Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations. - Wikidata - awgldk - TriplyDB

Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations.

Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations.

http://www.wikidata.org/entity/Q30333186

about

Characterizing Protein Structure, Dynamics and Conformation in Lyophilized Solids Role of protein stabilizers on the conformation of the unfolded state of cytochrome c and its early folding kinetics: investigation at single molecular resolution.Physiochemical and biochemical factors influencing the pharmacokinetics of antibody therapeutics Analytical detection and characterization of biopharmaceutical glycosylation by MS.Protein aggregation and bioprocessing.Aggregates in monoclonal antibody manufacturing processes.Immunogenicity of therapeutic proteins: influence of aggregation.Solid-state protein formulations.Large-scale crystallization of proteins for purification and formulation.Monoclonal antibodies: formulations of marketed products and recent advances in novel delivery system.Feasibility study of semi-selective protein precipitation with salt-tolerant copolymers for industrial purification of therapeutic antibodies.Characterization of the physical stability of a lyophilized IgG1 mAb after accelerated shipping-like stress.Predicting protein aggregation during storage in lyophilized solids using solid state amide hydrogen/deuterium exchange with mass spectrometric analysis (ssHDX-MS)Thiol-disulfide interchange in the tocinoic acid/glutathione system during freezing and drying.Visual Detection of Denatured Glutathione Peptides: A Facile Method to Visibly Detect Heat Stressed Biomolecules.Thiol-disulfide exchange in peptides derived from human growth hormone during lyophilization and storage in the solid state.Mid-infrared spectroscopy-based antibody aggregate quantification in cell culture fluids.Multi-step conformational transitions in heat-treated protein therapeutics can be monitored in real time with temperature-controlled electrospray ionization mass spectrometry.Recent mass spectrometry-based techniques and considerations for disulfide bond characterization in proteins.Combination of SDS-PAGE and intact mass analysis for rapid determination of heterogeneities in monoclonal antibody therapeutics.Fast and scalable purification of a therapeutic full-length antibody based on process crystallization.Determination of Atenolol in Pharmaceutical Preparations by Gas Chromatography with Flame Ionization and Mass Spectrometric Detection

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P2860

Mechanisms of aggregate formation and carbohydrate excipient stabilization of lyophilized humanized monoclonal antibody formulations.

http://www.wikidata.org/entity/Q30333186

description

2003 nî lūn-bûn

@nan

2003 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2003年の論文

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2003年論文

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2003年論文

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2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

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name

Mechanisms of aggregate format ...... oclonal antibody formulations.

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Mechanisms of aggregate format ...... oclonal antibody formulations.

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type

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Mechanisms of aggregate format ...... oclonal antibody formulations.

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Mechanisms of aggregate format ...... oclonal antibody formulations.

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Mechanisms of aggregate format ...... oclonal antibody formulations.

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Mechanisms of aggregate format ...... oclonal antibody formulations.

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Mechanisms of aggregate format ...... oclonal antibody formulations.

@en

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Chung C Hsu

http://www.w3.org/2001/XMLSchema#string

James D Andya

http://www.w3.org/2001/XMLSchema#string

Steven J Shire

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P2860

Humanization of an anti-p185HER2 antibody for human cancer therapy

Humanization of an antibody directed against IgE

Dominant forces in protein folding

Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation.

A specific molar ratio of stabilizer to protein is required for storage stability of a lyophilized monoclonal antibody.

Stability of protein pharmaceuticals.

Ellman's reagent: 5,5'-dithiobis(2-nitrobenzoic acid)--a reexamination.

New insight into protein secondary structure from resolution-enhanced infrared spectra.

Solid-phase aggregation of proteins under pharmaceutically relevant conditions.

Rational design of stable lyophilized protein formulations: some practical advice.

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E10

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scholarly article

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10.1208/PS050210

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2

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12866937

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