Evidence map›Paper›PMID 7641680›Full record

ArticleThe EMBO journal1995

Membrane insertion and assembly of ductin: a polytopic channel with dual orientations.

J Dunlop, P C Jones, M E Finbow

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

42 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Impairment of the Glial Phagolysosomal System Drives Prion-Like Propagation in aThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
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  4. Reversible binding of divalent cations toFrontiers in molecular biosciences · 2023
    Review
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  6. Resolving the topological enigma in CaThe Journal of biological chemistry · 2019
    Review
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  12. Article
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  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. An emerging consensus for the structure of EmrE.Acta crystallographica. Section D, Biological crystallography · 2009
    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

3 authors at 1 institution in 1 country.

J DunlopCRC Beatson Laboratories, Beatson Institute for Cancer Research, Bearsden, Glasgow, UK.
P C Jones
M E Finbow
Cancer Research UK Scotland Institute · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Ductin is a highly conserved and polytopic transmembrane protein which is the subunit c component of the vacuolar H(+)-ATPase (V-ATPase) and a component of a connexon channel of gap junctions. Previous studies have suggested that ductin in the V-ATPase has the opposite orientation of ductin in a connexon. Using an in vitro translation system coupled to microsomes derived from the endoplasmic reticulum, we show that ductin is co-translationally inserted into the membrane bilayer, suggesting a dependency on the signal recognition particle for synthesis. By attaching a C-terminal polypeptide derived from beta-lactamase and by using cysteine replacement coupled to chemical labelling, we show that ductin is inserted into the microsomal membrane in both orientations in similar proportions. In contrast, squid rhodopsin appears to be inserted in a single orientation. Changing conserved charged residues at the N-terminus of ductin does not affect the ratio of the two orientations. Once in the microsomal membrane, ductin assembles into an oligomeric complex which contains a pore accessible to a water-soluble probe, reminiscent of the ductin complex found in the V-ATPase and a connexon.

Indexed as

Vacuolar Proton-Translocating ATPasesAmino Acid SequenceAnimalsBase Sequencebeta-LactamasesCysteineDecapodiformesFluoresceinsIntracellular MembranesMicrosomesMolecular Sequence DataMutationProtein BiosynthesisProtein ConformationProteolipidsProton-Translocating ATPasesbeta-LactamasesCysteineductinfluorescein 5-maleimideFluoresceinsProteolipidsProton-Translocating ATPasesRecombinant Fusion ProteinsRhodopsinVacuolar Proton-Translocating ATPases

Identifiers

PMID7641680
PMCPMC394434
OpenAlexW201895147

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.