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Protein aggregation and bioprocessing

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Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/(sici)1097-0290(19970905)55:5<737::aid-bit4>3.0.co;2-copenalex-snapshot
Linear scale ultrafiltration
inferredcites →https://doi.org/10.1002/bit.20416openalex-snapshot
Separation of monoclonal antibody alemtuzumab monomer and dimers using ultrafiltration
inferredcites →https://doi.org/10.1002/ddr.10344openalex-snapshot
Commercial manufacturing scale formulation and analytical characterization of therapeutic recombinant antibodies
inferredcites →https://doi.org/10.1002/jps.20347openalex-snapshot
Reversible Self-Association Increases the Viscosity of a Concentrated Monoclonal Antibody in Aqueous Solution
inferredcites →https://doi.org/10.1016/j.ab.2005.07.004openalex-snapshot
Effective elution of antibodies by arginine and arginine derivatives in affinity column chromatography
inferredcites →https://doi.org/10.1016/j.febslet.2005.10.058openalex-snapshot
What factor drives the fibrillogenic association of β‐sheets?
inferredcites →https://doi.org/10.1016/j.pep.2004.04.020openalex-snapshot
Protein aggregation during overexpression limited by peptide extensions with large net negative charge
inferredcites →https://doi.org/10.1016/s0076-6879(94)33042-5openalex-snapshot
[39] Dityrosine: A marker for oxidatively modified proteins and selective proteolysis
inferredcites →https://doi.org/10.1016/s0958-1669(00)00201-9openalex-snapshot
Membrane separations in biotechnology
inferredcites →https://doi.org/10.1016/s0962-8924(00)01745-1openalex-snapshot
Pathways for protein disulphide bond formation
inferredcites →https://doi.org/10.1021/bi9905516openalex-snapshot
Kinetics and Thermodynamics of Dimer Formation and Dissociation for a Recombinant Humanized Monoclonal Antibody to Vascular Endothelial Growth Factor
inferredcites →https://doi.org/10.1021/bk-1994-0567.ch006openalex-snapshot
Disulfide-Linked Oligomerization of Basic Fibroblast Growth Factor
inferredcites →https://doi.org/10.1021/bp025511zopenalex-snapshot
Free Sulfhydryl in Recombinant Monoclonal Antibodies
inferredcites →https://doi.org/10.1021/bp0497029openalex-snapshot
Effect of Copper Sulfate on Performance of a Serum-Free CHO Cell Culture Process and the Level of Free Thiol in the Recombinant Antibody Expressed
inferredcites →https://doi.org/10.1023/a:1025771421906openalex-snapshot
Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation
inferredcites →https://doi.org/10.1080/146532401753174061openalex-snapshot
Manufacture and quality control of CAMPATH-1 antibodies for clinical trials
inferredcites →https://doi.org/10.1111/j.1751-1097.1984.tb03891.xopenalex-snapshot
THE PHOTOPHYSICS AND PHOTOCHEMISTRY OF THE NEAR‐UV ABSORBING AMINO ACIDS–II. TYROSINE AND ITS SIMPLE DERIVATIVES
inferredcites →https://doi.org/10.1128/jvi.73.2.1392-1398.1999openalex-snapshot
Coxsackievirus and Adenovirus Receptor Amino-Terminal Immunoglobulin V-Related Domain Binds Adenovirus Type 2 and Fiber Knob from Adenovirus Type 12
inferredcites →https://doi.org/10.1208/aapsj080359openalex-snapshot
Effects of protein aggregates: An immunologic perspective
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/10.2337/diab.37.8.1059openalex-snapshot
Pharmacokinetic Model of Circulating Covalent Aggregates of Insulin

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.3969644openalex-extracted
inferred← citeshttps://doi.org/10.1002/0471266949.bmc160openalex-snapshot
Process Development of Protein Therapeutics
inferred← citeshttps://doi.org/10.1002/0471266949.bmc160.pub2openalex-snapshot
Process Development of Protein Therapeutics
inferred← citeshttps://doi.org/10.1002/14356007.o22_o08openalex-snapshot
Process Systems Engineering, 4. Process and Product Synthesis, Design, and Analysis
inferred← citeshttps://doi.org/10.1002/9780470027318.a9092openalex-snapshot
Dynamic Light Scattering for Protein Characterization
inferred← citeshttps://doi.org/10.1002/9780470054581.eib516openalex-snapshot
Temperature‐Dependent Molecular Adaptations, Microbial Proteins
inferred← citeshttps://doi.org/10.1002/9780470444894.ch5openalex-snapshot
Purification of Human Monoclonal Antibodies: Non‐Protein A Strategies
inferred← citeshttps://doi.org/10.1002/9780470595886.ch16openalex-snapshot
Development of Formulations for Therapeutic Monoclonal Antibodies and Fc Fusion Proteins
