Evidence map›Paper›PMID 19651031›Full record

ArticleBiophysical journal2009

Modulation of the conductance-voltage relationship of the BK(Ca) channel by shortening the cytosolic loop connecting two RCK domains.

Ju-Ho Lee, Hyun-Ju Kim, Hae-Deun Kim, Byoung-Cheol Lee, Jang-Soo Chun, Chul-Seung Park

Abstract read
In one paragraph

Article in Biophysical journal, 2009. 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
–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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Alternatively spliced domains interact to regulate BK potassium channel gating.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  6. Article
  7. Article
  8. 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

6 authors.

Ju-Ho LeeDepartment of Life Science, Gwangju Institute of Science and Technology, Gwangju, Korea.
Hyun-Ju Kim
Hae-Deun Kim
Byoung-Cheol Lee
Jang-Soo Chun
Chul-Seung Park

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calcium-dependent gating of large-conductance calcium-activated potassium (BK(Ca)) channels is mediated by the intracellular carboxyl terminus, which contains two domains of regulator of K(+) conductance (RCK). In mammalian BK(Ca) channels, the two RCK domains are separated by a protein segment of 101 residues that is poorly conserved in evolution and predicted to have no regular secondary structures. We investigated the functional importance of this loop using a series of deletion mutations. We found that the length, rather than the specific sequence at the central region of the segment, is critical for the functionality of the channel. As the length of the loop is progressively shorted, the conductance-voltage relationship gradually shifts toward more positive voltages with a minimum length of 70 amino acids, in an apparent response to increased tension within the loop. Thus, the functional activity of the BK(Ca) channel can be modulated by altering the tension of this loop region.

Indexed as

Amino Acid SequenceAnimalsBiotinylationCHO CellsCricetinaeCricetulusDensitometryImmunoblottingLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsMembrane PotentialsMutationPatch-Clamp TechniquesPotassium ChannelsProtein Structure, TertiaryRatsSequence HomologyKcnma1 protein, ratLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsPotassium Channels

Identifiers

PMID19651031
PMCPMC2718151

What OpenQuestion holds

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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.