Evidence map›Paper›PMID 30166577›Full record

ArticleScientific reports2018

A fundamental catalytic difference between zinc and manganese dependent enzymes revealed in a bacterial isatin hydrolase.

Theis Sommer, Kaare Bjerregaard-Andersen, Lalita Uribe, Michael Etzerodt, Gregor Diezemann, Jürgen Gauss, Michele Cascella, J Preben Morth

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 37% 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

6 citing papers in PubMed, 15 citations in OpenAlex.

  1. A Thermostable Bacterial Metallohydrolase that Degrades Organophosphate Plasticizers.Chembiochem : a European journal of chemical biology · 2025
    Article
  2. An aldolase-dependent phloroglucinol degradation pathway inApplied and environmental microbiology · 2024
    Article
  3. Article
  4. Utilization of diverse organophosphorus pollutants by marine bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. 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

8 authors at 4 institutions in 3 countries.

Theis SommerNorwegian Center for Molecular Medicine, Nordic EMBL Partnership University of Oslo, Gaustadalléen 21, 0349, Oslo, Norway.
Kaare Bjerregaard-AndersenDepartment of Chemistry, University of Oslo, Sem Sælands vei 26, 0371, Oslo, Norway.ORCID 0000-0003-3609-3408
Lalita UribeInstitut für Physikalische Chemie, Johannes Gutenberg-Universität Mainz, Duesbergweg 10-14, 55128, Mainz, Germany.
Michael EtzerodtDepartment of Molecular Biology and Genetics, Aarhus University, Gustav Wieds vej 10C, 8000, Aarhus, Denmark.
Gregor DiezemannInstitut für Physikalische Chemie, Johannes Gutenberg-Universität Mainz, Duesbergweg 10-14, 55128, Mainz, Germany.
Jürgen GaussInstitut für Physikalische Chemie, Johannes Gutenberg-Universität Mainz, Duesbergweg 10-14, 55128, Mainz, Germany.
Michele CascellaDepartment of Chemistry, University of Oslo, Sem Sælands vei 26, 0371, Oslo, Norway. michele.cascella@kjemi.uio.no.ORCID 0000-0003-2266-5399
J Preben MorthNorwegian Center for Molecular Medicine, Nordic EMBL Partnership University of Oslo, Gaustadalléen 21, 0349, Oslo, Norway. premo@dtu.dk.
Johannes Gutenberg University Mainz · DEUniversity of Oslo · NOAarhus University · DKOslo University Hospital · NO

Funding

Lundbeckfonden (Lundbeck Foundation) R34-A3616Norges Forskningsråd (Research Council of Norway) 262695Norges Forskningsråd (Research Council of Norway) ES486454
6 · The paper itself

Abstract

The catalytic mechanism of the cyclic amidohydrolase isatin hydrolase depends on a catalytically active manganese in the substrate-binding pocket. The Mn

Indexed as

BiocatalysisAmidohydrolasesAmino Acid SequenceArylformamidaseBacterial ProteinsCatalytic DomainConserved SequenceEvolution, MolecularGlutamineHydrolysisIsatinKynurenineManganeseModels, MolecularProtonsQuantum TheoryAmidohydrolasesArylformamidaseBacterial ProteinsGlutamineIsatinKynurenineManganeseProtonsZinc

Identifiers

PMID30166577
PMCPMC6117287
OpenAlexW2887996201

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.