ArticleInternational journal of molecular sciences2018
High Affinity Promotes Internalization of Engineered Antibodies Targeting FGFR1.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Understanding the Therapeutic Potential of PD-1 Agonism in Inflammatory and Autoimmune Disorders.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- Development of Glypican 3-Targeting Antibody-Drug Conjugates for Hepatocellular Carcinoma Therapy.Cancer research communications · 2026Article
- Dissecting the disconnect between circuit activation and dominant adaptive evolution in cytoplasmic phage-assisted continuous evolution (PACE) of an EGFR nanobody.Frontiers in bioengineering and biotechnology · 2026Article
- Review
- Affinity Affects the Functional Potency of Anti-GD2 Antibodies by Target-Mediated Drug Disposition.Cancers · 2025Article
- Pincer-Type Pt(II)-NHC Antibody-Drug Conjugate for HER-2-Targeted Chemoimmunotherapy.Advanced healthcare materials · 2025Article
- Novel FRET-based Immunological Synapse Biosensor for the Prediction of Chimeric Antigen Receptor-T Cell Function.Small methods · 2025Article
- Refined target-mediated drug disposition modeling of the anti-tissue factor pathway inhibitor antibody MG1113 in cynomolgus monkeys and rabbits.Frontiers in pharmacology · 2025Article
- The diverse dependence of galectin-1 and -8 on multivalency for the modulation of FGFR1 endocytosis.Cell communication and signaling : CCS · 2024Article
- N-glycosylation acts as a switch for FGFR1 trafficking between the plasma membrane and nuclear envelope.Cell communication and signaling : CCS · 2023Article
- New developments in the biology of fibroblast growth factors.WIREs mechanisms of disease · 2022Review
- Possible Therapeutic Utility of anti-Cell Adhesion Molecule 1 Antibodies for Malignant Pleural Mesothelioma.Frontiers in cell and developmental biology · 2022Article
- Intrinsically Fluorescent Oligomeric Cytotoxic Conjugates Toxic for FGFR1-Overproducing Cancers.Biomacromolecules · 2021Article
- Enzymatic ligation of an antibody and arginine 9 peptide for efficient and cell-specific siRNA delivery.Scientific reports · 2021Article
- Modular self-assembly system for development of oligomeric, highly internalizing and potent cytotoxic conjugates targeting fibroblast growth factor receptors.Journal of biomedical science · 2021Article
- FGF1 Fusions with the Fc Fragment of IgG1 for the Assembly of GFPpolygons-Mediated Multivalent Complexes Recognizing FGFRs.Biomolecules · 2021Article
- FGFR1 clustering with engineered tetravalent antibody improves the efficiency and modifies the mechanism of receptor internalization.Molecular oncology · 2020Article
- Rapid Evaluation of Antibody Fragment Endocytosis for Antibody Fragment-Drug Conjugates.Biomolecules · 2020Article
- Considerations for the Design of Antibody-Based Therapeutics.Journal of pharmaceutical sciences · 2020Review
- Targeting Cellular Trafficking of Fibroblast Growth Factor Receptors as a Strategy for Selective Cancer Treatment.Journal of clinical medicine · 2018Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fibroblast growth factor receptor 1 (FGFR1) is a plasma membrane protein that transmits signals from the extracellular environment, regulating cell homeostasis and function. Dysregulation of FGFR1 leads to the development of human cancers and noncancerous diseases. Numerous tumors overproduce FGFR1, making this receptor a perspective target for cancer therapies. Antibody-drug conjugates (ADCs) are highly potent and selective anticancer agents. ADCs are composed of antibodies (targeting factors) fused to highly cytotoxic drugs (warheads). The efficiency of ADC strategy largely depends on the internalization of cytotoxic conjugate into cancer cells. Here, we have studied an interplay between affinity of anti-FGFR1 antibodies and efficiency of their cellular uptake. We have developed a unique set of engineered anti-FGFR1 antibodies that bind the same epitope in the extracellular part of FGFR1, but with different affinities. We have demonstrated that these antibodies are effectively taken up by cancer cells in the FGFR1-dependent manner. Interestingly, we have found that efficiency, defined as rate and level of antibody internalization, largely depends on the affinity of engineered antibodies towards FGFR1, as high affinity antibody displays fastest internalization kinetics. Our data may facilitate design of therapeutically relevant targeting molecules for selective treatment of FGFR1 overproducing cancers.
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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.