Weak interactions govern the viscosity of concentrated antibody solutions: high-throughput analysis using the diffusion interaction parameter - Wikidata - awgldk - TriplyDB

Weak interactions govern the viscosity of concentrated antibody solutions: high-throughput analysis using the diffusion interaction parameter

Weak interactions govern the viscosity of concentrated antibody solutions: high-throughput analysis using the diffusion interaction parameter

http://www.wikidata.org/entity/Q42154434

about

Early implementation of QbD in biopharmaceutical development: a practical example Improving monoclonal antibody selection and engineering using measurements of colloidal protein interactions Protein aggregation and its impact on product quality Advances in Antibody Design Role of anisotropic interactions for proteins and patchy nanoparticles.Structure based descriptors for the estimation of colloidal interactions and protein aggregation propensities In silico selection of therapeutic antibodies for development: viscosity, clearance, and chemical stability.Critical examination of the colloidal particle model of globular proteins The limitations of an exclusively colloidal view of protein solution hydrodynamics and rheology.Accelerated formulation development of monoclonal antibodies (mAbs) and mAb-based modalities: review of methods and tools.Preferential interactions of trehalose, L-arginine.HCl and sodium chloride with therapeutically relevant IgG1 monoclonal antibodies.Molecular basis of high viscosity in concentrated antibody solutions: Strategies for high concentration drug product development High-throughput screening for developability during early-stage antibody discovery using self-interaction nanoparticle spectroscopy.In-silico prediction of concentration-dependent viscosity curves for monoclonal antibody solutions.Assessment and significance of protein-protein interactions during development of protein biopharmaceuticals.A novel screening method to assess developability of antibody-like molecules.High concentration biotherapeutic formulation and ultrafiltration: Part 1 pressure limits.Monoclonal antibodies: formulations of marketed products and recent advances in novel delivery system.Influence of structure properties on protein-protein interactions-QSAR modeling of changes in diffusion coefficients.Colloidal Stability & Conformational Changes in β-Lactoglobulin: Unfolding to Self-Assembly Intermolecular Interactions and the Viscosity of Highly Concentrated Monoclonal Antibody Solutions.Early developability screen of therapeutic antibody candidates using Taylor dispersion analysis and UV area imaging detection.An alternative assay to hydrophobic interaction chromatography for high-throughput characterization of monoclonal antibodies.High throughput detection of antibody self-interaction by bio-layer interferometry.Characterization of highly concentrated antibody solution - A toolbox for the description of protein long-term solution stability Charge-mediated Fab-Fc interactions in an IgG1 antibody induce reversible self-association, cluster formation, and elevated viscosity.Hydrogen exchange mass spectrometry reveals protein interfaces and distant dynamic coupling effects during the reversible self-association of an IgG1 monoclonal antibody.Challenges in Predicting Protein-Protein Interactions from Measurements of Molecular Diffusivity Rational design of viscosity reducing mutants of a monoclonal antibody: hydrophobic versus electrostatic inter-molecular interactions.Both protein adsorption and aggregation contribute to shear yielding and viscosity increase in protein solutions.Intrinsically disordered sequences enable modulation of protein phase separation through distributed tyrosine motifs.Predicting protein-protein interactions of concentrated antibody solutions using dilute solution data and coarse-grained molecular models.Viscosity Control of Protein Solution by Small Solutes: A Review.Characterizing protein-protein-interaction in high-concentration monoclonal antibody systems with the quartz crystal microbalance.Viscosity Analysis of Dual Variable Domain Immunoglobulin Protein Solutions: Role of Size, Electroviscous Effect and Protein-Protein Interactions.Quantitative Correlation between Viscosity of Concentrated MAb Solutions and Particle Size Parameters Obtained from Small-Angle X-ray Scattering.Protein-protein interactions controlling interfacial aggregation of rhIL-1ra are not described by simple colloid models.Charge Shielding Prevents Aggregation of Supercharged GFP Variants at High Protein Concentration.Concentration dependent viscosity of monoclonal antibody solutions: explaining experimental behavior in terms of molecular properties.MAbDelivery: Administration routes for antibody therapy Third LabEx MAbImprove industrial workshop, July 2, 2015 Tours, France.