inferred← citeshttps://doi.org/10.1002/9780470595886.ch24openalex-snapshot
Manufacturing Fundamentals for Biopharmaceuticals
inferred← citeshttps://doi.org/10.1002/9780470595886.ch25openalex-snapshot
Protein Stability During Bioprocessing
inferred← citeshttps://doi.org/10.1002/9780470595886.ch27openalex-snapshot
Strategies for Bulk Storage and Shipment of Proteins
inferred← citeshttps://doi.org/10.1002/9780470595886.ch3openalex-snapshot
Physical Stability of Protein Pharmaceuticals
inferred← citeshttps://doi.org/10.1002/9780470595886.ch33openalex-snapshot
Filling Processes and Technologies for Liquid Biopharmaceuticals
inferred← citeshttps://doi.org/10.1002/9780470769829.ch1openalex-snapshot
Fundamental Structures and Behaviors of Proteins
inferred← citeshttps://doi.org/10.1002/9780470769829.ch3openalex-snapshot
Identification and Impact of Aggregation‐Prone Regions in Proteins and Therapeutic Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1002/9780470769829.ch4openalex-snapshot
External Factors Affecting Protein Aggregation
inferred← citeshttps://doi.org/10.1002/9780470769829.ch5openalex-snapshot
Experimental Detection and Characterization of Protein Aggregates
inferred← citeshttps://doi.org/10.1002/9780470769829.ch6openalex-snapshot
Approaches to Control Protein Aggregation during Bulk Production
inferred← citeshttps://doi.org/10.1002/9780470769829.ch7openalex-snapshot
Protein Aggregation and Particle Formation: Effects of Formulation, Interfaces, and Drug Product Manufacturing Operations
inferred← citeshttps://doi.org/10.1002/9780470769829.ch8openalex-snapshot
Approaches to Managing Protein Aggregation in Product Development
inferred← citeshttps://doi.org/10.1002/9781118150573.ch14openalex-snapshot
Protein Purification and its Relation to Protein Aggregation and Particles
inferred← citeshttps://doi.org/10.1002/9781118150573.ch15openalex-snapshot
Formulation Development and its Relation to Protein Aggregation and Particles
inferred← citeshttps://doi.org/10.1002/9781118150573.ch2openalex-snapshot
Separation‐Based Analytical Methods for Measuring Protein Aggregation
inferred← citeshttps://doi.org/10.1002/9781118150573.ch7openalex-snapshot
Characterization of Aggregates and Particles Using Emerging Techniques
inferred← citeshttps://doi.org/10.1002/9781118183373.ch15openalex-snapshot
Modifiers of Protein Aggregation—From Nonspecific to Specific Interactions
inferred← citeshttps://doi.org/10.1002/9781118354599.ch8openalex-snapshot
Peptide‐Fc Fusion Therapeutics: Applications and Challenges
inferred← citeshttps://doi.org/10.1002/9781118354698.ch11openalex-snapshot
Late‐Stage Product Characterization: Applications in Formulation, Process, and Manufacturing Development
inferred← citeshttps://doi.org/10.1002/9781118733813.ch14openalex-snapshot
Cognate Techniques to ACOMP
inferred← citeshttps://doi.org/10.1002/9781118992432.ch4openalex-snapshot
Excipients Used in Biotechnology Products
inferred← citeshttps://doi.org/10.1002/9781119126942.ch6openalex-snapshot
PURIFICATION OF HUMAN MONOCLONAL ANTIBODIES: NON‐PROTEIN A STRATEGIES
inferred← citeshttps://doi.org/10.1002/9781119313786.ch12openalex-snapshot
HPLC and UHPLC for Biopharmaceutical Analysis
inferred← citeshttps://doi.org/10.1002/9781119490258.furread2openalex-snapshot
Further Reading
inferred← citeshttps://doi.org/10.1002/9781119564690.ch6openalex-snapshot
Pivotal Biology, Chemistry, Biochemistry, and Biophysical Concepts of Biologics and Biosimilars
inferred← citeshttps://doi.org/10.1002/9783527632909.ch10openalex-snapshot
Formulation Strategies for Recombinant Protein and Related Biotech Drugs
inferred← citeshttps://doi.org/10.1002/9783527807390.ch3openalex-snapshot
Applications of Freeze‐drying in Pharmaceuticals, Biopharmaceuticals, and Foods
inferred← citeshttps://doi.org/10.1002/9783527811410.ch13openalex-snapshot
Mammalian Fed‐batch Cell Culture for Biopharmaceuticals
inferred← citeshttps://doi.org/10.1002/amp2.10142openalex-snapshot
Engineering a ceramic piston pump to minimize particle formation for a therapeutic immunoglobulin: A combined factorial and modeling approach
inferred← citeshttps://doi.org/10.1002/bab.2236openalex-snapshot
Process development exploiting competitive adsorption‐based displacement effects in monoclonal antibody aggregate removal—A new high‐throughput screening procedure for membrane chromatography
inferred← citeshttps://doi.org/10.1002/biot.201000001openalex-snapshot
Technical refolding of proteins: Do we have freedom to operate?
