The influence of charge distribution on self-association and viscosity behavior of monoclonal antibody solutions.
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Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Improving monoclonal antibody selection and engineering using measurements of colloidal protein interactionsPredictive approach for protein aggregation: Correlation of protein surface characteristics and conformational flexibility to protein aggregation propensity.Effects of localized interactions and surface properties on stability of protein-based therapeutics.Charge matters.Structure based descriptors for the estimation of colloidal interactions and protein aggregation propensitiesCytokinergic IgE Action in Mast Cell Activation.Selective targeting of the IL23 pathway: Generation and characterization of a novel high-affinity humanized anti-IL23A antibody.Silk-based stabilization of biomacromolecules.Do clustering monoclonal antibody solutions really have a concentration dependence of viscosity?Small-angle neutron scattering characterization of monoclonal antibody conformations and interactions at high concentrations.The limitations of an exclusively colloidal view of protein solution hydrodynamics and rheology.Lysine and arginine content of proteins: computational analysis suggests a new tool for solubility design.Accelerated formulation development of monoclonal antibodies (mAbs) and mAb-based modalities: review of methods and tools.Antibody-Drug Conjugates: Design, Formulation and Physicochemical Stability.Optimizing the Bioavailability of Subcutaneously Administered Biotherapeutics Through Mechanochemical Drivers.Assessment and significance of protein-protein interactions during development of protein biopharmaceuticals.High concentration biotherapeutic formulation and ultrafiltration: Part 1 pressure limits.Challenges in Determining Intrinsic Viscosity Under Low Ionic Strength Solution Conditions.Investigating the Role of Artemin Glycosylation.Intermolecular Interactions and the Viscosity of Highly Concentrated Monoclonal Antibody Solutions.A strategy for risk mitigation of antibodies with fast clearance.Early developability screen of therapeutic antibody candidates using Taylor dispersion analysis and UV area imaging detection.Mitigation of reversible self-association and viscosity in a human IgG1 monoclonal antibody by rational, structure-guided Fv engineeringComputational tool for the early screening of monoclonal antibodies for their viscositiesCharge-mediated Fab-Fc interactions in an IgG1 antibody induce reversible self-association, cluster formation, and elevated viscosity.Conjugation site heterogeneity causes variable electrostatic properties in Fc conjugates.Physical stability comparisons of IgG1-Fc variants: effects of N-glycosylation site occupancy and Asp/Gln residues at site Asn 297.Hydrogen exchange mass spectrometry reveals protein interfaces and distant dynamic coupling effects during the reversible self-association of an IgG1 monoclonal antibody.Rational design of viscosity reducing mutants of a monoclonal antibody: hydrophobic versus electrostatic inter-molecular interactions.Intermediate range order and structure in colloidal dispersions with competing interactions.Effects of ionic strength and sugars on the aggregation propensity of monoclonal antibodies: influence of colloidal and conformational stabilities.Both protein adsorption and aggregation contribute to shear yielding and viscosity increase in protein solutions.Prediction of delayed retention of antibodies in hydrophobic interaction chromatography from sequence using machine learning.Effect of Aggregation on the Hydrodynamic Properties of Bovine Serum Albumin.Multi-step conformational transitions in heat-treated protein therapeutics can be monitored in real time with temperature-controlled electrospray ionization mass spectrometry.Viscosity Control of Protein Solution by Small Solutes: A Review.Viscosity Analysis of Dual Variable Domain Immunoglobulin Protein Solutions: Role of Size, Electroviscous Effect and Protein-Protein Interactions.Charge Shielding Prevents Aggregation of Supercharged GFP Variants at High Protein Concentration.Intermolecular interactions involving an acidic patch on immunoglobulin variable domain and the γ2 constant region mediate crystalline inclusion body formation in the endoplasmic reticulum.
P2860
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P2860
The influence of charge distribution on self-association and viscosity behavior of monoclonal antibody solutions.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh-hant
name
The influence of charge distri ...... monoclonal antibody solutions.
@en
The influence of charge distri ...... monoclonal antibody solutions.
@nl
type
label
The influence of charge distri ...... monoclonal antibody solutions.
@en
The influence of charge distri ...... monoclonal antibody solutions.
@nl
prefLabel
The influence of charge distri ...... monoclonal antibody solutions.
@en
The influence of charge distri ...... monoclonal antibody solutions.
@nl
P2093
P356
P1476
The influence of charge distri ...... monoclonal antibody solutions.
@en
P2093
Devendra S Kalonia
Sandeep Yadav
Shubhadra N Singh
Steven J Shire
Thomas M Laue
P304
P356
10.1021/MP200566K
P407
P577
2012-03-19T00:00:00Z