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(28)
, 29953-29965. https://doi.org/10.1021/acsomega.4c03344
- I-Te Chu, Brent O. Hutcheson, Hudson R. Malsch, Gary J. Pielak. Macromolecular Crowding by Polyethylene Glycol Reduces Protein Breathing. The Journal of Physical Chemistry Letters 2023, 14
(10)
, 2599-2605. https://doi.org/10.1021/acs.jpclett.3c00271
- Shivkumar Sharma Irukuvajjula, Jithender G. Reddy, Ramakrishna Vadrevu. Crowding by Poly(ethylene glycol) Destabilizes Chemotaxis Protein Y (CheY). Biochemistry 2022, 61
(14)
, 1431-1443. https://doi.org/10.1021/acs.biochem.2c00030
- Xue Wang, Nataraja S. Yadavalli, Amine M. Laradji, Sergiy Minko. Grafting through Method for Implanting of Lysozyme Enzyme in Molecular Brush for Improved Biocatalytic Activity and Thermal Stability. Macromolecules 2018, 51
(14)
, 5039-5047. https://doi.org/10.1021/acs.macromol.8b00991
- Chandan
Kumar Choudhury, Sidong Tu, Igor Luzinov, Sergiy Minko, Olga Kuksenok. Designing Highly Thermostable Lysozyme–Copolymer Conjugates: Focus on Effect of Polymer Concentration. Biomacromolecules 2018, 19
(4)
, 1175-1188. https://doi.org/10.1021/acs.biomac.8b00027
- Nataraja S. Yadavalli, Nikolay Borodinov, Chandan K. Choudhury, Tatiana Quiñones-Ruiz, Amine M. Laradji, Sidong Tu, Igor K. Lednev, Olga Kuksenok, Igor Luzinov, and Sergiy Minko . Thermal Stabilization of Enzymes with Molecular Brushes. ACS Catalysis 2017, 7
(12)
, 8675-8684. https://doi.org/10.1021/acscatal.7b03138
- Isabella Panovic, James R. D. Montgomery, Christopher S. Lancefield, Dhivya Puri, Tomas Lebl, and Nicholas J. Westwood . Grafting of Technical Lignins through Regioselective Triazole Formation on β-O-4 Linkages. ACS Sustainable Chemistry & Engineering 2017, 5
(11)
, 10640-10648. https://doi.org/10.1021/acssuschemeng.7b02575
- Hang Kuen Lau, Linqing Li, Anna K. Jurusik, Chandran R. Sabanayagam, and Kristi L. Kiick . Aqueous Liquid–Liquid Phase Separation of Resilin-Like Polypeptide/Polyethylene Glycol Solutions for the Formation of Microstructured Hydrogels. ACS Biomaterials Science & Engineering 2017, 3
(5)
, 757-766. https://doi.org/10.1021/acsbiomaterials.6b00076
- Yang Liu, Juneyoung Lee, Kathryn M. Mansfield, Jeong Hoon Ko, Sahar Sallam, Chrys Wesdemiotis, and Heather D. Maynard . Trehalose Glycopolymer Enhances Both Solution Stability and Pharmacokinetics of a Therapeutic Protein. Bioconjugate Chemistry 2017, 28
(3)
, 836-845. https://doi.org/10.1021/acs.bioconjchem.6b00659
- D. B. Knowles, Irina A. Shkel, Noel M. Phan, Matt Sternke, Emily Lingeman, Xian Cheng, Lixue Cheng, Kevin O’Connor, and M. Thomas Record . Chemical Interactions of Polyethylene Glycols (PEGs) and Glycerol with Protein Functional Groups: Applications to Effects of PEG and Glycerol on Protein Processes. Biochemistry 2015, 54
(22)
, 3528-3542. https://doi.org/10.1021/acs.biochem.5b00246
- Michael Senske, Lisa Törk, Benjamin Born, Martina Havenith, Christian Herrmann, and Simon Ebbinghaus . Protein Stabilization by Macromolecular Crowding through Enthalpy Rather Than Entropy. Journal of the American Chemical Society 2014, 136
(25)
, 9036-9041. https://doi.org/10.1021/ja503205y
