ArticleProceedings of the National Academy of Sciences of the United States of America2022
Switchable assembly and function of antibody complexes in vivo using a small molecule.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- P329G-engager: a universal mix & match antibody-based adaptor platform for cancer immunotherapy.mAbs · 2026Article
- A Drug-Gated, Modular STAb-T Immunotherapy With External Control.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- T cell engagers in autoimmune diseases.Nature reviews. Immunology · 2026Review
- Repurposing nuclear receptors for ligand-responsive liquid condensate formation and gene regulation.Nature communications · 2026Article
- Conditionally Activatable Antibody Platforms: Mechanisms, Modalities, and Clinical Translation Potential.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- Ligand-induced assembly of antibody variable fragments for the chemical regulation of biological processes.Cell chemical biology · 2025Article
- Article
- Bispecific antibody drug conjugates: Making 1+1>2.Acta pharmaceutica Sinica. B · 2024Review
- Photoactivatable Nanobody Conjugate Dimerizer Temporally Resolves Tiam1-Rac1 Signaling Axis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- A simeprevir-inducible molecular switch for the control of cell and gene therapies.Nature communications · 2023Article
- Rational design of small-molecule responsive protein switches.Protein science : a publication of the Protein Society · 2023Review
- Rational Design of Chemically Controlled Antibodies and Protein Therapeutics.ACS chemical biology · 2023Article
Corrections and comments
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
Abstract
The antigen specificity and long serum half-life of monoclonal antibodies have made them a critical part of modern therapeutics. These properties have been coopted in a number of synthetic formats, such as antibody-drug conjugates, bispecific antibodies, or Fc-fusion proteins to generate novel biologic drug modalities. Historically, these new therapies have been generated by covalently linking multiple molecular moieties through chemical or genetic methods. This irreversible fusion of different components means that the function of the molecule is static, as determined by the structure. Here, we report the development of a technology for switchable assembly of functional antibody complexes using chemically induced dimerization domains. This approach enables control of the antibody's intended function in vivo by modulating the dose of a small molecule. We demonstrate this switchable assembly across three therapeutically relevant functionalities in vivo, including localization of a radionuclide-conjugated antibody to an antigen-positive tumor, extension of a cytokine's half-life, and activation of bispecific, T cell-engaging antibodies.
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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.