Evidence map›Paper›PMID 37876809›Full record

ArticleiScience2023

Deciphering the role of recurrent FAD-dependent enzymes in bacterial phosphonate catabolism.

Erika Zangelmi, Francesca Ruffolo, Tamara Dinhof, Marco Gerdol, Marco Malatesta, Jason P Chin, Claudio Rivetti, Andrea Secchi, Katharina Pallitsch, Alessio Peracchi

Open access · goldAbstract read
In one paragraph

Article in iScience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. The Substrate Versatility of ΔMolecules (Basel, Switzerland) · 2026
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  5. Article
  6. Draft genome sequence of glyphosate-degradingMicrobiology resource announcements · 2025
    Article
  7. Article
  8. Laundry IsolateMicroorganisms · 2024
    Article
  9. Glyphosate-Induced Phosphonatase Operons in Soil Bacteria of the GenusInternational journal of molecular sciences · 2024
    Article
  10. Discovery of a glyphosate oxidase in nature.FEMS microbiology letters · 2024
    Article
  11. 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

10 authors at 4 institutions in 3 countries.

Erika ZangelmiDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy.
Francesca RuffoloDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy.
Tamara DinhofInstitute of Organic Chemistry, Faculty of Chemistry, University of Vienna, 1090 Vienna, Austria.
Marco GerdolDepartment of Life Sciences, University of Trieste, Via Giorgieri 5, 34127 Trieste, Italy.
Marco MalatestaDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy.
Jason P ChinSchool of Biological Sciences and Institute for Global Food Security, Queen's University Belfast, 19 Chlorine Gardens, BT9 5DL Belfast, UK.
Claudio RivettiDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy.
Andrea SecchiDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy.
Katharina PallitschInstitute of Organic Chemistry, Faculty of Chemistry, University of Vienna, 1090 Vienna, Austria.
Alessio PeracchiDepartment of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy.
University of Parma · ITUniversity of Vienna · ATQueen's University Belfast · GBUniversity of Trieste · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphonates-compounds containing a direct C-P bond-represent an important source of phosphorus in some environments. The most common natural phosphonate is 2-aminoethylphosphonate (AEP). Many bacteria can break AEP down through specialized "hydrolytic" pathways, which start with the conversion of AEP into phosphonoacetaldehyde (PAA), catalyzed by the transaminase PhnW. However, the substrate scope of these pathways is very narrow, as PhnW cannot process other common AEP-related phosphonates, notably

Indexed as

BacteriologyEnzymologyMicrobial metabolism

Identifiers

PMID37876809
PMCPMC10590968
OpenAlexW4387339870

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.