Evidence map›Paper›PMID 9184217›Full record

ArticleThe EMBO journal1997

Cell-free synthesis and assembly of connexins into functional gap junction membrane channels.

M M Falk, L K Buehler, N M Kumar, N B Gilula

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

47 citing papers in PubMed, 160 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. The Role of Connexin 43 in Lung Disease.Life (Basel, Switzerland) · 2020
    Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Cell-free expression of a functional pore-only sodium channel.Protein expression and purification · 2015
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Gap junctions.Comprehensive Physiology · 2012
    Review
  19. Review
  20. 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

4 authors at 1 institution in 1 country.

M M FalkDepartment of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
L K Buehler
N M Kumar
N B Gilula
Scripps Research Institute · US

Funding

GAP JUNCTIONS AND CELL-CELL COMMUNICATIONR37GM037904 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI GILULA, NORTON B · 1991 to 2000
$536k
GAP JUNCTION AND CELL-CELL COMMUNICATIONR01GM037904 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI GILULA, NORTON B · 1986 to 1989
–
NIGMS NIH HHS GM 37904
6 · The paper itself

Abstract

Several different gap junction channel subunit isotypes, known as connexins, were synthesized in a cell-free translation system supplemented with microsomal membranes to study the mechanisms involved in gap junction channel assembly. Previous results indicated that the connexins were synthesized as membrane proteins with their relevant transmembrane topology. An integrated biochemical and biophysical analysis indicated that the connexins assembled specifically with other connexin subunits. No interactions were detected between connexin subunits and other co-translated transmembrane proteins. The connexins that were integrated into microsomal vesicles assembled into homo- and hetero-oligomeric structures with hydrodynamic properties of a 9S particle, consistent with the properties reported for hexameric gap junction connexons derived from gap junctions in vivo. Further, cell-free assembled homo-oligomeric connexons composed of beta1 or beta2 connexin were reconstituted into synthetic lipid bilayers. Single channel conductances were recorded from these bilayers that were similar to those measured for these connexons produced in vivo. Thus, this is the first direct evidence that the synthesis and assembly of a gap junction connexon can take place in microsomal membranes. Finally, the cell-free system has been used to investigate the properties of alpha1, beta1 and beta2 connexin to assemble into hetero-oligomers. Evidence has been obtained for a selective interaction between individual connexin isotypes and that a signal determining the potential hetero-oligomeric combinations of connexin isotypes may be located in the N-terminal sequence of the connexins.

Indexed as

Cell-Free SystemConnexinsGap JunctionsIon ChannelsLipid BilayersMembrane FusionMicrosomesMutationPatch-Clamp TechniquesProtein BindingProtein BiosynthesisProtein Processing, Post-TranslationalSequence DeletionConnexinsIon ChannelsLipid Bilayers

Identifiers

PMID9184217
PMCPMC1169881
OpenAlexW2137579188

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.