Evidence map›Paper›PMID 19536535›Full record

ArticleEuropean biophysics journal : EBJ2009

Electrostatic interactions during Kv1.2 N-type inactivation: random-walk simulation.

Krzysztof Małysiak, Zbigniew J Grzywna

Abstract read
PubMed Publisher
In one paragraph

Article in European biophysics journal : EBJ, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 45% of its field
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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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 at 1 institution in 1 country.

Krzysztof MałysiakDepartment of Physical Chemistry and Technology of Polymers, Faculty of Chemistry, Silesian University of Technology, Strzody 9, Gliwice, Poland. krzysztof.malysiak@polsl.pl
Zbigniew J Grzywna
Silesian University of Technology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-type inactivation of the Kv1.2 voltage-gated potassium channel is a process in which the N-terminal of the protein (its first 20 amino acids) binds to the open-channel surface, extends and occludes its pore. This process has been experimentally studied in both intact and ShBDelta6-46 channels in which the inactivating peptides are supplied in the bath solution. In this work we provide a qualitative description of N-type inactivation by simulating the random walk of charged inactivating peptides in the electrostatic field that originates from the charges present in the channel and in the cellular membrane. Our results give a deeper insight into the previously reported influence of electrostatics on the rate of N-type inactivation of ShBDelta6-46. We also show how the enchaining of the peptides, i.e., considering the intact form of the channel, influences the N-type inactivation with different charges of those peptides.

Indexed as

Models, MolecularStatic ElectricityCell MembraneDiffusionKineticsKv1.2 Potassium ChannelMembrane LipidsModels, BiologicalPeptidesProtein ConformationKv1.2 Potassium ChannelMembrane LipidsPeptides

Identifiers

PMID19536535
OpenAlexW2081468588

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.