ReviewmAbs
Engineered CH2 domains (nanoantibodies).
Review in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed.
- A Festschrift Celebrating Dr. Dimiter Stanchev Dimitrov: Antibodies, Innovation, and Impact on Infectious Disease and Cancer Research.Antibodies (Basel, Switzerland) · 2026Article
- Vaccinal antibodies: Fc antibody engineering to improve the antiviral antibody response and induce vaccine-like effects.Human vaccines & immunotherapeutics · 2021Review
- The reduced form of the antibody CH2 domain.Protein science : a publication of the Protein Society · 2021Article
- Brain Disposition of Antibody-Based Therapeutics: Dogma, Approaches and Perspectives.International journal of molecular sciences · 2021Review
- Recent Advances in the Molecular Design and Applications of Multispecific Biotherapeutics.Antibodies (Basel, Switzerland) · 2021Review
- A single residue switch reveals principles of antibody domain integrity.The Journal of biological chemistry · 2018Article
- Article
- A dual-specific IGF-I/II human engineered antibody domain inhibits IGF signaling in breast cancer cells.International journal of biological sciences · 2018Article
- Mechanistic understanding of nanoparticles' interactions with extracellular matrix: the cell and immune system.Particle and fibre toxicology · 2017Review
- Engineered antibody CH2 domains binding to nucleolin: Isolation, characterization and improvement of aggregation.Biochemical and biophysical research communications · 2017Article
- Single-Domain Antibodies As Therapeutics against Human Viral Diseases.Frontiers in immunology · 2017Review
- Engineering of Fc Fragments with Optimized Physicochemical Properties Implying Improvement of Clinical Potentials for Fc-Based Therapeutics.Frontiers in immunology · 2017Review
- High Affinity Binders to EphA2 Isolated from Abdurin Scaffold Libraries; Characterization, Binding and Tumor Targeting.PloS one · 2015Article
- Engineered Fc based antibody domains and fragments as novel scaffolds.Biochimica et biophysica acta · 2014Review
- Discovery of novel candidate therapeutics and diagnostics based on engineered human antibody domains.Current drug discovery technologies · 2014Review
- Engineered soluble monomeric IgG1 CH3 domain: generation, mechanisms of function, and implications for design of biological therapeutics.The Journal of biological chemistry · 2013Article
- N-terminal truncation of an isolated human IgG1 CH2 domain significantly increases its stability and aggregation resistance.Molecular pharmaceutics · 2013Article
- Strategies to stabilize compact folding and minimize aggregation of antibody-based fragments.Advances in bioscience and biotechnology (Print) · 2013Article
- Human monoclonal antibodies as candidate therapeutics against emerging viruses and HIV-1.Virologica Sinica · 2013Review
- Therapeutic antibodies against cancer.Hematology/oncology clinics of North America · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
Currently, almost all FDA approved therapeutic antibodies (except ReoPro, Lucentis and Cimzia which are Fabs), and the vast majority of those in clinical trials are full-size antibodies mostly in IgG1 format of about 150 kDa size. A fundamental problem for such large molecules is their poor penetration into tissues (e.g., solid tumors) and poor or absent binding to regions on the surface of some molecules (e.g., on the HIV envelope glycoprotein) which are fully accessible only by molecules of smaller size. Therefore, much work especially during the last decade has been aimed at developing novel scaffolds of much smaller size and high stability. Here I briefly describe a proposition to use the immunoglobulin (Ig) constant CH2 domain (CH3 for IgE and IgM) as a scaffold. CH2 is critical for the Ig effector functions. Isolated CH2 is stable monomer in contrast to all other constant domains and most of the variable domains. CH2 and engineered CH2 domains with improved stability can be used as scaffolds for construction of libraries containing diverse binders to various antigens. Such binders based on a CH2 scaffold could also confer some effector functions. Because the CH2 domains are the smallest independently folded antibody domains that can be engineered to contain simultaneously antigen-binding sites and binding sites mediating effector and stability functions, and to distinguish them from domain antibodies which are used to denote engineered VH or VL domains or nanobodies which are used to denote camelid VHH, I termed them nanoantibodies (nAbs).
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.