| review article | Q7318358 |
| scholarly article | Q13442814 |
| P356 | DOI | 10.2174/1389203719666171213114919 |
| P8608 | Fatcat ID | release_7cdnjotqbja7tdckjijbno2r2q |
| P932 | PMC publication ID | 6182935 |
| P698 | PubMed publication ID | 29237380 |
| P2093 | author name string | Kentaro Shiraki | |
| Taehun Hong | |||
| Kazuki Iwashita | |||
| P2860 | cites work | Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences | Q24644640 |
| High-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: implication of suppression of protein aggregation by arginine | Q27665935 | ||
| Some factors in the interpretation of protein denaturation | Q28202994 | ||
| The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media | Q28209077 | ||
| Effect of ions on the structure of water: structure making and breaking | Q28236044 | ||
| Interactions between macromolecules and ions: The Hofmeister series | Q28268014 | ||
| Effect of additives on protein aggregation. | Q30377982 | ||
| Stability of protein structure and hydrophobic interaction. | Q30403599 | ||
| Stabilization of protein structure by sugars | Q30415582 | ||
| Ultrasonic storage modulus as a novel parameter for analyzing protein-protein interactions in high protein concentration solutions: correlation with static and dynamic light scattering measurements | Q30499156 | ||
| Why water reorientation slows without iceberg formation around hydrophobic solutes. | Q33405581 | ||
| The hydration structure of guanidinium and thiocyanate ions: implications for protein stability in aqueous solution | Q33716764 | ||
| Do we underestimate the importance of water in cell biology? | Q33999254 | ||
| Protein interactions in solution characterized by light and neutron scattering: comparison of lysozyme and chymotrypsinogen | Q34169496 | ||
| Calculation of weak protein-protein interactions: the pH dependence of the second virial coefficient | Q34174894 | ||
| Interfaces and the driving force of hydrophobic assembly | Q34455286 | ||
| Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli | Q34626779 | ||
| Critical examination of the colloidal particle model of globular proteins | Q35050644 | ||
| Hydrophobic salts markedly diminish viscosity of concentrated protein solutions | Q83234340 | ||
| Concentrated dispersions of equilibrium protein nanoclusters that reversibly dissociate into active monomers | Q83283515 | ||
| Arginine increases the solubility of alkyl gallates through interaction with the aromatic ring | Q83324940 | ||
| Effect of sugar molecules on the viscosity of high concentration monoclonal antibody solutions | Q84107141 | ||
| Specific interactions in high concentration antibody solutions resulting in high viscosity | Q84461630 | ||
| Long- and short-range electrostatic interactions affect the rheology of highly concentrated antibody solutions | Q84609560 | ||
| Behavior of monoclonal antibodies: relation between the second virial coefficient (B (2)) at low concentrations and aggregation propensity and viscosity at high concentrations | Q84792220 | ||
| Viscosity of aqueous solutions and local microscopic structure | Q84805565 | ||
| Can salting-in/salting-out ions be classified as chaotropes/kosmotropes? | Q85053078 | ||
| Stress Tolerance of Antibody-Poly(Amino Acid) Complexes for Improving the Stability of High Concentration Antibody Formulations | Q85280491 | ||
| Feasibility of antibody-poly(glutamic acid) complexes: preparation of high-concentration antibody formulations and their pharmaceutical properties | Q86990411 | ||
| Protein-poly(amino acid) precipitation stabilizes a therapeutic protein l-asparaginase against physicochemical stress | Q87317889 | ||
| Charge state of arginine as an additive on heat-induced protein aggregation | Q87480491 | ||
| Specific decrease in solution viscosity of antibodies by arginine for therapeutic formulations | Q87579491 | ||
| Protein-poly(amino acid) complex precipitation for high-concentration protein formulation | Q88084676 | ||
| Effect of counter ions of arginine as an additive for the solubilization of protein and aromatic compounds | Q89302559 | ||
| Specific ion effects on macromolecular interactions in Escherichia coli extracts. | Q35158356 | ||
| Overcoming the challenges in administering biopharmaceuticals: formulation and delivery strategies | Q35684362 | ||
| Influence of macromolecular crowding upon the stability and state of association of proteins: predictions and observations | Q36178505 | ||
| Viscosity B-coefficients and standard partial molar volumes of amino acids, and their roles in interpreting the protein (enzyme) stabilization | Q36475636 | ||
