ArticlemAbs
Do antibody CDR loops change conformation upon binding?
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Tokenizing loops of antibodies.mAbs · 2026Article
- Efficient generation of epitope-targeted antibodies with Germinal.Nature biotechnology · 2026Article
- Integrative Computational Prediction Strategy for Antibody-Antigen Binding: A Case Study on Interleukin-1 Beta.Journal of chemical information and modeling · 2026Article
- Disulphide and sequence-encoded conformational priors guide nanobody structure prediction.bioRxiv : the preprint server for biology · 2026Article
- What does AlphaFold3 learn about antibody and nanobody docking, and what remains unsolved?mAbs · 2025Article
- Article
- Enhancing antibody-antigen interaction prediction with atomic flexibility.PLoS computational biology · 2025Article
- AI-augmented physics-based docking for antibody-antigen complex prediction.Bioinformatics (Oxford, England) · 2025Article
- Predicting the conformational flexibility of antibody and T cell receptor complementarity-determining regions.Nature machine intelligence · 2025Article
- Reconciling specificity and non-specificity in antibody binding: an energy landscape framework for immunology education.Frontiers in immunology · 2025Article
- Determining key residues of engineered scFv antibody variants with improved MMP-9 binding using deep sequencing and machine learning.Computational and structural biotechnology journal · 2024Article
- Quantifying conformational changes in the TCR:pMHC-I binding interface.Frontiers in immunology · 2024Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Antibodies have increasingly been developed as drugs with over 100 now licensed in the US or EU. During development, it is often necessary to increase or reduce the affinity of an antibody and rational attempts to do so rely on having a structure of the antibody-antigen complex often obtained by modeling. The antigen-binding site consists primarily of six loops known as complementarity-determining regions (CDRs), and an open question has been whether these loops change their conformation when they bind to an antigen. Existing surveys of antibody-antigen complex structures have only examined CDR conformational change in case studies or small-scale surveys. With an increasing number of antibodies where both free and complexed structures have been deposited in the Protein Data Bank, a large-scale survey of CDR conformational change during binding is now possible. To this end, we built a dataset, AbAgDb, that currently includes 177 antibodies with high-quality CDRs, each of which has at least one bound and one unbound structure. We analyzed the conformational change of the C
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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.