Evidence map›Paper›PMID 40612260›Full record

ArticleMethodsX2025

Innovation of new Florescent-epitope technique for immune assay methods.

Zahra Farjami, Mohammad Mehdi Akbarin

Abstract read
In one paragraph

Article in MethodsX, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Zahra FarjamiDepartment of Modern Sciences and Technologies, Faculty of Medicine, Mashhad University of Medical, Mashhad, Iran.
Mohammad Mehdi AkbarinBiological Sciences Department- Faculty of Higher Education Studies, FESC, UNAM, Mexico City, Mexico.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The proposed method, which utilizes a FAM fluorescent dye and a BHQ1 quencher complex for indirect analyte assessment through antigen-antibody reactions, represents a significant advancement in immune assay technology. By leveraging the unique physical properties of the FAM-BHQ1 complex, we achieve enhanced accuracy and efficiency in analyte quantification. The complex's fluorescence characteristics, along with its inherent stability and resistance to photobleaching, contribute to improved data reproducibility. Furthermore, the system's adaptability to multiplex assays allows for simultaneous detection of multiple analytes within a single reaction, significantly increasing throughput and reducing assay time. Favorable conditions enhance the method's performance, including a broad dynamic range and minimal background signal. The inherent advantages of this approach-increased sensitivity and specificity, coupled with streamlined workflow-promise to revolutionize immunological research and diagnostics. Implementing this FAM-BHQ1-based method will facilitate more precise and reliable detection and quantification of a broader range of analytes, leading to improved diagnostic accuracy and more effective therapeutic interventions.•Despite the importance of immune assays, these assays face challenges such as standardization, variability, and issues with sensitivity.•Our propose is the use of the FAM fluorescent day, which can attach to the Fc region of the antibody and BHQ1•This limitation is the time and number of epitope-to-paratope attachments.

Indexed as

BHQ-1Epitope-paratope reactionFAMFlorescent dyeImmunoassayProb antibody

Identifiers

PMID40612260
PMCPMC12226053

What Socratic holds

Textmetadata
LicenceCC BY
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Registered trials

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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 Socratic graph.