Evidence map›Paper›PMID 33568718›Full record

ArticleScientific reports2021

Flagellin-based electrochemical sensing layer for arsenic detection in water.

Hajnalka Jankovics, Patrik Szekér, Éva Tóth, Balázs Kakasi, Zoltán Lábadi, András Saftics, Benjamin Kalas, Miklós Fried, Péter Petrik, Ferenc Vonderviszt

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

1 citing paper in PubMed, 11 citations in OpenAlex.

  1. 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

10 authors at 2 institutions in 1 country.

Hajnalka JankovicsResearch Institute of Biomolecular and Chemical Engineering, University of Pannonia, P.O. Box 125, Veszprém, 8200, Hungary. jankovicsh@almos.uni-pannon.hu.
Patrik SzekérResearch Institute of Biomolecular and Chemical Engineering, University of Pannonia, P.O. Box 125, Veszprém, 8200, Hungary.
Éva TóthResearch Institute of Biomolecular and Chemical Engineering, University of Pannonia, P.O. Box 125, Veszprém, 8200, Hungary.
Balázs KakasiResearch Institute of Biomolecular and Chemical Engineering, University of Pannonia, P.O. Box 125, Veszprém, 8200, Hungary.
Zoltán LábadiInstitute of Technical Physics and Materials Science, Centre for Energy Research, P.O. Box 49, Budapest, 1525, Hungary.
András SafticsInstitute of Technical Physics and Materials Science, Centre for Energy Research, P.O. Box 49, Budapest, 1525, Hungary.
Benjamin KalasInstitute of Technical Physics and Materials Science, Centre for Energy Research, P.O. Box 49, Budapest, 1525, Hungary.
Miklós FriedInstitute of Technical Physics and Materials Science, Centre for Energy Research, P.O. Box 49, Budapest, 1525, Hungary.
Péter PetrikInstitute of Technical Physics and Materials Science, Centre for Energy Research, P.O. Box 49, Budapest, 1525, Hungary.
Ferenc VondervisztResearch Institute of Biomolecular and Chemical Engineering, University of Pannonia, P.O. Box 125, Veszprém, 8200, Hungary.
Centre for Energy Research · HUUniversity of Pannonia · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regular monitoring of arsenic concentrations in water sources is essential due to the severe health effects. Our goal was to develop a rapidly responding, sensitive and stable sensing layer for the detection of arsenic. We have designed flagellin-based arsenic binding proteins capable of forming stable filament structures with high surface binding site densities. The D3 domain of Salmonella typhimurium flagellin was replaced with an arsenic-binding peptide motif of different bacterial ArsR transcriptional repressor factors. We have shown that the fusion proteins developed retain their polymerization ability and have thermal stability similar to that of wild-type filament. The strong arsenic binding capacity of the monomeric proteins was confirmed by isothermal titration calorimetry (ITC), and dissociation constants (K

Indexed as

WaterArsenicElectrodesFlagellinGoldProtein ConformationProteinsSalmonella typhimuriumArsenicFlagellinGoldProteinsWater

Identifiers

PMID33568718
PMCPMC7876115
OpenAlexW3128806334

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.