| The multiple roles of histidine in protein interactions | Q36689701 | ||
| Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects | Q36719963 | ||
| Dynamics of hemoglobin in human erythrocytes and in solution: influence of viscosity studied by ultrafast vibrational echo experiments | Q36794135 | ||
| Investigation of cosolute-protein preferential interaction coefficients: new insight into the mechanism by which arginine inhibits aggregation | Q37190044 | ||
| The limitations of an exclusively colloidal view of protein solution hydrodynamics and rheology. | Q37338052 | ||
| Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature. | Q37345689 | ||
| Temperature dependence of the hydrophobic interaction in protein folding | Q37404841 | ||
| Chemistry of Hofmeister anions and osmolytes | Q37670141 | ||
| Protein aggregation--pathways and influencing factors | Q37699481 | ||
| Stability of IgG isotypes in serum | Q37734089 | ||
| Viscosity of concentrated therapeutic protein compositions | Q37947747 | ||
| Protein misfolding and aggregation research: some thoughts on improving quality and utility | Q38152435 | ||
| Multi-faceted arginine: mechanism of the effects of arginine on protein | Q38189882 | ||
| Structure-based analysis reveals hydration changes induced by arginine hydrochloride. | Q38288064 | ||
| Wrap-and-Strip Technology of Protein-Polyelectrolyte Complex for Biomedical Application. | Q38657105 | ||
| Coarse-Grained Antibody Models for "Weak" Protein-Protein Interactions from Low to High Concentrations | Q38851763 | ||
| Aggregative protein-polyelectrolyte complex for high-concentration formulation of protein drugs. | Q38861679 | ||
| Hard quasispherical model for the viscosity of hemoglobin solutions | Q39163501 | ||
| Structure-activity relationship for hydrophobic salts as viscosity-lowering excipients for concentrated solutions of monoclonal antibodies | Q39332318 | ||
| Kinetics of Monoclonal Antibody Aggregation from Dilute toward Concentrated Conditions. | Q39894470 | ||
| Macromolecular crowding: biochemical, biophysical, and physiological consequences | Q40488946 | ||
| Viscosity-Lowering Effect of Amino Acids and Salts on Highly Concentrated Solutions of Two IgG1 Monoclonal Antibodies | Q40925407 | ||
| Intermolecular Interactions and the Viscosity of Highly Concentrated Monoclonal Antibody Solutions | Q41127186 | ||
| Weak interactions govern the viscosity of concentrated antibody solutions: high-throughput analysis using the diffusion interaction parameter | Q42154434 | ||
| Arginine-assisted solubilization system for drug substances: solubility experiment and simulation | Q42868604 | ||
| Interaction of arginine with proteins and the mechanism by which it inhibits aggregation | Q42868627 | ||
| The effect of arginine glutamate on the stability of monoclonal antibodies in solution. | Q42875108 | ||
| Solubilization of aromatic and hydrophobic moieties by arginine in aqueous solutions | Q42938322 | ||
| Biophysical effect of amino acids on the prevention of protein aggregation | Q44163713 | ||
| Effect of Hierarchical Cluster Formation on the Viscosity of Concentrated Monoclonal Antibody Formulations Studied by Neutron Scattering | Q44272015 | ||
| The influence of charge distribution on self-association and viscosity behavior of monoclonal antibody solutions | Q44321777 | ||
| Arginine and lysine reduce the high viscosity of serum albumin solutions for pharmaceutical injection | Q44526735 | ||
| Establishing a link between amino acid sequences and self-associating and viscoelastic behavior of two closely related monoclonal antibodies | Q44528218 | ||
| Cluster-driven dynamical arrest in concentrated lysozyme solutions | Q44611254 | ||
| Influence of histidine on the stability and physical properties of a fully human antibody in aqueous and solid forms | Q44729469 | ||
| Preferential interaction coefficients of proteins in aqueous arginine solutions and their molecular origins | Q44994322 | ||
| The structure of aqueous guanidinium chloride solutions. | Q45058542 | ||
| Hydrophobicity: two faces of water. | Q46010891 | ||
| Reversible self-association of a concentrated monoclonal antibody solution mediated by Fab-Fab interaction that impacts solution viscosity | Q46054883 | ||
| Intermolecular Interactions of IgG1 Monoclonal Antibodies at High Concentrations Characterized by Light Scattering | Q46058466 | ||
| Monoclonal antibody self-association, cluster formation, and rheology at high concentrations | Q46119775 | ||
| Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution | Q46141707 | ||
