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Effects of subclass change on the structural stability of chimeric, humanized, and human antibodies under thermal stress
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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/jps.21104openalex-snapshot
Contribution of Variable Domains to the Stability of Humanized IgG1 Monoclonal Antibodies
inferredcites →https://doi.org/10.1002/jps.21834openalex-snapshot
Immunogenicity of aggregates of recombinant human growth hormone in mouse models
inferredcites →https://doi.org/10.1002/jps.21955openalex-snapshot
High throughput thermostability screening of monoclonal antibody formulations
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/pro.309openalex-snapshot
Aggregation of a multidomain protein: A coagulation mechanism governs aggregation of a model IgG1 antibody under weak thermal stress
inferredcites →https://doi.org/10.1002/pro.434openalex-snapshot
Increased aggregation propensity of IgG2 subclass over IgG1: Role of conformational changes and covalent character in isolated aggregates
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/10.1002/prot.21243openalex-snapshot
Effects of acid exposure on the conformation, stability, and aggregation of monoclonal antibodies
inferredcites →https://doi.org/10.1007/s11095-008-9606-3openalex-snapshot
Fragmentation of a Recombinant Monoclonal Antibody at Various pH
inferredcites →https://doi.org/10.1016/0161-5890(93)90432-bopenalex-snapshot
A single amino acid substitution abolishes the heterogeneity of chimeric mouse/human (IgG4) antibody
inferredcites →https://doi.org/10.1016/j.addr.2006.03.011openalex-snapshot
Formulation and delivery issues for monoclonal antibody therapeutics
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.coi.2008.05.010openalex-snapshot
When binding is enough: nonactivating antibody formats
inferredcites →https://doi.org/10.1016/j.jchromb.2004.12.033openalex-snapshot
Non-enzymatic hinge region fragmentation of antibodies in solution
inferredcites →https://doi.org/10.1016/j.jchromb.2007.08.043openalex-snapshot
Structural effect of a recombinant monoclonal antibody on hinge region peptide bond hydrolysis
inferredcites →https://doi.org/10.1016/j.jmb.2003.10.040openalex-snapshot
Optimization of the Antibody CH3 Domain by Residue Frequency Analysis of IgG Sequences
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/s0167-4838(99)00046-1openalex-snapshot
Conformation, pH-induced conformational changes, and thermal unfolding of anti-p24 (HIV-1) monoclonal antibody CB4-1 and its Fab and Fc fragments
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/bi800576copenalex-snapshot
Disulfide Connectivity of Human Immunoglobulin G2 Structural Isoforms
inferredcites →https://doi.org/10.1021/ja0705994openalex-snapshot
β-Elimination and Peptide Bond Hydrolysis: Two Distinct Mechanisms of Human IgG1 Hinge Fragmentation upon Storage
inferredcites →https://doi.org/10.1038/nbt1207-1369openalex-snapshot
Isotype selection in antibody engineering
inferredcites →https://doi.org/10.1038/nrd3365openalex-snapshot
Advances in the assessment and control of the effector functions of therapeutic antibodies
inferredcites →https://doi.org/10.1038/nri1766openalex-snapshot
IgG effector function: a question of balance
inferredcites →https://doi.org/10.1038/nri2747openalex-snapshot
Strategies and challenges for the next generation of therapeutic antibodies
inferredcites →https://doi.org/10.1038/nri2761openalex-snapshot
Therapeutic antibodies for autoimmunity and inflammation
inferredcites →https://doi.org/10.1046/j.1365-2567.1999.00845.xopenalex-snapshot
Normal human immunoglobulin G4 is bispecific: it has two different antigen‐combining sites
inferredcites →https://doi.org/10.1074/jbc.m111.297697openalex-snapshot
Elucidation of Acid-induced Unfolding and Aggregation of Human Immunoglobulin IgG1 and IgG2 Fc
inferredcites →https://doi.org/10.1074/jbc.m709987200openalex-snapshot
Human IgG2 Antibodies Display Disulfide-mediated Structural Isoforms
inferredcites →https://doi.org/10.1074/jbc.m709988200openalex-snapshot
Structural and Functional Characterization of Disulfide Isoforms of the Human IgG2 Subclass
inferredcites →https://doi.org/10.1074/jbc.m804787200openalex-snapshot
Human IgG2 Antibody Disulfide Rearrangement in Vivo
inferredcites →https://doi.org/10.1107/s0907444908007877openalex-snapshot
Structural characterization of a human Fc fragment engineered for lack of effector functions
inferredcites →https://doi.org/10.1111/j.1600-065x.1993.tb00838.xopenalex-snapshot
The B‐Cell Antigen Receptor: Structure and Function of Primary, Secondary, Tertiary and Quaternary Components
inferredcites →https://doi.org/10.1126/science.1144603openalex-snapshot
Anti-Inflammatory Activity of Human IgG4 Antibodies by Dynamic Fab Arm Exchange
inferredcites →https://doi.org/10.1146/annurev.iy.01.040183.000511openalex-snapshot
Structural Basis of Antibody Function
inferredcites →https://doi.org/10.1208/aapsj080359openalex-snapshot
Effects of protein aggregates: An immunologic perspective
inferredcites →https://doi.org/10.1248/bpb.33.1413openalex-snapshot
Influence of pH on Heat-Induced Aggregation and Degradation of Therapeutic Monoclonal Antibodies
inferredcites →https://doi.org/10.4049/jimmunol.137.11.3566openalex-snapshot
Serologic aspects of IgG4 antibodies. II. IgG4 antibodies form small, nonprecipitating immune complexes due to functional monovalency.
