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Examination of Thermal Unfolding and Aggregation Profiles of a Series of Developable Therapeutic Monoclonal Antibodies
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/biot.201100366openalex-snapshot
A screening tool for therapeutic monoclonal antibodies: Identifying the most stable protein and its best formulation based on thioflavin T binding
inferredcites →https://doi.org/10.1002/bit.23155openalex-snapshot
Aggregates in monoclonal antibody manufacturing processes
inferredcites →https://doi.org/10.1002/jctb.2657openalex-snapshot
Stabilization of a monoclonal antibody during purification and formulation by addition of basic amino acid excipients
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Antibody Structure, Instability, and Formulation
inferredcites →https://doi.org/10.1002/jps.20753openalex-snapshot
Highly Concentrated Monoclonal Antibody Solutions: Direct Analysis of Physical Structure and Thermal Stability
inferredcites →https://doi.org/10.1002/jps.21104openalex-snapshot
Contribution of Variable Domains to the Stability of Humanized IgG1 Monoclonal Antibodies
inferredcites →https://doi.org/10.1002/jps.21521openalex-snapshot
Principles, approaches, and challenges for predicting protein aggregation rates and shelf life
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High throughput thermostability screening of monoclonal antibody formulations
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Comparative Effects of pH and Ionic Strength on Protein–Protein Interactions, Unfolding, and Aggregation for IgG1 Antibodies
inferredcites →https://doi.org/10.1002/jps.22371openalex-snapshot
Formulation Development of Therapeutic Monoclonal Antibodies Using High-Throughput Fluorescence and Static Light Scattering Techniques: Role of Conformational and Colloidal Stability
inferredcites →https://doi.org/10.1002/jps.22448openalex-snapshot
Nonnative Aggregation of an IgG1 Antibody in Acidic Conditions: Part 1. Unfolding, Colloidal Interactions, and Formation of High-Molecular-Weight Aggregates
inferredcites →https://doi.org/10.1002/jps.22493openalex-snapshot
Evaluation of a Non-Arrhenius Model for Therapeutic Monoclonal Antibody Aggregation
inferredcites →https://doi.org/10.1002/jps.22633openalex-snapshot
Predicting accelerated aggregation rates for monoclonal antibody formulations, and challenges for low-temperature predictions
inferredcites →https://doi.org/10.1002/jps.22812openalex-snapshot
Forced Degradation of Therapeutic Proteins
inferredcites →https://doi.org/10.1002/jps.23008openalex-snapshot
Formulation Design and High-Throughput Excipient Selection Based on Structural Integrity and Conformational Stability of Dilute and Highly Concentrated IgG1 Monoclonal Antibody Solutions
inferredcites →https://doi.org/10.1002/jps.23076openalex-snapshot
Comparison of High-Throughput Biophysical Methods to Identify Stabilizing Excipients for a Model IgG2 Monoclonal Antibody: Conformational Stability and Kinetic Aggregation Measurements
inferredcites →https://doi.org/10.1002/jps.23187openalex-snapshot
Excipients Differentially Influence the Conformational Stability and Pretransition Dynamics of Two IgG1 Monoclonal Antibodies
inferredcites →https://doi.org/10.1002/jps.23219openalex-snapshot
Native-State Solubility and Transfer Free Energy as Predictive Tools for Selecting Excipients to Include in Protein Formulation Development Studies
inferredcites →https://doi.org/10.1002/jps.23788openalex-snapshot
Stability of Monoclonal Antibodies at High-Concentration: Head-to-Head Comparison of the IgG1 and IgG4 Subclass
inferredcites →https://doi.org/10.1002/jps.24130openalex-snapshot
Improving Monoclonal Antibody Selection and Engineering using Measurements of Colloidal Protein Interactions
inferredcites →https://doi.org/10.1002/pro.372openalex-snapshot
Improving the solubility of anti‐LINGO‐1 monoclonal antibody Li33 by isotype switching and targeted mutagenesis
inferredcites →https://doi.org/10.1002/pro.680openalex-snapshot
High‐throughput measurement, correlation analysis, and machine‐learning predictions for pH and thermal stabilities of Pfizer‐generated antibodies
inferredcites →https://doi.org/10.1007/978-1-59745-554-1_1openalex-snapshot
Therapeutic Antibodies: Current State and Future Trends – Is a Paradigm Change Coming Soon?
