On the public citation graph
High throughput thermostability screening of monoclonal antibody formulations
0 signed · 235 inferred · view as graph
Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.
Is this your work? Sign in with ORCID and put your name on the
claims that are yours.
Reference health. See whether every reference in this work resolves to a
known work and none has been retracted — and get a dated CiteStamped
badge you can embed.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/jps.1098openalex-snapshot
The Effects of Tween 20 and Sucrose on the Stability of Anti‐L‐Selectin during Lyophilization and Reconstitution
inferredcites →https://doi.org/10.1002/jps.20364openalex-snapshot
Mechanism of protein stabilization by sugars during freeze-drying and storage: Native structure preservation, specific interaction, and/or immobilization in a glassy matrix?
inferredcites →https://doi.org/10.1002/jps.20727openalex-snapshot
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.21110openalex-snapshot
Effects of Solution Conditions, Processing Parameters, and Container Materials on Aggregation of a Monoclonal Antibody during Freeze-Thawing
inferredcites →https://doi.org/10.1002/jps.21418openalex-snapshot
Evaluation of the physical stability of the EC5 domain of E-cadherin: Effects of pH, temperature, ionic strength, and disulfide bonds
inferredcites →https://doi.org/10.1002/jps.21508openalex-snapshot
Structural Stability of Vault Particles
inferredcites →https://doi.org/10.1002/jps.21514openalex-snapshot
Elucidation of Two Major Aggregation Pathways in an IgG2 Antibody
inferredcites →https://doi.org/10.1002/jps.21657openalex-snapshot
Structural stability of hepatitis C virus envelope glycoprotein E1: Effect of pH and dissociative detergents
inferredcites →https://doi.org/10.1002/jps.21749openalex-snapshot
The effect of sucrose hydrolysis on the stability of protein therapeutics during accelerated formulation studies
inferredcites →https://doi.org/10.1002/pro.20openalex-snapshot
Ion‐specific modulation of protein interactions: Anion‐induced, reversible oligomerization of a fusion protein
inferredcites →https://doi.org/10.1006/bbrc.2002.6549openalex-snapshot
Manipulation of Unfolding-Induced Protein Aggregation by Peptides Selected for Aggregate-Binding Ability through Phage Display Library Screening
inferredcites →https://doi.org/10.1007/978-1-4615-0549-5_1openalex-snapshot
Preformulation Studies as an Essential Guide to Formulation Development and Manufacture of Protein Pharmaceuticals
inferredcites →https://doi.org/10.1007/s11095-008-9722-0openalex-snapshot
Anion Binding Mediated Precipitation of a Peptibody
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/10.1016/0006-291x(84)91597-3openalex-snapshot
Human aglycosyl-IgG exhibits increased hydrophobicity
inferredcites →https://doi.org/10.1016/j.ab.2004.04.031openalex-snapshot
Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
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.ijpharm.2006.10.037openalex-snapshot
Spectroscopic evaluation of the stabilization of humanized monoclonal antibodies in amino acid formulations
inferredcites →https://doi.org/10.1016/j.jim.2007.07.014openalex-snapshot
Contrasting glycosylation profiles between Fab and Fc of a human IgG protein studied by electrospray ionization mass spectrometry
inferredcites →https://doi.org/10.1016/j.jmb.2008.03.006openalex-snapshot
Denaturant-induced Expansion and Compaction of a Multi-domain Protein: IgG
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/s0006-3495(00)76602-1openalex-snapshot
The Thermal Stability of Immunoglobulin: Unfolding and Aggregation of a Multi-Domain Protein
inferredcites →https://doi.org/10.1016/s0006-3495(85)83932-1openalex-snapshot
The stabilization of proteins by osmolytes
inferredcites →https://doi.org/10.1016/s0006-3495(96)79859-4openalex-snapshot
Simulations of reversible protein aggregate and crystal structure
inferredcites →https://doi.org/10.1016/s0161-5890(00)00105-xopenalex-snapshot
The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms
inferredcites →https://doi.org/10.1021/bi700645kopenalex-snapshot
Two-Dimensional Correlation Spectroscopy Reveals Coupled Immunoglobulin Regions of Differential Flexibility that Influence Stability
inferredcites →https://doi.org/10.1021/bi971062dopenalex-snapshot
Thermodynamics of the Complex Protein Unfolding Reaction of Barstar
inferredcites →https://doi.org/10.1021/ja8049063openalex-snapshot
High-Throughput Thermal Scanning: A General, Rapid Dye-Binding Thermal Shift Screen for Protein Engineering
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/js9801384openalex-snapshot
Aggregation of Recombinant Human Interferon Gamma: Kinetics and Structural Transitions
inferredcites →https://doi.org/10.1023/a:1015108115452openalex-snapshot
Inverse Relationship of Protein Concentration and Aggregation
inferredcites →https://doi.org/10.1038/nprot.2007.321openalex-snapshot
The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
