Evidence map›Paper›PMID 18046402›Full record

ReviewNature2007

Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes.

Tom A Rapoport

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 453 papers.

0numbers the graph read from it
0cells of the map it votes in
453citing papers in PubMed
32.8field-weighted citation impact, top 1% 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

453 citing papers in PubMed, 966 citations in OpenAlex.

  1. Systematic optimization ofEngineering microbiology · 2026
    Review
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  12. The Zn(II)2Cys6 transcription factorApplied and environmental microbiology · 2026
    Article
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  15. Review
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  19. Review
  20. Article

393 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Tom A RapoportHoward Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA. tom_rapoport@hms.harvard.edu
Harvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A decisive step in the biosynthesis of many proteins is their partial or complete translocation across the eukaryotic endoplasmic reticulum membrane or the prokaryotic plasma membrane. Most of these proteins are translocated through a protein-conducting channel that is formed by a conserved, heterotrimeric membrane-protein complex, the Sec61 or SecY complex. Depending on channel binding partners, polypeptides are moved by different mechanisms: the polypeptide chain is transferred directly into the channel by the translating ribosome, a ratcheting mechanism is used by the endoplasmic reticulum chaperone BiP, and a pushing mechanism is used by the bacterial ATPase SecA. Structural, genetic and biochemical data show how the channel opens across the membrane, releases hydrophobic segments of membrane proteins laterally into lipid, and maintains the membrane barrier for small molecules.

Indexed as

BacteriaCell MembraneEndoplasmic ReticulumEukaryotic CellsMembrane Transport ProteinsProtein TransportMembrane Transport Proteins

Identifiers

PMID18046402
OpenAlexW2122550753

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.