- Srinivasan Damodaran . Electrodynamic Pressure Modulation of Protein Stability in Cosolvents. Biochemistry 2013, 52
(46)
, 8363-8373. https://doi.org/10.1021/bi400656a
- Srinivasan Damodaran . On the Molecular Mechanism of Stabilization of Proteins by Cosolvents: Role of Lifshitz Electrodynamic Forces. Langmuir 2012, 28
(25)
, 9475-9486. https://doi.org/10.1021/la300953n
- Yatin R. Gokarn, Matthew McLean, and Thomas M. Laue . Effect of PEGylation on Protein Hydrodynamics. Molecular Pharmaceutics 2012, 9
(4)
, 762-773. https://doi.org/10.1021/mp200470c
- Seyed Habib-Allah Mousavi, Jean-Marc Chobert, Abdol-Khalegh Bordbar and Thomas Haertlé . Ethanol Effect on the Structure of β-Lactoglobulin B and Its Ligand Binding. Journal of Agricultural and Food Chemistry 2008, 56
(18)
, 8680-8684. https://doi.org/10.1021/jf801383m
- Dany Doucet,, Sylvie F. Gauthier,, Don E. Otter, and, E. Allen Foegeding. Enzyme-Induced Gelation of Extensively Hydrolyzed Whey Proteins by Alcalase: Comparison with the Plastein Reaction and Characterization of Interactions. Journal of Agricultural and Food Chemistry 2003, 51
(20)
, 6036-6042. https://doi.org/10.1021/jf026041r
- Géraldine F. Drevon,, Judith Hartleib,, Eileen Scharff,, Heinz Rüterjans, and, Alan J. Russell. Thermoinactivation of Diisopropylfluorophosphatase-Containing Polyurethane Polymers. Biomacromolecules 2001, 2
(3)
, 664-671. https://doi.org/10.1021/bm000136p
- Hadi Moini,, Qiong Guo, and, Lester Packer. Enzyme Inhibition and Protein-Binding Action of the Procyanidin-Rich French Maritime Pine Bark Extract, Pycnogenol: Effect on Xanthine Oxidase. Journal of Agricultural and Food Chemistry 2000, 48
(11)
, 5630-5639. https://doi.org/10.1021/jf000618s
- Jonathan Heller and, Adam Heller. Loss of Activity or Gain in Stability of Oxidases upon Their Immobilization in Hydrated Silica: Significance of the Electrostatic Interactions of Surface Arginine Residues at the Entrances of the Reaction Channels. Journal of the American Chemical Society 1998, 120
(19)
, 4586-4590. https://doi.org/10.1021/ja973911q
- Rong Guo,, Meining Guo, and, Ganesan Narsimhan. Thermodynamics of Precipitation of Globular Proteins by Nonionic Polymers. Industrial & Engineering Chemistry Research 1996, 35
(9)
, 3015-3026. https://doi.org/10.1021/ie950745r
- Federico Cioci. Effect of Surface Tension on the Stability of Heat-Stressed Proteins: A Molecular Thermodynamic Interpretation. The Journal of Physical Chemistry 1996, 100
(43)
, 17400-17405. https://doi.org/10.1021/jp961458j
- Sergey M. Bezrukov,, Igor Vodyanoy,, Rafik A. Brutyan, and, John J. Kasianowicz. Dynamics and Free Energy of Polymers Partitioning into a Nanoscale Pore. Macromolecules 1996, 29
(26)
, 8517-8522. https://doi.org/10.1021/ma960841j
- Kimia Ahadi-Amandi, Seyyed Abolghasem Ghadami, Narges Sayari, Reza Khodarahmi. Purification of α-lactalbumin and β-lactoglobulin from cow milk. Protein Expression and Purification 2024, 223 , 106555. https://doi.org/10.1016/j.pep.2024.106555
- Kang Ni, Anhong Liu, Yanwei Ding, Xiaodong Ye. Thermal properties of glycinin in crowded environments. International Journal of Biological Macromolecules 2024, 263 , 130192. https://doi.org/10.1016/j.ijbiomac.2024.130192
