Evidence map›Paper›PMID 15041654›Full record

ArticleBiophysical journal2004

Functional influence of the pore helix glutamate in the KcsA K+ channel.

HoSook Choi, Lise Heginbotham

Abstract read
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 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Protonation state of E71 in KcsA and its role for channel collapse and inactivation.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  3. Mechanism for selectivity-inactivation coupling in KcsA potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
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  5. 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

2 authors.

HoSook ChoiDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114, USA.
Lise Heginbotham

Funding

HOMOLOGOUS RECOMBINATION IN E COLI AND IN OOCYTESR01GM041747 · NIGMS · UNIVERSITY OF UTAH · PI CARROLL, DANA · 1989 to 1990
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NIGMS NIH HHS GM41747
6 · The paper itself

Abstract

The E71 residue is buried near the selectivity filter in the KcsA K+ channel and forms a carboxyl-carboxylate bridge with D80. We have investigated the importance of E71 by examining neutralization mutants at this position using biochemical and electrophysiological methods. E71 mutations differentially destabilize the detergent-solubilized tetramer; among them, the E71V neutralization mutant has a relatively subtle effect. The E71V channel displays electrical activity when reconstituted into planar lipid bilayers. In single channel recordings, the mutant retains K+/Na+ selectivity, and its conductance in the outward direction is unaltered. Some conduction properties are changed: inward conductance is increased. Our results show that that the E71 side chain is not a primary determinant of ion selectivity or conduction in the wild-type channel, either directly or through the E71:D80 carboxyl-carboxylate bridge.

Indexed as

Amino Acid SequenceBacterial ProteinsEscherichia coliLipid BilayersModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPatch-Clamp TechniquesPotassiumPotassium ChannelsRecombinant ProteinsSodiumBacterial ProteinsLipid BilayersPotassiumPotassium Channelsprokaryotic potassium channelRecombinant ProteinsSodium

Identifiers

PMID15041654
PMCPMC1304065

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.