inferredcites →https://doi.org/10.1007/s11095-006-0018-yopenalex-snapshot
Protein Structural Conformation and Not Second Virial Coefficient Relates to Long-Term Irreversible Aggregation of a Monoclonal Antibody and Ovalbumin in Solution
inferredcites →https://doi.org/10.1007/s11095-006-0142-8openalex-snapshot
FTIR and nDSC as Analytical Tools for High-Concentration Protein Formulations
inferredcites →https://doi.org/10.1007/s11095-006-0283-9openalex-snapshot
A Critical Evaluation of Tm(FTIR) Measurements of High-Concentration IgG1 Antibody Formulations as a Formulation Development Tool
inferredcites →https://doi.org/10.1007/s11095-008-9792-zopenalex-snapshot
Effect of Ions on Agitation- and Temperature-Induced Aggregation Reactions of Antibodies
inferredcites →https://doi.org/10.1007/s11095-009-0045-6openalex-snapshot
Stability of Protein Pharmaceuticals: An Update
inferredcites →https://doi.org/10.1007/s11095-012-0914-2openalex-snapshot
Liquid Formulations for Stabilizing IgMs During Physical Stress and Long-Term Storage
inferredcites →https://doi.org/10.1016/0022-1759(81)90274-xopenalex-snapshot
Intrinsically stable IgG aggregates
inferredcites →https://doi.org/10.1016/j.ab.2003.10.031openalex-snapshot
Characterization and analysis of thermal denaturation of antibodies by size exclusion high-performance liquid chromatography with quadruple detection
inferredcites →https://doi.org/10.1016/j.ab.2006.07.027openalex-snapshot
Thermofluor-based high-throughput stability optimization of proteins for structural studies
inferredcites →https://doi.org/10.1016/j.ab.2013.02.014openalex-snapshot
Monitoring protein aggregation kinetics with simultaneous multiple sample light scattering
inferredcites →https://doi.org/10.1016/j.ab.2013.08.015openalex-snapshot
Ligand binding analysis and screening by chemical denaturation shift
inferredcites →https://doi.org/10.1016/j.addr.2011.07.006openalex-snapshot
Protein–excipient interactions: Mechanisms and biophysical characterization applied to protein formulation development
inferredcites →https://doi.org/10.1016/j.bbrc.2007.02.042openalex-snapshot
A broad range of Fab stabilities within a host of therapeutic IgGs
inferredcites →https://doi.org/10.1016/j.bpc.2012.12.004openalex-snapshot
Aggregation of anti-streptavidin immunoglobulin gamma‐1 involves Fab unfolding and competing growth pathways mediated by pH and salt concentration
inferredcites →https://doi.org/10.1016/j.ejpb.2012.12.017openalex-snapshot
A critical evaluation of microcalorimetry as a predictive tool for long term stability of liquid protein formulations: Granulocyte Colony Stimulating Factor (GCSF)
inferredcites →https://doi.org/10.1016/j.febslet.2013.01.006openalex-snapshot
The new view of hydrophobic free energy
inferredcites →https://doi.org/10.1016/j.tca.2009.10.012openalex-snapshot
Using heat conduction microcalorimetry to study thermal aggregation kinetics of proteins
inferredcites →https://doi.org/10.1016/s0006-3495(00)76462-9openalex-snapshot
The Unfolding/Denaturation of Immunogammaglobulin of Isotype 2b and its Fab and Fc Fragments
inferredcites →https://doi.org/10.1016/s0065-3233(08)60460-xopenalex-snapshot
Stability of Proteins Small Globular Proteins
inferredcites →https://doi.org/10.1021/ac201995copenalex-snapshot
Investigation of Protein Conformational Stability Employing a Multimodal Spectrometer
inferredcites →https://doi.org/10.1021/bi100841uopenalex-snapshot
Acid-Induced Aggregation of Human Monoclonal IgG1 and IgG2: Molecular Mechanism and the Effect of Solution Composition
inferredcites →https://doi.org/10.1021/mp200404copenalex-snapshot
Advancements in High Throughput Biophysical Technologies: Applications for Characterization and Screening during Early Formulation Development of Monoclonal Antibodies
inferredcites →https://doi.org/10.1021/mp400075fopenalex-snapshot
N-Terminal Truncation of an Isolated Human IgG1 CH2 Domain Significantly Increases Its Stability and Aggregation Resistance
inferredcites →https://doi.org/10.1023/a:1011902215383openalex-snapshot
Interleukin-1 Receptor (IL-1R) Liquid Formulation Development Using Differential Scanning Calorimetry
inferredcites →https://doi.org/10.1023/a:1018990001310openalex-snapshot
Degradation Pathways for Recombinant Human Macrophage Colony-Stimulating Factor in Aqueous Solution
inferredcites →https://doi.org/10.1038/nbt.2447openalex-snapshot
Setting the stage for biosimilar monoclonal antibodies
inferredcites →https://doi.org/10.1038/nbt1363openalex-snapshot