inferredcites →https://doi.org/10.1073/pnas.0605224103openalex-snapshot
Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination
inferredcites →https://doi.org/10.1093/jb/mvm145openalex-snapshot
Effect of Buffer Species on the Unfolding and the Aggregation of Humanized IgG
inferredcites →https://doi.org/10.1093/nar/gkg563openalex-snapshot
ExPASy: the proteomics server for in-depth protein knowledge and analysis
inferredcites →https://doi.org/10.1110/ps.0235703openalex-snapshot
Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony‐stimulating factor
inferredcites →https://doi.org/10.1110/ps.051917406openalex-snapshot
Monitoring protein aggregation during thermal unfolding in circular dichroism experiments
inferredcites →https://doi.org/10.1110/ps.062491906openalex-snapshot
Identifying protein construct variants with increased crystallization propensity––A case study
inferredcites →https://doi.org/10.1110/ps.073332408openalex-snapshot
Structural and thermodynamic effects of ANS binding to human interleukin‐1 receptor antagonist
inferredcites →https://doi.org/10.1177/108705710100600609openalex-snapshot
High-Density Miniaturized Thermal Shift Assays as a General Strategy for Drug Discovery
inferredcites →https://doi.org/10.1208/ps050210openalex-snapshot
Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations
inferredcites →https://doi.org/10.3109/08820138709055709openalex-snapshot
Thermodynamics of Monoclonal and Mixed Cryoimmunoglobin Solubilization
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/10.1002/9781118354698.ch12openalex-snapshot
Biophysical Analyses Suitable for Chemistry, Manufacturing, and Control Sections of the Biologic License Application (BLA)
inferred← citeshttps://doi.org/10.1002/9781118354698.ch3openalex-snapshot
Solubility and Early Assessment of Stability for Protein Therapeutics
inferred← citeshttps://doi.org/10.1002/9781118573983.ch7openalex-snapshot
Molecular Modeling for Protein Aggregation and Formulation
inferred← citeshttps://doi.org/10.1002/advs.76551openalex-snapshot
Automation and Active Learning for the Multi‐Objective Optimization of Antibody Formulations
inferred← citeshttps://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
inferred← citeshttps://doi.org/10.1002/bit.26329openalex-snapshot
Multi‐criteria manufacturability indices for ranking high‐concentration monoclonal antibody formulations
inferred← citeshttps://doi.org/10.1002/bit.27802openalex-snapshot
Pragmatic mAb lead molecule engineering from a developability perspective
inferred← citeshttps://doi.org/10.1002/btpr.1906openalex-snapshot
Control of galactosylated glycoforms distribution in cell culture system
inferred← citeshttps://doi.org/10.1002/btpr.2464openalex-snapshot
Differential scanning calorimetry and fluorimetry measurements of monoclonal antibodies and reference proteins: Effect of scanning rate and dye selection
inferred← citeshttps://doi.org/10.1002/jctb.2657openalex-snapshot
Stabilization of a monoclonal antibody during purification and formulation by addition of basic amino acid excipients
inferred← citeshttps://doi.org/10.1002/jps.22036openalex-snapshot
Detection of IgG Aggregation by a High Throughput Method Based on Extrinsic Fluorescence
inferred← citeshttps://doi.org/10.1002/jps.22282openalex-snapshot
Application of Extrinsic Fluorescence Spectroscopy for the High Throughput Formulation Screening of Aluminum-Adjuvanted Vaccines
inferred← citeshttps://doi.org/10.1002/jps.22350openalex-snapshot
Application of a High-Throughput Screening Procedure with PEG-Induced Precipitation to Compare Relative Protein Solubility During Formulation Development with IgG1 Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1002/jps.22368openalex-snapshot
Probing bis-ANS Binding Sites of Different Affinity on Aggregated IgG by Steady-State Fluorescence, Time-Resolved Fluorescence and Isothermal Titration Calorimetry
inferred← citeshttps://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
inferred← citeshttps://doi.org/10.1002/jps.22384openalex-snapshot
Screening of Monoclonal Antibody Formulations Based on High-Throughput Thermostability and Viscosity Measurements: Design of Experiment and Statistical Analysis
inferred← citeshttps://doi.org/10.1002/jps.22450openalex-snapshot
High Throughput Formulation Screening for Global Aggregation Behaviors of Three Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1002/jps.22712openalex-snapshot
High‐Throughput Assessment of Thermal and Colloidal Stability Parameters for Monoclonal Antibody Formulations
inferred← citeshttps://doi.org/10.1002/jps.22812openalex-snapshot
Forced Degradation of Therapeutic Proteins
inferred← citeshttps://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
inferred← citeshttps://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
inferred← citeshttps://doi.org/10.1002/jps.23242openalex-snapshot
Protein particles: What we know and what we do not know
inferred← citeshttps://doi.org/10.1002/jps.23405openalex-snapshot
