ArticlemAbs2016
Cross-arm binding efficiency of an EGFR x c-Met bispecific antibody.
Article in mAbs, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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.
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
28 citing papers in PubMed.
- MET Enhances Amivantamab Binding to EGFR and Antibody-Dependent Cellular Toxicity.Cancer science · 2026Article
- The User's Guide to Amivantamab.Targeted oncology · 2025Review
- Quantitative pharmacology of dual-targeted bicistronic CAR-T-cell therapy using multiscale mechanistic modeling.CPT: pharmacometrics & systems pharmacology · 2025Article
- A CD25×TIGIT bispecific antibody induces anti-tumor activity through selective intratumoral Treg cell depletion.Molecular therapy : the journal of the American Society of Gene Therapy · 2024Article
- c-MET and the immunological landscape of cancer: novel therapeutic strategies for enhanced anti-tumor immunity.Frontiers in immunology · 2024Review
- Targeting lung cancer with clinically relevant EGFR mutations using anti-EGFR RNA aptamer.Molecular therapy. Nucleic acids · 2023Article
- The PD-1- and LAG-3-targeting bispecific molecule tebotelimab in solid tumors and hematologic cancers: a phase 1 trial.Nature medicine · 2023Article
- The development of amivantamab for the treatment of non-small cell lung cancer.Respiratory research · 2023Review
- Bispecific antibodies in cancer therapy: Target selection and regulatory requirements.Acta pharmaceutica Sinica. B · 2023Review
- Design and selection of optimal ErbB-targeting bispecific antibodies in pancreatic cancer.Frontiers in immunology · 2023Article
- Avidity in antibody effector functions and biotherapeutic drug design.Nature reviews. Drug discovery · 2022Review
- Trispecific T-cell engagers for dual tumor-targeting of colorectal cancer.Oncoimmunology · 2022Article
- Bioassay Development for Bispecific Antibodies-Challenges and Opportunities.International journal of molecular sciences · 2021Review
- Antibody-based cancer therapy.Oncogene · 2021Review
- Antibody Structure and Function: The Basis for Engineering Therapeutics.Antibodies (Basel, Switzerland) · 2019Review
- Bispecific antibodies: a mechanistic review of the pipeline.Nature reviews. Drug discovery · 2019Review
- Next generation antibody drugs: pursuit of the 'high-hanging fruit'.Nature reviews. Drug discovery · 2018Review
- Cell-type specific potent Wnt signaling blockade by bispecific antibody.Scientific reports · 2018Article
- Decomposing Dynamical Couplings in Mutated scFv Antibody Fragments into Stabilizing and Destabilizing Effects.Journal of the American Chemical Society · 2017Article
- Enhanced tumor-targeting selectivity by modulating bispecific antibody binding affinity and format valence.Scientific reports · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multispecific proteins, such as bispecific antibodies (BsAbs), that bind to two different ligands are becoming increasingly important therapeutic agents. Such BsAbs can exhibit markedly increased target binding and target residence time when both pharmacophores bind simultaneously to their targets. The cross-arm binding efficiency (χ) describes an increase in apparent affinity when a BsAb binds to the second target or receptor (R2) following its binding to the first target or receptor (R1) on the same cell. χ is an intrinsic characteristic of a BsAb mostly related to the binding epitopes on R1 and R2. χ can have significant impacts on the binding to R2 for BsAbs targeting two receptors on the same cell. JNJ-61186372, a BsAb that targets epidermal growth factor receptor (EGFR) and c-Met, was used as the model compound for establishing a method to characterize χ. The χ for JNJ-61186372 was successfully determined via fitting of in vitro cell binding data to a ligand binding model that incorporated χ. The model-derived χ value was used to predict the binding of JNJ-61186372 to individual EGFR and c-Met receptors on tumor cell lines, and the results agreed well with the observed IC50 for EGFR and c-Met phosphorylation inhibition by JNJ-61186372. Consistent with the model, JNJ-61186372 was shown to be more effective than the combination therapy of anti-EGFR and anti-c-Met monovalent antibodies at the same dose level in a mouse xenograft model. Our results showed that χ is an important characteristic of BsAbs, and should be considered for rationale design of BsAbs targeting two membrane bound targets on the same cell.
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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.