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(12)
, 105439. https://doi.org/10.1016/j.jbc.2023.105439
- I-Te Chu, Gary J. Pielak. Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in cosolutes, under crowded conditions in vitro and in cells. Magnetic Resonance Letters 2023, 3
(4)
, 319-326. https://doi.org/10.1016/j.mrl.2023.04.003
- Jayanta Mondal, Narayan Chandra Maity, Ranjit Biswas. Detection of ultrafast solvent dynamics employing a streak camera. Journal of Chemical Sciences 2023, 135
(3)
https://doi.org/10.1007/s12039-023-02208-8
- Markus Mozgovicz, Andreas Fischer, Cécile Brocard, Alois Jungbauer, Nico Lingg. L-Arginine sulfate reduces irreversible protein binding in immobilized metal affinity chromatography. Journal of Chromatography A 2023, 1706 , 464246. https://doi.org/10.1016/j.chroma.2023.464246
- Tsutomu Arakawa, Yui Tomioka, Yasunori Kurosawa, Teruo Akuta. Elucidating the mechanisms of additive effects at high concentrations on hydrophobic interaction chromatography. Journal of Chromatography A 2023, 1702 , 464091. https://doi.org/10.1016/j.chroma.2023.464091
- Claire J. Stewart, Gil I. Olgenblum, Ashlee Propst, Daniel Harries, Gary J. Pielak. Resolving the enthalpy of protein stabilization by macromolecular crowding. Protein Science 2023, 32
(3)
https://doi.org/10.1002/pro.4573
- Carolin Stange, Supriyadi Hafiz, Nelli Erwin, Mathias Hafner, Christian Frech. Two peak elution behavior of a monoclonal antibody in cation exchange chromatography as a screening tool for excipients. Journal of Chromatography B 2023, 1214 , 123563. https://doi.org/10.1016/j.jchromb.2022.123563
- Angel J. Castañeda Ruiz, Maryam A. Shetab Boushehri, Tamara Phan, Stefan Carle, Patrick Garidel, Julia Buske, Alf Lamprecht. Alternative Excipients for Protein Stabilization in Protein Therapeutics: Overcoming the Limitations of Polysorbates. Pharmaceutics 2022, 14
(12)
, 2575. https://doi.org/10.3390/pharmaceutics14122575
- Amruta Joshi, Nand Kishore. Macromolecular crowding and preferential exclusion counteract the effect of protein denaturant: Biophysical aspects. Journal of Molecular Liquids 2022, 360 , 119429. https://doi.org/10.1016/j.molliq.2022.119429
- Shannon L. Speer, Claire J. Stewart, Liel Sapir, Daniel Harries, Gary J. Pielak. Macromolecular Crowding Is More than Hard-Core Repulsions. Annual Review of Biophysics 2022, 51
(1)
, 267-300. https://doi.org/10.1146/annurev-biophys-091321-071829
- Fabian Henneberg, Ashwin Chari. Chromatography-Free Purification Strategies for Large Biological Macromolecular Complexes Involving Fractionated PEG Precipitation and Density Gradients. Life 2021, 11
(12)
, 1289. https://doi.org/10.3390/life11121289
- Crissy L. Tarver, Qunying Yuan, Marc L. Pusey. Ionic Liquids as Protein Crystallization Additives. Crystals 2021, 11
(10)
, 1166. https://doi.org/10.3390/cryst11101166
- Rubaiya Anjum, Shin-nosuke Nishimura, Shingo Kobayashi, Kei Nishida, Takahisa Anada, Masaru Tanaka. Protein Stabilization Effect of Zwitterionic Osmolyte-bearing Polymer. Chemistry Letters 2021, 50
(9)
, 1699-1702. https://doi.org/10.1246/cl.210335