The growth and potential of human antiviral monoclonal antibody therapeutics
inferredcites →https://doi.org/10.1038/nchembio.575openalex-snapshot
A postreductionist framework for protein biochemistry
inferredcites →https://doi.org/10.1038/nrd3229openalex-snapshot
Development trends for human monoclonal antibody therapeutics
inferredcites →https://doi.org/10.1093/protein/gzq037openalex-snapshot
Structure-based engineering of a monoclonal antibody for improved solubility
inferredcites →https://doi.org/10.1208/aapsj080366openalex-snapshot
Protein aggregation and bioprocessing
inferredcites →https://doi.org/10.1208/s12248-013-9485-3openalex-snapshot
Non-Arrhenius Protein Aggregation
inferredcites →https://doi.org/10.1529/biophysj.104.042473openalex-snapshot
Rational Design of Solution Additives for the Prevention of Protein Aggregation
inferredcites →https://doi.org/10.1529/biophysj.105.078980openalex-snapshot
How Aggregation and Conformational Scrambling of Unfolded States Govern Fluorescence Emission Spectra
inferredcites →https://doi.org/10.1529/biophysj.107.116954openalex-snapshot
Tryptophan Fluorescence Reveals the Presence of Long-Range Interactions in the Denatured State of Ribonuclease Sa
inferredcites →https://doi.org/10.2174/138920109788488932openalex-snapshot
Mechanisms of Protein Aggregation
inferredcites →https://doi.org/10.2174/138920109789978711openalex-snapshot
Effects of Arginine on Photostability and Thermal Stability of IgG1 Monoclonal Antibodies
inferredcites →https://doi.org/10.2174/157016313804998915openalex-snapshot
Methods of High Throughput Biophysical Characterization in Biopharmaceutical Development
inferredcites →https://doi.org/10.4161/mabs.3.3.15234openalex-snapshot
Engineering the variable region of therapeutic IgG antibodies
inferredcites →https://doi.org/10.4161/mabs.4.2.19000openalex-snapshot
Dual targeting strategies with bispecific antibodies
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4656901openalex-extracted
Extrapolating Differential Scanning Calorimetry Data for Monoclonal Antibodies to Low Temperatures
inferred← citeshttps://doi.org/10.1002/0471266949.bmc160openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/0471266949.bmc160.pub2openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/ddr.21624openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/eng2.12147openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/pro.3170openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/pro.3518openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/pro.4129openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/pro.4589openalex-snapshot
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inferred← citeshttps://doi.org/10.1002/wnan.1438openalex-snapshot
Advances in the development of aptamer drug conjugates for targeted drug delivery
inferred← citeshttps://doi.org/10.1007/978-1-4939-7686-7_15openalex-snapshot
Stability Testing Considerations for Biologicals and Biotechnology Products
inferred← citeshttps://doi.org/10.1007/978-3-030-31415-6_6openalex-snapshot
Chapter 6: High-Throughput Conformational and Colloidal Stability Screening of Biologic Molecules
inferred← citeshttps://doi.org/10.1007/978-3-031-62007-2_14openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s00216-021-03608-wopenalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s10930-024-10237-6openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s11095-018-2500-8openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s11095-020-02792-1openalex-snapshot
Thermodynamic Unfolding and Aggregation Fingerprints of Monoclonal Antibodies Using Thermal Profiling
inferred← citeshttps://doi.org/10.1007/s11095-021-03120-xopenalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s11095-022-03448-yopenalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s11095-023-03498-wopenalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s12257-024-00147-wopenalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s12551-017-0361-8openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s12649-025-03346-5openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/s13361-019-02292-6openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/b978-0-323-90600-5.00001-4openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/b978-0-444-64173-1.00005-6openalex-snapshot
UV-absorbance, fluorescence and FT-IR spectroscopy in biopharmaceutical development
inferred← citeshttps://doi.org/10.1016/b978-0-444-64173-1.00017-2openalex-snapshot
