Evidence map›Paper›PMID 15130123›Full record

ArticleMolecular microbiology2004

Branching sites and morphological abnormalities behave as ectopic poles in shape-defective Escherichia coli.

Trine Nilsen, Anindya S Ghosh, Marcia B Goldberg, Kevin D Young

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

36 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Sculpting the bacterial cell.Current biology : CB · 2009
    Review
  16. Article
  17. Cell shape and cell-wall organization in Gram-negative bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  18. Article
  19. Article
  20. Bacterial growth and cell division: a mycobacterial perspective.Microbiology and molecular biology reviews : MMBR · 2008
    Review
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

4 authors at 1 institution in 1 country.

Trine NilsenInfectious Disease Division, Massachusetts General Hospital/Harvard Medical School, Boston, MA 02114, USA.
Anindya S Ghosh
Marcia B Goldberg
Kevin D Young
University of North Dakota · US

Funding

Glycan Expression Analysis using an Odyssey CLx Infrared Imaging SystemR01GM061019 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI VOTH, DANIEL E · 2000 to 2021
$8.0M
MECHANISM AND FUNCTION OF UNIPOLARITY OF SHIGELLA ICSAR01AI035817 · NIAID · YESHIVA UNIVERSITY · PI GOLDBERG, MARCIA B · 1994 to 2009
$3.9M
NIAID NIH HHS AI35817NIAID NIH HHS R01 AI035817NIGMS NIH HHS GM61019NIGMS NIH HHS R01 GM061019
6 · The paper itself

Abstract

Certain mutants in Escherichia coli lacking multiple penicillin-binding proteins (PBPs) produce misshapen cells containing kinks, bends and branches. These deformed regions exhibit two structural characteristics of normal cell poles: the peptidoglycan is inert to dilution by new synthesis or turnover, and a similarly stable patch of outer membrane caps the sites. To test the premise that these aberrant sites represent biochemically functional but misplaced cell poles, we assessed the intracellular distribution of proteins that localize specifically to bacterial poles. Green fluorescent protein (GFP) hybrids containing polar localization sequences from the Shigella flexneri IcsA protein or from the Vibrio cholerae EpsM protein formed foci at the poles of wild-type E. coli and at the poles and morphological abnormalities in PBP mutants. In addition, secreted wild-type IcsA localized to the outer membrane overlying these aberrant domains. We conclude that the morphologically deformed sites in these mutants represent fully functional poles or pole fragments. The results suggest that prokaryotic morphology is driven, at least in part, by the controlled placement of polar material, and that one or more of the low-molecular-weight PBPs participate in this process. Such mutants may help to unravel how particular proteins are targeted to bacterial poles, thereby creating important biochemical and functional asymmetries.

Indexed as

MutationBacterial Outer Membrane ProteinsBacterial ProteinsCarrier ProteinsDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsGenes, ReporterGreen Fluorescent ProteinsHexosyltransferasesLuminescent ProteinsMembrane ProteinsMuramoylpentapeptide CarboxypeptidasePenicillin-Binding ProteinsPeptidoglycanPeptidyl TransferasesBacterial Outer Membrane ProteinsBacterial ProteinsCarrier ProteinsDNA-Binding ProteinsEpsM protein, Vibrio choleraeEscherichia coli ProteinsGreen Fluorescent ProteinsHexosyltransferasesLuminescent ProteinsMembrane ProteinsMuramoylpentapeptide CarboxypeptidasePenicillin-Binding ProteinsPeptidoglycanPeptidyl TransferasesProtein Sorting SignalsRecombinant Fusion ProteinsTranscription FactorsvirG protein, Shigella flexneri

Identifiers

PMID15130123
PMCPMC3097518
OpenAlexW2111890954

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.