ArticlemAbs
Oligomeric forms of single chain immunoglobulin (scIgG).
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 20 citations in OpenAlex.
- Engineering a single-chain immunoglobulin scaffold loaded with a latent-releasable cytotoxic pore-forming peptide.Communications biology · 2025Article
- Engineering resilient CAR T cells for immunosuppressive environment.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Review
- Toward Antibody Production in Genome-MinimizedACS synthetic biology · 2025Article
- Comparative performance of scFv-based anti-BCMA CAR formats for improved T cell therapy in multiple myeloma.Cancer immunology, immunotherapy : CII · 2024Article
- "Hurdles race for CAR T-cell therapy in digestive tract cancer".Immunological reviews · 2023Review
- Targeting CD22 for B-cell hematologic malignancies.Experimental hematology & oncology · 2023Review
- CAR-T cell potency: from structural elements to vector backbone components.Biomarker research · 2022Review
- Antigen-independent activation enhances the efficacy of 4-1BB-costimulated CD22 CAR T cells.Nature medicine · 2021Article
- Conjugation of an scFab domain to the oligomeric HIV envelope protein for use in immune targeting.PloS one · 2019Article
- Guiding bispecific monovalent antibody formation through proteolysis of IgG1 single-chain.mAbs · 2017Article
- A Shorter Route to Antibody Binders via Quantitative in vitro Bead-Display Screening and Consensus Analysis.Scientific reports · 2016Article
- An improved single-chain Fab platform for efficient display and recombinant expression.Journal of molecular biology · 2015Article
- A novel glycoengineered bispecific antibody format for targeted inhibition of epidermal growth factor receptor (EGFR) and insulin-like growth factor receptor type I (IGF-1R) demonstrating unique molecular properties.The Journal of biological chemistry · 2014Article
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Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Assembly of immunoglobulin G (IgG) molecules from two heavy and two light chains can be facilitated by connecting the light chain to the heavy chain by an oligopeptide linker. Production of the anti-lysozyme D1.3-single chain (sc) IgG1 in HEK293T cells yielded up to 8 mg/L functional scIgG polypeptide. Size exclusion chromatography of material purified by protein-A affinity chromatography revealed that the majority of the D1.3-scIgG1 molecules were 150 kDa monomers, with a K(D) of 1.8 x 10(-10) M measured by surface plasmon resonance; however, significant fractions of scIgG dimers and oligomers with molecular masses of 300 kDa and >600 kDa, respectively, were identified. The oligomerization resulted in an increased avidity. The observed oligomerization capability may allow new approaches for the generation of bispecific/multivalent antibodies.
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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.