inferred← citeshttps://doi.org/10.1002/biot.201200065openalex-snapshot
Minimizing immunogenicity of biopharmaceuticals by controlling critical quality attributes of proteins
inferred← citeshttps://doi.org/10.1002/biot.201600427openalex-snapshot
Choosing the right protein A affinity chromatography media can remove aggregates efficiently
inferred← citeshttps://doi.org/10.1002/biot.202400249openalex-snapshot
Dialysis rolled scaffold bioreactor allows extended production of monoclonal antibody with reduced media use
inferred← citeshttps://doi.org/10.1002/bit.21627openalex-snapshot
Non‐native protein aggregation kinetics
inferred← citeshttps://doi.org/10.1002/bit.22014openalex-snapshot
Stabilization of α‐chymotrypsin upon PEGylation correlates with reduced structural dynamics
inferred← citeshttps://doi.org/10.1002/bit.22126openalex-snapshot
A clone screening method using mRNA levels to determine specific productivity and product quality for monoclonal antibodies
inferred← citeshttps://doi.org/10.1002/bit.22336openalex-snapshot
Response of a concentrated monoclonal antibody formulation to high shear
inferred← citeshttps://doi.org/10.1002/bit.22392openalex-snapshot
Biospecific protein immobilization for rapid analysis of weak protein interactions using self‐interaction nanoparticle spectroscopy
inferred← citeshttps://doi.org/10.1002/bit.22572openalex-snapshot
Transient expression of human TorsinA enhances secretion of two functionally distinct proteins in cultured Chinese hamster ovary (CHO) cells
inferred← citeshttps://doi.org/10.1002/bit.22894openalex-snapshot
Defining process design space for a hydrophobic interaction chromatography (HIC) purification step: Application of quality by design (QbD) principles
inferred← citeshttps://doi.org/10.1002/bit.22902openalex-snapshot
Detection and reduction of microaggregates in insulin preparations
inferred← citeshttps://doi.org/10.1002/bit.23155openalex-snapshot
Aggregates in monoclonal antibody manufacturing processes
inferred← citeshttps://doi.org/10.1002/bit.23188openalex-snapshot
Quaternary conformational stability: The effect of reversible self‐association on the fibrillation of two insulin analogs
inferred← citeshttps://doi.org/10.1002/bit.23220openalex-snapshot
Evaluation of protein engineering and process optimization approaches to enhance antibody drug manufacturability
inferred← citeshttps://doi.org/10.1002/bit.23288openalex-snapshot
Culture temperature modulates aggregation of recombinant antibody in cho cells
inferred← citeshttps://doi.org/10.1002/bit.24341openalex-snapshot
Removal versus fragmentation of amyloid‐forming precursors via membrane filtration
inferred← citeshttps://doi.org/10.1002/bit.25495openalex-snapshot
Air sparging for prevention of antibody disulfide bond reduction in harvested CHO cell culture fluid
inferred← citeshttps://doi.org/10.1002/bit.25626openalex-snapshot
miR‐2861 as novel HDAC5 inhibitor in CHO cells enhances productivity while maintaining product quality
inferred← citeshttps://doi.org/10.1002/bit.25949openalex-snapshot
Predictive approach for protein aggregation: Correlation of protein surface characteristics and conformational flexibility to protein aggregation propensity
inferred← citeshttps://doi.org/10.1002/bit.26543openalex-snapshot
Using extensional flow to reveal diverse aggregation landscapes for three IgG1 molecules
inferred← citeshttps://doi.org/10.1002/bit.26547openalex-snapshot
Isotype dependent on‐column non‐reversible aggregation of monoclonal antibodies
inferred← citeshttps://doi.org/10.1002/bit.26985openalex-snapshot
Novel, linked bioreactor system for continuous production of biologics
inferred← citeshttps://doi.org/10.1002/bit.27212openalex-snapshot
Synergistic effects of flow and interfaces on antibody aggregation
inferred← citeshttps://doi.org/10.1002/bit.27776openalex-snapshot
Antibody capture process based on magnetic beads from very high cell density suspension
inferred← citeshttps://doi.org/10.1002/bit.27790openalex-snapshot
Antibody disulfide bond reduction and recovery during biopharmaceutical process development—A review
inferred← citeshttps://doi.org/10.1002/bit.28230openalex-snapshot
Manipulation of mRNA translation elongation influences the fragmentation of a biotherapeutic Fc‐fusion protein produced in CHO cells
inferred← citeshttps://doi.org/10.1002/btm2.10215openalex-snapshot
Formulation‐based approaches for dermal delivery of vaccines and therapeutic nucleic acids: Recent advances and future perspectives
inferred← citeshttps://doi.org/10.1002/btpr.1767openalex-snapshot
