ArticleThe Biochemical journal2017
IgG light chain-independent secretion of heavy chain dimers: consequence for therapeutic antibody production and design.
Article in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 22 citations in OpenAlex.
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- Uncommon Entities, Uncommon Challenges: A Review of Rare Plasma Cell Disorders.Hematology reports · 2025Review
- High-throughput optimization of antibody production in CHO cells by tuning heavy- and light-chain promoter strength.Frontiers in bioengineering and biotechnology · 2025Article
- The dispensability of VFrontiers in molecular biosciences · 2024Article
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- A mammalian cell display platform based on scFab transposition.Antibody therapeutics · 2023Article
- A Recombinant Ig Fragment (IgCw-γεκ) Comprising the CγJournal of immunology (Baltimore, Md. : 1950) · 2022Article
- Plant-made antibody against miroestrol: a new platform for expression of full-length immunoglobulin G against small-molecule targets in immunoassays.Plant cell reports · 2021Article
- Crystal Structure and Characterization of Human Heavy-Chain Only Antibodies Reveals a Novel, Stable Dimeric Structure Similar to Monoclonal Antibodies.Antibodies (Basel, Switzerland) · 2020Article
- Systematic use of synthetic 5'-UTR RNA structures to tune protein translation improves yield and quality of complex proteins in mammalian cell factories.Nucleic acids research · 2020Article
- Design and characterization of novel dual Fc antibody with enhanced avidity for Fc receptors.Proteins · 2020Article
- Antigen-binding affinity and thermostability of chimeric mouse-chicken IgY and mouse-human IgG antibodies with identical variable domains.Scientific reports · 2019Article
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Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Rodent monoclonal antibodies with specificity towards important biological targets are developed for therapeutic use by a process of humanisation. This process involves the creation of molecules, which retain the specificity of the rodent antibody but contain predominantly human coding sequence. Here, we show that some humanised heavy chains (HCs) can fold, form dimers and be secreted even in the absence of a light chain (LC). Quality control of recombinant antibody assembly
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.