Evidence map›Paper›PMID 23510438›Full record

ArticleJournal of the American Chemical Society2013

Reactions of the three AmpD enzymes of Pseudomonas aeruginosa.

Weilie Zhang, Mijoon Lee, Dusan Hesek, Elena Lastochkin, Bill Boggess, Shahriar Mobashery

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2013. 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
2.2field-weighted citation impact, top 12% 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, 51 citations in OpenAlex.

  1. Outer Membrane-Peptidoglycan Anchoring inJournal of the American Chemical Society · 2026
    Article
  2. Article
  3. Transferable AmpCs inAntimicrobial agents and chemotherapy · 2024
    Article
  4. Article
  5. Article
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  8. Article
  9. Article
  10. Article
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  14. Article
  15. Constructing and deconstructing the bacterial cell wall.Protein science : a publication of the Protein Society · 2020
    Review
  16. Article
  17. Article
  18. Comparative Analysis of Peptidoglycans FromFrontiers in microbiology · 2019
    Article
  19. Interplay between Peptidoglycan Biology and Virulence in Gram-Negative Pathogens.Microbiology and molecular biology reviews : MMBR · 2018
    Review
  20. 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

6 authors at 1 institution in 1 country.

Weilie ZhangDepartment of Chemistry and Biochemistry, University of Notre Dame , Notre Dame, Indiana 46556, United States.
Mijoon Lee
Dusan Hesek
Elena Lastochkin
Bill Boggess
Shahriar Mobashery
University of Notre Dame · US

Funding

Penicillin-Binding Proteins, Mechanism and InhibitionR01GM061629 · NIGMS · WAYNE STATE UNIVERSITY · PI MOBASHERY, SHAHRIAR · 2001 to 2018
$5.1M
NIGMS NIH HHS GM61629NIGMS NIH HHS R01 GM061629
6 · The paper itself

Abstract

A group of Gram-negative bacteria, including the problematic pathogen Pseudomonas aeruginosa, has linked the steps in cell-wall recycling with the ability to manifest resistance to β-lactam antibiotics. A key step at the crossroads of the two events is performed by the protease AmpD, which hydrolyzes the peptide in the metabolite that influences these events. In contrast to other organisms that harbor this elaborate system, the genomic sequences of P. aeruginosa reveal it to have three paralogous genes for this protease, designated as ampD, ampDh2, and ampDh3. The recombinant gene products were purified to homogeneity, and their functions were assessed by the use of synthetic samples of three bacterial metabolites in cell-wall recycling and of three surrogates of cell-wall peptidoglycan. The results unequivocally identify AmpD as the bona fide recycling enzyme and AmpDh2 and AmpDh3 as enzymes involved in turnover of the bacterial cell wall itself. These findings define for the first time the events mediated by these three enzymes that lead to turnover of a key cell-wall recycling metabolite as well as the cell wall itself in its maturation.

Indexed as

Bacterial ProteinsChromatography, High Pressure LiquidMetalloproteasesPseudomonas aeruginosaVirulence FactorsAmpDh2 protein, Pseudomonas aeruginosaBacterial ProteinsMetalloproteasesVirulence Factors

Identifiers

PMID23510438
PMCPMC3735781
OpenAlexW2314300617

What OpenQuestion holds

Textmetadata
LicenceTDM
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.