ReviewMicrobial drug resistance (Larchmont, N.Y.)2016
Orthologous and Paralogous AmpD Peptidoglycan Amidases from Gram-Negative Bacteria.
Review in Microbial drug resistance (Larchmont, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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.
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.
Who cites it
11 citing papers in PubMed, 30 citations in OpenAlex.
- Mutations inMicrobiology spectrum · 2025Article
- A comparative in silico analysis of the vlhA gene regions of Mycoplasma gallisepticum and Mycoplasma synoviae isolates from commercial hen farms in Mexico.Access microbiology · 2025Article
- YgfB increases β-lactam resistance in Pseudomonas aeruginosa by counteracting AlpA-mediated ampDh3 expression.Communications biology · 2023Article
- Role of peptidoglycan recycling enzymes AmpD and AnmK inFrontiers in cellular and infection microbiology · 2022Article
- Fluorescence Assessment of the AmpR-Signaling Network ofACS chemical biology · 2020Article
- Constructing and deconstructing the bacterial cell wall.Protein science : a publication of the Protein Society · 2020Review
- Peptidoglycomics reveals compositional changes in peptidoglycan between biofilm- and planktonic-derivedThe Journal of biological chemistry · 2020Article
- Regulation of AmpC-Driven β-Lactam Resistance in Pseudomonas aeruginosa: Different Pathways, Different Signaling.mSystems · 2019Article
- A New Suite of Allelic-Exchange Vectors for the Scarless Modification of Proteobacterial Genomes.Applied and environmental microbiology · 2019Article
- Interplay between Peptidoglycan Biology and Virulence in Gram-Negative Pathogens.Microbiology and molecular biology reviews : MMBR · 2018Review
- Cell-Wall Recycling of the Gram-Negative Bacteria and the Nexus to Antibiotic Resistance.Chemical reviews · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Cell wall recycling and β-lactam antibiotic resistance are linked in Enterobacteriaceae and in Pseudomonas aeruginosa. This process involves a large number of murolytic enzymes, among them a cytoplasmic peptidoglycan amidase AmpD, which plays an essential role by cleaving the peptide stem from key intermediates en route to the β-lactamase production (a resistance mechanism) and cell wall recycling. Uniquely, P. aeruginosa has two additional paralogues of AmpD, designated AmpDh2 and AmpDh3, which are periplasmic enzymes. Despite the fact that AmpDh2 and AmpDh3 share a common motif for their respective catalytic domains, they are each comprised of multidomain architectures and exhibit distinct oligomerization properties. We review herein the structural and biochemical properties of orthologous and paralogous AmpD proteins and discuss their implication in cell wall recycling and antibiotic resistance processes.
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Identifiers
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Registered trials
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.