Developability in biophysical characterization
inferred← citeshttps://doi.org/10.1016/bs.apcsb.2018.01.005openalex-snapshot
Rational Design of Liquid Formulations of Proteins
inferred← citeshttps://doi.org/10.1016/bs.mie.2015.08.029openalex-snapshot
Orthogonal Methods for Characterizing the Unfolding of Therapeutic Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1016/j.ab.2015.07.013openalex-snapshot
Denatured state aggregation parameters derived from concentration dependence of protein stability
inferred← citeshttps://doi.org/10.1016/j.ab.2018.05.008openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ab.2020.113948openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ab.2021.114240openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ab.2024.115533openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.addr.2021.02.007openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bbrc.2021.04.070openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.bej.2022.108644openalex-snapshot
Understanding unfolding and refolding of the antibody fragment (Fab) III: Mapping covalent and non-covalent interactions during in-vitro refolding of light chain, heavy chain, and Fab.
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2023.108192openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.carres.2025.109560openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.chroma.2018.07.027openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.chroma.2024.465212openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.csbj.2021.04.047openalex-snapshot
Machine learning reveals hidden stability code in protein native fluorescence
inferred← citeshttps://doi.org/10.1016/j.drudis.2015.11.007openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ejca.2016.01.008openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ejpb.2017.01.025openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ejpb.2018.01.004openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ejpb.2019.02.018openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ejpb.2019.05.017openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ejpb.2019.06.001openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ejpb.2020.03.011openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ejpb.2020.04.002openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ejpb.2026.115077openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.heliyon.2023.e22463openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2026.151036openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ijpharm.2017.07.057openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ijpharm.2018.08.043openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ijpharm.2019.03.025openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ijpharm.2019.118505openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ijpharm.2021.120737openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ijpharm.2024.124626openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ijpharm.2024.124735openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.jchromb.2020.121984openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.jconrel.2019.10.044openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.jconrel.2020.08.013openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.jconrel.2021.06.023openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.jddst.2026.108193openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.jpba.2017.03.052openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.saa.2021.119436openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2016.10.017openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2016.10.023openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2016.12.023openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2017.04.039openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2017.06.002openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2018.07.024openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2018.08.004openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2018.09.018openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2019.10.038openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2019.10.048openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2020.01.029openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2020.03.011openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2020.04.006openalex-snapshot
