ReviewBiochimica et biophysica acta2014
Engineered Fc based antibody domains and fragments as novel scaffolds.
Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed.
- Topical delivery of a human single-domain antibody targeting IL-33 to inhibit mucosal inflammation.Cellular & molecular immunology · 2025Article
- Fully human single-domain antibody targeting a highly conserved cryptic epitope on the Nipah virus G protein.Nature communications · 2024Article
- Half-life extension of single-domain antibody-drug conjugates by albumin binding moiety enhances antitumor efficacy.MedComm · 2024Article
- Effects of glycans and hinge on dynamics in the IgG1 Fc.Journal of biomolecular structure & dynamics · 2024Article
- A neutralizing bispecific single-chain antibody against SARS-CoV-2 Omicron variant produced based on CR3022.Frontiers in cellular and infection microbiology · 2023Article
- Review
- The reduced form of the antibody CH2 domain.Protein science : a publication of the Protein Society · 2021Article
- Engineering a Novel Antibody-Peptide Bispecific Fusion Protein Against MERS-CoV.Antibodies (Basel, Switzerland) · 2019Article
- CD24 targeting bi-specific antibody that simultaneously stimulates NKG2D enhances the efficacy of cancer immunotherapy.Journal of cancer research and clinical oncology · 2019Article
- Biotherapeutics: Challenges and Opportunities for Predictive Toxicology of Monoclonal Antibodies.International journal of molecular sciences · 2018Review
- In Silico Methods in Antibody Design.Antibodies (Basel, Switzerland) · 2018Review
- Article
- Engineered Soluble Monomeric IgG1 Fc with Significantly Decreased Non-Specific Binding.Frontiers in immunology · 2017Article
- Engineering of Fc Fragments with Optimized Physicochemical Properties Implying Improvement of Clinical Potentials for Fc-Based Therapeutics.Frontiers in immunology · 2017Review
- CD44v6-Targeted Imaging of Head and Neck Squamous Cell Carcinoma: Antibody-Based Approaches.Contrast media & molecular imaging · 2017Review
- Immuno-PET for Clinical Theranostic Approaches.International journal of molecular sciences · 2016Review
- Engineered IgG1-Fc--one fragment to bind them all.Immunological reviews · 2016Review
- Site-Specifically Labeled Immunoconjugates for Molecular Imaging--Part 1: Cysteine Residues and Glycans.Molecular imaging and biology · 2016Review
- Article
- 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
5 authors.
Funding
Abstract
Therapeutic monoclonal antibodies (mAbs) have been successful for the therapy of a number of diseases mostly cancer and immune disorders. However, the vast majority of mAbs approved for clinical use are full size, typically in IgG1 format. These mAbs may exhibit relatively poor tissue penetration and restricted epitope access due to their large size. A promising solution to this fundamental limitation is the engineering of smaller scaffolds based on the IgG1 Fc region. These scaffolds can be used for the generation of libraries of mutants from which high-affinity binders can be selected. Comprised of the CH2 and CH3 domains, the Fc region is important not only for the antibody effector function but also for its long half-life. This review focuses on engineered Fc based antibody fragments and domains including native (dimeric) Fc and monomeric Fc as well as CH2 and monomeric CH3, and their use as novel scaffolds and binders. The Fc based binders are promising candidate therapeutics with optimized half-life, enhanced tissue penetration and access to sterically restricted binding sites resulting in an increased therapeutic efficacy. This article is part of a Special Issue entitled: Recent advances in molecular engineering of antibody.
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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.