ArticleACS chemical biology2024
Development of Luminescent Biosensors for Calprotectin.
Article in ACS chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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.
Who cites it
7 citing papers in PubMed.
- Triple-Helix Biomolecules Construct Self-Adaptive Multi-Phase Interfaces for Dendrites Immunized Zinc Metal Anodes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Biosensor-Based Detection of Calprotectin and Lactoferrin as Neutrophil-Derived Markers of Inflammatory Bowel Diseases: From Molecular Pathophysiology to Point-of-Care Platforms.International journal of molecular sciences · 2026Review
- RAPPID-M: A Mix-and-Measure Bioluminescent Sandwich Immunoassay Based on Generic Antibody-Binding Protein M.ACS sensors · 2025Article
- Article
- The Role of Calprotectin in the Diagnosis and Treatment of Inflammatory Bowel Disease.International journal of molecular sciences · 2025Review
- Engineered protein G variants for multifunctional antibody-based assemblies.Protein science : a publication of the Protein Society · 2025Article
- Enzyme fragment complementation driven by nucleic acid hybridization sans self-labeling protein.Bioorganic chemistry · 2025Article
Corrections and comments
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Authors and funding
15 authors.
Funding
Abstract
Calprotectin, a metal ion-binding protein complex, plays a crucial role in the innate immune system and has gained prominence as a biomarker for various intestinal and systemic inflammatory and infectious diseases, including inflammatory bowel disease (IBD) and tuberculosis (TB). Current clinical testing methods rely on enzyme-linked immunosorbent assays (ELISAs), limiting accessibility and convenience. In this study, we introduce the Fab-Enabled Split-luciferase Calprotectin Assay (FESCA), a novel quantitative method for calprotectin measurement. FESCA utilizes two new fragment antigen binding proteins (Fabs), CP16 and CP17, that bind to different epitopes of the calprotectin complex. These Fabs are fused with split NanoLuc luciferase fragments, enabling the reconstitution of active luciferase upon binding to calprotectin either in solution or in varied immobilized assay formats. FESCA's output luminescence can be measured with standard laboratory equipment as well as consumer-grade cell phone cameras. FESCA can detect physiologically relevant calprotectin levels across various sample types, including serum, plasma, and whole blood. Notably, FESCA can detect abnormally elevated native calprotectin from TB patients. In summary, FESCA presents a convenient, low-cost, and quantitative method for assessing calprotectin levels in various biological samples, with the potential to improve the diagnosis and monitoring of inflammatory diseases, especially in at-home or point-of-care settings.
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Registered trials
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.