High-Throughput Melting-Temperature Analysis of a Monoclonal Antibody by Differential Scanning Fluorimetry in the Presence of Surfactants
inferred← citeshttps://doi.org/10.1002/jps.23543openalex-snapshot
Correlating Excipient Effects on Conformational and Storage Stability of an IgG1 Monoclonal Antibody with Local Dynamics as Measured by Hydrogen/Deuterium-Exchange Mass Spectrometry
inferred← citeshttps://doi.org/10.1002/jps.23618openalex-snapshot
Application of a Kosmotrope-Based Solubility Assay to Multiple Protein Therapeutic Classes Indicates Broad Use as a High-Throughput Screen for Protein Therapeutic Aggregation Propensity
inferred← citeshttps://doi.org/10.1002/jps.23633openalex-snapshot
DSF Method Optimization and Its Application in Predicting Protein Thermal Aggregation Kinetics
inferred← citeshttps://doi.org/10.1002/jps.23730openalex-snapshot
High-Throughput Biophysical Analysis and Data Visualization of Conformational Stability of an IgG1 Monoclonal Antibody After Deglycosylation
inferred← citeshttps://doi.org/10.1002/jps.23822openalex-snapshot
Understanding the Relationship Between Biotherapeutic Protein Stability and Solid–Liquid Interfacial Shear in Constant Region Mutants of IgG1 and IgG4
inferred← citeshttps://doi.org/10.1002/jps.23827openalex-snapshot
Temperature-Ramped Studies on the Aggregation, Unfolding, and Interaction of a Therapeutic Monoclonal Antibody
inferred← citeshttps://doi.org/10.1002/jps.24408openalex-snapshot
Application of a High-Throughput Relative Chemical Stability Assay to Screen Therapeutic Protein Formulations by Assessment of Conformational Stability and Correlation to Aggregation Propensity
inferred← citeshttps://doi.org/10.1002/jps.24430openalex-snapshot
Developability Assessment During the Selection of Novel Therapeutic Antibodies
inferred← citeshttps://doi.org/10.1002/pro.2118openalex-snapshot
Relative stabilities of IgG1 and IgG4 Fab domains: Influence of the light–heavy interchain disulfide bond architecture
inferred← citeshttps://doi.org/10.1002/pro.2340openalex-snapshot
Effects of subclass change on the structural stability of chimeric, humanized, and human antibodies under thermal stress
inferred← citeshttps://doi.org/10.1002/pro.3278openalex-snapshot
Analysis of IgG kinetic stability by differential scanning calorimetry, probe fluorescence and light scattering
inferred← citeshttps://doi.org/10.1002/pro.3595openalex-snapshot
Evaluation of a noncanonical Cys40‐Cys55 disulfide linkage for stabilization of single‐domain antibodies
inferred← citeshttps://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
inferred← citeshttps://doi.org/10.1002/prot.25354openalex-snapshot
Temperature stability of proteins: Analysis of irreversible denaturation using isothermal calorimetry
inferred← citeshttps://doi.org/10.1007/978-1-4614-4316-2_2openalex-snapshot
High-Throughput Biophysical Approaches to Therapeutic Protein Development
inferred← citeshttps://doi.org/10.1007/978-1-4614-4316-2_3openalex-snapshot
Techniques for Higher-Order Structure Determination
inferred← citeshttps://doi.org/10.1007/978-1-4614-5380-2_6openalex-snapshot
High Throughput Screening for Stabilizers of Vaccine Antigens
inferred← citeshttps://doi.org/10.1007/978-1-4939-2316-8_20openalex-snapshot
Automation and High-Throughput Technologies in Biopharmaceutical Drug Product Development with QbD Approaches
inferred← citeshttps://doi.org/10.1007/978-1-4939-2316-8_5openalex-snapshot
Development of Drug Product Formulations: Molecular Design and Early Candidates Screening
inferred← citeshttps://doi.org/10.1007/978-1-4939-3387-7_49openalex-snapshot
Practical Approaches to Forced Degradation Studies of Vaccines
inferred← citeshttps://doi.org/10.1007/978-1-4939-9678-0_9openalex-snapshot
Differential Scanning Calorimetry to Quantify Heat-Induced Aggregation in Concentrated Protein Solutions
inferred← citeshttps://doi.org/10.1007/978-1-4939-9929-3_22openalex-snapshot
Biophysical Methods for Characterization of Antibody-Drug Conjugates
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/10.1007/978-3-642-20910-9_9openalex-snapshot
The Design and Engineering of IgG-Like Bispecific Antibodies
inferred← citeshttps://doi.org/10.1007/s00249-021-01510-yopenalex-snapshot
Protein formulation through automated screening of pH and buffer conditions, using the Robotein® high throughput facility
inferred← citeshttps://doi.org/10.1007/s00253-014-6085-9openalex-snapshot
Characterization of a tannin acyl hydrolase from Streptomyces sviceus with substrate preference for digalloyl ester bonds
inferred← citeshttps://doi.org/10.1007/s10529-013-1445-6openalex-snapshot
Biopharmaceutical liquid formulation: a review of the science of protein stability and solubility in aqueous environments
inferred← citeshttps://doi.org/10.1007/s10822-023-00501-9openalex-snapshot
Structural mechanism of Fab domain dissociation as a measure of interface stability
inferred← citeshttps://doi.org/10.1007/s10930-024-10237-6openalex-snapshot
