Evidence map›Paper›PMID 32601479›Full record

ArticleScientific reports2020

A novel FRET peptide assay reveals efficient Helicobacter pylori HtrA inhibition through zinc and copper binding.

Sabine Bernegger, Cyrill Brunner, Matej Vizovišek, Marko Fonovic, Gaetano Cuciniello, Flavia Giordano, Vesna Stanojlovic, Miroslaw Jarzab, Philip Simister, Stephan M Feller and 6 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

17 citing papers in PubMed, 33 citations in OpenAlex.

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  17. Cells · 2020
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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

16 authors at 5 institutions in 6 countries.

Sabine BerneggerMicrobiology, Department of Biosciences, University of Salzburg, Billrothstrasse 11, 5020, Salzburg, Austria.
Cyrill BrunnerInstitut für Pharmazeutische Wissenschaften, ETH Zürich, Vladimir-Prelog-Weg 4, 8093, Zurich, Switzerland.
Matej VizovišekDepartment of Biochemistry and Molecular and Structural Biology, Jozef Stefan Institute, Jamova 39, 1000, Ljubljana, Slovenia.
Marko FonovicDepartment of Biochemistry and Molecular and Structural Biology, Jozef Stefan Institute, Jamova 39, 1000, Ljubljana, Slovenia.
Gaetano CucinielloMicrobiology, Department of Biosciences, University of Salzburg, Billrothstrasse 11, 5020, Salzburg, Austria.
Flavia GiordanoOrganic Chemistry and NMR Spectroscopy for Protein Research, Department of Biosciences, University of Salzburg, Billrothstrasse 11, 5020, Salzburg, Austria.
Vesna StanojlovicOrganic Chemistry and NMR Spectroscopy for Protein Research, Department of Biosciences, University of Salzburg, Billrothstrasse 11, 5020, Salzburg, Austria.
Miroslaw JarzabMicrobiology, Department of Biosciences, University of Salzburg, Billrothstrasse 11, 5020, Salzburg, Austria.
Philip SimisterBiological Systems Architecture Group, Department of Oncology, Weatherall Institute of Molecular Medicine, University of Oxford, Oxford, UK.
Stephan M FellerTumor Biology Unit, Institute of Molecular Medicine, Charles Tanford Protein Center, Martin-Luther-University Halle-Wittenberg, Halle, Germany.
Gerhard ObermeyerMembrane Physics, Department of Biosciences, University of Salzburg, Billrothstrasse 11, 5020, Salzburg, Austria.
Gernot PosseltMicrobiology, Department of Biosciences, University of Salzburg, Billrothstrasse 11, 5020, Salzburg, Austria.
Boris TurkDepartment of Biochemistry and Molecular and Structural Biology, Jozef Stefan Institute, Jamova 39, 1000, Ljubljana, Slovenia.
Chiara CabreleOrganic Chemistry and NMR Spectroscopy for Protein Research, Department of Biosciences, University of Salzburg, Billrothstrasse 11, 5020, Salzburg, Austria.
Gisbert SchneiderInstitut für Pharmazeutische Wissenschaften, ETH Zürich, Vladimir-Prelog-Weg 4, 8093, Zurich, Switzerland.
Silja WesslerMicrobiology, Department of Biosciences, University of Salzburg, Billrothstrasse 11, 5020, Salzburg, Austria. silja.wessler@sbg.ac.at.
University of Salzburg · ATJožef Stefan Institute · SIETH Zurich · CHMartin Luther University Halle-Wittenberg · DEMRC Weatherall Institute of Molecular Medicine · GB

Funding

Austrian Science Fund FWF I 4360Austrian Science Fund FWF I_4360Austrian Science Fund FWF P 31507Austrian Science Fund FWF P_31507
6 · The paper itself

Abstract

Helicobacter pylori (H. pylori) secretes the chaperone and serine protease high temperature requirement A (HtrA) that cleaves gastric epithelial cell surface proteins to disrupt the epithelial integrity and barrier function. First inhibitory lead structures have demonstrated the essential role of HtrA in H. pylori physiology and pathogenesis. Comprehensive drug discovery techniques allowing high-throughput screening are now required to develop effective compounds. Here, we designed a novel fluorescence resonance energy transfer (FRET) peptide derived from a gel-based label-free proteomic approach (direct in-gel profiling of protease specificity) as a valuable substrate for H. pylori HtrA. Since serine proteases are often sensitive to metal ions, we investigated the influence of different divalent ions on the activity of HtrA. We identified Zn

Indexed as

Bacterial ProteinsCadherinsCopperDrug Evaluation, PreclinicalFluorescence Resonance Energy TransferHelicobacter InfectionsHelicobacter pyloriMolecular ChaperonesPeptidesProteomicsSerine EndopeptidasesSerine ProteasesZincBacterial ProteinsCadherinsCopperHtrA protein, H pyloriMolecular ChaperonesPeptidesSerine EndopeptidasesSerine ProteasesZinc

Identifiers

PMID32601479
PMCPMC7324608
OpenAlexW3037223166

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.