Evidence map›Paper›PMID 30191734›Full record

ArticleJournal of enzyme inhibition and medicinal chemistry2018

In the quest for new targets for pathogen eradication: the adenylosuccinate synthetase from the bacterium Helicobacter pylori.

Ante Bubić, Natalia Mrnjavac, Igor Stuparević, Marta Łyczek, Beata Wielgus-Kutrowska, Agnieszka Bzowska, Marija Luić, Ivana Leščić Ašler

Open access · goldAbstract read
In one paragraph

Article in Journal of enzyme inhibition and medicinal chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

7 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
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  3. Vitamin B6 inhibits activity ofJournal of enzyme inhibition and medicinal chemistry · 2024
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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 3 institutions in 2 countries.

Ante Bubića Division of Physical Chemistry , Ruđer Bošković Institute , Zagreb , Croatia.ORCID http://orcid.org/0000-0003-4548-9455
Natalia Mrnjavaca Division of Physical Chemistry , Ruđer Bošković Institute , Zagreb , Croatia.
Igor Stuparevićb Department of Chemistry and Biochemistry, Faculty of Food Technology and Biotechnology , University of Zagreb , Zagreb , Croatia.ORCID http://orcid.org/0000-0002-9878-5007
Marta Łyczekc Division of Biophysics, Institute of Experimental Physics, Faculty of Physics , University of Warsaw , Warsaw , Poland.
Beata Wielgus-Kutrowskac Division of Biophysics, Institute of Experimental Physics, Faculty of Physics , University of Warsaw , Warsaw , Poland.
Agnieszka Bzowskac Division of Biophysics, Institute of Experimental Physics, Faculty of Physics , University of Warsaw , Warsaw , Poland.
Marija Luića Division of Physical Chemistry , Ruđer Bošković Institute , Zagreb , Croatia.
Ivana Leščić Ašlera Division of Physical Chemistry , Ruđer Bošković Institute , Zagreb , Croatia.ORCID http://orcid.org/0000-0002-0826-7493
Ruđer Bošković Institute · HRUniversity of Warsaw · PLUniversity of Zagreb · HR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adenylosuccinate synthetase (AdSS) is an enzyme at regulatory point of purine metabolism. In pathogenic organisms which utilise only the purine salvage pathway, AdSS asserts itself as a promising drug target. One of these organisms is Helicobacter pylori, a wide-spread human pathogen involved in the development of many diseases. The rate of H. pylori antibiotic resistance is on the increase, making the quest for new drugs against this pathogen more important than ever. In this context, we describe here the properties of H. pylori AdSS. This enzyme exists in a dimeric active form independently of the presence of its ligands. Its narrow stability range and pH-neutral optimal working conditions reflect the bacterium's high level of adaptation to its living environment. Efficient inhibition of H. pylori AdSS with hadacidin and adenylosuccinate gives hope of finding novel drugs that aim at eradicating this dangerous pathogen.

Indexed as

Adenosine MonophosphateAdenylosuccinate SynthaseDose-Response Relationship, DrugEnzyme InhibitorsGlycineHelicobacter pyloriMolecular StructureStructure-Activity RelationshipAdenosine MonophosphateadenylosuccinateAdenylosuccinate SynthaseEnzyme InhibitorsGlycinehadacidinadenylosuccinate synthetaseanalytical ultracentrifugationenzyme inhibitionenzyme kineticsHelicobacter pylorioligomeric state

Identifiers

PMID30191734
PMCPMC6136348
OpenAlexW2892006227

What OpenQuestion holds

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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.