Evidence map›Paper›PMID 29186829›Full record

ArticleMolecules (Basel, Switzerland)2017

Inhibition by Commercial Aminoglycosides of Human Connexin Hemichannels Expressed in Bacteria.

Mariana C Fiori, Srinivasan Krishnan, Abbey Kjellgren, Luis G Cuello, Guillermo A Altenberg

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

8 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Mechanisms Underlying Connexin Hemichannel Activation in Disease.International journal of molecular sciences · 2021
    Review
  7. Article
  8. 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

5 authors at 1 institution in 1 country.

Mariana C FioriDepartment of Cell Physiology and Molecular Biophysics, and Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430-6551, USA. mariana.fiori@ttuhsc.edu.
Srinivasan KrishnanDepartment of Cell Physiology and Molecular Biophysics, and Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430-6551, USA. srinivas.krishnan21@gmail.com.
Abbey KjellgrenDepartment of Cell Physiology and Molecular Biophysics, and Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430-6551, USA. abbey.kjellgren@ttu.edu.
Luis G CuelloDepartment of Cell Physiology and Molecular Biophysics, and Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430-6551, USA. luis.cuello@ttuhsc.edu.ORCID 0000-0001-5192-7568
Guillermo A AltenbergDepartment of Cell Physiology and Molecular Biophysics, and Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430-6551, USA. g.altenberg@ttuhsc.edu.ORCID 0000-0002-8932-740X
Texas Tech University · US

Funding

High-resolution crystallographic and functional studies of K+ channel gatingR01GM097159 · NIGMS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI CUELLO, LUIS GONZALO · 2012 to 2021
$2.7M
Architecture of the transmembrane pore formed by connexin 43R01GM079629 · NIGMS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI ALTENBERG, GUILLERMO A · 2007 to 2011
$1.7M
NIGMS NIH HHS R01 GM079629NIGMS NIH HHS R01 GM097159
6 · The paper itself

Abstract

In addition to gap junctional channels that mediate cell-to-cell communication, connexins form hemichannels that are present at the plasma membrane. Since hemichannels are permeable to small hydrophilic compounds, including metabolites and signaling molecules, their abnormal opening can cause or contribute to cell damage in disorders such as cardiac infarct, stroke, deafness, skin diseases, and cataracts. Therefore, hemichannels are potential pharmacological targets. A few aminoglycosides, well-known broad-spectrum antibiotics, have been shown to inhibit hemichannels. Here, we tested several commercially available aminoglycosides for inhibition of human connexin hemichannels using a cell-based bacterial growth complementation assay that we developed recently. We found that kanamycin A, kanamycin B, geneticin, neomycin, and paromomycin are effective inhibitors of hemichannels formed by connexins 26, 43, and 46 (Cx26, Cx43, and Cx46). Because of the >70 years of clinical experience with aminoglycosides and the fact that several of the aminoglycosides tested here have been used in humans, they are promising starting points for the development of effective connexin hemichannel inhibitors.

Indexed as

AminoglycosidesBacteriaConnexinsDose-Response Relationship, DrugGene Expression Regulation, BacterialHumansMolecular StructureProtein IsoformsAminoglycosidesConnexinsProtein Isoformsantibioticcell-based assaychannelCx26Cx43Cx46gap junctionLB2003screeningtransport

Identifiers

PMID29186829
PMCPMC6149774
OpenAlexW2768572333

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.