ReviewImmunological reviews2016
Engineered IgG1-Fc--one fragment to bind them all.
Review in Immunological reviews, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed.
- Label-Free Profiling of Immunoglobulin Isotypes Using Solid-State Nanopores.Small methods · 2026Article
- Next-Generation Therapeutic Antibodies for Cancer Treatment: Advancements, Applications, and Challenges.Molecular biotechnology · 2025Review
- Augmentation of Solid Tumor Immunotherapy With IL-12.The journal of gene medicine · 2024Review
- A comprehensive overview of recent advances in generative models for antibodies.Computational and structural biotechnology journal · 2024Review
- Effects of glycans and hinge on dynamics in the IgG1 Fc.Journal of biomolecular structure & dynamics · 2024Article
- CD98hc is a target for brain delivery of biotherapeutics.Nature communications · 2023Article
- Designing receptor agonists with enhanced pharmacokinetics by grafting macrocyclic peptides into fragment crystallizable regions.Nature biomedical engineering · 2023Article
- Surface Design Options in Polymer- and Lipid-Based siRNA Nanoparticles Using Antibodies.International journal of molecular sciences · 2022Review
- A Novel Anti-B7-H3 × Anti-CD3 Bispecific Antibody with Potent Antitumor Activity.Life (Basel, Switzerland) · 2022Article
- Therapeutic Antibodies Targeting Potassium Ion Channels.Handbook of experimental pharmacology · 2021Article
- Loop Grafting between Similar Local Environments for Fc-Silent Antibodies.Journal of chemical information and modeling · 2020Article
- Human IgG1 Fc pH-dependent optimization from a constant pH molecular dynamics simulation analysis.RSC advances · 2020Article
- Direct Blood Culturing ofJournal of clinical microbiology · 2020Article
- Polymer conjugation of proteins as a synthetic post-translational modification to impact their stability and activity.Polymer chemistry · 2019Article
- Therapeutic Bispecific T-Cell Engager Antibody Targeting the Transferrin Receptor.Frontiers in immunology · 2019Article
- Preclinical optimization of antibody-based radiopharmaceuticals for cancer imaging and radionuclide therapy-Model, vector, and radionuclide selection.Journal of labelled compounds & radiopharmaceuticals · 2018Review
- Article
- Bispecific Antibodies as a Development Platform for New Concepts and Treatment Strategies.International journal of molecular sciences · 2016Review
- Three Dimensional Conjugation of Recombinant N-Cadherin to a Hydrogel forJournal of materials chemistry. B · 2016Article
- Engineered Autonomous Human Variable Domains.Current pharmaceutical design · 2016Review
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.
Funding
Abstract
The crystallizable fragment (Fc) of the immunoglobulin class G (IgG) is a very attractive scaffold for the design of novel therapeutics due to its quality of uniting all essential antibody functions. This article reviews the functionalization of this homodimeric glycoprotein by diversification of structural loops of CH3 domains for the design of Fcabs, i.e. antigen-binding Fc proteins. It reports the design of libraries for the selection of nanomolar binders with wildtype-like in vivo half-life and correlation of Fc receptor binding and ADCC. The in vitro and preclinical biological activity of selected Fcabs is compared with that of clinically approved antibodies. Recently, the great potential of the scaffold for the development of therapeutics for clinical use has been shown when the HER2-binding Fcab FS102 entered clinical phase I. Furthermore, methods for the engineering of biophysical properties of Fcabs applicable to proteins in general are presented as well as the different approaches in the design of heterodimeric Fc-based scaffolds used in the generation of bispecific monoclonal antibodies. Finally, this work critically analyzes and compares the various efforts in the design of highly diverse and functional libraries that have been made in the engineering of IgG1-Fc and structurally similar scaffolds.
Indexed as
Identifiers
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.