Comprehensive Temperature Excursion Management Program for the Commercial Distribution of Biopharmaceutical Drug Products
inferred← citeshttps://doi.org/10.1016/j.xphs.2020.10.045openalex-snapshot
Room Temperature Intrinsic Emission Ratio of BSA Correlates With Percent Aggregates During Long-Term Storage
inferred← citeshttps://doi.org/10.1016/j.xphs.2021.09.005openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2022.01.016openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2023.03.021openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2024.03.019openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2024.10.004openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.xphs.2024.12.017openalex-snapshot
Higher concentration of trehalose dihydrate stabilizes recombinant IgG1 under forced stress conditions
inferred← citeshttps://doi.org/10.1021/acs.analchem.7b03831openalex-snapshot
Purity Determination by Capillary Electrophoresis Sodium Hexadecyl Sulfate (CE-SHS): A Novel Application For Therapeutic Protein Characterization
inferred← citeshttps://doi.org/10.1021/acs.analchem.8b00573openalex-snapshot
Signature of Antibody Domain Exchange by Native Mass Spectrometry and Collision-Induced Unfolding
inferred← citeshttps://doi.org/10.1021/acs.analchem.8b03452openalex-snapshot
PULSE SPR: A High Throughput Method to Evaluate the Domain Stability of Antibodies
inferred← citeshttps://doi.org/10.1021/acs.analchem.9b05748openalex-snapshot
Isothermal Chemical Denaturation: Data Analysis, Error Detection, and Correction by PARAFAC2
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.0c00231openalex-snapshot
Structural Fingerprints of an Intact Monoclonal Antibody Acquired under Formulated Storage Conditions via 15N Direct Detection Nuclear Magnetic Resonance
inferred← citeshttps://doi.org/10.1021/acs.jmedchem.1c02010openalex-snapshot
Aggregation Time Machine: A Platform for the Prediction and Optimization of Long-Term Antibody Stability Using Short-Term Kinetic Analysis
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.0c01028openalex-snapshot
High-Throughput Screening for Colloidal Stability of Peptide Formulations Using Dynamic and Static Light Scattering
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.2c00092openalex-snapshot
A Biopharmaceutical Perspective on Higher-Order Structure and Thermal Stability of mRNA Vaccines
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.4c00332openalex-snapshot
Molecular Dynamics Simulations Reveal How Competing Protein–Surface Interactions for Glycine, Citrate, and Water Modulate Stability in Antibody Fragment Formulations
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.4c00829openalex-snapshot
Rationalizing mAb Candidate Screening Using a Single Holistic Developability Parameter
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.4c00859openalex-snapshot
Predictive Model Building for Aggregation Kinetics Based on Molecular Dynamics Simulations of an Antibody Fragment
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.5b00387openalex-snapshot
Mapping the Aggregation Kinetics of a Therapeutic Antibody Fragment
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.5b00643openalex-snapshot
Viscosity-Lowering Effect of Amino Acids and Salts on Highly Concentrated Solutions of Two IgG1 Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.5c00540openalex-snapshot
Magnetic Nanoworm-Based Screening of Yeast Library for Anti-PEG Nanobodies
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.5c01398openalex-snapshot
Deconvoluting Biophysical Factors that Influence Long-Term Aggregation Rates of High-Concentration Monoclonal Antibody Formulations
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.5c01669openalex-snapshot
Photoinduced Trp and Tyr Side Chain Cleavage in IgG4-Fc: Impact on Physicochemical Stability and Receptor Binding and Effect of N - vs O -Glycosylation
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.8b00115openalex-snapshot
Protein Aggregation and Performance Optimization Based on Microconformational Changes of Aromatic Hydrophobic Regions
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.8b00186openalex-snapshot
Computational Design To Reduce Conformational Flexibility and Aggregation Rates of an Antibody Fab Fragment
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.8b00690openalex-snapshot
Submicron Aggregation of Chemically Denatured Monoclonal Antibody
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.9b00687openalex-snapshot
