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Predicting accelerated aggregation rates for monoclonal antibody formulations, and challenges for low-temperature predictions
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Non‐native protein aggregation kinetics
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Irreversible aggregation of recombinant bovine granulocyte-colony stimulating factor (bG-CSF) and implications for predicting protein shelf life
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Principles, approaches, and challenges for predicting protein aggregation rates and shelf life
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Conformational Implications of an Inversed pH-Dependent Antibody Aggregation
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Protein aggregation: Pathways, induction factors and analysis
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Multi-variate approach to global protein aggregation behavior and kinetics: Effects of pH, NaCl, and temperature for α-chymotrypsinogen A
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Comparative Effects of pH and Ionic Strength on Protein–Protein Interactions, Unfolding, and Aggregation for IgG1 Antibodies
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Nonnative Aggregation of an IgG1 Antibody in Acidic Conditions, Part 2: Nucleation and Growth Kinetics with Competing Growth Mechanisms
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Nonnative Aggregation of an IgG1 Antibody in Acidic Conditions: Part 1. Unfolding, Colloidal Interactions, and Formation of High-Molecular-Weight Aggregates
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Protein aggregation and its inhibition in biopharmaceutics
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Nature and consequences of protein–protein interactions in high protein concentration solutions
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Prediction of the Absolute Aggregation Rates of Amyloidogenic Polypeptide Chains
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Protein Interactions in Solution Characterized by Light and Neutron Scattering: Comparison of Lysozyme and Chymotrypsinogen
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Prediction of the heat capacity change on thermal denaturation of globular proteins
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Stability of Proteins Small Globular Proteins
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An alternative approach in the structure-based predictions of the thermodynamics of protein unfolding
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Protein aggregation: folding aggregates, inclusion bodies and amyloid
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The Hofmeister series: salt and solvent effects on interfacial phenomena
inferredcites →https://doi.org/10.1021/bi700296fopenalex-snapshot
Non-Native Aggregation of α-Chymotrypsinogen Occurs through Nucleation and Growth with Competing Nucleus Sizes and Negative Activation Energies
inferredcites →https://doi.org/10.1021/bi7019244openalex-snapshot
Nucleation, Growth, and Activation Energies for Seeded and Unseeded Aggregation of α-Chymotrypsinogen A
inferredcites →https://doi.org/10.1021/jf970751topenalex-snapshot
Kinetics of Heat-Induced Aggregation of β-Lactoglobulin
inferredcites →https://doi.org/10.1021/jp070212jopenalex-snapshot
A Lumry−Eyring Nucleated Polymerization Model of Protein Aggregation Kinetics: 1. Aggregation with Pre-Equilibrated Unfolding
inferredcites →https://doi.org/10.1021/jp710061aopenalex-snapshot
Immunoglobulin Dynamics, Conformational Fluctuations, and Nonlinear Elasticity and Their Effects on Stability
inferredcites →https://doi.org/10.1021/jp8083088openalex-snapshot
Lumry−Eyring Nucleated-Polymerization Model of Protein Aggregation Kinetics. 2. Competing Growth via Condensation and Chain Polymerization
inferredcites →https://doi.org/10.1023/a:1018955031042openalex-snapshot
Is Stability Prediction Possible for Protein Drugs? Denaturation Kinetics of β- Galactosidase in Solution
inferredcites →https://doi.org/10.1023/a:1025771421906openalex-snapshot
Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation
inferredcites →https://doi.org/10.1073/pnas.18.1.1openalex-snapshot
The Gompertz Curve as a Growth Curve
inferredcites →https://doi.org/10.2174/138920109788488941openalex-snapshot
Effect of Additives on Protein Aggregation
inferredcites →https://doi.org/10.2174/157341207782418811openalex-snapshot
New Trends in Analysis of Biopharmaceutical Products
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Extrapolating Differential Scanning Calorimetry Data for Monoclonal Antibodies to Low Temperatures
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Arginine dipeptides affect insulin aggregation in a pH‐ and ionic strength‐dependent manner
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Formulation Design and High-Throughput Excipient Selection Based on Structural Integrity and Conformational Stability of Dilute and Highly Concentrated IgG1 Monoclonal Antibody Solutions
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Analysis of IgG kinetic stability by differential scanning calorimetry, probe fluorescence and light scattering
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Parallel chromatography and in situ scattering to interrogate competing protein aggregation pathways
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Isotonic concentrations of excipients control the dimerization rate of a therapeutic immunoglobulin G1 antibody during refrigerated storage based on their rank order of native‐state interaction
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Impact of deglycosylation and thermal stress on conformational stability of a full length murine igG2a monoclonal antibody: Observations from molecular dynamics simulations
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Evaluation of Temporal Aggregation Processes Using Spatial Intensity Distribution Analysis
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Chapter 14: Practical Considerations in High Concentration Formulation Development for Monoclonal Antibody Drug Products
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Significance of Unfolding Thermodynamics for Predicting Aggregation Kinetics: A Case Study on High Concentration Solutions of a Multi-Domain Protein
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Pharmaceutical aspects of mAbs: formulation, characterization, and current route of administration of monoclonal antibody therapies
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Protein Refolding/Renaturation
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Orthogonal Methods for Characterizing the Unfolding of Therapeutic Monoclonal Antibodies
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Extrapolating differential scanning calorimetry data for monoclonal antibodies to low temperatures
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Liquid formulation for antibody drugs
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Physicochemical factors of bioprocessing impact the stability of therapeutic proteins
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Aggregation of anti-streptavidin immunoglobulin gamma‐1 involves Fab unfolding and competing growth pathways mediated by pH and salt concentration
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An accelerated antibody aggregation test based on time sequenced dynamic light scattering
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Native and Non-Native aggregation pathways of antibodies anticipated by cold-accelerated studies
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Global kinetic analysis of seeded BSA aggregation
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Antibody fragments functionalized with non-canonical amino acids preserving structure and functionality - A door opener for new biological and therapeutic applications
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Antimicrobial preservatives induce aggregation of interferon alpha-2a: The order in which preservatives induce protein aggregation is independent of the protein
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Prediction and characterization of the stability enhancing effect of the Cherry-Tag™ in highly concentrated protein solutions by complex rheological measurements and MD simulations
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Novel salts of dipicolinic acid as viscosity modifiers for high concentration antibody solutions
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Relating Protein–Protein Interactions and Aggregation Rates From Low to High Concentrations
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Accelerated Aggregation Studies of Monoclonal Antibodies: Considerations for Storage Stability
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Room Temperature Intrinsic Emission Ratio of BSA Correlates With Percent Aggregates During Long-Term Storage
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A Rapid, Small-Volume Approach to Evaluate Protein Aggregation at Air-Water Interfaces
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Evaluating the Combined Impact of Temperature and Application of Interfacial Dilatational Stresses on Surface-mediated Protein Particle Formation in Monoclonal Antibody Formulations
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Effects of Salts and Surface Charge on the Biophysical Stability of a Low pI Monoclonal Antibody
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DSC Derived (Ea & ΔG) Energetics and Aggregation Predictions for mAbs
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pH- and temperature-dependent mechanisms of non-native aggregation of anti-CD40 IgG1
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A REVIEW ON THERAPEUTIC PROTEINS: STABILITY ASPECTS AND CLINICAL IMPLICATIONS
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