- Amir Erfani, Abanoub Hanna, Payam Zarrintaj, Saeed Manouchehri, Katie Weigandt, Clint P. Aichele, Joshua D. Ramsey. Biodegradable zwitterionic poly(carboxybetaine) microgel for sustained delivery of antibodies with extended stability and preserved function. Soft Matter 2021, 17
(21)
, 5349-5361. https://doi.org/10.1039/D1SM00154J
- Alexander D. Dergunov, Dmitry Y. Litvinov, Artem A. Malkov, Veronika B. Baserova, Elena V. Nosova, Liudmila V. Dergunova. Denaturation of human plasma high-density lipoproteins by urea studied by apolipoprotein A-I dissociation. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 2021, 1866
(1)
, 158814. https://doi.org/10.1016/j.bbalip.2020.158814
- Chunyu Zhang, Yang Liu, Yan Sun, Xiaoyan Dong. Complicated effects of a zwitterionic polymer containing dimethyl chains on the structures, activities and stabilities of different enzymes. Biochemical Engineering Journal 2021, 165 , 107813. https://doi.org/10.1016/j.bej.2020.107813
- Anirban Purohit, Lauren G. Douma, Linda B. Bloom, Marcia Levitus. Potassium Glutamate and Glycine Betaine Induce Self-Assembly of the PCNA and β-Sliding Clamps. Biophysical Journal 2021, 120
(1)
, 73-85. https://doi.org/10.1016/j.bpj.2020.11.013
- Birgit Köhn, Michael Kovermann. All atom insights into the impact of crowded environments on protein stability by NMR spectroscopy. Nature Communications 2020, 11
(1)
https://doi.org/10.1038/s41467-020-19616-w
- Khalida Nasreen, Zahoor Ahmad Parray, Shahzaib Ahamad, Faizan Ahmad, Anwar Ahmed, Salman Freeh Alamery, Tajamul Hussain, Md. Imtaiyaz Hassan, Asimul Islam. Interactions Under Crowding Milieu: Chemical-Induced Denaturation of Myoglobin is Determined by the Extent of Heme Dissociation on Interaction with Crowders. Biomolecules 2020, 10
(3)
, 490. https://doi.org/10.3390/biom10030490
- Hae Yeong Kang, Sun-Hyung Ha, Taehyun Yoo, Hee-Jin Park, Jin-A. Lee, Jeong-Ran Kim. Enhancement of the stability of Mycobacterium tuberculosis recombinant antigen expressed in Escherichia coli using cell lysis additives. Protein Expression and Purification 2019, 164 , 105453. https://doi.org/10.1016/j.pep.2019.105453
- Ankit Sharma. Effect of Residual Reactive Impurities in Excipients on the Stability of Pharmaceutical Products. 2019, 91-118. https://doi.org/10.1002/9783527812172.ch3
- Kavya Bhakuni, Pannuru Venkatesu. Does macromolecular crowding compatible with enzyme stem bromelain structure and stability?. International Journal of Biological Macromolecules 2019, 131 , 527-535. https://doi.org/10.1016/j.ijbiomac.2019.03.090
- Robin Curtis, James Austerberry, Luke Holloway. Protein Refolding/Renaturation. 2019, 860-878. https://doi.org/10.1016/B978-0-444-64046-8.00465-1
- Nirnay Samanta, Debasish Das Mahanta, Animesh Patra, Rajib Kumar Mitra. Soft interaction and excluded volume effect compete as polyethylene glycols modulate enzyme activity. International Journal of Biological Macromolecules 2018, 118 , 209-215. https://doi.org/10.1016/j.ijbiomac.2018.06.073
- Adeline Y. Robin, Sweta Iyer, Richard W. Birkinshaw, Jarrod Sandow, Ahmad Wardak, Cindy S. Luo, Melissa Shi, Andrew I. Webb, Peter E. Czabotar, Ruth M. Kluck, Peter M. Colman. Ensemble Properties of Bax Determine Its Function. Structure 2018, 26
(10)
