Evidence map›Paper›PMID 28276312›Full record

ReviewEcoSal Plus2017

Targeting and Insertion of Membrane Proteins.

Andreas Kuhn, Hans-Georg Koch, Ross E Dalbey

Open access · greenAbstract readReview
In one paragraph

Review in EcoSal Plus, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
8.8field-weighted citation impact, top 2% 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

45 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
  2. Article
  3. Twin-arginine transport complex plays an essential role inbioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Role of the CagY antenna projection inInfection and immunity · 2023
    Article
  11. Article
  12. Oriented Insertion of ESR-Containing Hybrid Proteins in Proteoliposomes.International journal of molecular sciences · 2023
    Article
  13. Article
  14. Article
  15. Cotranslational Biogenesis of Membrane Proteins in Bacteria.Frontiers in molecular biosciences · 2022
    Review
  16. Article
  17. Lateral gate dynamics of the bacterial translocon during cotranslational membrane protein insertion.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Article
  19. Article
  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

3 authors at 3 institutions in 2 countries.

Andreas KuhnInstitute for Microbiology and Molecular Biology, University of Hohenheim, 70599 Stuttgart, Germany.
Hans-Georg KochInstitute for Biochemistry and Molecular Biology, Faculty of Medicine, Albert-Ludwigs-University of Freiburg, 79104, Freiburg, Germany.
Ross E DalbeyDepartment of Chemistry, The Ohio State University, Columbus, OH 43210.
The Ohio State University · USUniversity of Freiburg · DEUniversity of Hohenheim · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The insertion and assembly of proteins into the inner membrane of bacteria are crucial for many cellular processes, including cellular respiration, signal transduction, and ion and pH homeostasis. This process requires efficient membrane targeting and insertion of proteins into the lipid bilayer in their correct orientation and proper conformation. Playing center stage in these events are the targeting components, signal recognition particle (SRP) and the SRP receptor FtsY, as well as the insertion components, the Sec translocon and the YidC insertase. Here, we will discuss new insights provided from the recent high-resolution structures of these proteins. In addition, we will review the mechanism by which a variety of proteins with different topologies are inserted into the inner membrane of Gram-negative bacteria. Finally, we report on the energetics of this process and provide information on how membrane insertion occurs in Gram-positive bacteria and Archaea. It should be noted that most of what we know about membrane protein assembly in bacteria is based on studies conducted in Escherichia coli.

Indexed as

ArchaeaBacterial ProteinsEscherichia coliEscherichia coli ProteinsGram-Positive BacteriaMembrane ProteinsMembrane Transport ProteinsMolecular StructureProtein TransportReceptors, Cytoplasmic and NuclearReceptors, PeptideSEC Translocation ChannelsSignal Recognition ParticleBacterial ProteinsEscherichia coli ProteinsFtsY protein, BacteriaMembrane ProteinsMembrane Transport ProteinsReceptors, Cytoplasmic and NuclearReceptors, PeptideSEC Translocation Channelssignal peptide receptorSignal Recognition ParticleYIDC protein, E coli

Identifiers

PMID28276312
PMCPMC11575690
OpenAlexW2593064515

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.