ArticleRSC chemical biology2021
Finding and characterizing a catalytic antibody light chain, H34, capable of degrading the PD-1 molecule.
Article in RSC chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The trial behind it
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Experimental and Computational Studies on Domain-Swapped Structure Stabilization of an Antibody Light Chain by Disulfide Bond Introduction.Journal of medicinal chemistry · 2024Article
- Structural and thermodynamic insights into antibody light chain tetramer formation through 3D domain swapping.Nature communications · 2023Article
- 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
- A new catalytic site functioning in antigen cleavage by H34 catalytic antibody light chain.Scientific reports · 2022Article
- Experimental Autoimmune Encephalomyelitis of Mice: Enzymatic Cross Site-Specific Hydrolysis of H4 Histone by IgGs against Histones and Myelin Basic Protein.International journal of molecular sciences · 2022Article
- Zinc Status Impacts the Epidermal Growth Factor Receptor and Downstream Protein Expression in A549 Cells.International journal of molecular sciences · 2022Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Programmed cell death 1 (PD-1) is an immune checkpoint molecule regulating T-cell function. Preventing PD-1 binding to its ligand PD-L1 has emerged as an important tool in immunotherapy. Here, we describe a unique human catalytic antibody light chain, H34, which mediates enzymatic degradation of human PD-1 peptides and recombinant human PD-1 protein and thus functions to prevent the binding of PD-1 with PD-L1. H34 degraded one half of the PD-1 molecules within about 6 h under the experimental conditions. Investigating the acquisition of the catalytic function by H34, which belongs to subgroup I and lacks a Pro
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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 Socratic graph.