Free light chain content in culture media reflects recombinant monoclonal antibody productivity and quality
inferred← citeshttps://doi.org/10.1002/btpr.1908openalex-snapshot
Resolution of heterogeneous charged antibody aggregates via multimodal chromatography: A comparison to conventional approaches
inferred← citeshttps://doi.org/10.1002/btpr.2089openalex-snapshot
Tailoring recombinant protein quality by rational media design
inferred← citeshttps://doi.org/10.1002/btpr.211openalex-snapshot
Factors influencing antibody stability at solid–liquid interfaces in a high shear environment
inferred← citeshttps://doi.org/10.1002/btpr.2289openalex-snapshot
Cell culture media impact on drug product solution stability
inferred← citeshttps://doi.org/10.1002/btpr.2836openalex-snapshot
Effect of protein cryoconcentration and processing conditions on kinetics of dimer formation for a monoclonal antibody: A case study on bioprocessing
inferred← citeshttps://doi.org/10.1002/btpr.3055openalex-snapshot
High throughput screening setup of a scale‐down device for membrane chromatography‐aggregate removal of monoclonal antibodies
inferred← citeshttps://doi.org/10.1002/btpr.3230openalex-snapshot
Streamlined process development procedure incorporating the selection of various stationary phase types established in a mAb aggregate reduction study with different mixed mode ligands
inferred← citeshttps://doi.org/10.1002/btpr.3391openalex-snapshot
Size‐based analysis of virus removal filter fouling using fractionated protein aggregates
inferred← citeshttps://doi.org/10.1002/btpr.456openalex-snapshot
Glucocorticoid receptor‐mediated reduction of IgG‐fusion protein aggregation in Chinese hamster ovary cells
inferred← citeshttps://doi.org/10.1002/btpr.579openalex-snapshot
Effect of chemical chaperone addition on production and aggregation of recombinant flag‐tagged COMP‐angiopoietin 1 in chinese hamster ovary cells
inferred← citeshttps://doi.org/10.1002/btpr.740openalex-snapshot
Bioprocessing of bacteriophages via rapid drying onto microcrystals
inferred← citeshttps://doi.org/10.1002/cbic.201600299openalex-snapshot
Influence of Label and Charge Density on the Association of the Therapeutic Monoclonal Antibodies Trastuzumab and Cetuximab Conjugated to Anionic Fluorophores
inferred← citeshttps://doi.org/10.1002/cbic.202000577openalex-snapshot
Fc‐Binding Antibody‐Recruiting Molecules Targeting Prostate‐Specific Membrane Antigen: Defucosylation of Antibody for Efficacy Improvement**
inferred← citeshttps://doi.org/10.1002/elsc.201400210openalex-snapshot
Systematic purification of salt‐intolerant proteins by ion‐exchange chromatography: The example of human α‐galactosidase A
inferred← citeshttps://doi.org/10.1002/eng2.12147openalex-snapshot
The uniqueness of flow in probing the aggregation behavior of clinically relevant antibodies
inferred← citeshttps://doi.org/10.1002/jctb.6920openalex-snapshot
Process analytical technique ( PAT ) miniaturization for monoclonal antibody aggregate detection in continuous downstream processing
inferred← citeshttps://doi.org/10.1002/jps.21419openalex-snapshot
IgG particle formation during filling pump operation: A case study of heterogeneous nucleation on stainless steel nanoparticles
inferred← citeshttps://doi.org/10.1002/jps.21504openalex-snapshot
Effects of glycosylation on the stability of protein pharmaceuticals
inferred← citeshttps://doi.org/10.1002/jps.21521openalex-snapshot
Principles, approaches, and challenges for predicting protein aggregation rates and shelf life
inferred← citeshttps://doi.org/10.1002/jps.21530openalex-snapshot
Overlooking Subvisible Particles in Therapeutic Protein Products: Gaps That May Compromise Product Quality
inferred← citeshttps://doi.org/10.1002/jps.21566openalex-snapshot
Protein aggregation: Pathways, induction factors and analysis
inferred← citeshttps://doi.org/10.1002/jps.21726openalex-snapshot
Characterization of High-Molecular-Weight Nonnative Aggregates and Aggregation Kinetics by Size Exclusion Chromatography With Inline Multi-Angle Laser Light Scattering
inferred← citeshttps://doi.org/10.1002/jps.21869openalex-snapshot
Multi-variate approach to global protein aggregation behavior and kinetics: Effects of pH, NaCl, and temperature for α-chymotrypsinogen A
inferred← citeshttps://doi.org/10.1002/jps.21938openalex-snapshot
Use of a folding model and in situ spectroscopic techniques for rational formulation development and stability testing of monoclonal antibody therapeutics**Gauri Rao and Vandana Iyer contributed equally to this work.