P2860

Q26830466-A5F160DA-684E-4D05-AD50-BB3EF46B8744 Q27002558-D21F509E-B214-4FF7-9898-24245DD2F078 Q27010661-EB487F51-83AC-4C0D-A8FF-52154E52C725 Q28817608-D17FDFE0-D7AD-4D1B-8F48-5AFDC476CAE9 Q34481834-FDAC3AE9-CE15-425C-B1DD-37B6027E8619 Q34658019-641F3866-ED47-41DA-A80F-9466855A9262 Q34831383-F6D20527-4153-4C1E-BDE3-0D964B8F340A Q35050644-A51AF437-74CB-4B24-8092-3EC7F18B5B56 Q37338052-221C5120-11F1-4576-8D62-949771574EAF Q38313350-3D454425-EC17-47E8-A210-371C7289D8AF Q38652096-31A9B914-5C1C-485D-A068-0A844BE3A99C Q38688235-AE3D004F-2DA7-49D9-BDE0-CF7CCD04B632 Q38718094-C385B844-BDC7-4BD9-AC62-51FD9EA02421 Q38765564-65598A7B-7D30-4F60-9D64-56F685C888A5 Q38783040-610D63CF-CF8A-418D-AA18-35BA94D2FE8E Q38876656-35AB9C59-D26B-4F4B-95B9-95D9AFACCC39 Q38906930-E3982378-C133-421C-ABC8-059A74F3947B Q39066090-7098C82E-ED75-4D77-8599-80042DB10CE5 Q39228104-41A0B3B5-B908-4C73-BF77-5954DC3CA8E6 Q40654144-775D00F9-49BF-4B02-AD9F-416C4D95A0CF Q41127186-260B4BB1-BA68-4A8B-A5E7-E4785E1F2BED Q41596017-9FC7D277-F622-4A25-8BFD-89D145D768C4 Q41845586-E6043C85-A237-4A4A-B496-5F3DDF4832F2 Q41880645-5F6D2EB3-06EE-4CC6-8ADB-D6CCDC56C022 Q42111378-029179C3-C2DA-4068-BD79-7F8016888724 Q42129206-30BEB11D-E8FE-42B3-AAF8-D00F9C86FB7E Q42601309-021463DB-E289-405A-A581-51AC91162A56 Q42693191-9EA36589-CA08-4477-8F9A-36C43B2CC2BF Q43199562-C01B7A77-66C0-4566-8C51-8AA50504EF5B Q44796408-B2C82B31-F65B-406E-8399-A7E9DE0FD735 Q47137715-4532434C-D36F-4DDD-84DF-7BBF3BDF9CA5 Q47221856-6B25F222-0699-4C0D-B881-3CE52091C599 Q47297020-EA29F918-CFF2-48D9-B3FA-44230A984436 Q47336739-DA8F4B3C-717B-41D2-8E75-671A26A9E2EA Q47367882-5728E40B-FA61-4604-89CF-27427905FD91 Q47380764-EBBD2EC0-463B-4E87-80B2-8457896AAD7C Q47693273-E8B9E322-4C89-459F-84C6-B4C95D9B0F9A Q47718842-351649C7-4026-4C67-8E5A-B2D9B6F1A7EE Q51080917-D2917BA8-7EA3-4C38-875C-6F10EB80FBC6 Q51084133-EB11CD6F-012A-4ADC-A1B0-D7183BF5CDD0

P2860

Weak interactions govern the viscosity of concentrated antibody solutions: high-throughput analysis using the diffusion interaction parameter

http://www.wikidata.org/entity/Q42154434

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-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