Antibody Aggregation: A Problem Within the Biopharmaceutical Industry and Its Role in AL Amyloidosis Disease
inferred← citeshttps://doi.org/10.1007/s11095-011-0388-7openalex-snapshot
Effect of Sugar Molecules on the Viscosity of High Concentration Monoclonal Antibody Solutions
inferred← citeshttps://doi.org/10.1007/s11095-012-0914-2openalex-snapshot
Liquid Formulations for Stabilizing IgMs During Physical Stress and Long-Term Storage
inferred← citeshttps://doi.org/10.1007/s11095-013-1274-2openalex-snapshot
Assessment of Physical Stability of an Antibody Drug Conjugate by Higher Order Structure Analysis: Impact of Thiol- Maleimide Chemistry
inferred← citeshttps://doi.org/10.1007/s11095-014-1409-0openalex-snapshot
Concentration Dependent Viscosity of Monoclonal Antibody Solutions: Explaining Experimental Behavior in Terms of Molecular Properties
inferred← citeshttps://doi.org/10.1007/s11095-018-2361-1openalex-snapshot
High Throughput Differential Scanning Fluorimetry (DSF) Formulation Screening with Complementary Dyes to Assess Protein Unfolding and Aggregation in Presence of Surfactants
inferred← citeshttps://doi.org/10.1007/s11095-024-03801-3openalex-snapshot
Rapid Development of High Concentration Protein Formulation Driven by High-Throughput Technologies
inferred← citeshttps://doi.org/10.1007/s12010-012-0084-zopenalex-snapshot
Liquid Formulations for Long-Term Storage of Monoclonal IgGs
inferred← citeshttps://doi.org/10.1007/s12010-014-0889-zopenalex-snapshot
Biosynthesis of Glucosyl Glycerol, a Compatible Solute, Using Intermolecular Transglycosylation Activity of Amylosucrase from Methylobacillus flagellatus KT
inferred← citeshttps://doi.org/10.1007/s12268-011-0035-1openalex-snapshot
Die richtige Formulierung zum Erhalt der Qualität therapeutischer Proteine
inferred← citeshttps://doi.org/10.1016/b978-0-12-374279-7.05002-5openalex-snapshot
IgG Structure and Function
inferred← citeshttps://doi.org/10.1016/b978-0-12-386483-3.00004-5openalex-snapshot
Aggregation, stability, and formulation of human antibody therapeutics
inferred← citeshttps://doi.org/10.1016/b978-0-128-24465-4.00024-7openalex-snapshot
IgG Structure and Function
inferred← citeshttps://doi.org/10.1016/b978-0-443-15369-3.00020-1openalex-snapshot
Conformational changes of biomolecules in ion-exchange chromatography
inferred← citeshttps://doi.org/10.1016/b978-0-444-59573-7.00005-1openalex-snapshot
The Value of UV, Fluorescence, and FTIR Spectroscopy in Biopharmaceutical Development
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/b978-1-907568-63-3.00002-5openalex-snapshot
Early candidate selection and formulation development
inferred← citeshttps://doi.org/10.1016/b978-1-907568-63-3.00005-0openalex-snapshot
Analysis of high-throughput data
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/bs.mie.2019.07.016openalex-snapshot
Biochemical and structural analysis of N-terminal acetyltransferases
inferred← citeshttps://doi.org/10.1016/j.ab.2020.113581openalex-snapshot
Nano differential scanning fluorimetry for comparability studies of therapeutic proteins
inferred← citeshttps://doi.org/10.1016/j.ab.2024.115533openalex-snapshot
Extrapolating differential scanning calorimetry data for monoclonal antibodies to low temperatures
inferred← citeshttps://doi.org/10.1016/j.abb.2012.09.008openalex-snapshot
Differential scanning calorimetry as a tool for protein folding and stability
inferred← citeshttps://doi.org/10.1016/j.aca.2025.344331openalex-snapshot
Dual-strain detection of norovirus GI.1 and GII.4 in food samples using epitope-imprinted polymers
inferred← citeshttps://doi.org/10.1016/j.addr.2011.07.006openalex-snapshot
Protein–excipient interactions: Mechanisms and biophysical characterization applied to protein formulation development
inferred← citeshttps://doi.org/10.1016/j.bbalip.2014.07.022openalex-snapshot
Stabilisation and characterisation of the isolated regulatory domain of human 5-lipoxygenase
inferred← citeshttps://doi.org/10.1016/j.bioorg.2019.103391openalex-snapshot
Thermostability detection and optimization of glycoengineered antibodies and antibody-drug conjugates based on differential scanning flouremitry analysis
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2019.06.011openalex-snapshot
Advances in liquid formulations of parenteral therapeutic proteins
inferred← citeshttps://doi.org/10.1016/j.cbpa.2011.03.015openalex-snapshot
Protein stability by number: high-throughput and statistical approaches to one of protein science's most difficult problems
inferred← citeshttps://doi.org/10.1016/j.cels.2021.05.009openalex-snapshot
Fundamentals to function: Quantitative and scalable approaches for measuring protein stability
inferred← citeshttps://doi.org/10.1016/j.chroma.2012.06.037openalex-snapshot
Cation exchange surface-mediated denaturation of an aglycosylated immunoglobulin (IgG1)
inferred← citeshttps://doi.org/10.1016/j.chroma.2014.06.037openalex-snapshot
Unfolding and aggregation of a glycosylated monoclonal antibody on a cation exchange column. Part I. Chromatographic elution and batch adsorption behavior