inferred← citeshttps://doi.org/10.1002/jps.21989openalex-snapshot
Potential inaccurate quantitation and sizing of protein aggregates by size exclusion chromatography: Essential need to use orthogonal methods to assure the quality of therapeutic protein products
inferred← citeshttps://doi.org/10.1002/jps.22046openalex-snapshot
Quantification and Characterization of Subvisible Proteinaceous Particles in Opalescent mAb Formulations Using Micro-Flow Imaging
inferred← citeshttps://doi.org/10.1002/jps.22276openalex-snapshot
Impact of Product-Related Factors on Immunogenicity of Biotherapeutics
inferred← citeshttps://doi.org/10.1002/jps.22290openalex-snapshot
Degradation of Polysorbates 20 and 80: Studies on Thermal Autoxidation and Hydrolysis
inferred← citeshttps://doi.org/10.1002/jps.22345openalex-snapshot
BIOTECHNOLOGY: Aggregation of Recombinant Human Botulinum Protein Antigen Serotype C in Varying Solution Conditions: Implications of Conformational Stability for Aggregation Kinetics
inferred← citeshttps://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
inferred← citeshttps://doi.org/10.1002/jps.22597openalex-snapshot
Effects of Surfaces and Leachables on the Stability of Biopharmaceuticals
inferred← citeshttps://doi.org/10.1002/jps.22676openalex-snapshot
Characterization of Subvisible Particle Formation During the Filling Pump Operation of a Monoclonal Antibody Solution
inferred← citeshttps://doi.org/10.1002/jps.22705openalex-snapshot
Aggregation in Protein-Based Biotherapeutics: Computational Studies and Tools to Identify Aggregation-Prone Regions
inferred← citeshttps://doi.org/10.1002/jps.22749openalex-snapshot
Individual Second Virial Coefficient Determination of Monomer and Oligomers in Heat-Stressed Protein Samples Using Size-Exclusion Chromatography-Light Scattering
inferred← citeshttps://doi.org/10.1002/jps.22812openalex-snapshot
Forced Degradation of Therapeutic Proteins
inferred← citeshttps://doi.org/10.1002/jps.23105openalex-snapshot
Raster Image Correlation Spectroscopy As a Novel Tool for the Quantitative Assessment of Protein Diffusional Behaviour in Solution
inferred← citeshttps://doi.org/10.1002/jps.23150openalex-snapshot
Accelerated Stability Studies of Abatacept Formulations: Comparison of Freeze–Thawing- and Agitation-induced Stresses
inferred← citeshttps://doi.org/10.1002/jps.23157openalex-snapshot
Transient Molten Globules and Metastable Aggregates Induced by Brief Exposure of a Monoclonal IgG to Low pH
inferred← citeshttps://doi.org/10.1002/jps.23369openalex-snapshot
A Systematic Multitechnique Approach for Detection and Characterization of Reversible Self-Association during Formulation Development of Therapeutic Antibodies
inferred← citeshttps://doi.org/10.1002/jps.23421openalex-snapshot
Characterization of Fc-Fusion Protein Aggregates Derived from Extracellular Domain Disulfide Bond Rearrangements
inferred← citeshttps://doi.org/10.1002/jps.23654openalex-snapshot
A systematic multitechnique approach for detection and characterization of reversible self-association during formulation development of therapeutic antibodies
inferred← citeshttps://doi.org/10.1002/jps.23746openalex-snapshot
Utilizing Dynamic Light Scattering as a Process Analytical Technology for Protein Folding and Aggregation Monitoring in Vaccine Manufacturing
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.23839openalex-snapshot
Structural Characterization of IgG1 mAb Aggregates and Particles Generated Under Various Stress Conditions
inferred← citeshttps://doi.org/10.1002/jps.23861openalex-snapshot
Control of Protein Particle Formation During Ultrafiltration/Diafiltration Through Interfacial Protection
inferred← citeshttps://doi.org/10.1002/jps.24130openalex-snapshot
Improving Monoclonal Antibody Selection and Engineering using Measurements of Colloidal Protein Interactions
inferred← citeshttps://doi.org/10.1002/jps.24157openalex-snapshot
Transmission Electron Microscopy as an Orthogonal Method to Characterize Protein Aggregates
inferred← citeshttps://doi.org/10.1002/jps.24357openalex-snapshot
Particle Shedding from Peristaltic Pump Tubing in Biopharmaceutical Drug Product Manufacturing
inferred← citeshttps://doi.org/10.1002/jps.24379openalex-snapshot
Physical Characterization and In Vitro Biological Impact of Highly Aggregated Antibodies Separated into Size-Enriched Populations by Fluorescence-Activated Cell Sorting
inferred← citeshttps://doi.org/10.1002/jps.24411openalex-snapshot
Characterization of Submicron (0.1–1 μm) Particles in Therapeutic Proteins by Nanoparticle Tracking Analysis
inferred← citeshttps://doi.org/10.1002/jrs.4679openalex-snapshot