, 1346-1359.e5. https://doi.org/10.1016/j.str.2018.07.006
- Juneyoung Lee, Jeong Hoon Ko, Kathryn M. Mansfield, Peter C. Nauka, Erhan Bat, Heather D. Maynard. Glucose‐Responsive Trehalose Hydrogel for Insulin Stabilization and Delivery. Macromolecular Bioscience 2018, 18
(5)
https://doi.org/10.1002/mabi.201700372
- Luisa Duque, Martin Körber, Roland Bodmeier. Impact of change of matrix crystallinity and polymorphism on ovalbumin release from lipid-based implants. European Journal of Pharmaceutical Sciences 2018, 117 , 128-137. https://doi.org/10.1016/j.ejps.2018.02.019
- Irina A. Shkel, D. B. Knowles, M. Thomas Record. Separating chemical and excluded volume interactions of polyethylene glycols with native proteins: Comparison with PEG effects on DNA helix formation. Biopolymers 2015, 103
(9)
, 517-527. https://doi.org/10.1002/bip.22662
- Xiaoyan Ni, Aixue Dong, Qiang Wang, Xuerong Fan, Jiugang Yuan, Yuanyuan Yu, Ping Wang. Characterization and performance of ramie fabrics treated with modified cellulase. The Journal of The Textile Institute 2015, 106
(7)
, 780-786. https://doi.org/10.1080/00405000.2014.942502
- David Gnutt, Mimi Gao, Oliver Brylski, Matthias Heyden, Simon Ebbinghaus. Effekte des Volumenausschlusses in lebenden Zellen. Angewandte Chemie 2015, 127
(8)
, 2578-2581. https://doi.org/10.1002/ange.201409847
- David Gnutt, Mimi Gao, Oliver Brylski, Matthias Heyden, Simon Ebbinghaus. Excluded‐Volume Effects in Living Cells. Angewandte Chemie International Edition 2015, 54
(8)
, 2548-2551. https://doi.org/10.1002/anie.201409847
- Sebastian J. Kapp, Iben Larsson, Marco Van De Weert, Marité Cárdenas, Lene Jorgensen. Competitive Adsorption of Monoclonal Antibodies and Nonionic Surfactants at Solid Hydrophobic Surfaces. Journal of Pharmaceutical Sciences 2015, 104
(2)
, 593-601. https://doi.org/10.1002/jps.24265
- Mario Lebendiker, Michal Maes, Assaf Friedler. A Screening Methodology for Purifying Proteins with Aggregation Problems. 2015, 261-281. https://doi.org/10.1007/978-1-4939-2205-5_14
- Nabanita Sadhukhan, Takahiro Muraoka, Mihoko Ui, Satoru Nagatoishi, Kouhei Tsumoto, Kazushi Kinbara. Protein stabilization by an amphiphilic short monodisperse oligo(ethylene glycol). Chemical Communications 2015, 51
(40)
, 8457-8460. https://doi.org/10.1039/C4CC10301G
- Wei Liu, Jun-Ping Liu, Li-Qiang Zou, Zhao-Qin Zhang, Cheng-Mei Liu, Rui-Hong Liang, Ming-Yong Xie, Jie Wan. Stability and conformational change of methoxypolyethylene glycol modification for native and unfolded trypsin. Food Chemistry 2014, 146 , 278-283. https://doi.org/10.1016/j.foodchem.2013.09.067
- Anurag S. Rathore, Pratap Bade, Varsha Joshi, Mili Pathak, Sudip K. Pattanayek. Refolding of biotech therapeutic proteins expressed in bacteria: review. Journal of Chemical Technology & Biotechnology 2013, 88
(10)
, 1794-1806. https://doi.org/10.1002/jctb.4152
- Denis Arutyunov, Elena Schmalhausen, Victor Orlov, Sophie Rahuel-Clermont, Natalia Nagradova, Guy Branlant, Vladimir Muronetz. An unusual effect of NADP
+
on the thermostability of the nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from
Streptococcus
mutans. Biochemistry and Cell Biology 2013, 91
(5)
, 295-302. https://doi.org/10.1139/bcb-2012-0104