inferred← citeshttps://doi.org/10.1016/j.chroma.2022.463410openalex-snapshot
Influence of ligand density variations on the two peak elution behavior of a monoclonal antibody in cation exchange chromatography
inferred← citeshttps://doi.org/10.1016/j.csbj.2022.09.035openalex-snapshot
Discovery of compounds with viscosity-reducing effects on biopharmaceutical formulations with monoclonal antibodies
inferred← citeshttps://doi.org/10.1016/j.drudis.2013.06.005openalex-snapshot
Chemical denaturation as a tool in the formulation optimization of biologics
inferred← citeshttps://doi.org/10.1016/j.ejpb.2010.09.006openalex-snapshot
Differences between reversible (self-association) and irreversible aggregation of rHuG-CSF in carbohydrate and polyol formulations
inferred← citeshttps://doi.org/10.1016/j.ejpb.2011.03.001openalex-snapshot
Addressing new analytical challenges in protein formulation development
inferred← citeshttps://doi.org/10.1016/j.ejpb.2014.01.004openalex-snapshot
Agitation-induced aggregation and subvisible particulate formation in model proteins
inferred← citeshttps://doi.org/10.1016/j.ejpb.2017.01.019openalex-snapshot
The effect of charge mutations on the stability and aggregation of a human single chain Fv fragment
inferred← citeshttps://doi.org/10.1016/j.ejpb.2018.01.004openalex-snapshot
Isothermal chemical denaturation as a complementary tool to overcome limitations of thermal differential scanning fluorimetry in predicting physical stability of protein formulations
inferred← citeshttps://doi.org/10.1016/j.ejpb.2018.07.014openalex-snapshot
Buffer exchange path influences the stability and viscosity upon storage of a high concentration protein
inferred← citeshttps://doi.org/10.1016/j.ejpb.2019.05.017openalex-snapshot
Application of interpretable artificial neural networks to early monoclonal antibodies development
inferred← citeshttps://doi.org/10.1016/j.ejpb.2019.06.001openalex-snapshot
Novel non-linear curve fitting to resolve protein unfolding transitions in intrinsic fluorescence differential scanning fluorimetry
inferred← citeshttps://doi.org/10.1016/j.ejpb.2022.05.017openalex-snapshot
Simplified choice of suitable excipients within biologics formulation design using protein-protein interaction- and water activity-maps
inferred← citeshttps://doi.org/10.1016/j.ejps.2014.05.014openalex-snapshot
Thermally induced degradation pathways of three different antibody-based drug development candidates
inferred← citeshttps://doi.org/10.1016/j.ejps.2016.11.016openalex-snapshot
Diversity selection, screening and quantitative structure–activity relationships of osmolyte-like additive effects on the thermal stability of a monoclonal antibody
inferred← citeshttps://doi.org/10.1016/j.febslet.2014.01.051openalex-snapshot
Competing aggregation pathways for monoclonal antibodies
inferred← citeshttps://doi.org/10.1016/j.heliyon.2024.e33895openalex-snapshot
Computational analysis to comprehend the structure-function properties of fibrinolytic enzymes from Bacillus spp for their efficient integration into industrial applications
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2024.131285openalex-snapshot
A high-throughput differential scanning fluorimetry method for rapid detection of thermal stability and iron saturation in lactoferrin
inferred← citeshttps://doi.org/10.1016/j.ijpharm.2012.07.046openalex-snapshot
Evaluating the effects of buffer conditions and extremolytes on thermostability of granulocyte colony-stimulating factor using high-throughput screening combined with design of experiments
inferred← citeshttps://doi.org/10.1016/j.ijpharm.2012.08.033openalex-snapshot
Quality by design: Impact of formulation variables and their interactions on quality attributes of a lyophilized monoclonal antibody
inferred← citeshttps://doi.org/10.1016/j.ijpharm.2012.11.035openalex-snapshot
Differential scanning fluorescence approach using a fluorescent molecular rotor to detect thermostability of proteins in surfactant-containing formulations
inferred← citeshttps://doi.org/10.1016/j.ijpharm.2019.04.080openalex-snapshot
The effect of new compounds in stabilizing downstream monoclonal antibody (mAb) process intermediates
inferred← citeshttps://doi.org/10.1016/j.ijpharm.2019.118505openalex-snapshot
Science and art of protein formulation development
inferred← citeshttps://doi.org/10.1016/j.ijpharm.2020.120170openalex-snapshot
Evaluation of ionic equilibria in mixed-buffer isothermal titration calorimetry and continuously stirred tank reactors
inferred← citeshttps://doi.org/10.1016/j.ijpharm.2024.124735openalex-snapshot
Aggregation of therapeutic monoclonal antibodies due to thermal and air/liquid interfacial agitation stress: Occurrence, stability assessment strategies, aggregation mechanism, influencing factors, and ways to enhance stability
inferred← citeshttps://doi.org/10.1016/j.jconrel.2026.115034openalex-snapshot
From discovery to therapeutic development of monoclonal antibodies
inferred← citeshttps://doi.org/10.1016/j.jpba.2013.01.006openalex-snapshot
