Evidence map›Paper›PMID 30401746›Full record

ArticleThe Journal of biological chemistry2019

Regulation of Connexin32 by ephrin receptors and T-cell protein-tyrosine phosphatase.

Andrew J Trease, Hanjun Li, Gaelle Spagnol, Li Zheng, Kelly L Stauch, Paul L Sorgen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.1field-weighted citation impact, top 51% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Cx45 regulation by kinases and impact of expression in heart failure.Journal of molecular and cellular cardiology · 2025
    Article
  2. Review
  3. Article
  4. 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

6 authors at 2 institutions in 2 countries.

Andrew J TreaseDepartment of Biochemistry and Molecular Biology.
Hanjun LiDepartment of Biochemistry and Molecular Biology; Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska 68198.
Gaelle SpagnolDepartment of Biochemistry and Molecular Biology.
Li ZhengDepartment of Biochemistry and Molecular Biology.
Kelly L StauchDepartment of Biochemistry and Molecular Biology.
Paul L SorgenDepartment of Biochemistry and Molecular Biology. Electronic address: psorgen@unmc.edu.
Institute of Molecular Biology · BGNebraska Medical Center · US

Funding

UNMC Structural Biology CoreP20GM103427 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI PAUL L SORGEN · 2012 to 2026
$59.2M
Mechanisms of Gap Junction RegulationR01GM072631 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI SORGEN, PAUL L · 2006 to 2025
$6.4M
Phosphorylation and gating of cardiac connexin channelsR01HL131712 · NHLBI · UNIVERSITY OF ARIZONA · PI BURT, JANIS M, SORGEN, PAUL L · 2016 to 2019
$1.5M
NHLBI NIH HHS R01 HL131712NIGMS NIH HHS P20 GM103427NIGMS NIH HHS R01 GM072631
6 · The paper itself

Abstract

Gap junctions are intercellular conduits that permit the passage of ions, small metabolites, and signaling molecules between cells. Connexin32 (Cx32) is a major gap junction protein in the liver and brain. Phosphorylation is integral to regulating connexin assembly, degradation, and electrical and metabolic coupling, as well as to interactions with molecular partners. Cx32 contains two intracellular tyrosine residues, and tyrosine phosphorylation of Cx32 has been detected after activation of the epidermal growth factor receptor; however, the specific tyrosine residue and the functional implication of this phosphorylation remain unknown. To address the limited available information on Cx32 regulation by tyrosine kinases, here we used the Cx32 C-terminal (CT) domain in an

Indexed as

Caco-2 CellsConnexin 43ConnexinsGap Junction beta-1 ProteinGap JunctionsHeLa CellsHumansProtein Tyrosine Phosphatase, Non-Receptor Type 2Receptor, EphA1Receptor, EphB1Connexin 43ConnexinsGap Junction beta-1 ProteinProtein Tyrosine Phosphatase, Non-Receptor Type 2Receptor, EphA1Receptor, EphB1connexinEphA1EphB1ephringap junctionintercellular communicationintrinsically disordered proteinnuclear magnetic resonance (NMR)protein phosphorylationTC-PTPtyrosine kinase

Identifiers

PMID30401746
PMCPMC6322898
OpenAlexW2899933741

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.