ReviewJournal of pharmaceutical sciences2014
Improving monoclonal antibody selection and engineering using measurements of colloidal protein interactions.
Review in Journal of pharmaceutical sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed.
- In Situ Online Spectroscopy and Light Scattering Techniques.Advances in biochemical engineering/biotechnology · 2026Review
- Review
- Prediction of Self-Association and Solution Behavior of Monoclonal Antibodies Using the QCM-D Metric of Loosely Interacting Layer.Molecular pharmaceutics · 2025Article
- Predictive Model Building for Aggregation Kinetics Based on Molecular Dynamics Simulations of an Antibody Fragment.Molecular pharmaceutics · 2024Article
- Molecular Dynamics Simulations Reveal How Competing Protein-Surface Interactions for Glycine, Citrate, and Water Modulate Stability in Antibody Fragment Formulations.Molecular pharmaceutics · 2024Article
- Developability assessment at early-stage discovery to enable development of antibody-derived therapeutics.Antibody therapeutics · 2023Review
- Improving antibody drug development using bionanotechnology.Current opinion in biotechnology · 2022Review
- Utility of High Resolution 2D NMR Fingerprinting in Assessing Viscosity of Therapeutic Monoclonal Antibodies.Pharmaceutical research · 2022Article
- Measuring Self-Association of Antibody Lead Candidates with Dynamic Light Scattering.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Global multi-method analysis of interaction parameters for reversibly self-associating macromolecules at high concentrations.Scientific reports · 2021Article
- Characterization and Modeling of Reversible Antibody Self-Association Provide Insights into Behavior, Prediction, and Correction.Antibodies (Basel, Switzerland) · 2021Article
- Studying Excipient Modulated Physical Stability and Viscosity of Monoclonal Antibody Formulations Using Small-Angle Scattering.Molecular pharmaceutics · 2019Article
- Germinality does not necessarily define mAb expression and thermal stability.Applied microbiology and biotechnology · 2019Article
- Optimizing selectivity of anion hydrophobic multimodal chromatography for purification of a single-chain variable fragment.Engineering in life sciences · 2019Article
- Constructive approach for synthesis of a functional IgG using a reconstituted cell-free protein synthesis system.Scientific reports · 2019Article
- Biophysical characterization and molecular simulation of electrostatically driven self-association of a single-chain antibody.Protein science : a publication of the Protein Society · 2018Article
- Tracking Antibody Distribution with Near-Infrared Fluorescent Dyes: Impact of Dye Structure and Degree of Labeling on Plasma Clearance.Molecular pharmaceutics · 2017Article
- A new approach to quantification of mAb aggregates using peptide affinity probes.Scientific reports · 2017Article
- Biophysical properties of the clinical-stage antibody landscape.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Challenges in Predicting Protein-Protein Interactions from Measurements of Molecular Diffusivity.Biophysical journal · 2016Article
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
Abstract
A limitation of using mAbs as therapeutic molecules is their propensity to associate with themselves and/or with other molecules via nonaffinity (colloidal) interactions. This can lead to a variety of problems ranging from low solubility and high viscosity to off-target binding and fast antibody clearance. Measuring such colloidal interactions is challenging given that they are weak and potentially involve diverse target molecules. Nevertheless, assessing these weak interactions-especially during early antibody discovery and lead candidate optimization-is critical to preventing problems that can arise later in the development process. Here we review advances in developing and implementing sensitive methods for measuring antibody colloidal interactions as well as using these measurements for guiding antibody selection and engineering. These systematic efforts to minimize nonaffinity interactions are expected to yield more effective and stable mAbs for diverse therapeutic applications. © 2014 Wiley Periodicals, Inc. and the American Pharmacists Association J Pharm Sci 103:3356-3363, 2014.
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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.