Differential scanning fluorimetry: Rapid screening of formulations that promote the stability of reference preparations
inferred← citeshttps://doi.org/10.1016/j.jpba.2018.08.017openalex-snapshot
Investigation of the thermal shift assay and its power to predict protein and virus stabilizing conditions
inferred← citeshttps://doi.org/10.1016/j.jpba.2019.113065openalex-snapshot
Thermal shift assay: Strengths and weaknesses of the method to investigate the ligand-induced thermostabilization of soluble guanylyl cyclase
inferred← citeshttps://doi.org/10.1016/j.molimm.2017.07.006openalex-snapshot
A disulfide-stabilized human V L single-domain antibody library is a source of soluble and highly thermostable binders
inferred← citeshttps://doi.org/10.1016/j.trac.2013.05.005openalex-snapshot
Analytical approaches to assess the degradation of therapeutic proteins
inferred← citeshttps://doi.org/10.1016/j.vaccine.2020.02.068openalex-snapshot
In-situ and sensitive stability study of emulsion and aluminum adjuvanted inactivated foot-and-mouth disease virus vaccine by differential scanning fluorimetry analysis
inferred← citeshttps://doi.org/10.1016/j.xphs.2017.04.039openalex-snapshot
Utility of High Throughput Screening Techniques to Predict Stability of Monoclonal Antibody Formulations During Early Stage Development
inferred← citeshttps://doi.org/10.1016/j.xphs.2018.08.004openalex-snapshot
A New Approach to Study the Physical Stability of Monoclonal Antibody Formulations—Dilution From a Denaturant
inferred← citeshttps://doi.org/10.1016/j.xphs.2019.06.025openalex-snapshot
Characterization of a Novel Bispecific Antibody With Improved Conformational and Chemical Stability
inferred← citeshttps://doi.org/10.1016/j.xphs.2019.07.009openalex-snapshot
Framework Mutations of the 10-1074 bnAb Increase Conformational Stability, Manufacturability, and Stability While Preserving Full Neutralization Activity
inferred← citeshttps://doi.org/10.1016/j.xphs.2019.10.065openalex-snapshot
Orthogonal Techniques to Study the Effect of pH, Sucrose, and Arginine Salts on Monoclonal Antibody Physical Stability and Aggregation During Long-Term Storage
inferred← citeshttps://doi.org/10.1016/j.xphs.2020.03.011openalex-snapshot
Formulations That Suppress Aggregation During Long-Term Storage of a Bispecific Antibody are Characterized by High Refoldability and Colloidal Stability
inferred← citeshttps://doi.org/10.1016/j.xphs.2021.09.027openalex-snapshot
Miniaturized Forced Degradation of Therapeutic Proteins and ADCs by Agitation-Induced Aggregation Using Orbital Shaking of Microplates
inferred← citeshttps://doi.org/10.1016/j.xphs.2022.05.015openalex-snapshot
Microtiter Plate-Based Differential Scanning Fluorimetry: A High-Throughput Method for Efficient Formulation Development
inferred← citeshttps://doi.org/10.1016/j.xphs.2022.11.010openalex-snapshot
Effects of Salts and Surface Charge on the Biophysical Stability of a Low pI Monoclonal Antibody
inferred← citeshttps://doi.org/10.1016/j.xphs.2023.03.021openalex-snapshot
Predictive Nature of High-Throughput Assays in ADC Formulation Screening
inferred← citeshttps://doi.org/10.1016/j.xphs.2023.07.013openalex-snapshot
Automated High-Throughput Matrix Assisted Laser Desorption Ionization Mass Spectrometry Methodology for Formulation Assessment of Polyethylene-Glycol-Conjugated Cytokine Proteins
inferred← citeshttps://doi.org/10.1016/j.xphs.2024.12.029openalex-snapshot
Potential risk factors of protein aggregation in syringe handling during antibody drug dilution for intravenous administration
inferred← citeshttps://doi.org/10.1016/j.xphs.2025.103899openalex-snapshot
Impact of electrostatics on the aggregation, genome release, and self-interactions of AAV9 capsids
inferred← citeshttps://doi.org/10.1016/j.xphs.2025.104054openalex-snapshot
To platform or not to platform: Strategic considerations for antibody formulation in early clinical development
inferred← citeshttps://doi.org/10.1021/acs.biochem.8b00575openalex-snapshot
Structural Changes and Aggregation Mechanisms of Two Different Dimers of an IgG2 Monoclonal Antibody
inferred← citeshttps://doi.org/10.1021/acs.bioconjchem.5b00603openalex-snapshot
Characterization and Higher-Order Structure Assessment of an Interchain Cysteine-Based ADC: Impact of Drug Loading and Distribution on the Mechanism of Aggregation
inferred← citeshttps://doi.org/10.1021/acs.jafc.3c07554openalex-snapshot
High-Throughput Screening Techniques for the Selection of Thermostable Enzymes
inferred← citeshttps://doi.org/10.1021/acs.langmuir.6b02267openalex-snapshot
A Method To Measure Protein Unfolding at an Air–Liquid Interface
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.1c00280openalex-snapshot
Ultradilute Measurements of Self-Association for the Identification of Antibodies with Favorable High-Concentration Solution Properties
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.5c00169openalex-snapshot
