ArticlemAbs2017
Characterization of highly concentrated antibody solution - A toolbox for the description of protein long-term solution stability.
Article in mAbs, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed.
- Delivery devices and container closure systems for co-formulated and co-administered biologics.Antibody therapeutics · 2026Review
- Therapeutic peptides and proteins: Status and developments in drug delivery.Journal of controlled release : official journal of the Controlled Release Society · 2026Review
- A Review on the Stability Challenges of Advanced Biologic Therapeutics.Pharmaceutics · 2025Review
- Rapid Development of High Concentration Protein Formulation Driven by High-Throughput Technologies.Pharmaceutical research · 2025Article
- Investigation on environmental factors contributing to bispecific antibody stability and the reversal of self-associated aggregates.Bioresources and bioprocessing · 2024Article
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Exploiting the intrinsic misfolding propensity of the KRAS oncoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Assessment of Therapeutic Antibody Developability by Combinations of In Vitro and In Silico Methods.Methods in molecular biology (Clifton, N.J.) · 2022Article
- An experimental approach probing the conformational transitions and energy landscape of antibodies: a glimmer of hope for reviving lost therapeutic candidates using ionic liquid.Chemical science · 2021Article
- Advancements in the co-formulation of biologic therapeutics.Journal of controlled release : official journal of the Controlled Release Society · 2020Review
- Protein aggregation and immunogenicity of biotherapeutics.International journal of pharmaceutics · 2020Review
- Computational prediction of protein aggregation: Advances in proteomics, conformation-specific algorithms and biotechnological applications.Computational and structural biotechnology journal · 2020Review
- Antibody Structure and Function: The Basis for Engineering Therapeutics.Antibodies (Basel, Switzerland) · 2019Review
- Current Advancements in Addressing Key Challenges of Therapeutic Antibody Design, Manufacture, and Formulation.Antibodies (Basel, Switzerland) · 2019Review
- Evaluating the Effects of Hinge Flexibility on the Solution Structure of Antibodies at Concentrated Conditions.Journal of pharmaceutical sciences · 2019Article
- Web-based display of protein surface and pH-dependent properties for assessing the developability of biotherapeutics.Scientific reports · 2019Article
- Hydrodynamic radius coincides with the slip plane position in the electrokinetic behavior of lysozyme.Proteins · 2018Article
- Challenges and Opportunities for the Subcutaneous Delivery of Therapeutic Proteins.Journal of pharmaceutical sciences · 2018Review
- 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
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High protein titers are gaining importance in biopharmaceutical industry. A major challenge in the development of highly concentrated mAb solutions is their long-term stability and often incalculable viscosity. The complexity of the molecule itself, as well as the various molecular interactions, make it difficult to describe their solution behavior. To study the formulation stability, long- and short-range interactions and the formation of complex network structures have to be taken into account. For a better understanding of highly concentrated solutions, we combined established and novel analytical tools to characterize the effect of solution properties on the stability of highly concentrated mAb formulations. In this study, monoclonal antibody solutions in a concentration range of 50-200 mg/ml at pH 5-9 with and without glycine, PEG4000, and Na
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.