Use of Raman and Raman optical activity for the structural characterization of a therapeutic monoclonal antibody formulation subjected to heat stress
inferred← citeshttps://doi.org/10.1002/jssc.202101034openalex-snapshot
Synthetic pharmaceutical peptides characterization by chromatography principles and method development
inferred← citeshttps://doi.org/10.1002/nano.202200251openalex-snapshot
Conjugated surfactant micelles: A non‐denaturing purification platform for concentrated human immunoglobulin G
inferred← citeshttps://doi.org/10.1002/pro.20openalex-snapshot
Ion‐specific modulation of protein interactions: Anion‐induced, reversible oligomerization of a fusion protein
inferred← citeshttps://doi.org/10.1002/pro.2775openalex-snapshot
Insert engineering and solubility screening improves recovery of virus‐like particle subunits displaying hydrophobic epitopes
inferred← citeshttps://doi.org/10.1002/pro.3598openalex-snapshot
A stable engineered human IgG3 antibody with decreased aggregation during antibody expression and low pH stress
inferred← citeshttps://doi.org/10.1002/pro.3852openalex-snapshot
Engineering a human IgG2 antibody stable at low pH
inferred← citeshttps://doi.org/10.1002/pro.396openalex-snapshot
The use of native cation‐exchange chromatography to study aggregation and phase separation of monoclonal antibodies
inferred← citeshttps://doi.org/10.1002/pro.70149openalex-snapshot
Modulation of insulin aggregation by betaine and proline directly observed via real‐time super‐resolution microscopy
inferred← citeshttps://doi.org/10.1002/prot.25594openalex-snapshot
AggScore: Prediction of aggregation‐prone regions in proteins based on the distribution of surface patches
inferred← citeshttps://doi.org/10.1002/psc.1167openalex-snapshot
Quality specifications for peptide drugs: a regulatory‐pharmaceutical approach
inferred← citeshttps://doi.org/10.1002/psc.70001openalex-snapshot
Regulatory Guidelines for the Analysis of Therapeutic Peptides and Proteins
inferred← citeshttps://doi.org/10.1007/10_2013_214openalex-snapshot
Product Quality Considerations for Mammalian Cell Culture Process Development and Manufacturing
inferred← citeshttps://doi.org/10.1007/12_2011_128openalex-snapshot
Aptamer: Biology to Applications
inferred← citeshttps://doi.org/10.1007/978-1-0716-0389-5_12openalex-snapshot
A New Approach to Assess mAb Aggregation
inferred← citeshttps://doi.org/10.1007/978-1-0716-1450-1_4openalex-snapshot
Assessment of Therapeutic Antibody Developability by Combinations of In Vitro and In Silico Methods
inferred← citeshttps://doi.org/10.1007/978-1-0716-1859-2_27openalex-snapshot
Characterizing Soluble Protein Aggregates Using Native Mass Spectrometry Coupled with Temperature-Controlled Electrospray Ionization and Size-Excl usion Chromatography
inferred← citeshttps://doi.org/10.1007/978-1-0716-1859-2_3openalex-snapshot
A3D 2.0 Update for the Prediction and Optimization of Protein Solubility
inferred← citeshttps://doi.org/10.1007/978-1-4614-4316-2_11openalex-snapshot
Higher-Order Structure and Protein Aggregate Characterization of Protein Therapeutics: Perspectives from Good Manufacturing Practices and Regulatory Guidance
inferred← citeshttps://doi.org/10.1007/978-1-4614-4316-2_4openalex-snapshot
Biophysical Techniques for Protein Size Distribution Analysis
inferred← citeshttps://doi.org/10.1007/978-1-4614-4316-2_7openalex-snapshot
Application of Biophysics in Formulation, Process, and Product Characterization: Selected Case Studies
inferred← citeshttps://doi.org/10.1007/978-1-4614-6916-2_9openalex-snapshot
Molecular Structural Analysis
inferred← citeshttps://doi.org/10.1007/978-1-4614-7978-9_2openalex-snapshot
Molecule and Manufacturability Assessment Leading to Robust Commercial Formulation for Therapeutic Proteins
inferred← citeshttps://doi.org/10.1007/978-1-4939-2205-5_14openalex-snapshot
A Screening Methodology for Purifying Proteins with Aggregation Problems
inferred← citeshttps://doi.org/10.1007/978-1-4939-2316-8_12openalex-snapshot
Application of QbD Elements in the Development and Scale-Up of a Commercial Filtration Process
inferred← citeshttps://doi.org/10.1007/978-1-4939-2316-8_13openalex-snapshot
Application of QbD Elements in the Development and Scale-up of Commercial Filling Process
inferred← citeshttps://doi.org/10.1007/978-1-4939-3389-1_27openalex-snapshot
Formulation Studies During Preclinical Development of Influenza Hemagglutinin and Virus-Like Particle Vaccine Candidates
inferred← citeshttps://doi.org/10.1007/978-1-4939-4014-1_12openalex-snapshot
Characterization of Chemical and Physical Modifications of Human Serum Albumin by Capillary Zone Electrophoresis