Additivity of Transfer Free Energies Enables the Description of Complex Protein Formulations in Implicit Solvent Molecular Dynamics Simulations
inferred← citeshttps://doi.org/10.1021/acs.molpharmaceut.8b00867openalex-snapshot
Developability Assessment of Engineered Monoclonal Antibody Variants with a Complex Self-Association Behavior Using Complementary Analytical and in Silico Tools
inferred← citeshttps://doi.org/10.1021/acs.oprd.7b00337openalex-snapshot
Process Development and Structural Characterization of an Anti-Notch 3 Antibody–Drug Conjugate
inferred← citeshttps://doi.org/10.1021/bc400439xopenalex-snapshot
Auristatin Antibody Drug Conjugate Physical Instability and the Role of Drug Payload
inferred← citeshttps://doi.org/10.1021/bk-2015-1201.ch006openalex-snapshot
Biophysical Techniques for Characterizing the Higher Order Structure and Interactions of Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1021/co400013vopenalex-snapshot
High-Throughput Thermal Scanning for Protein Stability: Making a Good Technique More Robust
inferred← citeshttps://doi.org/10.1021/mp200404copenalex-snapshot
Advancements in High Throughput Biophysical Technologies: Applications for Characterization and Screening during Early Formulation Development of Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1021/mp400666bopenalex-snapshot
Examination of Thermal Unfolding and Aggregation Profiles of a Series of Developable Therapeutic Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1038/ncomms10278openalex-snapshot
Rational engineering of a mesohalophilic carbonic anhydrase to an extreme halotolerant biocatalyst
inferred← citeshttps://doi.org/10.1039/c5cc01877copenalex-snapshot
Inhibited fragmentation of mAbs in buffered ionic liquids
inferred← citeshttps://doi.org/10.1039/c6ra16254aopenalex-snapshot
Impact of PEGylation and non-ionic surfactants on the physical stability of the therapeutic protein filgrastim (G-CSF)
inferred← citeshttps://doi.org/10.1039/c7an01655gopenalex-snapshot
Multi-step conformational transitions in heat-treated protein therapeutics can be monitored in real time with temperature-controlled electrospray ionization mass spectrometry
inferred← citeshttps://doi.org/10.1039/d2fo00394eopenalex-snapshot
Investigating the interaction between dietary polyphenols, the SARS CoV-2 spike protein and the ACE-2 receptor
inferred← citeshttps://doi.org/10.1073/pnas.1301810110openalex-snapshot
RETRACTED: Somatic hypermutation maintains antibody thermodynamic stability during affinity maturation
inferred← citeshttps://doi.org/10.1074/jbc.m110.204362openalex-snapshot
In Vivo Crystallization of Human IgG in the Endoplasmic Reticulum of Engineered Chinese Hamster Ovary (CHO) Cells
inferred← citeshttps://doi.org/10.1080/03639045.2025.2584353openalex-snapshot
High-throughput excipient screening using 384-well plates and a pipetting robot: assessing protein stability after freeze-drying to pre-select viable formulations
inferred← citeshttps://doi.org/10.1080/07391102.2025.2474684openalex-snapshot
Solvent-mediated dynamics of diphtheria toxin and NAD interaction
inferred← citeshttps://doi.org/10.1080/10826076.2013.794738openalex-snapshot
PHYSICOCHEMICAL PROPERTIES OF RITUXIMAB
inferred← citeshttps://doi.org/10.1080/19420862.2016.1259047openalex-snapshot
Improving the developability of an anti-EphA2 single-chain variable fragment for nanoparticle targeting
inferred← citeshttps://doi.org/10.1080/19420862.2017.1421880openalex-snapshot
Monoclonal antibody higher order structure analysis by high throughput protein conformational array
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/10.1080/19420862.2018.1553476openalex-snapshot
Structure, heterogeneity and developability assessment of therapeutic antibodies
inferred← citeshttps://doi.org/10.1080/19420862.2021.1951426openalex-snapshot
Highly sensitive detection of antibody nonspecific interactions using flow cytometry
inferred← citeshttps://doi.org/10.1089/adt.2011.0390openalex-snapshot
Thermal Denaturation Assays in Chemical Biology
inferred← citeshttps://doi.org/10.1093/abt/tbac029openalex-snapshot
Developability assessment at early-stage discovery to enable development of antibody-derived therapeutics
inferred← citeshttps://doi.org/10.1093/protein/gzt022openalex-snapshot
Engineered antibody Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIaR131 and FcγRIIaH131
inferred← citeshttps://doi.org/10.1093/protein/gzt047openalex-snapshot
Addressing polyspecificity of antibodies selected from an in vitro yeast presentation system: a FACS-based, high-throughput selection and analytical tool
inferred← citeshttps://doi.org/10.1101/724146openalex-snapshot
Hot-spots and their contribution to the self-assembly of the viral capsid: in-vitro validation
inferred← citeshttps://doi.org/10.1107/s1399004714009626openalex-snapshot
Unprecedented conformational flexibility revealed in the ligand-binding domains of the Bovicola ovis ecdysone receptor (EcR) and ultraspiracle (USP) subunits
inferred← citeshttps://doi.org/10.1128/aem.00808-12openalex-snapshot
