Evidence map›Paper›PMID 33110101›Full record

ArticleScientific reports2020

Phosphorylation of Connexin36 near the C-terminus switches binding affinities for PDZ-domain and 14-3-3 proteins in vitro.

Stephan Tetenborg, Helen Y Wang, Lena Nemitz, Anne Depping, Alexsandra B Espejo, Jaya Aseervatham, Mark T Bedford, Ulrike Janssen-Bienhold, John O'Brien, Karin Dedek

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-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

6 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Trafficking of Connexin36 (Cx36) in the early secretory pathway.bioRxiv : the preprint server for biology · 2024
    Article
  6. The Roles of Calmodulin and CaMKII in Cx36 Plasticity.International journal of molecular sciences · 2021
    Review
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

10 authors at 3 institutions in 2 countries.

Stephan TetenborgAnimal Navigation/Neurosensorics, Institute for Biology and Environmental Sciences, University of Oldenburg, Oldenburg, Germany.
Helen Y WangRuiz Department of Ophthalmology & Visual Science, The University of Texas Health Science Center at Houston, Houston, TX, 77030, USA.
Lena NemitzVisual Neuroscience, Dept. of Neuroscience, University of Oldenburg, Oldenburg, Germany.
Anne DeppingAnimal Navigation/Neurosensorics, Institute for Biology and Environmental Sciences, University of Oldenburg, Oldenburg, Germany.
Alexsandra B EspejoDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas M.D. Anderson Cancer Center, Smithville, TX, 78957, USA.
Jaya AseervathamRuiz Department of Ophthalmology & Visual Science, The University of Texas Health Science Center at Houston, Houston, TX, 77030, USA.
Mark T BedfordDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas M.D. Anderson Cancer Center, Smithville, TX, 78957, USA.
Ulrike Janssen-BienholdVisual Neuroscience, Dept. of Neuroscience, University of Oldenburg, Oldenburg, Germany.
John O'BrienRuiz Department of Ophthalmology & Visual Science, The University of Texas Health Science Center at Houston, Houston, TX, 77030, USA.
Karin DedekAnimal Navigation/Neurosensorics, Institute for Biology and Environmental Sciences, University of Oldenburg, Oldenburg, Germany. karin.dedek@uol.de.
Carl von Ossietzky Universität Oldenburg · DEThe University of Texas Health Science Center at Houston · USThe University of Texas MD Anderson Cancer Center · US

Funding

REGULATION OF RETINAL GAP JUNCTIONSR01EY012857 · NEI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI JOHN O'BRIEN · 2000 to 2026
$8.3M
UTHouston Core Center for Vision ResearchP30EY028102 · NEI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI MASSEY, STEPHEN C · 2017 to 2021
$3.1M
NEI NIH HHS P30 EY028102NEI NIH HHS R01 EY012857NIH HHS EY012857
6 · The paper itself

Abstract

Connexin36 (Cx36) is the most abundant connexin in central nervous system neurons. It forms gap junction channels that act as electrical synapses. Similar to chemical synapses, Cx36-containing gap junctions undergo activity-dependent plasticity and complex regulation. Cx36 gap junctions represent multimolecular complexes and contain cytoskeletal, regulatory and scaffolding proteins, which regulate channel conductance, assembly and turnover. The amino acid sequence of mammalian Cx36 harbors a phosphorylation site for the Ca

Indexed as

PDZ Domains14-3-3 ProteinsAnimalsConnexinsElectrical SynapsesGap Junction delta-2 ProteinGap JunctionsHeLa CellsHumansPhosphorylationProtein Binding14-3-3 ProteinsConnexinsGap Junction delta-2 Protein

Identifiers

PMID33110101
PMCPMC7592057
OpenAlexW3096764497

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.