ArticleProceedings of the National Academy of Sciences of the United States of America2019
Application of antihelix antibodies in protein structure determination.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 20 citations in OpenAlex.
- Article
- PEPNet: a two-stage point cloud framework with hierarchical embedding and antigen-antibody interaction modeling for epitope prediction.Briefings in bioinformatics · 2026Article
- Grafting the ALFA tag for structural studies of aquaporin Z.Journal of structural biology: X · 2024Article
- Computational Protein Design - Where it goes?Current medicinal chemistry · 2024Review
- Crystal Structure ofJournal of the American Chemical Society · 2023Article
- Unique Peptides of Cathelicidin-1 in the Early Detection of Mastitis-In Silico Analysis.International journal of molecular sciences · 2023Article
- Cryo-EM for Small Molecules.Current protocols · 2022Review
- Structural basis of an epitope tagging system derived from Haloarcula marismortui bacteriorhodopsin I D94N and its monoclonal antibody GD-26.The FEBS journal · 2022Article
- Development of a universal nanobody-binding Fab module for fiducial-assisted cryo-EM studies of membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- N-terminal Transmembrane-Helix Epitope Tag for X-ray Crystallography and Electron Microscopy of Small Membrane Proteins.Journal of molecular biology · 2021Article
- Use of cyclic peptides to induce crystallization: case study with prolyl hydroxylase domain 2.Scientific reports · 2020Article
- Synthetic antibodies against BRIL as universal fiducial marks for single-particle cryoEM structure determination of membrane proteins.Nature communications · 2020Article
- Repurposing off-the-shelf antihelix antibodies for enabling structural biology.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
- Commented on by
Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibodies are indispensable tools in protein engineering and structural biology. Antibodies suitable for structural studies should recognize the 3-dimensional (3D) conformations of target proteins. Generating such antibodies and characterizing their complexes with antigens take a significant amount of time and effort. Here, we show that we can expand the application of well-characterized antibodies by "transplanting" the epitopes that they recognize to proteins with completely different structures and sequences. Previously, several antibodies have been shown to recognize the alpha-helical conformation of antigenic peptides. We demonstrate that these antibodies can be made to bind to a variety of unrelated "off-target" proteins by modifying amino acids in the preexisting alpha helices of such proteins. Using X-ray crystallography, we determined the structures of the engineered protein-antibody complexes. All of the antibodies bound to the epitope-transplanted proteins, forming accurately predictable structures. Furthermore, we showed that binding of these antihelix antibodies to the engineered target proteins can modulate their catalytic activities by trapping them in selected functional states. Our method is simple and efficient, and it will have applications in protein X-ray crystallography, electron microscopy, and nanotechnology.
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.