- Shunsuke Tomita, Yumiko Tanabe, Kentaro Shiraki. Oligoethylene glycols prevent thermal aggregation of α‐chymotrypsin in a temperature‐dependent manner: Implications for design guidelines. Biotechnology Progress 2013, 29
(5)
, 1325-1330. https://doi.org/10.1002/btpr.1762
- Ilhem F. Hakem, Anna M. Leech, Justin Bohn, Jeremy P. Walker, Michael R. Bockstaller. Analysis of heterogeneity in nonspecific PEGylation reactions of biomolecules. Biopolymers 2013, 99
(7)
, 427-435. https://doi.org/10.1002/bip.22193
- Aya Kotake, Genichi Tajima, Yuusuke Maruyama, Jun Nakamura, Chikara Sato. Susceptibility Test of Two Ca2+-ATPase Conformers to Denaturants and Polyols to Outline Their Structural Difference. The Journal of Membrane Biology 2013, 246
(2)
, 141-149. https://doi.org/10.1007/s00232-012-9513-8
- Shermeen A. Abbas, Greta Gaspar, Vikas K. Sharma, Thomas W. Patapoff, Devendra S. Kalonia. Application of Second-Derivative Fluorescence Spectroscopy to Monitor Subtle Changes in a Monoclonal Antibody Structure. Journal of Pharmaceutical Sciences 2013, 102
(1)
, 52-61. https://doi.org/10.1002/jps.23354
- M. Thomas Record, Emily Guinn, Laurel Pegram, Michael Capp. Introductory Lecture: Interpreting and predicting Hofmeister salt ion and solute effects on biopolymer and model processes using the solute partitioning model. Faraday Discuss. 2013, 160 , 9-44. https://doi.org/10.1039/C2FD20128C
- Shunsuke Tomita, Yukio Nagasaki, Kentaro Shiraki. Different mechanisms of action of poly(ethylene glycol) and arginine on thermal inactivation of lysozyme and ribonuclease A. Biotechnology and Bioengineering 2012, 109
(10)
, 2543-2552. https://doi.org/10.1002/bit.24531
- Suntao Wang, Mark W. Tate, Sol M. Gruner. Protein crowding impedes pressure-induced unfolding of staphylococcal nuclease. Biochimica et Biophysica Acta (BBA) - General Subjects 2012, 1820
(7)
, 957-961. https://doi.org/10.1016/j.bbagen.2012.03.019
- Shermeen A. Abbas, Vikas K. Sharma, Thomas W. Patapoff, Devendra S. Kalonia. Opposite Effects of Polyols on Antibody Aggregation: Thermal Versus Mechanical Stresses. Pharmaceutical Research 2012, 29
(3)
, 683-694. https://doi.org/10.1007/s11095-011-0593-4
- Satoshi Ohtake, Yoshiko Kita, Tsutomu Arakawa. Interactions of formulation excipients with proteins in solution and in the dried state. Advanced Drug Delivery Reviews 2011, 63
(13)
, 1053-1073. https://doi.org/10.1016/j.addr.2011.06.011
- Mona Alibolandi, Hasan Mirzahosei. Retracted: Chemical Assistance in Refolding of Bacterial Inclusion Bodies. American Journal of Biochemistry and Molecular Biology 2011, 1
(3)
, 310-318. https://doi.org/10.3923/ajbmb.2011.310.318
- Muthiah Perumalsamy, Mohamed Iqbal Batcha. Synergistic extraction of bovine serum albumin using polyethylene glycol based aqueous biphasic system. Process Biochemistry 2011, 46
(2)
, 494-497. https://doi.org/10.1016/j.procbio.2010.09.023
- Mona Alibolandi, Hasan Mirzahoseini. Chemical Assistance in Refolding of Bacterial Inclusion Bodies. Biochemistry Research International 2011, 2011 , 1-6. https://doi.org/10.1155/2011/631607