inferredcites →https://doi.org/10.4049/jimmunol.159.7.3613openalex-snapshot
Human IgG2 variants of chimeric anti-CD3 are nonmitogenic to T cells
inferredcites →https://doi.org/10.4049/jimmunol.164.4.1925openalex-snapshot
Elimination of Fc Receptor-Dependent Effector Functions of a Modified IgG4 Monoclonal Antibody to Human CD4
inferredcites →https://doi.org/10.4049/jimmunol.170.6.3134openalex-snapshot
Human IgG2 Can Form Covalent Dimers
inferredcites →https://doi.org/10.4049/jimmunol.177.2.1129openalex-snapshot
Modulation of the Effector Functions of a Human IgG1 through Engineering of Its Hinge Region
inferredcites →https://doi.org/10.4161/mabs.1.6.10185openalex-snapshot
IgG2m4, an engineered antibody isotype with reduced Fc function
inferredcites →https://doi.org/10.4161/mabs.19931openalex-snapshot
Marketed therapeutic antibodies compendium
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
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A stable engineered human IgG3 antibody with decreased aggregation during antibody expression and low pH stress
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Constant domain polymorphisms influence monoclonal antibody stability and dynamics
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Comparison of enriched charge variants from different anti‐ CD3 bispecific antibodies reveals differential susceptibility of each bispecific arm to post‐translational modification
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Monoclonal Antibodies Follow Distinct Aggregation Pathways During Production-Relevant Acidic Incubation and Neutralization
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Heat denaturation of the antibody, a multi-domain protein
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Engineering of Protein A for improved purification of antibodies and Fc-fused proteins
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IgG Structure and Function
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IgG Structure and Function
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Stability analysis of monoclonal antibodies
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Glycosylation-dependent antitumor therapeutic monoclonal antibodies
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Reversibility and irreversibility in the temperature denaturation of monoclonal antibodies
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Extrapolating differential scanning calorimetry data for monoclonal antibodies to low temperatures
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Survey of chemical unfolding complexity as a unique stability assessment assay for monoclonal antibodies
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Strategies for overcoming protein and peptide instability in biodegradable drug delivery systems
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Antibody stability: A key to performance - Analysis, influences and improvement
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Thermal and Chemical Unfolding of a Monoclonal IgG1 Antibody: Application of the Multistate Zimm-Bragg Theory
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Highly selective Protein A resin allows for mild sodium chloride-mediated elution of antibodies
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Selecting and engineering monoclonal antibodies with drug-like specificity
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Treatment alternatives for multidrug-resistant fungal pathogens
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Light exacerbates local and global effects induced by pH unfolding of Ipilimumab
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Hierarchical clustering of therapeutic proteins based on agitation-induced aggregation propensity and its relation to physicochemical parameters
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Stability engineering of the human antibody repertoire
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Science and art of protein formulation development
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Assessing localized conformational stability of antibody-drug conjugate by protein conformation assay
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Considerations for the Design of Antibody-Based Therapeutics
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Forced Degradation of Monoclonal Antibodies After Compounding: Impact on Routine Hospital Quality Control
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Physicochemical Stability of Monoclonal Antibodies: A Review
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Circular Dichroism Spectroscopy as a Tool for Monitoring Aggregation in Monoclonal Antibody Therapeutics
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Structural Dynamics of a Thermally Stressed Monoclonal Antibody Characterized by Temperature-Dependent H/D Exchange Mass Spectrometry
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Investigating Therapeutic Protein Structure with Diethylpyrocarbonate Labeling and Mass Spectrometry
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Signature of Antibody Domain Exchange by Native Mass Spectrometry and Collision-Induced Unfolding
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PULSE SPR: A High Throughput Method to Evaluate the Domain Stability of Antibodies
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Role of Domain–Domain Interactions on the Self-Association and Physical Stability of Monoclonal Antibodies: Effect of pH and Salt
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Stabilizing the CH2 Domain of an Antibody by Engineering in an Enhanced Aromatic Sequon
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Pre-adsorption of antibodies enables targeting of nanocarriers despite a biomolecular corona
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Antigen-binding affinity and thermostability of chimeric mouse-chicken IgY and mouse-human IgG antibodies with identical variable domains
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Application of microfluidic modulation spectroscopy for simultaneous structural and thermal stability analysis of commercial mAbs under varying formulation conditions
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Assessment of IgG stability in a low pH elution buffer using ATR-FTIR spectroscopic imaging and microfluidics
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