Evidence map›Paper›PMID 36703359›Full record

ArticleCommunications chemistry2020

Enzymatic kinetic resolution of desmethylphosphinothricin indicates that phosphinic group is a bioisostere of carboxyl group.

Daniela De Biase, Francesca Cappadocio, Eugenia Pennacchietti, Fabio Giovannercole, Antonio Coluccia, Jouko Vepsäläinen, Alex Khomutov

Open access · goldAbstract read
In one paragraph

Article in Communications chemistry, 2020. 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
0.7field-weighted citation impact, top 34% 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, 18 citations in OpenAlex.

  1. Article
  2. Frontiers in microbiology · 2026
    Article
  3. Article
  4. Article
  5. Article
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  8. Article
  9. OrganophosphorusFrontiers in chemistry · 2024
    Article
  10. Article
  11. 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

7 authors at 3 institutions in 3 countries.

Daniela De BiaseDepartment of Medico-Surgical Sciences and Biotechnologies, Laboratory Affiliated to Istituto Pasteur Italia-Fondazione Cenci Bolognetti, Sapienza University of Rome, Corso della Repubblica 79, I-04100, Latina, Italy. daniela.debiase@uniroma1.it.ORCID http://orcid.org/0000-0003-3536-9927
Francesca CappadocioDepartment of Medico-Surgical Sciences and Biotechnologies, Laboratory Affiliated to Istituto Pasteur Italia-Fondazione Cenci Bolognetti, Sapienza University of Rome, Corso della Repubblica 79, I-04100, Latina, Italy.
Eugenia PennacchiettiDepartment of Medico-Surgical Sciences and Biotechnologies, Laboratory Affiliated to Istituto Pasteur Italia-Fondazione Cenci Bolognetti, Sapienza University of Rome, Corso della Repubblica 79, I-04100, Latina, Italy.
Fabio GiovannercoleDepartment of Medico-Surgical Sciences and Biotechnologies, Laboratory Affiliated to Istituto Pasteur Italia-Fondazione Cenci Bolognetti, Sapienza University of Rome, Corso della Repubblica 79, I-04100, Latina, Italy.ORCID http://orcid.org/0000-0003-0324-1398
Antonio ColucciaDepartment of Chemistry and Technology of Drugs, Laboratory Affiliated to Istituto Pasteur Italia-Fondazione Cenci Bolognetti, Sapienza University of Rome, Piazzale Aldo Moro 5, I-00185, Rome, Italy.ORCID http://orcid.org/0000-0002-7940-8206
Jouko VepsäläinenSchool of Pharmacy, Biocenter Kuopio, University of Eastern Finland, Kuopio Campus, P.O. Box 1627, Kuopio, FI-70211, Finland.ORCID http://orcid.org/0000-0001-5587-0706
Alex KhomutovEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov St., 32, Moscow, 119991, Russia. alexkhom@list.ru.ORCID http://orcid.org/0000-0001-6833-7855
Istituto Pasteur · ITEngelhardt Institute of Molecular Biology · RUUniversity of Eastern Finland · FI

Funding

Academy of Finland (Suomen Akatemia) 315487Russian Foundation for Basic Research (RFBR) 17-00-00395Sapienza Università di Roma (Sapienza University of Rome) RM11916B861B9985
6 · The paper itself

Abstract

Escherichia coli glutamate decarboxylase (EcGadB), a pyridoxal 5'-phosphate (PLP)-dependent enzyme, is highly specific for L-glutamate and was demonstrated to be effectively immobilised for the production of γ-aminobutyric acid (GABA), its decarboxylation product. Herein we show that EcGadB quantitatively decarboxylates the L-isomer of D,L-2-amino-4-(hydroxyphosphinyl)butyric acid (D,L-Glu-γ-P

Identifiers

PMID36703359
PMCPMC9814759
OpenAlexW3081796152

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.