- Ingrid J Castellanos, Giselle Flores, Kai Griebenow. Effect of the molecular weight of poly(ethylene glycol) used as emulsifier on α-chymotrypsin stability upon encapsulation in PLGA microspheres. Journal of Pharmacy and Pharmacology 2010, 57
(10)
, 1261-1269. https://doi.org/10.1211/jpp.57.10.0004
- Mohamed Taha, Ming-Jer Lee. Interactions of TRIS [tris(hydroxymethyl)aminomethane] and related buffers with peptide backbone: Thermodynamic characterization. Physical Chemistry Chemical Physics 2010, 12
(39)
, 12840. https://doi.org/10.1039/c0cp00253d
- Caitlin E. LaClair, Mark R. Etzel. Ingredients and pH are Key to Clear Beverages that Contain Whey Protein. Journal of Food Science 2010, 75
(1)
https://doi.org/10.1111/j.1750-3841.2009.01400.x
- Letícia C. de Lencastre Novaes, Priscila G. Mazzola, Adalberto Pessoa, Thereza C. Vessoni Penna. Effect of polyethylene glycol on the thermal stability of green fluorescent protein. Biotechnology Progress 2010, 26
(1)
, 252-256. https://doi.org/10.1002/btpr.296
- Yuqing Zhang, Linru Tang, Xuan An, Erhong Fu, Chaofan Ma. Modification of cellulase and its application to extraction of diosgenin from Dioscorea zingiberensis C.H. Wright. Biochemical Engineering Journal 2009, 47
(1-3)
, 80-86. https://doi.org/10.1016/j.bej.2009.07.006
- Brian J Jordan, Rui Hong, Gang Han, Subinoy Rana, Vincent M Rotello. Modulation of enzyme–substrate selectivity using tetraethylene glycol functionalized gold nanoparticles. Nanotechnology 2009, 20
(43)
, 434004. https://doi.org/10.1088/0957-4484/20/43/434004
- Bohuslav Rittich, Alena Španová, Petr Šálek, Petra Němcová, Štěpánka Trachtová, Daniel Horák. Separation of PCR-ready DNA from dairy products using magnetic hydrophilic microspheres and poly(ethylene glycol)–NaCl water solutions. Journal of Magnetism and Magnetic Materials 2009, 321
(10)
, 1667-1670. https://doi.org/10.1016/j.jmmm.2009.02.110
- JULIEN HUSSON, LIEDEWIJ LAAN, MARILEEN DOGTEROM. FORCE GENERATION BY MICROTUBULE BUNDLES. Biophysical Reviews and Letters 2009, 04
(01n02)
, 33-43. https://doi.org/10.1142/S1793048009000910
- Hyejung Mok, Ho Jeong Kim, Tae Gwan Park. Dissolution of biomacromolecules in organic solvents by nano-complexing with poly(ethylene glycol). International Journal of Pharmaceutics 2008, 356
(1-2)
, 306-313. https://doi.org/10.1016/j.ijpharm.2008.01.033
- Christian Lange, Rainer Rudolph. Production of Recombinant Proteins by In Vitro Folding. 2008, 1245-1280. https://doi.org/10.1002/9783527610754.tr07
- Ricky R. Lareu, Karthik S. Harve, Michael Raghunath. Emulating a crowded intracellular environment in vitro dramatically improves RT-PCR performance. Biochemical and Biophysical Research Communications 2007, 363
(1)
, 171-177. https://doi.org/10.1016/j.bbrc.2007.08.156
- Muthiah Perumalsamy, Thanapalan Murugesan. Partition Behavior of Bovine Serum Albumin in PEG2000‐Sodium Citrate‐Water Based Aqueous Two‐Phase System. Separation Science and Technology 2007, 42
(9)
, 2049-2065. https://doi.org/10.1080/15363830701313404
- Giovanni Rialdi, Ezio Battistel. Thermodynamics of proteins in unusual environments. Biophysical Chemistry 2007, 126
(1-3)
, 65-79. https://doi.org/10.1016/j.bpc.2006.05.029