2012年學術文章

@zh-hant

name

Weak interactions govern the v ...... iffusion interaction parameter

@en

Weak interactions govern the v ...... iffusion interaction parameter

@nl

type

label

Weak interactions govern the v ...... iffusion interaction parameter

@en

Weak interactions govern the v ...... iffusion interaction parameter

@nl

prefLabel

Weak interactions govern the v ...... iffusion interaction parameter

@en

Weak interactions govern the v ...... iffusion interaction parameter

@nl

P1433

Q42154434-EE68E574-1420-4287-A576-F733CF2EC8D8

P1476

Q42154434-E95BA2AB-A5BF-4B29-B214-585B7A030596

P2093

Q42154434-22DAC0E4-EA65-492A-9310-B7A0BD5DFC7F

Q42154434-420A12ED-5E01-4168-8531-0BADA0EA89A1

Q42154434-59A8B0F0-80B9-4A5C-9BF8-2CA1EF996F6D

Q42154434-78D90C5B-C69B-4144-BEE2-C10361BA2C64

Q42154434-8ECF3481-33C4-40C8-B13B-976C6E9B1417

Q42154434-A4FC4B4D-9201-4AD0-A428-125114F63B53

Q42154434-BEF86C9E-69D1-4645-871F-ED89D393B8B9

Q42154434-FB9F5885-1FE5-4DF8-A776-4727D313D0C6

P2860

Q42154434-0CD78619-3DCD-45C0-8A52-679773AD0ED9

Q42154434-1B9ED7C9-3C86-4BE2-9B74-4BA28823FF7B

Q42154434-23C4D9D7-DCC7-4B14-800F-D824726BB317

Q42154434-3DD32900-B760-400E-A855-A98BB29E7BCC

Q42154434-3EA9B0E9-126B-4C53-8515-D1992757E775

Q42154434-425EB69B-65FF-4A66-8F23-CEBA3E976080

Q42154434-45350F22-449C-40D5-8F38-7924F2E6A363

Q42154434-52A15554-A998-48F8-BED2-4A0E800E0335

Q42154434-6A9A574B-9E9B-4F80-9968-09BEEC1DEFF7

Q42154434-83C975A9-6C5A-4FB8-A630-9425EDF7BF50

P304

Q42154434-F678C25E-5E44-4EA7-9944-479680FFBBE7

P31

Q42154434-3215B1A1-2C65-487C-9472-B550392E4216

P356

Q42154434-A4D81B39-59A3-4CB1-AC87-FEC4F9096253

P407

Q42154434-76A74BBD-326F-4262-BD47-CF22B987F7E9

P433

Q42154434-8C8DA916-E87D-4350-A6DD-D5FD9BC735DB

P478

Q42154434-28E64F22-B3F6-43D4-892D-7A4C5D3F0491

P577

Q42154434-07322C6C-43BB-46BA-A3B0-F95256B8473A

P5875

Q42154434-FEA09894-D556-4250-B30D-9426AECFEAA7

P698

Q42154434-F84F34B3-31DB-47FF-BC37-72193EA19372

P921

Q42154434-B8820C85-52EA-470E-B67A-3973FAEB2131

P932

Q42154434-D72FD1C0-75BE-4E4E-9E25-FD5A91A9D2BB

P356

J.BPJ.2012.04.047

P1433

Biophysical Journal

P1476

Weak interactions govern the v ...... iffusion interaction parameter

@en

P2093

Barthélemy Demeule

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

Brian D Connolly

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

Chris Petry

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

Jamie M R Moore

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

Natalie Ciaccio

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

Sandeep Yadav

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

Steven J Shire

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

Yatin R Gokarn

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

P2860

Free-solution, label-free protein-protein interactions characterized by dynamic light scattering

Protein misfolding, functional amyloid, and human disease

Protein aggregation and neurodegenerative disease

Molecular origins of osmotic second virial coefficients of proteins.

Determination of second virial coefficient of proteins using a dual-detector cell for simultaneous measurement of scattered light intensity and concentration in SEC-HPLC.

Rapid quantitative characterization of protein interactions by composition gradient static light scattering.

Aggregation of γ-crystallins associated with human cataracts via domain swapping at the C-terminal β-strands.

Determination of the net charge (valence) of a protein: a fundamental but elusive parameter.

Factors affecting pharmacokinetics of monoclonal antibodies: A review article.

Challenges in the development of high protein concentration formulations.

P304

69-78

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

P31

scholarly article

P356

10.1016/J.BPJ.2012.04.047

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

P407

P433

1

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

P478

103

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

P577

2012-07-01T00:00:00Z

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

P5875

230564662

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

P698

22828333

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

P921

P932

3388210

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