Evidence map›Paper›PMID 18166647›Full record

ReviewThe Journal of cell biology2007

The expanding role of the ER translocon in membrane protein folding.

William R Skach

Abstract readReviewComment
In one paragraph

Review in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Membrane protein folding makes the transition.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  14. Article
  15. Article
  16. Article
  17. Insertion of short transmembrane helices by the Sec61 translocon.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  18. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author.

William R SkachDepartment of Biochemistry and Molecular Biology, Oregon Health & Sciences University, Portland, OR 97239, USA. skachw@ohsu.edu

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic polytopic membrane proteins are cotranslationally inserted into the ER membrane by a multisubunit protein-conducting channel called the Sec61 translocon. Although most major translocon components have been identified and reconstituted, their stoichiometry and functional organization remain unknown. This has led to speculative and sometimes conflicting models describing how multiple transmembrane (TM) segments might be oriented and integrated during nascent polytopic protein biogenesis. Kida et al. (see p. 1441 of this issue) shed new insight into this area by demonstrating that functional translocons exhibit a remarkable flexibility by simultaneously accommodating at least two hydrophilic translocating peptides that are separated by multiple hydrophobic TMs. These surprising findings support an expanded role for the translocon in membrane protein biogenesis and require reassessment of current views based on a single small functional pore.

Indexed as

AnimalsCalcium-Binding ProteinsEndoplasmic ReticulumHumansIntracellular MembranesMembrane GlycoproteinsMembrane LipidsMembrane ProteinsPeptidesProtein FoldingProtein TransportReceptors, Cytoplasmic and NuclearReceptors, PeptideSEC Translocation ChannelsCalcium-Binding ProteinsMembrane GlycoproteinsMembrane LipidsMembrane ProteinsPeptidesReceptors, Cytoplasmic and NuclearReceptors, PeptideSEC Translocation Channelssignal sequence receptor

Identifiers

PMID18166647
PMCPMC2373491

What OpenQuestion holds

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Registered trials

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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.