Studying Excipient Modulated Physical Stability and Viscosity of Monoclonal Antibody Formulations Using Small-Angle Scattering
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.9b00852openalex-snapshot
Advancing Therapeutic Protein Discovery and Development through Comprehensive Computational and Biophysical Characterization
inferred← citeshttps://doi.org/10.1021/acsami.9b19551openalex-snapshot
Metal–Organic Framework Preserves the Biorecognition of Antibodies on Nanoscale Surfaces Validated by Single-Molecule Force Spectroscopy
inferred← citeshttps://doi.org/10.1021/bk-2015-1201.ch007openalex-snapshot
Developability Assessment of a Proposed NIST Monoclonal Antibody
inferred← citeshttps://doi.org/10.1021/bk-2015-1202.ch006openalex-snapshot
Simultaneous Multiple Sample Light Scattering (SMSLS) for Continuous Monitoring of Protein Aggregation
inferred← citeshttps://doi.org/10.1038/s41598-020-66636-zopenalex-snapshot
In Pursuit of Stability Enhancement of a Prostate Cancer Targeting Antibody Derived from a Transgenic Animal Platform
inferred← citeshttps://doi.org/10.1039/c7ce02189eopenalex-snapshot
Application of protein crystallization methodologies to enhance the solubility, stability and monodispersity of proteins
inferred← citeshttps://doi.org/10.1039/c7tb02720fopenalex-snapshot
Synthetic glycopolymers as modulators of protein aggregation: influences of chemical composition, topology and concentration
inferred← citeshttps://doi.org/10.1039/d0ma00760aopenalex-snapshot
Review of the current state of protein aggregation inhibition from a materials chemistry perspective: special focus on polymeric materials
inferred← citeshttps://doi.org/10.1051/medsci/2019232openalex-snapshot
Exemples d’études de développabilité apportant un éclairage à la prise de décision
inferred← citeshttps://doi.org/10.1080/10837450.2020.1829641openalex-snapshot
Developability assessment for monoclonal antibody drug candidates: a case study
inferred← citeshttps://doi.org/10.1080/17425247.2022.2105318openalex-snapshot
Long-acting injectable formulation technologies: challenges and opportunities for the delivery of fragile molecules
inferred← citeshttps://doi.org/10.1080/19420862.2015.1127492openalex-snapshot
CHO cell production and sequence improvement in the 13C6FR1 anti-Ebola antibody
inferred← citeshttps://doi.org/10.1080/19420862.2016.1189048openalex-snapshot
A comparison of biophysical characterization techniques in predicting monoclonal antibody stability
inferred← citeshttps://doi.org/10.1080/19420862.2016.1267089openalex-snapshot
Efficient production of bispecific IgG of different isotypes and species of origin in single mammalian cells
inferred← citeshttps://doi.org/10.1080/19420862.2018.1450126openalex-snapshot
Modification of the kinetic stability of immunoglobulin G by solvent additives
inferred← citeshttps://doi.org/10.1080/19420862.2018.1551044openalex-snapshot
Influence of N-glycosylation on effector functions and thermal stability of glycoengineered IgG1 monoclonal antibody with homogeneous glycoforms
inferred← citeshttps://doi.org/10.1080/19420862.2018.1553476openalex-snapshot
Structure, heterogeneity and developability assessment of therapeutic antibodies
inferred← citeshttps://doi.org/10.1080/19420862.2019.1596512openalex-snapshot
Improved monovalent TNF receptor 1-selective inhibitor with novel heterodimerizing Fc
inferred← citeshttps://doi.org/10.1080/19420862.2019.1599632openalex-snapshot
The impact of standard accelerated stability conditions on antibody higher order structure as assessed by mass spectrometry
inferred← citeshttps://doi.org/10.1080/19420862.2020.1736975openalex-snapshot
Interaction analysis of glycoengineered antibodies with CD16a: a native mass spectrometry approach
inferred← citeshttps://doi.org/10.1080/19420862.2020.1781743openalex-snapshot
Investigation of monoclonal antibody dimers in a final formulated drug by separation techniques coupled to native mass spectrometry
inferred← citeshttps://doi.org/10.1080/19420862.2020.1815995openalex-snapshot
An accelerated surface-mediated stress assay of antibody instability for developability studies
inferred← citeshttps://doi.org/10.1080/19420862.2021.2008790openalex-snapshot
Progress and challenges for the machine learning-based design of fit-for-purpose monoclonal antibodies
inferred← citeshttps://doi.org/10.1080/19420862.2022.2164459openalex-snapshot
Approaches to expand the conventional toolbox for discovery and selection of antibodies with drug-like physicochemical properties
