Evidence map›Paper›PMID 42129093›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Updates to Guidance on Using Biacore for Protein-Protein Interactions Analysis.

Hui Ma, Stephen Hearty, Paul Leonard, Richard O'Kennedy

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Article in Methods in molecular biology (Clifton, N.J.), 2026. 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
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0citing papers in PubMed
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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

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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

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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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

4 authors.

Hui MaSchool of Biochemistry & Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Dublin, Ireland.
Stephen HeartyRidgeline Discovery GmbH, Basel, Switzerland.
Paul LeonardSchool of Biotechnology, Dublin City University, Dublin, Ireland. Paul.leonard@dcu.ie.
Richard O'KennedySchool of Biotechnology, Dublin City University, Dublin, Ireland. Richard.okennedy@dcu.ie.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The use of optical biosensors for studying macromolecular interactions is now considered essential technology for understanding the biophysical properties of potential therapeutic and diagnostic reagents. Indeed, according to Cytiva (2025, Key-SPR-applications. https://www.cytivalifesciences.com/en/us/solutions/protein-research/Interaction-analysis-with-Biacore-surface-plasmon-resonance-SPR/Key-SPR-applications ), over 50 000 Biacore papers have been published to date, the sheer volume and variety of which present a daunting task for the burgeoning Biacore user to accumulate and decipher. This chapter is designed to provide the reader with the tools necessary to prepare, design, and efficiently execute a kinetic experiment on Biacore. This document is written to guide the Biacore user through basic theory, system maintenance, and assay setup, while also offering some practical tips that we find useful for Biacore-based studies. Many kinetic-based screening assays require rigorous sample preparation and purification prior to analysis. To highlight these procedures, this protocol describes the kinetic characterization of single-chain Fv (scFv) antibody fragments from crude bacterial lysates using an antibody affinity capture approach. Although we specifically describe the capture of HA-tagged scFv antibody fragments to an anti-HA tag monoclonal antibody-immobilized surface prior to kinetic analysis, these methodologies are universally applicable and can be used for practically any affinity pair and most Biacore systems.

Indexed as

Protein Interaction MappingProteinsSurface Plasmon ResonanceBiosensing TechniquesKineticsProtein BindingProteinsAnalysisAntibodyBiacoreBiosensorInteractionsKineticsPlasmonProtein–proteinResonanceSurface

Identifiers

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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 OpenQuestion graph.