Evidence map›Paper›PMID 38248420›Full record

ArticleBiosensors2024

Photonic Crystal Surface Mode Real-Time Imaging of RAD51 DNA Repair Protein Interaction with the ssDNA Substrate.

Galina Nifontova, Cathy Charlier, Nizar Ayadi, Fabrice Fleury, Alexander Karaulov, Alyona Sukhanova, Igor Nabiev

Open access · goldAbstract read
In one paragraph

Article in Biosensors, 2024. 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
0.7field-weighted citation impact, top 33% 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, 3 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

7 authors at 3 institutions in 2 countries.

Galina NifontovaLaboratoire de Recherche en Nanosciences, LRN-EA4682, Structure Fédérative de Recherche Cap Santé, UFR de Pharmacie, Université de Reims Champagne-Ardenne, 51100 Reims, France.ORCID 0000-0002-6956-5654
Cathy CharlierNantes Université, CNRS, US2B, UMR 6286, IMPACT Platform and SFR Bonamy, 44000 Nantes, France.
Nizar AyadiNantes Université, CNRS, US2B, UMR 6286, DNA Repair Group, 44000 Nantes, France.
Fabrice FleuryNantes Université, CNRS, US2B, UMR 6286, DNA Repair Group, 44000 Nantes, France.ORCID 0000-0002-6764-5060
Alexander KaraulovDepartment of Clinical Immunology and Allergology, Institute of Molecular Medicine, Sechenov First Moscow State Medical University (Sechenov University), 119146 Moscow, Russia.ORCID 0000-0002-1930-5424
Alyona SukhanovaLaboratoire de Recherche en Nanosciences, LRN-EA4682, Structure Fédérative de Recherche Cap Santé, UFR de Pharmacie, Université de Reims Champagne-Ardenne, 51100 Reims, France.ORCID 0000-0003-2796-7898
Igor NabievLaboratoire de Recherche en Nanosciences, LRN-EA4682, Structure Fédérative de Recherche Cap Santé, UFR de Pharmacie, Université de Reims Champagne-Ardenne, 51100 Reims, France.ORCID 0000-0002-8391-040X
Centre National de la Recherche Scientifique · FRLaboratoire de Recherche en NanosciencesSechenov University · RU

Funding

Agence Nationale de Recherche, France 20-CE19-009-02Ministry of Science and Higher Education of the Russian Federation 075-15-2021-935
6 · The paper itself

Abstract

Photonic crystals (PCs) are promising tools for label-free sensing in drug discovery screening, diagnostics, and analysis of ligand-receptor interactions. Imaging of PC surface modes has emerged as a novel approach to the detection of multiple binding events at the sensor surface. PC surface modification and decoration with recognition units yield an interface providing the highly sensitive detection of cancer biomarkers, antibodies, and oligonucleotides. The RAD51 protein plays a central role in DNA repair via the homologous recombination pathway. This recombinase is essential for the genome stability and its overexpression is often correlated with aggressive cancer. RAD51 is therefore a potential target in the therapeutic strategy for cancer. Here, we report the designing of a PC-based array sensor for real-time monitoring of oligonucleotide-RAD51 recruitment by means of surface mode imaging and validation of the concept of this approach. Our data demonstrate that the designed biosensor ensures the highly sensitive multiplexed analysis of association-dissociation events and detection of the biomarker of DNA damage using a microfluidic PC array. The obtained results highlight the potential of the developed technique for testing the functionality of candidate drugs, discovering new molecular targets and drug entities. This paves the way to further adaption and bioanalytical use of the biosensor for high-content screening to identify new DNA repair inhibitor drugs targeting the RAD51 nucleoprotein filament or to discover new molecular targets.

Indexed as

AntibodiesNeoplasmsBiomarkers, TumorDiagnostic ImagingDNA RepairDNA, Single-StrandedHumansOligonucleotidesRad51 RecombinaseAntibodiesBiomarkers, TumorDNA, Single-StrandedOligonucleotidesRAD51 protein, humanRad51 Recombinaseassociation–dissociation kineticsDNA repair proteinlabel-free detectionmicrofluidic arrayone-dimensional photonic crystalRAD51surface mode imaging

Identifiers

PMID38248420
PMCPMC10813746
OpenAlexW4390878698

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.