ArticleProceedings of the National Academy of Sciences of the United States of America2008
Immunochemical termination of self-tolerance.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.
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
37 citing papers in PubMed, 1 synthesis or guideline pooled it, 71 citations in OpenAlex.
- Antibody-recruiting molecules: an emerging paradigm for engaging immune function in treating human disease.ACS chemical biology · 2012Pooled it
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- Homogeneous multi-payload antibody-drug conjugates.Nature chemistry · 2024Review
- Applications of genetic code expansion technology in eukaryotes.Protein & cell · 2024Review
- Selective and Site-Specific Incorporation of Nonstandard Amino Acids Within Proteins for Therapeutic Applications.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Nitro Biosciences:: Enhancing immune response via an expanded genetic code.Delaware journal of public health · 2023Article
- Advances in Biosynthesis of Non-Canonical Amino Acids (ncAAs) and the Methods of ncAAs Incorporation into Proteins.Molecules (Basel, Switzerland) · 2023Review
- A platform for distributed production of synthetic nitrated proteins in live bacteria.Nature chemical biology · 2023Article
- Epitope-Directed Antibody Elicitation by Genetically Encoded Chemical Cross-Linking Reactivity in the Antigen.ACS central science · 2023Article
- Molecular Peptide Grafting as a Tool to Create Novel Protein Therapeutics.Molecules (Basel, Switzerland) · 2023Review
- Therapeutic peptides: current applications and future directions.Signal transduction and targeted therapy · 2022Review
- Making Sense of "Nonsense" and More: Challenges and Opportunities in the Genetic Code Expansion, in the World of tRNA Modifications.International journal of molecular sciences · 2022Review
- Genetic-Code-Expansion Strategies for Vaccine Development.Chembiochem : a European journal of chemical biology · 2020Review
- Enhancement of a Heroin Vaccine through Hapten Deuteration.Journal of the American Chemical Society · 2020Article
- Efficient Acquisition of Fully Human Antibody Genes against Self-Proteins by Sorting Single B Cells Stimulated with Vaccines Based on Nitrated T Helper Cell Epitopes.Journal of immunology research · 2019Article
- Therapeutic applications of genetic code expansion.Synthetic and systems biotechnology · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 3 institutions in 1 country.
Funding
Abstract
The ability to selectively induce a strong immune response against self-proteins, or increase the immunogenicity of specific epitopes in foreign antigens, would have a significant impact on the production of vaccines for cancer, protein-misfolding diseases, and infectious diseases. Here, we show that site-specific incorporation of an immunogenic unnatural amino acid into a protein of interest produces high-titer antibodies that cross-react with WT protein. Specifically, mutation of a single tyrosine residue (Tyr(86)) of murine tumor necrosis factor-alpha (mTNF-alpha) to p-nitrophenylalanine (pNO(2)Phe) induced a high-titer antibody response in mice, whereas no significant antibody response was observed for a Tyr(86) --> Phe mutant. The antibodies generated against the pNO(2)Phe are highly cross-reactive with native mTNF-alpha and protect mice against lipopolysaccharide (LPS)-induced death. This approach may provide a general method for inducing an antibody response to specific epitopes of self- and foreign antigens that lead to a neutralizing immune response.
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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.