ArticlemAbs
The structure of dual-variable-domain immunoglobulin molecules alone and bound to antigen.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed.
- Functional Characteristics Derived from the Structural Design of Bispecific Antibodies.Pharmaceuticals (Basel, Switzerland) · 2026Review
- EGFR-selective activation of CD27 co-stimulatory signaling by a bispecific antibody enhances anti-tumor activity of T cells.Frontiers in immunology · 2023Article
- Investigation of SARS-CoV-2 nucleocapsid protein interaction with a specific antibody by combined spectroscopic ellipsometry and quartz crystal microbalance with dissipation.Journal of colloid and interface science · 2022Article
- A novel tetravalent bispecific antibody targeting programmed death 1 and tyrosine-protein kinase Met for treatment of gastric cancer.Investigational new drugs · 2019Article
- Single-Molecule 3D Images of "Hole-Hole" IgG1 Homodimers by Individual-Particle Electron Tomography.Scientific reports · 2019Article
- An Integrated Approach to Aggregate Control for Therapeutic Bispecific Antibodies Using an Improved Three Column Mab Platform-Like Purification Process.Biotechnology progress · 2019Article
- Immunoglobulin Gamma-Like Therapeutic Bispecific Antibody Formats for Tumor Therapy.Journal of immunology research · 2019Review
- An Algorithm for Enhancing the Image Contrast of Electron Tomography.Scientific reports · 2018Article
- IgG Antibody 3D Structures and Dynamics.Antibodies (Basel, Switzerland) · 2018Review
- Article
- Bispecific antibodies: design, therapy, perspectives.Drug design, development and therapy · 2018Review
- Higher order structures of Adalimumab, Infliximab and their complexes with TNFα revealed by electron microscopy.Protein science : a publication of the Protein Society · 2017Article
- Reconstruction of 3D structures of MET antibodies from electron microscopy 2D class averages.PloS one · 2017Article
- Article
- 3D Structural Fluctuation of IgG1 Antibody Revealed by Individual Particle Electron Tomography.Scientific reports · 2015Article
- Transmission electron microscopy as an orthogonal method to characterize protein aggregates.Journal of pharmaceutical sciences · 2015Article
- Optimized negative staining: a high-throughput protocol for examining small and asymmetric protein structure by electron microscopy.Journal of visualized experiments : JoVE · 2014Article
- Identification of anti-ErbB2 dual variable domain immunoglobulin (DVD-Ig™) proteins with unique activities.PloS one · 2014Article
- Review
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
A dual-specific, tetravalent immunoglobulin G-like molecule, termed dual variable domain immunoglobulin (DVD-Ig™), is engineered to block two targets. Flexibility modulates Fc receptor and complement binding, but could result in undesirable cross-linking of surface antigens and downstream signaling. Understanding the flexibility of parental mAbs is important for designing and retaining functionality of DVD-Ig™ molecules. The architecture and dynamics of a DVD-Ig™ molecule and its parental mAbs was examined using single particle electron microscopy. Hinge angles measured for the DVD-Ig™ molecule were similar to the inner antigen parental mAb. The outer binding domain of the DVD-Ig™ molecule was highly mobile and three-dimensional (3D) analysis showed binding of inner antigen caused the outer domain to fold out of the plane with a major morphological change. Docking high-resolution X-ray structures into the 3D electron microscopy map supports the extraordinary domain flexibility observed in the DVD-Ig™ molecule allowing antigen binding with minimal steric hindrance.
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.