| Shear rheology of hard-sphere, dispersed, and aggregated suspensions, and filler-matrix composites. | Q46225712 | ||
| Role of Cosolute-Protein Interactions in the Dissociation of Monoclonal Antibody Clusters | Q46378472 | ||
| Arginine increases the solubility of coumarin: comparison with salting-in and salting-out additives | Q46516343 | ||
| Rheological and syringeability properties of highly concentrated human polyclonal immunoglobulin solutions | Q46839916 | ||
| Quantitative Correlation between Viscosity of Concentrated MAb Solutions and Particle Size Parameters Obtained from Small-Angle X-ray Scattering | Q47380764 | ||
| Kinetics of Antibody Aggregation at Neutral pH and Ambient Temperatures Triggered by Temporal Exposure to Acid. | Q50594551 | ||
| Hofmeister Effects in Monoclonal Antibody Solution Interactions. | Q50877696 | ||
| Influence of Arginine Salts on the Thermal Stability and Aggregation Kinetics of Monoclonal Antibody: Dominant Role of Anions. | Q51192570 | ||
| Short-Time Glassy Dynamics in Viscous Protein Solutions with Competing Interactions. | Q51613476 | ||
| Factors affecting the viscosity in high concentration solutions of different monoclonal antibodies. | Q51663592 | ||
| Preferential interactions of proteins with salts in concentrated solutions. | Q52712617 | ||
| Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin. | Q52894666 | ||
| Impact of aggregate formation on the viscosity of protein solutions. | Q53472781 | ||
| The role of electrostatics in protein-protein interactions of a monoclonal antibody. | Q53535082 | ||
| Thermodynamic and fluorescence analyses to determine mechanisms of IgG1 stabilization and destabilization by arginine. | Q53663332 | ||
| Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli | Q54701477 | ||
| Dipole-dipole interaction in antibody solutions: correlation with viscosity behavior at high concentration | Q57124127 | ||
| Water structure and chaotropicity: their uses, abuses and biological implications | Q57203260 | ||
| Specific Ion and Buffer Effects on Protein–Protein Interactions of a Monoclonal Antibody | Q57362747 | ||
| Distinguishing the monomer to cluster phase transition in concentrated lysozyme solutions by studying the temperature dependence of the short-time dynamics | Q58046834 | ||
| Lysozyme Protein Solution with an Intermediate Range Order Structure | Q58046880 | ||
| Equilibrium cluster formation in concentrated protein solutions and colloids | Q59063283 | ||
| Equilibrium Cluster Phases and Low-Density Arrested Disordered States: The Role of Short-Range Attraction and Long-Range Repulsion | Q60179413 | ||
| Ground-State Clusters for Short-Range Attractive and Long-Range Repulsive Potentials | Q60179417 | ||
| The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale | Q71785195 | ||
| A comparative study on viscosity of human, bovine and pig IgG immunoglobulins in aqueous solutions | Q73074069 | ||
| Negligible effect of ions on the hydrogen-bond structure in liquid water | Q73687415 | ||
| Energy of interaction in colloids and its implications in rheological modeling | Q74290652 | ||
| Urea effects on protein stability: hydrogen bonding and the hydrophobic effect | Q74566093 | ||
| Aggregation and dispersion of small hydrophobic particles in aqueous electrolyte solutions | Q79339181 | ||
| Ions from the Hofmeister series and osmolytes: effects on proteins in solution and in the crystallization process | Q80484302 | ||
| Dynamical arrest in attractive colloids: the effect of long-range repulsion | Q81031260 | ||
| Observation of immobilized water molecules around hydrophobic groups | Q81427452 | ||
| P433 | issue | 8 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | molecular biology | Q7202 |
| P304 | page(s) | 746-758 | |
| P577 | publication date | 2017-12-12 | |
| P1433 | published in | Current Protein and Peptide Science | Q15745198 |
| P1476 | title | Viscosity Control of Protein Solution by Small Solutes: A Review | |
| P478 | volume | 19 |
| Q92720018 | Characterization of Excipient Effects on Reversible Self-Association, Backbone Flexibility, and Solution Properties of an IgG1 Monoclonal Antibody at High Concentrations: Part 2 |
| Q92456656 | Making Concentrated Antibody Formulations Accessible for Vibrating-Mesh Nebulization |
| Q99604129 | Resolving Liquid-Liquid Phase Separation for a Peptide Fused Monoclonal Antibody by Formulation Optimization |
| Q90448065 | Structure, heterogeneity and developability assessment of therapeutic antibodies |
| Q101155834 | Toward Biotherapeutics Formulation Composition Engineering using Site-Identification by Ligand Competitive Saturation (SILCS) |
Search more.