Evidence map›Paper›PMID 31440780›Full record

ArticleThe Journal of membrane biology2019

The Effects of Calcium on Lipid-Protein Interactions and Ion Flux in the Cx26 Connexon Embedded into a POPC Bilayer.

Juan M R Albano, Gabriel E Jara, M Laura Fernández, Julio C Facelli, Marta B Ferraro, Monica Pickholz

Abstract read
PubMed Publisher
In one paragraph

Article in The Journal of membrane biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Special Issue: Membrane and Receptor Dynamics.The Journal of membrane biology · 2019
    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 at 3 institutions in 3 countries.

Juan M R AlbanoDepartamento de Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires and IFIBA, CONICET, Ciudad Universitaria, Pabellon 1, 1428, Buenos Aires, Argentina.
Gabriel E JaraInstitute of Chemistry, University of Campinas, Campinas, SP, 13083-861, Brazil.
M Laura FernándezDepartamento de Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina.
Julio C FacelliDepartment of Biomedical Informatics and Center for Clinical and Translational Research, The University of Utah, 421 Wakara Way, Suite 140, Salt Lake City, UT, 84108, USA.
Marta B FerraroDepartamento de Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires and IFIBA, CONICET, Ciudad Universitaria, Pabellon 1, 1428, Buenos Aires, Argentina.
Monica PickholzDepartamento de Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires and IFIBA, CONICET, Ciudad Universitaria, Pabellon 1, 1428, Buenos Aires, Argentina. monicapickholz@gmail.com.ORCID 0000-0002-0172-2748
Consejo Nacional de Investigaciones Científicas y Técnicas · ARUniversidade Estadual de Campinas (UNICAMP) · BRUniversity of Utah · US

Funding

Speech-Recognition Difficulties of the Hearing ImpairedR01AG008293 · NIA · TRUSTEES OF INDIANA UNIVERSITY · PI HUMES, LARRY E · 1990 to 2018
$5.1M
Consejo Nacional de Investigaciones Científicas y Técnicas 11220130100377Fondo para la Investigación Científica y Tecnológica 3653/14Fondo para la Investigación Científica y Tecnológica 3802/17Foundation for the National Institutes of Health 1S10OD021644-01A1Fundação Amazônia Paraense de Amparo à Pesquisa 2013/08293-7
6 · The paper itself

Abstract

Gap junctions provide a communication pathway between adjacent cells. They are formed by paired connexons that reside in the plasma membrane of their respective cell and their activity can be modulated by the bilayer composition. In this work, we study the dynamic behavior of a Cx26 connexon embedded in a POPC lipid bilayer, studying: the membrane protein interactions and the ion flux though the connexon pore. We analyzed extensive atomistic molecular dynamics simulations for different conditions, with and without calcium ions. We found that lipid-protein interactions were mainly mediated by hydrogen bonds. Specific amino acids were identified forming hydrogen bonds with the POPC lipids (ARG98, ARG127, ARG165, ARG216, LYS22, LYS221, LYS223, LYS224, SER19, SER131, SER162, SER219, SER222, THR18 and TYR97, TYR155, TYR212, and TYR217). In the presence of calcium ions, we found subtle differences on the HB lifetimes. Finally, these MD simulations are able to identify and explain differential chlorine flux through the pore depending on the presence or absence of the calcium ions and its distribution within the pore.

Indexed as

Molecular Dynamics SimulationCalciumConnexin 26ConnexinsHumansHydrogen BondingLipid BilayersPhosphatidylcholines1-palmitoyl-2-oleoylphosphatidylcholineCalciumConnexin 26ConnexinsGJB2 protein, humanLipid BilayersPhosphatidylcholinesAPBSConnexonCx26 hemichannelMolecular dynamicsPOPC

Identifiers

PMID31440780
OpenAlexW2969724737

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.