Evidence map›Paper›PMID 19450462›Full record

ArticleBiophysical journal2009

K+/Na+ selectivity in toy cation binding site models is determined by the 'host'.

David L Bostick, Karunesh Arora, Charles L Brooks

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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. The Molecular Mechanism of Ion Selectivity in Nanopores.Molecules (Basel, Switzerland) · 2024
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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.

David L BostickDepartment of Chemistry and Program in Biophysics, University of Michigan, Ann Arbor, Michigan 48109, USA.
Karunesh Arora
Charles L Brooks

Funding

YEAST ER MOLECULAR CHAPERONE TRANSLOCATION: GENOME DATABANK HOMOLOGSP41RR006009 · NCRR · MELLON PITTS CORPORATION (MPC CORP) · PI KNOLL, ERIC · 1990 to 2011
$22.0M
NCRR NIH HHS P41 RR006009NCRR NIH HHS RR06009
6 · The paper itself

Abstract

The macroscopic ion-selective behavior of K(+) channels is mediated by a multitude of physiological factors. However, considering the carbonyl-lined binding site of a conductive K(+) channel as a canonical eightfold coordinated construct can be useful in understanding the principles that correlate the channel's structure with its function. We probe the effects of structure and chemical composition on the K(+)/Na(+) selectivity provided by a variety of simplified droplet-like ion binding site models. We find that when carbonyl- and water-based models capture the qualitative structural features of the K(+) channel binding site, a selective preference for K(+) emerges. Thus our findings suggest that the preference for K(+) over Na(+) exhibited by such models is principally built-in, and is not due to a unique K(+)-selective property of carbonyl functional groups. This suggestion is confirmed by a general thermodynamic assessment, which provides a basis for using simplified models to study the design principles underlying the molecular evolution of K(+) channels.

Indexed as

Models, MolecularBinding SitesLigandsPotassiumPotassium ChannelsProtein ConformationSodiumSolventsSubstrate SpecificityWaterLigandsPotassiumPotassium ChannelsSodiumSolventsWater

Identifiers

PMID19450462
PMCPMC2712193

What OpenQuestion holds

Textmetadata
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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.