inferred← citeshttps://doi.org/10.1007/978-1-4939-9929-3_21openalex-snapshot
Physical Stability Studies of Antibody-Drug Conjugates (ADCs) Under Stressed Conditions
inferred← citeshttps://doi.org/10.1007/978-1-61779-433-9_32openalex-snapshot
Engineering the Chaperone Network of CHO Cells for Optimal Recombinant Protein Production and Authenticity
inferred← citeshttps://doi.org/10.1007/978-3-030-31415-6_1openalex-snapshot
Chapter 1: Monoclonal Antibodies: Structure, Physicochemical Stability, and Protein Engineering
inferred← citeshttps://doi.org/10.1007/978-3-030-31415-6_17openalex-snapshot
Chapter 17: Scale-Down Models for Robust Biologics Drug Product Process Development
inferred← citeshttps://doi.org/10.1007/978-3-030-32622-7_34openalex-snapshot
ANTISOMA: A Computational Pipeline for the Reduction of the Aggregation Propensity of Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1007/978-3-030-76367-1_17openalex-snapshot
Ophthalmic Product Development for Biologics
inferred← citeshttps://doi.org/10.1007/978-3-031-59478-6_19openalex-snapshot
Peptides, Proteins and Antibodies
inferred← citeshttps://doi.org/10.1007/978-3-031-62007-2_14openalex-snapshot
Biopharmaceutical Informatics: A Strategic Vision for Discovering Developable Biotherapeutic Drug Candidates
inferred← citeshttps://doi.org/10.1007/978-3-031-63164-1_4openalex-snapshot
Changes in Structure, Dispersity and Phase Behavior of Proteins: The Virus-Like Particles in the Presence of Nucleic Acids
inferred← citeshttps://doi.org/10.1007/978-3-319-90603-4_2openalex-snapshot
Polysorbate Degradation and Quality
inferred← citeshttps://doi.org/10.1007/978-3-319-90603-4_5openalex-snapshot
Solubility, Opalescence, and Particulate Matter
inferred← citeshttps://doi.org/10.1007/978-3-319-90603-4_6openalex-snapshot
Analytical Characterization and Predictive Tools for Highly Concentrated Protein Formulations
inferred← citeshttps://doi.org/10.1007/978-3-319-98428-5_2openalex-snapshot
Therapeutic Proteins
inferred← citeshttps://doi.org/10.1007/978-4-431-55985-6_19openalex-snapshot
Use of Analytical Ultracentrifugation as an Orthogonal Method for Size Exclusion Chromatography: Assuring Quality for Therapeutic Protein Products and Meeting Regulatory Expectations
inferred← citeshttps://doi.org/10.1007/978-81-322-2467-9_4openalex-snapshot
Protein Folding and Aggregation: A Revisit of Basic Conception
inferred← citeshttps://doi.org/10.1007/978-94-007-1257-7_13openalex-snapshot
Quality Issues Arising from Post-translational Modification of Recombinant Antibodies
inferred← citeshttps://doi.org/10.1007/978-94-024-1069-3_7openalex-snapshot
Prediction of Protein Aggregation and Amyloid Formation
inferred← citeshttps://doi.org/10.1007/s00114-013-1013-xopenalex-snapshot
Serous cutaneous glands in anurans: Fourier transform analysis of the repeating secretory granule substructure
inferred← citeshttps://doi.org/10.1007/s00216-013-7462-4openalex-snapshot
Hollow-fiber flow field-flow fractionation with multi-angle laser scattering detection for aggregation studies of therapeutic proteins
inferred← citeshttps://doi.org/10.1007/s00216-014-8065-4openalex-snapshot
Separation and quantification of monoclonal-antibody aggregates by hollow-fiber-flow field-flow fractionation
inferred← citeshttps://doi.org/10.1007/s00216-014-8108-xopenalex-snapshot
Post-translational structural modifications of immunoglobulin G and their effect on biological activity
inferred← citeshttps://doi.org/10.1007/s00216-015-8672-8openalex-snapshot
Fluorescence dye-based detection of mAb aggregates in CHO culture supernatants
inferred← citeshttps://doi.org/10.1007/s00216-017-0362-2openalex-snapshot
High-throughput analysis of sub-visible mAb aggregate particles using automated fluorescence microscopy imaging
inferred← citeshttps://doi.org/10.1007/s00249-009-0404-6openalex-snapshot
Insights into protein–polysorbate interactions analysed by means of isothermal titration and differential scanning calorimetry
inferred← citeshttps://doi.org/10.1007/s00253-012-4347-yopenalex-snapshot
RETRACTED ARTICLE: Simultaneous expression of antibody light and heavy chains in Pichia pastoris: improving retransformation outcome by linearizing vector at a different site
inferred← citeshttps://doi.org/10.1007/s00253-017-8312-7openalex-snapshot
Different fermentation processes produced variants of an anti-CD52 monoclonal antibody that have divergent in vitro and in vivo characteristics
inferred← citeshttps://doi.org/10.1007/s00253-020-10744-3openalex-snapshot
Investigation into the impact of tyrosine on the product formation and quality attributes of mAbs in rCHO cell cultures
inferred← citeshttps://doi.org/10.1007/s00253-022-11977-0openalex-snapshot