Enhancement of the Structural Stability of Full-Length Clostridial Collagenase by Calcium Ions
inferred← citeshttps://doi.org/10.1146/annurev-chembioeng-062011-081052openalex-snapshot
Engineering Aggregation-Resistant Antibodies
inferred← citeshttps://doi.org/10.1177/1087057114542431openalex-snapshot
High-Throughput Screening and Stability Optimization of Anti-Streptavidin IgG1 and IgG2 Formulations
inferred← citeshttps://doi.org/10.1177/1087057114557781openalex-snapshot
High-Throughput Screening of Formulations to Optimize the Thermal Stability of a Therapeutic Monoclonal Antibody
inferred← citeshttps://doi.org/10.1177/1087057114565593openalex-snapshot
Accelerated Formulation Development of Monoclonal Antibodies (mAbs) and mAb-Based Modalities: Review of Methods and Tools
inferred← citeshttps://doi.org/10.1177/1087057116646553openalex-snapshot
Simultaneous High-Throughput Conformational and Colloidal Stability Screening Using a Fluorescent Molecular Rotor Dye, 4-(4-(Dimethylamino)styryl)-N-Methylpyridinium Iodide (DASPMI)
inferred← citeshttps://doi.org/10.1201/b19023-12openalex-snapshot
Best Practices in Assessing the Developability of Biopharmaceutical Candidates
inferred← citeshttps://doi.org/10.1208/s12248-013-9539-6openalex-snapshot
High-Throughput Biophysical Analysis of Protein Therapeutics to Examine Interrelationships Between Aggregate Formation and Conformational Stability
inferred← citeshttps://doi.org/10.1208/s12249-013-0026-2openalex-snapshot
Orthogonal High-Throughput Thermal Scanning Method for Rank Ordering Protein Formulations
inferred← citeshttps://doi.org/10.1371/journal.pone.0065384openalex-snapshot
Structurally Designed Attenuated Subunit Vaccines for S. aureus LukS-PV and LukF-PV Confer Protection in a Mouse Bacteremia Model
inferred← citeshttps://doi.org/10.1517/17460441.2013.806479openalex-snapshot
Recent developments in the use of differential scanning fluorometry in protein and small molecule discovery and characterization
inferred← citeshttps://doi.org/10.18130/v34g8dopenalex-snapshot
Unfolding and Aggregation of Monoclonal Antibodies during Cation Exchange Chromoatography
inferred← citeshttps://doi.org/10.2298/jsc190513067dopenalex-snapshot
Maltose-mediated long-term stabilization of freeze- and spray- dried forms of bovine and porcine hemoglobin
inferred← citeshttps://doi.org/10.3389/fimmu.2017.01860openalex-snapshot
Engineering of Fc Fragments with Optimized Physicochemical Properties Implying Improvement of Clinical Potentials for Fc-Based Therapeutics
inferred← citeshttps://doi.org/10.3389/fphar.2014.00039openalex-snapshot
Protein comparability assessments and potential applicability of high throughput biophysical methods and data visualization tools to compare physical stability profiles
inferred← citeshttps://doi.org/10.3390/ijms161126037openalex-snapshot
TriFabs—Trivalent IgG-Shaped Bispecific Antibody Derivatives: Design, Generation, Characterization and Application for Targeted Payload Delivery
inferred← citeshttps://doi.org/10.3390/molecules30040965openalex-snapshot
Promiscuity in Polyphenol–Protein Interactions—Monitoring Protein Conformational Change upon Polyphenol–Protein Binding by Nano-Differential Fluorimetry (Nano-DSF)
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/10.4155/tde.12.68openalex-snapshot
High-dose Monoclonal Antibodies Via the Subcutaneous Route: Challenges and Technical solutions, an Industry Perspective
inferred← citeshttps://doi.org/10.4161/mabs.23452openalex-snapshot
Novel asymmetrically engineered antibody Fc variant with superior FcγR binding affinity and specificity compared with afucosylated Fc variant
inferred← citeshttps://doi.org/10.4161/mabs.24218openalex-snapshot
A fully synthetic human Fab antibody library based on fixed VH/VL framework pairings with favorable biophysical properties
inferred← citeshttps://doi.org/10.4161/mabs.27431openalex-snapshot
High-throughput screening for developability during early-stage antibody discovery using self-interaction nanoparticle spectroscopy
inferred← citeshttps://doi.org/10.4161/mabs.3.4.15677openalex-snapshot
Conformational stability and aggregation of therapeutic monoclonal antibodies studied with ANS and Thioflavin T binding
inferred← citeshttps://doi.org/10.4161/mabs.3.6.17922openalex-snapshot
The impact of glycosylation on monoclonal antibody conformation and stability
inferred← citeshttps://doi.org/10.5282/edoc.17520openalex-snapshot
Temperature-induced unfolding, aggregation, and interaction of therapeutic monoclonal antibodies
inferred← citeshttps://doi.org/10.7554/elife.88898openalex-snapshot
Development and biophysical characterization of a humanized FSH–blocking monoclonal antibody therapeutic formulated at an ultra-high concentration
Editorial review for independent work. ICSAC — the Institute for Complexity
Science and Advanced Computing — runs a structured editorial panel for researchers
publishing outside journals, and publishes on CiteStamp rails. Submission is free
and goes through ORCID: icsacinstitute.org/submit.