ArticleMolecular cell2009
An unfolded CH1 domain controls the assembly and secretion of IgG antibodies.
Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.
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Who cites it
137 citing papers in PubMed, 235 citations in OpenAlex.
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- New insights into antibody structure with implications for specificity, variable region restriction and isotype choice.Nature reviews. Immunology · 2025Review
- Biochemical and structural characterization of the human gut microbiome metallopeptidase IgAse provides insight into its unique specificity for the Fab' region of IgA1 and IgA2.PLoS pathogens · 2025Article
- Molecular Determinants of TMC Protein Biogenesis and Trafficking.International journal of molecular sciences · 2025Article
- Heterohybridomas producing human immunoglobulin light chains using CD138-selected bone marrow cells.Biochemistry and biophysics reports · 2025Article
- High-throughput optimization of antibody production in CHO cells by tuning heavy- and light-chain promoter strength.Frontiers in bioengineering and biotechnology · 2025Article
- In vivo affinity maturation of the CD4 domains of an HIV-1-entry inhibitor.Nature biomedical engineering · 2024Article
- The CH1 domain influences the expression and antigen sensing of the HIV-specific CH31 IgM-BCR and IgG-BCR.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The Essential Functions of Molecular Chaperones and Folding Enzymes in Maintaining Endoplasmic Reticulum Homeostasis.Journal of molecular biology · 2024Review
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- Biophysical Analysis of Therapeutic Antibodies in the Early Development Pipeline.Biologics : targets & therapy · 2024Review
- The dispensability of VFrontiers in molecular biosciences · 2024Article
- Design and engineering of bispecific antibodies: insights and practical considerations.Frontiers in bioengineering and biotechnology · 2024Review
- Molecular mechanisms controlling the biogenesis of the TGF-β signal Vg1.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Expression ofEPJ web of conferences · 2023Article
- A disruptive clickable antibody design for the generation of antibody-drug conjugates.Antibody therapeutics · 2023Article
- Enhancing CAR T-cell Therapy Using Fab-Based Constitutively Heterodimeric Cytokine Receptors.Cancer immunology research · 2023Article
77 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
A prerequisite for antibody secretion and function is their assembly into a defined quaternary structure, composed of two heavy and two light chains for IgG. Unassembled heavy chains are actively retained in the endoplasmic reticulum (ER). Here, we show that the C(H)1 domain of the heavy chain is intrinsically disordered in vitro, which sets it apart from other antibody domains. It folds only upon interaction with the light-chain C(L) domain. Structure formation proceeds via a trapped intermediate and can be accelerated by the ER-specific peptidyl-prolyl isomerase cyclophilin B. The molecular chaperone BiP recognizes incompletely folded states of the C(H)1 domain and competes for binding to the C(L) domain. In vivo experiments demonstrate that requirements identified for folding the C(H)1 domain in vitro, including association with a folded C(L) domain and isomerization of a conserved proline residue, are essential for antibody assembly and secretion in the cell.
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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.