ReviewAntibodies (Basel, Switzerland)2016
Antibody Aggregation: Insights from Sequence and Structure.
Review in Antibodies (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 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
72 citing papers in PubMed.
- Screening of Unexplored FDA-approved Inactive Ingredients as Stabilizers for Monoclonal Antibody Products.Pharmaceutical research · 2026Article
- Polar vs Non-polar Excipients in BSA Aggregation.Pharmaceutical research · 2026Article
- Electrostatic Interactions Guide the Detrimental Effect of Oleic Acid on Monoclonal Antibody Stability.Pharmaceutical research · 2026Article
- Hypervariable loop profiling decodes sequence determinants of antibody stability.Nature structural & molecular biology · 2026Article
- Formulation Matters: The Overlooked Engine of Stability and Success in Antibody-Drug Conjugates.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Characterization of Conformational Instability of Monoclonal Antibodies During Chromatographic Purification.International journal of molecular sciences · 2026Review
- A new era in CAR-NK cell therapy: from technological innovations to clinical applications.World journal of pediatrics : WJP · 2026Review
- Artificial intelligence advancements in monoclonal antibody development technology.Frontiers in immunology · 2026Review
- VNpj viruses · 2025Article
- Solving the light chain mismatch of IgG-like bispecific antibody by utilizing 2A peptide based FaBody platform.Biotechnology reports (Amsterdam, Netherlands) · 2025Article
- Removal of Aggregates During Bispecific Antibody Purification Using Hydrophobic Interaction Chromatography.Membranes · 2025Article
- Interdomain disulfide bonds of rabbit kappa light chain allotypes influence mouse-rabbit chimeric antibody performance.bioRxiv : the preprint server for biology · 2025Article
- Hinge Truncation to Improve Aggregation Kinetics and Thermal Stability of an Antibody Fab Fragment.Molecular pharmaceutics · 2025Article
- Investigating Local Sequence-Structural Attributes of Amyloidogenic Light Chain Variable Domains.Proteins · 2025Article
- Fate of Stressed Oligoclonal Antibodies Tracked by Fluorescence Cross-Correlation Spectroscopy: IgG Aggregation Proceeds across the Species Barrier.Analytical chemistry · 2025Article
- Expression and functional characterization of an anti-CD22 scFv targeting B-cell malignancies.Research in pharmaceutical sciences · 2025Article
- Highly variable aggregation and glycosylation profiles and their roles in immunogenicity to protein-based therapeutics.Journal of pharmaceutical sciences · 2025Review
- Antibody Aggregate Removal by Multimodal Chromatography.Molecules (Basel, Switzerland) · 2025Review
- IgG Biomarkers in Multiple Sclerosis: Deciphering Their Puzzling Protein A Connection.Biomolecules · 2025Review
- From Cell Clones to Recombinant Protein Product Heterogeneity in Chinese Hamster Ovary Cell Systems.International journal of molecular sciences · 2025Review
12 more citing papers are in PubMed but not listed here.
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monoclonal antibodies (mAbs) are the fastest-growing biological therapeutics with important applications ranging from cancers, autoimmunity diseases and metabolic disorders to emerging infectious diseases. Aggregation of mAbs continues to be a major problem in their developability. Antibody aggregation could be triggered by partial unfolding of its domains, leading to monomer-monomer association followed by nucleation and growth. Although the aggregation propensities of antibodies and antibody-based proteins can be affected by the external experimental conditions, they are strongly dependent on the intrinsic antibody properties as determined by their sequences and structures. In this review, we describe how the unfolding and aggregation susceptibilities of IgG could be related to their cognate sequences and structures. The impact of antibody domain structures on thermostability and aggregation propensities, and effective strategies to reduce aggregation are discussed. Finally, the aggregation of antibody-drug conjugates (ADCs) as related to their sequence/structure, linker payload, conjugation chemistry and drug-antibody ratio (DAR) is reviewed.
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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.