Investigation of cosolute-protein preferential interaction coefficients: new insight into the mechanism by which arginine inhibits aggregation.
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Quantifying the molecular origins of opposite solvent effects on protein-protein interactionsEffects of solute-solute interactions on protein stability studied using various counterions and dendrimersQuantitative characterization of local protein solvation to predict solvent effects on protein structure.Mobile phase modifier effects in multimodal cation exchange chromatography.Arginine and the Hofmeister Series: the role of ion-ion interactions in protein aggregation suppression.The effects of N-ethyl-N'-methyl imidazolium chloride on the solubility, stability and aggregation of tc-rPA.Recent trends in stabilising peptides and proteins in pharmaceutical formulation - considerations in the choice of excipients.Biopharmaceutical formulations for pre-filled delivery devices.Preferential interactions of trehalose, L-arginine.HCl and sodium chloride with therapeutically relevant IgG1 monoclonal antibodies.A change in the aggregation pathway of bovine serum albumin in the presence of arginine and its derivatives.The effects of arginine glutamate, a promising excipient for protein formulation, on cell viability: Comparisons with NaClPredictive tools for stabilization of therapeutic proteins.Solubilization of aromatic and hydrophobic moieties by arginine in aqueous solutions.Preventing Aggregation of Recombinant Interferon beta-1b in Solution by Additives: Approach to an Albumin-Free Formulation.Arginine controls heat-induced cluster-cluster aggregation of lysozyme at around the isoelectric point.Oligoethylene glycols prevent thermal aggregation of α-chymotrypsin in a temperature-dependent manner: implications for design guidelines.Interactions between L-arginine/L-arginine derivatives and lysozyme and implications to their inhibition effects on protein aggregation.Viscosity Control of Protein Solution by Small Solutes: A Review.Effect of guanidine and arginine on protein-ligand interactions in multimodal cation-exchange chromatography.Retracted: Molecular characterization of excipients' preferential interactions with therapeutic monoclonal antibodies.Probing of some compounds as anti-aggregatory additives in the protein refolding process from Escherichia coli inclusion bodies.
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P2860
Investigation of cosolute-protein preferential interaction coefficients: new insight into the mechanism by which arginine inhibits aggregation.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on February 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Investigation of cosolute-prot ...... arginine inhibits aggregation.
@en
Investigation of cosolute-prot ...... arginine inhibits aggregation.
@nl
type
label
Investigation of cosolute-prot ...... arginine inhibits aggregation.
@en
Investigation of cosolute-prot ...... arginine inhibits aggregation.
@nl
prefLabel
Investigation of cosolute-prot ...... arginine inhibits aggregation.
@en
Investigation of cosolute-prot ...... arginine inhibits aggregation.
@nl
P2860
P356
P1476
Investigation of cosolute-prot ...... arginine inhibits aggregation.
@en
P2093
Bernhardt L Trout
Curtiss P Schneider
P2860
P304
P356
10.1021/JP808042W
P407
P577
2009-02-01T00:00:00Z