ArticleNature communications2022
De novo design of immunoglobulin-like domains.
Article in Nature communications, 2022. 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.
- Prediction of antibody non-specificity using protein language models and biophysical parameters.mAbs · 2026Article
- Genetic insights into congenital and infantile nephrotic syndrome: predicting severity and informing care.Pediatric nephrology (Berlin, Germany) · 2026Review
- A systematic evaluation framework for universal antibody-antigen binding affinity prediction and candidate recommendation.iScience · 2026Article
- Expanding the landscape of BREX diversity: uncovering multi-layered functional frameworks and identification of novel BREX-related defense systems.Nucleic acids research · 2026Article
- Dissecting Cytophagalysin: Structural and Biochemical Studies of a Bacterial Pappalysin-Family Metallopeptidase.Biomolecules · 2024Article
- Broad-Spectrum Engineered Multivalent Nanobodies Against SARS-CoV-1/2.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Structure of the human heparan-α-glucosaminideeLife · 2024Article
- P-NADs:Heliyon · 2024Article
- Validation of de novo designed water-soluble and transmembrane β-barrels by in silico folding and melting.Protein science : a publication of the Protein Society · 2024Article
- Article
- The Effect of β-Sheet Secondary Structure on All-β Proteins by Molecular Dynamics Simulations.Molecules (Basel, Switzerland) · 2024Article
- Structure of the human heparan-α-glucosaminidebioRxiv : the preprint server for biology · 2024Article
- The structural landscape of the immunoglobulin fold by large-scale de novo design.Protein science : a publication of the Protein Society · 2024Article
- Reappraisal of the DNA phosphorothioate modification machinery: uncovering neglected functional modalities and identification of new counter-invader defense systems.Nucleic acids research · 2024Article
- Review
- Intelligent Protein Design and Molecular Characterization Techniques: A Comprehensive Review.Molecules (Basel, Switzerland) · 2023Review
- Single-chain dimers from de novo immunoglobulins as robust scaffolds for multiple binding loops.Nature communications · 2023Article
- Artificial intelligence-aided protein engineering: from topological data analysis to deep protein language models.Briefings in bioinformatics · 2023Review
- SARS-CoV-2 antibodies recognize 23 distinct epitopic sites on the receptor binding domain.Communications biology · 2023Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors.
Funding
Abstract
Antibodies, and antibody derivatives such as nanobodies, contain immunoglobulin-like (Ig) β-sandwich scaffolds which anchor the hypervariable antigen-binding loops and constitute the largest growing class of drugs. Current engineering strategies for this class of compounds rely on naturally existing Ig frameworks, which can be hard to modify and have limitations in manufacturability, designability and range of action. Here, we develop design rules for the central feature of the Ig fold architecture-the non-local cross-β structure connecting the two β-sheets-and use these to design highly stable Ig domains de novo, confirm their structures through X-ray crystallography, and show they can correctly scaffold functional loops. Our approach opens the door to the design of antibody-like scaffolds with tailored structures and superior biophysical properties.
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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.