Evidence map›Paper›PMID 20937866›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Ion sensing in the RCK1 domain of BK channels.

Guohui Zhang, Sheng-You Huang, Junqiu Yang, Jingyi Shi, Xiao Yang, Alyssa Moller, Xiaoqin Zou, Jianmin Cui

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed.

  1. Article
  2. Redox-dependent CdBiophysical journal · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Coronary Large Conductance CaFrontiers in physiology · 2021
    Review
  14. FeACS chemical biology · 2020
    Article
  15. Article
  16. The Journal of general physiology · 2019
    Review
  17. Article
  18. Effects of Single Nucleotide Polymorphisms in HumanFrontiers in molecular neuroscience · 2019
    Article
  19. Article
  20. CO-independent modification of KEuropean journal of pharmacology · 2017
    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

8 authors.

Guohui ZhangDepartment of Biomedical Engineering, Center for the Investigation of Membrane Excitability Disorders, Washington University, St. Louis, MO 63130, USA.
Sheng-You Huang
Junqiu Yang
Jingyi Shi
Xiao Yang
Alyssa Moller
Xiaoqin Zou
Jianmin Cui

Funding

Ca2+ Dependent K+ Channels: Allosteric GatingR01HL070393 · NHLBI · WASHINGTON UNIVERSITY · PI CUI, JIANMIN · 2002 to 2015
$4.9M
SUBUNITS INTERACTION IN THE FUNCTION OF BK CHANNELSR01NS060706 · NINDS · WASHINGTON UNIVERSITY · PI CUI, JIANMIN · 2010 to 2013
$1.3M
A new scoring framework for selecting structural modelsR21GM088517 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI ZOU, XIAOQIN · 2009 to 2010
$417k
NHLBI NIH HHS R01 HL070393NHLBI NIH HHS R01-HL70393NIGMS NIH HHS R21 GM088517NIGMS NIH HHS R21GM088517NINDS NIH HHS R01 NS060706
6 · The paper itself

Abstract

BK-type K(+) channels are activated by voltage and intracellular Ca(2+), which is important in modulating muscle contraction, neural transmission, and circadian pacemaker output. Previous studies suggest that the cytosolic domain of BK channels contains two different Ca(2+) binding sites, but the molecular composition of one of the sites is not completely known. Here we report, by systematic mutagenesis studies, the identification of E535 as part of this Ca(2+) binding site. This site is specific for binding to Ca(2+) but not Cd(2+). Experimental results and molecular modeling based on the X-ray crystallographic structures of the BK channel cytosolic domain suggest that the binding of Ca(2+) by the side chains of E535 and the previously identified D367 changes the conformation around the binding site and turns the side chain of M513 into a hydrophobic core, providing a basis to understand how Ca(2+) binding at this site opens the activation gate of the channel that is remotely located in the membrane.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesCalciumFemaleIn Vitro TechniquesLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedOocytesProtein Structure, TertiaryRecombinant ProteinsCalciumKcnma1 protein, mouseLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsRecombinant Proteins

Identifiers

PMID20937866
PMCPMC2972974

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.