Evidence map›Paper›PMID 39957177›Full record

ReviewmAbs2025

Quantifying antibody binding: techniques and therapeutic implications.

James Lodge, Lewis Kajtar, Rachel Duxbury, David Hall, Glenn A Burley, Joanna Cordy, James W T Yates, Zahra Rattray

Abstract readReview
In one paragraph

Review in mAbs, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. ACS central science · 2026
    Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. 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

8 authors.

James LodgeLarge Molecule Discovery, GSK, Stevenage, UK.ORCID 0000-0003-0663-6264
Lewis KajtarLarge Molecule Discovery, GSK, Stevenage, UK.
Rachel DuxburyLarge Molecule Discovery, GSK, Stevenage, UK.
David HallLarge Molecule Discovery, GSK, Stevenage, UK.
Glenn A BurleyDepartment of Pure and Applied Chemistry, University of Strathclyde, Glasgow, UK.
Joanna CordyLarge Molecule Discovery, GSK, Stevenage, UK.
James W T YatesPreclinical sciences, DMPK, GSK, Stevenage, UK.
Zahra RattrayStrathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, Glasgow, UK.ORCID 0000-0002-8371-8549

Funding

UK Biotechnology and Biological Sciences Research Council BB/Y003268/1
6 · The paper itself

Abstract

The binding kinetics of an antibody for its target antigen represent key determinants of its biological function and success as a novel biotherapeutic. Defining these interactions and kinetics is critical for understanding the pharmacological and pharmacodynamic profiles of antibodies in therapeutic applications, with line of sight to clinical translation. In this review, we discuss the latest developments in approaches to measure and modulate antibody-antigen interactions, including antibody engineering, novel antibody formats, current, and emerging technologies for measuring antibody-antigen binding interactions, and emerging perspectives within the field. We also explore how emerging computational methods are set to become powerful tools for modeling antibody-binding interactions under physiologically relevant conditions. Finally, we consider the therapeutic implications of modulating target engagement in terms of pharmacodynamics and pharmacokinetics.

Indexed as

Antibodies, MonoclonalAntigen-Antibody ReactionsAnimalsHumansProtein BindingProtein EngineeringAntibodies, MonoclonalaffinityAntibodyaviditypharmacokineticspharmacologytarget engagement

Identifiers

PMID39957177
PMCPMC11834528

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.