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Recovery of Chinese hamster ovary host cell proteins for proteomic analysis.
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- Biotechnology Journal, 2014, v. 9, n. 1, p. 87, doi. 10.1002/biot.201300190
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Modeling scalability of impurity precipitation in downstream biomanufacturing.
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- Biotechnology Progress, 2024, v. 40, n. 4, p. 1, doi. 10.1002/btpr.3454
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Analytical characterization of host‐cell‐protein‐rich aggregates in monoclonal antibody solutions.
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- Biotechnology Progress, 2023, v. 39, n. 4, p. 1, doi. 10.1002/btpr.3343
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A comparative study of monoclonal antibodies. 1. phase behavior and protein-protein interactions.
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- Biotechnology Progress, 2015, v. 31, n. 1, p. 268, doi. 10.1002/btpr.2011
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Interactions and phase behavior of a monoclonal antibody.
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- Biotechnology Progress, 2011, v. 27, n. 1, p. 280, doi. 10.1002/btpr.536
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Factors affecting product association as a mechanism of host‐cell protein persistence in bioprocessing.
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- Biotechnology & Bioengineering, 2024, v. 121, n. 4, p. 1284, doi. 10.1002/bit.28658
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Identification and characterization of CHO host‐cell proteins in monoclonal antibody bioprocessing.
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- Biotechnology & Bioengineering, 2024, v. 121, n. 1, p. 291, doi. 10.1002/bit.28568
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Characterization and implications of host‐cell protein aggregates in biopharmaceutical processing.
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- Biotechnology & Bioengineering, 2023, v. 120, n. 4, p. 1068, doi. 10.1002/bit.28325
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Towards continuous mAb purification: Clearance of host cell proteins from CHO cell culture harvests via "flow‐through affinity chromatography" using peptide‐based adsorbents.
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- Biotechnology & Bioengineering, 2022, v. 119, n. 7, p. 1873, doi. 10.1002/bit.28096
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Displacement to separate host‐cell proteins and aggregates in cation‐exchange chromatography of monoclonal antibodies.
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- Biotechnology & Bioengineering, 2021, v. 118, n. 1, p. 164, doi. 10.1002/bit.27559
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Mechanisms of precipitate formation during the purification of an Fc‐fusion protein.
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- Biotechnology & Bioengineering, 2018, v. 115, n. 10, p. 2489, doi. 10.1002/bit.26746
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Contributions of depth filter components to protein adsorption in bioprocessing.
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- Biotechnology & Bioengineering, 2018, v. 115, n. 8, p. 1938, doi. 10.1002/bit.26707
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Knockout of a difficult-to-remove CHO host cell protein, lipoprotein lipase, for improved polysorbate stability in monoclonal antibody formulations.
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- Biotechnology & Bioengineering, 2017, v. 114, n. 5, p. 1006, doi. 10.1002/bit.26237
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Host cell protein impurities in chromatographic polishing steps for monoclonal antibody purification.
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- Biotechnology & Bioengineering, 2016, v. 113, n. 6, p. 1260, doi. 10.1002/bit.25882
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Expression of difficult-to-remove host cell protein impurities during extended Chinese hamster ovary cell culture and their impact on continuous bioprocessing.
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- Biotechnology & Bioengineering, 2015, v. 112, n. 6, p. 1232, doi. 10.1002/bit.25515
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Identification and characterization of host cell protein product-associated impurities in monoclonal antibody bioprocessing.
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- Biotechnology & Bioengineering, 2014, v. 111, n. 5, p. 904, doi. 10.1002/bit.25158
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Cell Therapy Biomanufacturing: Integrating Biomaterial and Flow‐Based Membrane Technologies for Production of Engineered T‐Cells.
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- Advanced Materials Technologies, 2023, v. 8, n. 6, p. 1, doi. 10.1002/admt.202201155
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Flow-dependent entrapment of large bioparticles in porous process media.
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- Biotechnology & Bioengineering, 2009, v. 104, n. 1, p. 127, doi. 10.1002/bit.22370
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Kinetics and equilibria of lysozyme precipitation and crystallization in concentrated ammonium sulfate solutions.
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- Biotechnology & Bioengineering, 2006, v. 94, n. 1, p. 177, doi. 10.1002/bit.20839
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Correlation of diafiltration sieving behavior of lysozyme-BSA mixtures with osmotic second virial cross-coefficients.
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- Biotechnology & Bioengineering, 2004, v. 87, n. 3, p. 303, doi. 10.1002/bit.20115
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Phase equilibria in the lysozyme-ammonium sulfate-water system.
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- Biotechnology & Bioengineering, 2000, v. 70, n. 5, p. 498, doi. 10.1002/1097-0290(20001205)70:5<498::AID-BIT4>3.0.CO;2-6
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Nanocrystalline protein domains via salting‐out.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2021, v. 77, n. 11, p. 412, doi. 10.1107/S2053230X21009961
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Partitioning of host and recombinant cells in aqueous two-phase polymer systems.
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- Biotechnology & Bioengineering, 1990, v. 36, n. 5, p. 484, doi. 10.1002/bit.260360508
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Predictive crystallization of ribonuclease A via rapid screening of osmotic second virial coefficients.
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- Proteins, 2003, v. 50, n. 2, p. 303, doi. 10.1002/prot.10249
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Closed‐loop modeling of central and intrinsic cardiac nervous system circuits underlying cardiovascular control.
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- AIChE Journal, 2023, v. 69, n. 4, p. 1, doi. 10.1002/aic.18033
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A natural interaction: Chemical engineering and molecular biophysics.
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- AIChE Journal, 2003, v. 49, n. 4, p. 806, doi. 10.1002/aic.690490402
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Excluded volume contribution to the osmotic second virial coefficient for proteins.
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- AIChE Journal, 1995, v. 41, n. 4, p. 1010, doi. 10.1002/aic.690410432
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STM and AFM in Biotechnology.
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- Biotechnology Progress, 1993, v. 9, n. 1, p. 1, doi. 10.1021/bp00019a001
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Optimization of protein sample preparation for two-dimensional electrophoresis.
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- Electrophoresis, 2012, v. 33, n. 13, p. 1947, doi. 10.1002/elps.201100659
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Patterns of protein-protein interactions in salt solutions and implications for protein crystallization.
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- Protein Science: A Publication of the Protein Society, 2007, v. 16, n. 9, p. 1867, doi. 10.1110/ps.072957907
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Effects of additives on surfactant phase behavior relevant to bacteriorhodopsin crystallization.
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- Protein Science: A Publication of the Protein Society, 2006, v. 15, n. 12, p. 2682, doi. 10.1110/ps.062370506
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Direct measurement of protein osmotic second virial cross coefficients by cross-interaction chromatography.
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- Protein Science: A Publication of the Protein Society, 2004, v. 13, n. 5, p. 1379, doi. 10.1110/ps.03419204
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A critical examination of the decoupling approximation for small-angle scattering from hard ellipsoids of revolution.
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- Journal of Applied Crystallography, 2016, v. 49, n. 5, p. 1734, doi. 10.1107/S1600576716012929
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Measured and calculated effects of mutations in bacteriophage T4 lysozyme on interactions in solution.
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- Proteins, 2000, v. 41, n. 1, p. 123, doi. 10.1002/1097-0134(20001001)41:1<123::AID-PROT140>3.0.CO;2-Q
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- Article