ArticleProceedings of the National Academy of Sciences of the United States of America2000
Using antibody catalysis to study the outcome of multiple evolutionary trials of a chemical task.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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
10 citing papers in PubMed.
- An Engineered Arginine Residue of Unusual pH-Sensitive Reactivity Facilitates Site-Selective Antibody Conjugation.Biochemistry · 2021Article
- Generation and validation of structurally defined antibody-siRNA conjugates.Nucleic acids research · 2020Article
- Site-Selective Antibody Functionalization via Orthogonally Reactive Arginine and Lysine Residues.Cell chemical biology · 2019Article
- Global profiling of lysine reactivity and ligandability in the human proteome.Nature chemistry · 2017Article
- Chemically programmed antibodies.Trends in biotechnology · 2014Review
- Multiple catalytic aldolase antibodies suitable for chemical programming.Bioorganic & medicinal chemistry letters · 2009Article
- Instant immunity through chemically programmable vaccination and covalent self-assembly.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Routes to covalent catalysis by reactive selection for nascent protein nucleophiles.Journal of the American Chemical Society · 2007Article
- Catalytic and binding poly-reactivities shared by two unrelated proteins: The potential role of promiscuity in enzyme evolution.Protein science : a publication of the Protein Society · 2001Article
- One site fits both: a model for the ternary complex of folate + NADPH in R67 dihydrofolate reductase, a D2 symmetric enzyme.Journal of computer-aided molecular design · 2001Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
Abstract
Catalytic aldolase antibodies generated by immunization with two different, but structurally related, beta-diketone haptens were cloned and sequenced to study similarities and differences between independently evolved catalysts. Kinetic and sequence analysis coupled with mutagenesis, structural, and modeling studies reveal that the defining event in the evolution of these catalysts was a somatic mutation that placed a lysine residue in a deep, yet otherwise unrefined, hydrophobic pocket. We suggest that covalent chemistries may be as readily selected from the immune repertoire as the traditional noncovalent interactions that have formed the basis of immunochemistry until this time. Further, we believe that these experiments recapitulate the defining events in the evolution of nature's enzymes, particularly as they relate to chemical mechanism, catalytic promiscuity, and gene duplication.
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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.