Evidence map›Paper›PMID 29104305›Full record

ArticleElectrochimica acta2017

Full-length antibodies versus single-chain antibody fragments for a selective impedimetric lectin-based glycoprofiling of prostate specific antigen.

Stefan Belicky, Pavel Damborsky, Julia Zapatero-Rodríguez, Richard O'Kennedy, Jan Tkac

Abstract read
In one paragraph

Article in Electrochimica acta, 2017. 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
1.9field-weighted citation impact, top 15% 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, 19 citations in OpenAlex.

  1. Synthesis of site-specific Fab-drug conjugates using ADP-ribosyl cyclases.Protein science : a publication of the Protein Society · 2024
    Article
  2. Characterization of NovelInternational journal of molecular sciences · 2024
    Article
  3. Nanobodies: a new potential for prostate cancer treatment.Journal of cancer research and clinical oncology · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Current Progress in CAR-T Cell Therapy for Solid Tumors.International journal of biological sciences · 2019
    Review
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

5 authors at 3 institutions in 2 countries.

Stefan BelickyInstitute of Chemistry, Slovak Academy of Sciences, Dubravska cesta 9, 845 38 Bratislava, Slovakia.
Pavel DamborskyInstitute of Chemistry, Slovak Academy of Sciences, Dubravska cesta 9, 845 38 Bratislava, Slovakia.
Julia Zapatero-RodríguezBiomedical Diagnostics Institute (BDI), Dublin City University, Glasnevin, Dublin 9, Ireland.
Richard O'KennedyBiomedical Diagnostics Institute (BDI), Dublin City University, Glasnevin, Dublin 9, Ireland.
Jan TkacInstitute of Chemistry, Slovak Academy of Sciences, Dubravska cesta 9, 845 38 Bratislava, Slovakia.
Dublin City University · IESlovak Academy of Sciences · SKInstitute of Chemistry of the Slovak Academy of Sciences · SK

Funding

European Research Council 311532
6 · The paper itself

Abstract

The main aim of the research was to design a functional impedimetric biosensor able to glycoprofile prostate specific antigen (PSA), a biomarker for prostate cancer (PCa), with high specificity using lectins as glycan recognising proteins. Traditionally, full-length antibody is immobilised on the biosensor interface for specific capture of PSA with subsequent glycoprofiling of PSA by addition of lectins. Since full-length antibodies contain glycans in the Fc domain, particular attention has to be paid to suppress direct binding of lectins to immobilised full-length antibodies, which would compromise accurate glycoprofiling. This issue is addressed here using a recombinant single-chain antibody fragments (scAb), which do not contain any carbohydrate moiety. Surface plasmon resonance was applied to prove negligible interaction of lectins with immobilised scAb fragments, while substantial binding of lectins to full length antibodies was observed. Eight different biosensor designs were tested for their ability to detect PSA. The biosensor device based on scAb fragments covalently immobilised on the gold electrode surface, patterned by a mixed SAM using standard amine coupling chemistry, proved to be the most sensitive. The scAb fragment-based biosensor exhibited sensitivity of 15.9 ± 0.8% decade

Indexed as

full-length antibodiesglycan analysisimpedimetric biosensorslectinsprostate cancersingle-chain antibody fragments (scAb)

Identifiers

PMID29104305
PMCPMC5667744
OpenAlexW2626730350

What OpenQuestion holds

Textmetadata
LicenceTDM
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.