Recombinant antibodies aggregation and overcoming strategies in CHO cells
inferred← citeshttps://doi.org/10.1007/s00449-013-1010-7openalex-snapshot
Development of a magnetic biocatalyst useful for the synthesis of ethyloleate
inferred← citeshttps://doi.org/10.1007/s00449-019-02103-yopenalex-snapshot
Precipitation of complex antibody solutions: influence of contaminant composition and cell culture medium on the precipitation behavior
inferred← citeshttps://doi.org/10.1007/s00449-019-02239-xopenalex-snapshot
Apparent protein cloud point temperature determination using a low volume high-throughput cryogenic device in combination with automated imaging
inferred← citeshttps://doi.org/10.1007/s00723-020-01227-9openalex-snapshot
NMR Relaxation of Nuclei of Buffer as a Probe for Monitoring Protein Solutions Including Aggregation Processes
inferred← citeshttps://doi.org/10.1007/s10068-018-0361-xopenalex-snapshot
Effects of homogenization on the molecular flexibility and emulsifying properties of soy protein isolate
inferred← citeshttps://doi.org/10.1007/s10157-007-0487-2openalex-snapshot
Through the looking glass: the protein science of biosimilars
inferred← citeshttps://doi.org/10.1007/s10295-010-0766-xopenalex-snapshot
Enzyme replacement therapy for Morquio A: an active recombinant N-acetylgalactosamine-6-sulfate sulfatase produced in Escherichia coli BL21
inferred← citeshttps://doi.org/10.1007/s10529-010-0469-4openalex-snapshot
Effects of shear on proteins in solution
inferred← citeshttps://doi.org/10.1007/s10600-014-1057-yopenalex-snapshot
Domain Organization of Lectin from the Mussel Crenomytilus grayanus
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/s10847-019-00947-1openalex-snapshot
Effect of macrocyclic compounds to protein aggregation
inferred← citeshttps://doi.org/10.1007/s10895-013-1162-5openalex-snapshot
Consequential secondary structure alterations and aggregation during prolonged casein glycation
inferred← citeshttps://doi.org/10.1007/s10930-019-09837-4openalex-snapshot
Investigation on Secondary Structure Alterations of Protein Drugs as an Indicator of Their Biological Activity Upon Thermal Exposure
inferred← citeshttps://doi.org/10.1007/s10930-025-10302-8openalex-snapshot
Strategic Approaches for Overcoming Peptide and Protein Drug Limitations
inferred← citeshttps://doi.org/10.1007/s10989-023-10492-8openalex-snapshot
A Review on Forced Degradation Strategies to Establish the Stability of Therapeutic Peptide Formulations
inferred← citeshttps://doi.org/10.1007/s11095-007-9516-9openalex-snapshot
Extrinsic Fluorescent Dyes as Tools for Protein Characterization
inferred← citeshttps://doi.org/10.1007/s11095-009-0045-6openalex-snapshot
Stability of Protein Pharmaceuticals: An Update
inferred← citeshttps://doi.org/10.1007/s11095-009-9963-6openalex-snapshot
Carboxylate-Dependent Gelation of a Monoclonal Antibody
inferred← citeshttps://doi.org/10.1007/s11095-010-0073-2openalex-snapshot
Critical Evaluation of Nanoparticle Tracking Analysis (NTA) by NanoSight for the Measurement of Nanoparticles and Protein Aggregates
inferred← citeshttps://doi.org/10.1007/s11095-010-0143-5openalex-snapshot
Potential Aggregation-Prone Regions in Complementarity-Determining Regions of Antibodies and Their Contribution Towards Antigen Recognition: A Computational Analysis
inferred← citeshttps://doi.org/10.1007/s11095-010-0224-5openalex-snapshot
Mass Spectrometric Analysis of Intact Human Monoclonal Antibody Aggregates Fractionated by Size-Exclusion Chromatography
inferred← citeshttps://doi.org/10.1007/s11095-011-0374-0openalex-snapshot
Fluorescence Single Particle Tracking for the Characterization of Submicron Protein Aggregates in Biological Fluids and Complex Formulations
inferred← citeshttps://doi.org/10.1007/s11095-011-0385-xopenalex-snapshot
The Degradation of Polysorbates 20 and 80 and its Potential Impact on the Stability of Biotherapeutics
inferred← citeshttps://doi.org/10.1007/s11095-011-0410-0openalex-snapshot
Establishing a Link Between Amino Acid Sequences and Self-Associating and Viscoelastic Behavior of Two Closely Related Monoclonal Antibodies
inferred← citeshttps://doi.org/10.1007/s11095-011-0416-7openalex-snapshot
Aggregation Stability of a Monoclonal Antibody During Downstream Processing
inferred← citeshttps://doi.org/10.1007/s11095-012-0732-6openalex-snapshot
Structure and Function of Purified Monoclonal Antibody Dimers Induced by Different Stress Conditions
inferred← citeshttps://doi.org/10.1007/s11095-012-0749-xopenalex-snapshot
Detection and Characterization of Subvisible Aggregates of Monoclonal IgG in Serum
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