ReviewBiophysical reviews2020
Biophysical characterization of dynamic structures of immunoglobulin G.
Review in Biophysical reviews, 2020. 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, 29 citations in OpenAlex.
- Bioactive Peptides from Bovine Colostrum: Sources, Structures, and Biomedical Applications.Probiotics and antimicrobial proteins · 2026Review
- Unlabeled NMR Approach with Site-Specific Methyl Assignments for Structural Evaluation of the IgG1 Fc Region.Journal of the American Chemical Society · 2026Article
- Key Role of Pro230 in the Hinge Region on the Architecture and Function of IgG1.Journal of medicinal chemistry · 2026Article
- Effect of guanidinoacetic acid on the growth performance, serum biochemical indices and metabolites, intestinal morphology, and intestinal flora of Cherry Valley broiler ducks.Poultry science · 2025Article
- Review
- Identification of potential C1-binding sites in the immunoglobulin CL domains.International immunology · 2024Article
- Article
- Application Progress of the Single Domain Antibody in Medicine.International journal of molecular sciences · 2023Review
- Biophysical Characterization of the Contribution of the Fab Region to the IgG-FcγRIIIa Interaction.Biochemistry · 2023Article
- IL-1β-dependent extravasation of preexisting lung-restricted autoantibodies during lung transplantation activates complement and mediates primary graft dysfunction.The Journal of clinical investigation · 2022Article
- Quantitative Visualization of the Interaction between Complement Component C1 and Immunoglobulin G: The Effect of CInternational journal of molecular sciences · 2022Article
- Effect of Dietary Zinc Methionine Supplementation on Growth Performance, Immune Function and Intestinal Health of Cherry Valley Ducks Challenged With Avian PathogenicFrontiers in microbiology · 2022Article
- Rigid monoclonal antibodies improve detection of SARS-CoV-2 nucleocapsid protein.bioRxiv : the preprint server for biology · 2021Article
- Antibodies Inhibiting the Type III Secretion System of Gram-Negative Pathogenic Bacteria.Antibodies (Basel, Switzerland) · 2020Review
- Biophysical Reviews-Quantitative analysis of biological phenomenon.Biophysical reviews · 2020Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Immunoglobulin G (IgG) is a major antibody and functions as a hub linking specific antigen binding and recruitment of effector molecules typified by Fcγ receptors (FcγRs). These activities are associated primarily with interactions involving its Fab and Fc sites, respectively. An IgG molecule is characterized by a multiple domain modular structure with conserved N-glycosylation in Fc. The molecule displays significant freedom in internal motion on various spatiotemporal scales. The consequent conformational flexibility and plasticity of IgG glycoproteins are functionally significant and potentially important factors for design and engineering of antibodies with enhanced functionality. In this article, experimental and computational approaches are outlined for characterizing the conformational dynamics of IgG molecules in solution. In particular, the importance of integration of these approaches is highlighted, as illustrated by dynamic intramolecular interactions between the pair of N-glycans and their proximal amino acid residues in Fc. These interactions can critically affect effector functions mediated by human IgG1 and FcγRIII. Further improvements in individual biophysical techniques and their integration will advance understanding of dynamic behaviors of antibodies in physiological and pathological conditions. Such understanding will provide opportunities for engineering antibodies through controlling allosteric networks in IgG molecules.
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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.