ReviewInternational journal of molecular sciences2022
Monoclonal Antibody Engineering and Design to Modulate FcRn Activities: A Comprehensive Review.
Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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
23 citing papers in PubMed, 37 citations in OpenAlex.
- Review
- Structure and function of therapeutic antibodies approved by the US FDA in 2025.Antibody therapeutics · 2026Review
- Predicting Aberrant Fc-fusion Protein Pharmacokinetics from In Silico Structural Properties and Physiologically Based Pharmacokinetic (PBPK) Modeling.The AAPS journal · 2026Article
- Emerging Therapeutics in Rheumatoid Arthritis.Current rheumatology reports · 2026Review
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- How to manage autoimmune hyperthyroidism (Graves' disease): from differential diagnosis to emerging immunological therapies.Drugs in context · 2026Review
- Antibody engineering for SFTS treatment: frontier progress and translational challenges.Frontiers in microbiology · 2026Review
- Changes in the Interaction Properties of Antibodies with Fc Receptors upon Binding to Target Antigens.Biosensors · 2025Article
- Does a Polycistronic 2A Design Enable Functional FcRn Production for Antibody Pharmacokinetic Studies?Pharmaceutics · 2025Article
- Advances in Techniques for the Structure and Functional Optimization of Therapeutic Monoclonal Antibodies.Biomedicines · 2025Review
- Light Chain Isotype and Antibody-Specificity Impact on Virus Neutralization.Antibodies (Basel, Switzerland) · 2025Article
- Nanobodies in animal infectious disease control: diagnosis and therapy.Frontiers in cellular and infection microbiology · 2025Review
- Exploring the Interplay Between Radioimmunoconjugates and Fcγ Receptors in Genetically Engineered Mouse Models of Cancer.ACS pharmacology & translational science · 2024Article
- Revolutionizing Cancer Treatment: Recent Advances in Immunotherapy.Biomedicines · 2024Review
- Monoclonal Antibodies Engineered with Fc Region Mutations to Extend Protection against Fentanyl Toxicity.Journal of immunology (Baltimore, Md. : 1950) · 2024Article
- Single-Domain Antibodies as Antibody-Drug Conjugates: From Promise to Practice-A Systematic Review.Cancers · 2024Review
- Long-Acting Strategies for Antibody Drugs: Structural Modification, Controlling Release, and Changing the Administration Route.European journal of drug metabolism and pharmacokinetics · 2024Review
- Two in one: the emerging concept of bifunctional antibodies.Current opinion in biotechnology · 2024Review
- Antibody-Drug Conjugates: The Dynamic Evolution from Conventional to Next-Generation Constructs.Cancers · 2024Review
- Matrixed CDR grafting: A neoclassical framework for antibody humanization and developability.The Journal of biological chemistry · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding the biological mechanisms underlying the pH-dependent nature of FcRn binding, as well as the various factors influencing the affinity to FcRn, was concurrent with the arrival of the first recombinant IgG monoclonal antibodies (mAbs) and IgG Fc-fusion proteins in clinical practice. IgG Fc-FcRn became a central subject of interest for the development of these drugs for the comfort of patients and good clinical responses. In this review, we describe (i) mAb mutations close to and outside the FcRn binding site, increasing the affinity for FcRn at acidic pH and leading to enhanced mAb half-life and biodistribution, and (ii) mAb mutations increasing the affinity for FcRn at acidic and neutral pH, blocking FcRn binding and resulting, in vivo, in endogenous IgG degradation. Mutations modifying FcRn binding are discussed in association with pH-dependent modulation of antigen binding and (iii) anti-FcRn mAbs, two of the latest innovations in anti-FcRn mAbs leading to endogenous IgG depletion. We discuss the pharmacological effects, the biological consequences, and advantages of targeting IgG-FcRn interactions and their application in human therapeutics.
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What OpenQuestion holds
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.