Evidence map›Paper›PMID 16672606›Full record

ArticleJournal of bacteriology2006

Direct visualization of red fluorescent lipoproteins indicates conservation of the membrane sorting rules in the family Enterobacteriaceae.

Shawn Lewenza, Dominique Vidal-Ingigliardi, Anthony P Pugsley

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

37 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
  2. Review
  3. Bacterial lipid biophysics and membrane organization.Current opinion in microbiology · 2023
    Review
  4. Article
  5. Measurement of Protein Mobility inFrontiers in microbiology · 2021
    Article
  6. Review
  7. Article
  8. The Tol-Pal system is required for peptidoglycan-cleaving enzymes to complete bacterial cell division.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Tracking Proteins Secreted by Bacteria: What's in the Toolbox?Frontiers in cellular and infection microbiology · 2017
    Review
  15. Article
  16. Article
  17. Outer membrane lipoprotein biogenesis: Lol is not the end.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015
    Review
  18. Review
  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 2 institutions in 1 country.

Shawn LewenzaMolecular Genetics Unit, Institut Pasteur, Paris, France.
Dominique Vidal-Ingigliardi
Anthony P Pugsley
Institut Pasteur · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chimeras created by fusing the monomeric red fluorescent protein (RFP) to a bacterial lipoprotein signal peptide (lipoRFPs) were visualized in the cell envelope by epifluorescence microscopy. Plasmolysis of the bacteria separated the inner and outer membranes, allowing the specific subcellular localization of lipoRFPs to be determined in situ. When equipped with the canonical inner membrane lipoprotein retention signal CDSR, lipoRFP was located in the inner membrane in Escherichia coli, whereas the outer membrane sorting signal CSSR caused lipoRFP to localize to the outer membrane. CFSR-RFP was also routed to the outer membrane, but CFNSR-RFP was located in the inner membrane, consistent with previous data showing that this sequence functions as an inner membrane retention signal. These four lipoproteins exhibited identical localization patterns in a panel of members of the family Enterobacteriaceae, showing that the lipoprotein sorting rules are conserved in these bacteria and validating the use of E. coli as a model system. Although most predicted inner membrane lipoproteins in these bacteria have an aspartate residue after the fatty acylated N-terminal cysteine residue, alternative signals such as CFN can and probably do function in parallel, as indicated by the existence of putative inner membrane lipoproteins with this sequence at their N termini.

Indexed as

Bacterial ProteinsBase SequenceCell MembraneDNA PrimersEnterobacteriaceaeLipoproteinsLuminescent ProteinsPectobacterium carotovorumPlasmidsRecombinant Fusion ProteinsRed Fluorescent ProteinSalmonella entericaShigella flexneriYersinia pseudotuberculosisBacterial ProteinsDNA PrimersLipoproteinsLuminescent ProteinsRecombinant Fusion ProteinsRed Fluorescent Protein

Identifiers

PMID16672606
PMCPMC1482850
OpenAlexW2150712367

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.