ArticleThe Journal of biological chemistry2009
A human germ line antibody light chain with hydrolytic properties associated with multimerization status.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 22 citations in OpenAlex.
- Physiological IgM class catalytic antibodies selective for transthyretin amyloid.The Journal of biological chemistry · 2014Trial
- Article
- Enzymatization of mouse monoclonal antibodies to the corresponding catalytic antibodies.Scientific reports · 2024Article
- Direct conversion of a general antibody to its catalytic antibody and corresponding applications -Importance and role of Pro95 in CDR-3.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2023Review
- Obtaining Highly Active Catalytic Antibodies Capable of Enzymatically Cleaving Antigens.International journal of molecular sciences · 2022Article
- Finding and characterizing a catalytic antibody light chain, H34, capable of degrading the PD-1 molecule.RSC chemical biology · 2021Article
- A new algorithm to convert a normal antibody into the corresponding catalytic antibody.Science advances · 2020Article
- New technologies to introduce a catalytic function into antibodies: A unique human catalytic antibody light chain showing degradation of β-amyloid molecule along with the peptidase activity.FASEB bioAdvances · 2019Article
- IgG Fab fragments forming bivalent complexes by a conformational mechanism that is reversible by osmolytes.The Journal of biological chemistry · 2012Article
- Constant domain-regulated antibody catalysis.The Journal of biological chemistry · 2012Article
- CD4 binding determinant mimicry for HIV vaccine design.Frontiers in immunology · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antibodies with nucleophilic or catalytic properties often have these characteristics encoded in their germ line genes. Because hydrolytic activity has been reported to be associated with light chain V regions, we have begun an analysis of germ line light chain proteins that could be the basis for affinity maturation into hydrolytic or other reactive antibodies. We produced the germ line A18b light chain and characterized its hydrolytic, nucleophilic, and tertiary structural activities. This light chain was purified to >99% purity and found to hydrolyze aminomethylcoumarin-peptide and larger protein substrates and bind a fluorophosphonate probe. Mutation of putative catalytic residues only resulted in loss of activity of a tetrameric but not dimeric form of the light chain. These biochemical properties provide a framework for understanding the structure-function relationships of germ line antibodies.
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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.