Evidence map›Paper›PMID 22683878›Full record

ReviewNature reviews. Microbiology2012

The twin-arginine translocation (Tat) protein export pathway.

Tracy Palmer, Ben C Berks

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 253 papers.

0numbers the graph read from it
0cells of the map it votes in
253citing papers in PubMed
22.3field-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

253 citing papers in PubMed, 525 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Chemical reviews · 2026
    Review
  9. Review
  10. Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2026
    Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Genomic Analysis ofMicroorganisms · 2025
    Article
  16. Article
  17. Review
  18. Twin-arginine transport complex plays an essential role inbioRxiv : the preprint server for biology · 2025
    Article
  19. Review
  20. Article

193 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

2 authors at 2 institutions in 1 country.

Tracy PalmerDivision of Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK. t.palmer@dundee.ac.uk
Ben C Berks
University of Dundee · GBUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D011140/1Medical Research Council G0901653Medical Research Council G1001640Medical Research Council G117/519Wellcome Trust
6 · The paper itself

Abstract

The twin-arginine translocation (Tat) protein export system is present in the cytoplasmic membranes of most bacteria and archaea and has the highly unusual property of transporting fully folded proteins. The system must therefore provide a transmembrane pathway that is large enough to allow the passage of structured macromolecular substrates of different sizes but that maintains the impermeability of the membrane to ions. In the Gram-negative bacterium Escherichia coli, this complex task can be achieved by using only three small membrane proteins: TatA, TatB and TatC. In this Review, we summarize recent advances in our understanding of how this remarkable machine operates.

Indexed as

Cell MembraneEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialMembrane Transport ProteinsEscherichia coli ProteinsMembrane Transport ProteinsTatA protein, E coliTatB protein, E coliTatC protein, E coli

Identifiers

PMID22683878
OpenAlexW2061385538

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.