- Guillermo Picó, Georgina Bassani, Beatriz Farruggia, Bibiana Nerli. Calorimetric investigation of the protein–flexible chain polymer interactions and its relationship with protein partition in aqueous two-phase systems. International Journal of Biological Macromolecules 2007, 40
(3)
, 268-275. https://doi.org/10.1016/j.ijbiomac.2006.08.008
- Anna Lupi, Sara Della Torre, Elena Campari, Ruggero Tenni, Giuseppe Cetta, Antonio Rossi, Antonella Forlino. Human recombinant prolidase from eukaryotic and prokaryotic sources. The FEBS Journal 2006, 273
(23)
, 5466-5478. https://doi.org/10.1111/j.1742-4658.2006.05538.x
- Andrew Kosky, Eva Kras, Arnold McAuley, Richard Remmele, Manmohan Singh. Excipients for Protein Drugs. 2006, 291-331. https://doi.org/10.1201/9781420004137.ch17
- Fang-Yi Jeng, Sung-Chyr Lin. Characterization and application of PEGylated horseradish peroxidase for the synthesis of poly(2-naphthol). Process Biochemistry 2006, 41
(7)
, 1566-1573. https://doi.org/10.1016/j.procbio.2006.02.021
- Ivan L. Shulgin, Eli Ruckenstein. Preferential hydration and solubility of proteins in aqueous solutions of polyethylene glycol. Biophysical Chemistry 2006, 120
(3)
, 188-198. https://doi.org/10.1016/j.bpc.2005.11.010
- Yan Jiang, Yong-Bin Yan, Hai-Meng Zhou. Polyvinylpyrrolidone 40 Assists the Refolding of Bovine Carbonic Anhydrase B by Accelerating the Refolding of the First Molten Globule Intermediate. Journal of Biological Chemistry 2006, 281
(14)
, 9058-9065. https://doi.org/10.1074/jbc.M507874200
- Guillermo Picó, Diana Romanini, Bibiana Nerli, Beatriz Farruggia. Polyethyleneglycol molecular mass and polydispersivity effect on protein partitioning in aqueous two-phase systems. Journal of Chromatography B 2006, 830
(2)
, 286-292. https://doi.org/10.1016/j.jchromb.2005.11.008
- Jin‐Woong Kim, Mi‐Ok Jung, Yong‐Jin Kim, Jee‐Hyun Ryu, Junoh Kim, Ih‐Seop Chang, Ok‐Sub Lee, Kyung‐Do Suh. Stabilization of Enzyme by Exclusive Volume Effect in Hydrophobically Controlled Polymer Microcapsules. Macromolecular Rapid Communications 2005, 26
(15)
, 1258-1261. https://doi.org/10.1002/marc.200500233
- K.S. Atia. Co-immobilization of cyclohexanone monooxygenase and glucose-6-phosphate dehydrogenase onto polyethylenimine-porous agarose polymeric composite using γ irradiation to use in biotechnological processes. Radiation Physics and Chemistry 2005, 73
(2)
, 91-99. https://doi.org/10.1016/j.radphyschem.2004.07.005
- Richard Remmele. Microcalorimetric Approaches to Biopharmaceutical Development. 2005, 327-381. https://doi.org/10.1201/9780824722258.ch13
- Christian Lange, Rainer Rudolph. Production of Recombinant Proteins for Therapy, Diagnostics, and Industrial Research by in Vitro Folding. 2005, 1245-1280. https://doi.org/10.1002/9783527619498.ch71
- Pedro Lamosa, David L. Turner, Rita Ventura, Christopher Maycock, Helena Santos. Protein stabilization by compatible solutes. European Journal of Biochemistry 2003, 270
(23)
, 4606-4614. https://doi.org/10.1046/j.1432-1033.2003.03861.x
- Tsutomu ARAKAWA, Daniel B. DIX, Byeong S. CHANG. The Effects of Protein Stabilizers on Aggregation Induced by Multiple-Stresses. YAKUGAKU ZASSHI 2003, 123
(11)
, 957-961. https://doi.org/10.1248/yakushi.123.957
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