ReviewThe AAPS journal2013
Non-Arrhenius protein aggregation.
Review in The AAPS journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.
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
43 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Pooled it
- Lactoferrin/κ-Carrageenan Interactions: Thermodynamic and Kinetic Insights through Surface Plasmon Resonance and Steady-State Fluorescence.ACS omega · 2026Article
- Thermodynamics and Kinetics of Supramolecular Complex Formation between Carboxymethylcellulose and Lactoferrin.ACS omega · 2026Article
- Enzyme-Assisted Extraction of Bioactive Compounds fromPlants (Basel, Switzerland) · 2026Article
- Article
- Simplified kinetic modeling for predicting the stability of complex biotherapeutics.Scientific reports · 2025Article
- Cataract-Causing Mutant R188C of βB2 Crystallin With Low Structural Stability is Sensitive to Environmental Stresses and Prone to Aggregates Formation.Exploration (Beijing, China) · 2025Article
- Rationalizing mAb Candidate Screening Using a Single Holistic Developability Parameter.Molecular pharmaceutics · 2025Article
- Molecular Dynamics Simulations Reveal How Competing Protein-Surface Interactions for Glycine, Citrate, and Water Modulate Stability in Antibody Fragment Formulations.Molecular pharmaceutics · 2024Article
- Exploring the Recognition Mechanism of Surfactant-Cyclodextrin Complex Formation: Insights from SPR Studies on Temperature and Ionic Liquid Influence.The journal of physical chemistry. B · 2024Article
- Advanced computational approaches to understand protein aggregation.Biophysics reviews · 2024Review
- DNA Released by Adeno-Associated Virus Strongly Alters Capsid Aggregation Kinetics in a Physiological Solution.Biomacromolecules · 2024Article
- Biophysical Analysis of Therapeutic Antibodies in the Early Development Pipeline.Biologics : targets & therapy · 2024Review
- Adeno-associated viral capsid stability on anion exchange chromatography column and its impact on empty and full capsid separation.Molecular therapy. Methods & clinical development · 2023Article
- A universal tool for stability predictions of biotherapeutics, vaccines and in vitro diagnostic products.Scientific reports · 2023Article
- Modeling study of long-term stability of the monoclonal antibody infliximab and biosimilars using liquid-chromatography-tandem mass spectrometry and size-exclusion chromatography-multi-angle light scattering.Analytical and bioanalytical chemistry · 2023Article
- Recombinant antibodies aggregation and overcoming strategies in CHO cells.Applied microbiology and biotechnology · 2022Review
- Aggregation Time Machine: A Platform for the Prediction and Optimization of Long-Term Antibody Stability Using Short-Term Kinetic Analysis.Journal of medicinal chemistry · 2022Article
- Assessment of Therapeutic Antibody Developability by Combinations of In Vitro and In Silico Methods.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Expanding the toolbox for predictive parameters describing antibody stability considering thermodynamic and kinetic determinants.Pharmaceutical research · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein aggregation presents one of the key challenges in the development of protein biotherapeutics. It affects not only product quality but also potentially impacts safety, as protein aggregates have been shown to be linked with cytotoxicity and patient immunogenicity. Therefore, investigations of protein aggregation remain a major focus in pharmaceutical companies and academic institutions. Due to the complexity of the aggregation process and temperature-dependent conformational stability, temperature-induced protein aggregation is often non-Arrhenius over even relatively small temperature windows relevant for product development, and this makes low-temperature extrapolation difficult based simply on accelerated stability studies at high temperatures. This review discusses the non-Arrhenius nature of the temperature dependence of protein aggregation, explores possible causes, and considers inherent hurdles for accurately extrapolating aggregation rates from conventional industrial approaches for selecting accelerated conditions and from conventional or more advanced methods of analyzing the resulting rate data.
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.