Abstract
Sora Hirano, Tatsuya Oshima, Asuka Inada, Takuya Uto, Toshihiro Tsuruda
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10.1002/bip.360250307 · doi-reference
Characterization of amyloidogenesis of hen egg lysozyme in concentrated ethanol solution
10.1016/j.bbrc.2008.06.018 · doi-reference
Hydration in deep eutectic solvents induces non-monotonic changes in the conformation and stability of proteins
10.1021/jacs.2c11190 · doi-reference
Characterization of expression, activity and role in antibacterial immunity of Anopheles gambiae lysozyme c-1
10.1016/j.cbpb.2009.11.012 · doi-reference
Turbidimetric determination of lysozyme with Micrococcus lysodeikticus cells: reexamination of reaction conditions
10.1016/0003-2697(83)90347-0 · doi-reference
A highly amyloidogenic region of hen lysozyme
10.1016/j.jmb.2004.05.056 · doi-reference
Thermal stability and refolding of hen egg-white lysozyme in aqueous deep eutectic solvent solutions
10.1016/j.molliq.2023.122939 · doi-reference
Thermal unfolding and refolding of lysozyme in deep eutectic solvents and their aqueous dilutions
10.1039/c3cp44299c · doi-reference
Refolding SDS-mediated partially-unfolded proteins: a distinguishing role of tetraalkylammonium ionic liquids via mixed micellar aggregation
10.1016/j.jphotochem.2024.115661 · doi-reference
Dynamics of ionic liquid-assisted refolding of denatured cytochrome c: a study of preferential interactions toward renaturation
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Tailoring properties of natural deep eutectic solvents with water to facilitate their applications
10.1016/j.foodchem.2015.03.123 · doi-reference
Natural deep eutectic solvents (NADES) in drug delivery systems: characteristics, applications, and future perspectives
10.1016/j.ijpharm.2025.125509 · doi-reference
Deep eutectic solvents—the vital link between ionic liquids and ionic solutions
10.1063/5.0072268 · doi-reference
Basics and properties of deep eutectic solvents: a review
10.1007/s10311-021-01225-8 · doi-reference
Confronting high-throughput protein refolding using high pressure and solution screens
10.1016/j.pep.2007.05.014 · doi-reference
In vitro protein refolding by chromatographic procedures
10.1016/j.pep.2003.08.023 · doi-reference
Important parameters affecting efficiency of protein refolding by reversed micelles
10.1021/bp000073m · doi-reference
Solubilization and refolding of inclusion body proteins in reverse micelles
10.1016/s0003-2697(03)00384-1 · doi-reference
Protein refolding assisted by self-assembled nanogels as novel artificial molecular chaperone
10.1016/s0014-5793(03)01028-7 · doi-reference
Heterologous expression and characterization of CYP61A1 from dandruff-causing Malassezia globosa
10.1016/j.pep.2015.07.002 · doi-reference
Artificial chaperones: protein refolding via sequential use of detergent and cyclodextrin
10.1021/ja00113a036 · doi-reference
The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation
10.1016/s0006-291x(03)00578-3 · doi-reference
Role of arginine in protein refolding, solubilization, and purification
10.1021/bp0498793 · doi-reference
Practical considerations in refolding proteins from inclusion bodies
10.1016/s1046-5928(02)00641-1 · doi-reference
Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process
10.1186/s12934-015-0222-8 · doi-reference
Protein refolding for industrial processes
10.1016/s0958-1669(00)00200-7 · doi-reference
Recombinant protein expression in Escherichia coli: advances and challenges
10.3389/fmicb.2014.00172 · doi-reference
Recombinant protein folding and misfolding in Escherichia coli
10.1038/nbt1029 · doi-reference
Current state and recent advances in biopharmaceutical production in Escherichia coli, yeasts and mammalian cells
10.1007/s10295-013-1235-0 · doi-reference
Production of biopharmaceuticals in E. Coli: current scenario and future perspectives
10.4014/jmb.1412.12079 · doi-reference