inferred← citeshttps://doi.org/10.1080/19420862.2023.2185924openalex-snapshot
Blueprint for antibody biologics developability
inferred← citeshttps://doi.org/10.1093/abt/tbz008openalex-snapshot
Effect of allotypic variation of human IgG1 on the thermal stability of disulfide-linked knobs-into-holes mutants of the Fc for stable bispecific antibody design
inferred← citeshttps://doi.org/10.1093/intimm/dxx038openalex-snapshot
Glycosylation of IgG-Fc: a molecular perspective
inferred← citeshttps://doi.org/10.1093/jb/mvac040openalex-snapshot
Effect of an intermolecular disulfide bond introduced into the first loop of CH1 domain of Adalimumab Fab on thermal stability and antigen-binding activity
inferred← citeshttps://doi.org/10.1093/protein/gzy008openalex-snapshot
Roles of the disulfide bond between the variable and the constant domains of rabbit immunoglobulin kappa chains in thermal stability and affinity
inferred← citeshttps://doi.org/10.1101/2025.10.21.683661openalex-snapshot
Characterization of deglycosylated anti-cocaine mAb by differential scanning fluorimetry and fluorescence labeling
inferred← citeshttps://doi.org/10.1186/s40643-024-00738-8openalex-snapshot
Modeling the behavior of monoclonal antibodies on hydrophobic interaction chromatography resins
inferred← citeshttps://doi.org/10.1208/s12248-024-00893-yopenalex-snapshot
Taurine, a Naturally Occurring Amino Acid, as a Physical Stability Enhancer of Different Monoclonal Antibodies
inferred← citeshttps://doi.org/10.2147/btt.s486345openalex-snapshot
Biophysical Analysis of Therapeutic Antibodies in the Early Development Pipeline
inferred← citeshttps://doi.org/10.2210/pdb6j7w/pdbopenalex-snapshot
Crystal Structure of Human BCMA in complex with UniAb(TM) VH
inferred← citeshttps://doi.org/10.3389/fchem.2019.00074openalex-snapshot
FTIR Spectroscopic Study of the Secondary Structure of Globular Proteins in Aqueous Protic Ionic Liquids
inferred← citeshttps://doi.org/10.3389/fimmu.2017.01554openalex-snapshot
Crystallizable Fragment Glycoengineering for Therapeutic Antibodies Development
inferred← citeshttps://doi.org/10.3389/fimmu.2018.03037openalex-snapshot
Multispecific Antibody Development Platform Based on Human Heavy Chain Antibodies
inferred← citeshttps://doi.org/10.3389/fimmu.2022.1063002openalex-snapshot
Generation of bispecific antibodies by structure-guided redesign of IgG constant regions
inferred← citeshttps://doi.org/10.3389/fimmu.2022.924542openalex-snapshot
Penpulimab, an Fc-Engineered IgG1 Anti-PD-1 Antibody, With Improved Efficacy and Low Incidence of Immune-Related Adverse Events
inferred← citeshttps://doi.org/10.3389/fmolb.2023.1221626openalex-snapshot
How can we discover developable antibody-based biotherapeutics?
inferred← citeshttps://doi.org/10.3390/ijms17060853openalex-snapshot
Identification of Protein–Excipient Interaction Hotspots Using Computational Approaches
inferred← citeshttps://doi.org/10.3390/md21110550openalex-snapshot
Novel Approach for Obtaining Variable Domain of New Antigen Receptor with Different Physicochemical Properties from Japanese Topeshark (Hemitriakis japanica)
inferred← citeshttps://doi.org/10.3390/pharmaceutics10040165openalex-snapshot
An Evaluation of the Potential of NMR Spectroscopy and Computational Modelling Methods to Inform Biopharmaceutical Formulations
inferred← citeshttps://doi.org/10.3390/vaccines9010005openalex-snapshot
Changes in Serum Biomarkers of Oxidative Stress in Cattle Vaccinated with Tick Recombinant Antigens: A Pilot Study
inferred← citeshttps://doi.org/10.6084/m9.figshare.26681359openalex-snapshot
Additional file 1 of Modeling the behavior of monoclonal antibodies on hydrophobic interaction chromatography resins
inferred← citeshttps://doi.org/10.6084/m9.figshare.26681362openalex-snapshot
Additional file 2 of Modeling the behavior of monoclonal antibodies on hydrophobic interaction chromatography resins
inferred← citeshttps://doi.org/10.6084/m9.figshare.26681368openalex-snapshot
Additional file 3 of Modeling the behavior of monoclonal antibodies on hydrophobic interaction chromatography resins
inferred← citeshttps://doi.org/10.70675/31550ddbz6cf7z4e25za126z01b3fb8737f1openalex-snapshot
Immunostimulatory and Oncolytic Properties of Rotavirus Can Overcome Resistance to Immune Checkpoint Blockade Therapy
inferred← citeshttps://doi.org/10.70675/8a131ef8z9b1az469fzb97aze35914486b73openalex-snapshot
Déterminants moléculaires de la pharmacocinétique des anticorps thérapeutiques
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