ReviewFrontiers in immunology2018
Understanding the Significance and Implications of Antibody Numbering and Antigen-Binding Surface/Residue Definition.
Review in Frontiers in immunology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 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.
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Who cites it
57 citing papers in PubMed, 108 citations in OpenAlex.
- The Evolution of Artificial Intelligence in Antibody Design: From Structure-Based Engineering to Generative Models.Antibodies (Basel, Switzerland) · 2026Review
- Discovery, Structural Characterization, and Preclinical Evaluation of Monoclonal Antibodies against Xylazine Poisoning.ACS pharmacology & translational science · 2026Article
- Mechanistic insight into the oxidative degradation of monoclonal antibodies: relevance to developability and the design of stable pharmaceutical formulations.Biochemical Society transactions · 2026Review
- ANARCII enables alignment-free antigen receptor numbering using a generalised language model.Communications biology · 2026Article
- Native Top-Down Mass Spectrometry Combined with High-Resolution Charge Variant Analysis of Trastuzumab Originator and Biosimilars.Journal of the American Society for Mass Spectrometry · 2026Article
- Deep coverage and extended sequence reads obtained with a single archaeal protease expedite de novo protein sequencing by mass spectrometry.Cell systems · 2026Article
- Structure-guided phage display discovery of antibodies for (S)Tn-glycans in protein context.Nature chemical biology · 2026Article
- Review
- Enhancing antibody-antigen interaction prediction with atomic flexibility.PLoS computational biology · 2025Article
- AntiBMPNN: Structure-Guided Graph Neural Networks for Precision Antibody Engineering.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Guidelines in the Preparation of Fully Synthetic, Human Single-Domain Antibody Phage Display Libraries.Antibodies (Basel, Switzerland) · 2025Article
- Article
- Conserved heavy/light contacts and germline preferences revealed by a large-scale analysis of natively paired human antibody sequences and structural data.Communications biology · 2025Article
- Cytoplasmic delivery of antibodies through grafting a functional single complementarity-determining region loop.FEBS letters · 2025Article
- Antibody numbering schemes: advances, comparisons and tools for antibody engineering.Protein engineering, design & selection : PEDS · 2025Review
- Development of the TSR-based computational method to investigate spike and monoclonal antibody interactions.Frontiers in chemistry · 2025Article
- The 3D Invariant Positioning for Protein Molecules / Molecular Complexes with Matching Subunits.Methods in molecular biology (Clifton, N.J.) · 2025Article
- 50 Years of Antibody Numbering Schemes: A Statistical and Structural Evaluation Reveals Key Differences and Limitations.Antibodies (Basel, Switzerland) · 2024Article
- Article
- AntiBinder: utilizing bidirectional attention and hybrid encoding for precise antibody-antigen interaction prediction.Briefings in bioinformatics · 2024Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monoclonal antibodies are playing an increasing role in both human and animal health. Different strategies of protein and chemical engineering, including humanization techniques of non-human antibodies were applied successfully to optimize clinical performances of antibodies. Despite the emergence of techniques allowing the development of fully human antibodies such as transgenic Xeno-mice, antibody humanization remains a standard procedure for therapeutic antibodies. An important prerequisite for antibody humanization requires standardized numbering methods to define precisely complementary determining regions (CDR), frameworks and residues from the light and heavy chains that affect the binding affinity and/or specificity of the antibody-antigen interaction. The recently generated deep-sequencing data and the increasing number of solved three-dimensional structures of antibodies from human and non-human origins have led to the emergence of numerous databases. However, these different databases use different numbering conventions and CDR definitions. In addition, the large fluctuation of the variable chain lengths, especially in CDR3 of heavy chains (CDRH3), hardly complicates the comparison and analysis of antibody sequences and the identification of the antigen binding residues. This review compares and discusses the different numbering schemes and "CDR" definition that were established up to date. Furthermore, it summarizes concepts and strategies used for numbering residues of antibodies and CDR residues identification. Finally, it discusses the importance of specific sets of residues in the binding affinity and/or specificity of immunoglobulins.
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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.