

Databases, ProteinSequence Homology, Amino AcidAnimalsChloride ChannelsHumansHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsIon ChannelsMicePredictive Value of TestsProtein Structure, TertiaryRatsSequence AlignmentChloride ChannelsCLC-1 channelHyperpolarization-Activated Cyclic Nucleotide-Gated ChannelsIon Channels

Identifiers

PMID16735758
PMCPMC2151544

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.