Evidence map›Paper›PMID 23460640›Full record

ArticleThe Journal of biological chemistry2013

Oligomeric structure and functional characterization of Caenorhabditis elegans Innexin-6 gap junction protein.

Atsunori Oshima, Tomohiro Matsuzawa, Kouki Nishikawa, Yoshinori Fujiyoshi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Unnexin is a protein subunit of a large-pore channel expressed by unicellular organisms.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Uncovering the genetic blueprint of theProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Review
  10. Article
  11. Review
  12. Control of oocyte meiotic maturation in C. elegans.Seminars in cell & developmental biology · 2018
    Review
  13. Review
  14. Review
  15. Review
  16. Characterization of the Tetraspan Junctional Complex (4JC) superfamily.Biochimica et biophysica acta. Biomembranes · 2017
    Article
  17. Article
  18. Article
  19. Mechanosensitive unpaired innexin channels in C. elegans touch neurons.American journal of physiology. Cell physiology · 2014
    Article
  20. The pannexins: past and present.Frontiers in physiology · 2014
    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

4 authors at 2 institutions in 1 country.

Atsunori OshimaCellular and Structural Physiology Institute (CeSPI), Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan. atsu@cespi.nagoya-u.ac.jp
Tomohiro Matsuzawa
Kouki Nishikawa
Yoshinori Fujiyoshi
Nagoya University · JPKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Innexin is the molecular component of invertebrate gap junctions. Here we successfully expressed and purified Caenorhabditis elegans innexin-6 (INX-6) gap junction channels and characterized the molecular dimensions and channel permeability using electron microscopy (EM) and microinjection of fluorescent dye tracers, respectively. Negative staining and thin-section EM of isolated INX-6 gap junction membranes revealed a loosely packed hexagonal lattice and a greater cross-sectional width than that of connexin26 and connexin43 (Cx43)-GFP. In gel filtration analysis, the elution profile of purified INX-6 channels in dodecyl maltoside solution exhibited a peak at ∼400 kDa that was shifted to ∼800 kDa in octyl glucose neopentyl glycol. We also obtained the class averages of purified INX-6 channels from these peak fractions by single particle analysis. The class average from the ∼800-kDa fraction showed features of the junction form with a longitudinal height of 220 Å, a channel diameter of 110 Å in the absence of detergent micelles, and an extracellular gap space of 60 Å, whereas the class averages from the ∼400-kDa fraction showed diameters of up to 140 Å in the presence of detergent micelles. These findings indicate that the purified INX-6 channels are predominantly hemichannels in dodecyl maltoside and docked junction channels in octyl glucose neopentyl glycol. Dye transfer experiments revealed that the INX-6-GFP-His channels are permeable to 3- and 10-kDa tracers, whereas no significant amounts of these tracers passed through the Cx43-GFP channels. Based on these findings, INX-6 channels have a larger overall structure and greater permeability than connexin channels.

Indexed as

Protein MultimerizationAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsConnexin 26ConnexinsGap JunctionsHumansMultiprotein ComplexesProtein Structure, QuaternaryCaenorhabditis elegans ProteinsConnexin 26ConnexinsGJB2 protein, humanMultiprotein Complexes

Identifiers

PMID23460640
PMCPMC3624433
OpenAlexW1980035364

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.