Diffusion and sedimentation interaction parameters for measuring the second virial coefficient and their utility as predictors of protein aggregation.
about
Improving monoclonal antibody selection and engineering using measurements of colloidal protein interactionsOptimization of the Production Process and Characterization of the Yeast-Expressed SARS-CoV Recombinant Receptor-Binding Domain (RBD219-N1), a SARS Vaccine Candidate.High-throughput analysis of concentration-dependent antibody self-association.Protein-protein interactions in dilute to concentrated solutions: α-chymotrypsinogen in acidic conditions.Reexamining protein-protein and protein-solvent interactions from Kirkwood-Buff analysis of light scattering in multi-component solutions.A comparison of biophysical characterization techniques in predicting monoclonal antibody stability.A multiscale view of therapeutic protein aggregation: a colloid science perspective.Preferential interactions of trehalose, L-arginine.HCl and sodium chloride with therapeutically relevant IgG1 monoclonal antibodies.High-throughput screening for developability during early-stage antibody discovery using self-interaction nanoparticle spectroscopy.Colloidal Stability & Conformational Changes in β-Lactoglobulin: Unfolding to Self-AssemblyUse of dynamic light scattering and small-angle X-ray scattering to characterize new surfactants in solution conditions for membrane-protein crystallization.Control of protein particle formation during ultrafiltration/diafiltration through interfacial protection.Weak interactions govern the viscosity of concentrated antibody solutions: high-throughput analysis using the diffusion interaction parameterChallenges in Predicting Protein-Protein Interactions from Measurements of Molecular DiffusivityRational design of viscosity reducing mutants of a monoclonal antibody: hydrophobic versus electrostatic inter-molecular interactions.Effects of ionic strength and sugars on the aggregation propensity of monoclonal antibodies: influence of colloidal and conformational stabilities.Intrinsically disordered sequences enable modulation of protein phase separation through distributed tyrosine motifs.Characterizing protein-protein-interaction in high-concentration monoclonal antibody systems with the quartz crystal microbalance.Brownian dynamics simulations of analytical ultracentrifugation experiments exhibiting hydrodynamic and thermodynamic non-ideality.High Throughput Prediction Approach for Monoclonal Antibody Aggregation at High Concentration.Discovery of highly soluble antibodies prior to purification using affinity-capture self-interaction nanoparticle spectroscopy.Impact of aggregate formation on the viscosity of protein solutions.Molecular Modeling for Protein Aggregation and FormulationMechanisms of precipitate formation during the purification of an Fc-fusion proteinSecond Osmotic Virial Coefficients and Aggregation of Monoclonal Antibodies by Static Laser Light Scattering
P2860
Q27002558-ED8FF560-C8E2-4BA3-B371-8217B5F96875Q30401512-79EA7665-2C75-439D-8251-E8A2165BBA5EQ30462680-31DCCA06-2B4D-488B-B721-DA0250E280D5Q33732547-96D3CB16-C592-45C4-94EF-5F5EDF1C9EF8Q35097145-192C70B8-1946-4647-A3EA-94FA805DFC14Q37287010-78C5FF11-17FD-4E85-9096-5552BE57D404Q38378651-147D2A07-846B-460D-8682-793E93EF755FQ38652096-755FFB08-3D0A-474C-8312-E524122B35F7Q38718094-5CE306F2-6302-4ECD-8106-ADB92918E73EQ40654144-4ADE2587-8563-413D-99EE-FB434CB289A6Q41138882-31C78564-BF37-49E9-8229-24CE80D56B08Q42009419-B0B8344F-019D-4F88-937F-575029582920Q42154434-C1DFBF1F-CC13-4863-A776-7EC9ED6526BCQ42693191-24F668AD-A3C5-4039-BEB1-56C0DF22444FQ43199562-3ECF7768-4B21-4AC6-BB30-A475DCF751D8Q44588569-3D471308-23E2-4D33-9826-AC1901F345C2Q47137715-DC9AC7F7-B91E-4DA0-A5D8-5DDDCA56DE8FQ47336739-07110E9E-45C6-463F-A173-8771376D7D26Q47608726-6AA682EC-6703-4D67-B265-6A6F40C18258Q47811451-C7FA606C-777C-4C0C-BF74-223C7FE4D14FQ51722272-7BAF446D-B998-4803-8BFE-C005628459AEQ53472781-0F2DED66-CC9B-4E50-96AC-A034A66E15A8Q57341107-78AA9A38-9078-488F-B5D8-E71EC427EA84Q57451910-2552E061-8C5C-418B-963C-DB8144B3EFF1Q58373511-AAC1980E-4BA3-4940-89C5-D0550882B12A
P2860
Diffusion and sedimentation interaction parameters for measuring the second virial coefficient and their utility as predictors of protein aggregation.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Diffusion and sedimentation in ...... ictors of protein aggregation.
@en
type
label
Diffusion and sedimentation in ...... ictors of protein aggregation.
@en
prefLabel
Diffusion and sedimentation in ...... ictors of protein aggregation.
@en
P2093
P2860
P1433
P1476
Diffusion and sedimentation in ...... ictors of protein aggregation.
@en
P2093
Atul Saluja
David N Brems
R Matthew Fesinmeyer
Sabine Hogan
Yatin R Gokarn
P2860
P304
P356
10.1016/J.BPJ.2010.08.020
P407
P577
2010-10-01T00:00:00Z