메뉴 건너뛰기




Volumn 102, Issue 12, 2013, Pages 4256-4267

Radar chart array analysis to visualize effects of formulation variables on IgG1 particle formation as measured by multiple analytical techniques

Author keywords

Archimedes; data visualization; formulation; microflow imaging; monoclonal antibody; morphology; particle size; protein aggregation; stability

Indexed keywords

IMMUNOGLOBULIN G1; MONOCLONAL ANTIBODY; SODIUM CHLORIDE;

EID: 84888199388     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23738     Document Type: Article
Times cited : (38)

References (50)
  • 2
    • 79960135244 scopus 로고    scopus 로고
    • Chemical modifications in therapeutic protein aggregates generated under different stress conditions
    • Luo Q, Joubert MK, Stevenson R, Ketchem RR, Narhi LO, Wypych J,. 2011. Chemical modifications in therapeutic protein aggregates generated under different stress conditions. J Biol Chem 286 (28): 25134-25144.
    • (2011) J Biol Chem , vol.286 , Issue.28 , pp. 25134-25144
    • Luo, Q.1    Joubert, M.K.2    Stevenson, R.3    Ketchem, R.R.4    Narhi, L.O.5    Wypych, J.6
  • 3
    • 79960128166 scopus 로고    scopus 로고
    • Classification and characterization of therapeutic antibody aggregates
    • Joubert MK, Luo Q, Nashed-Samuel Y, Wypych J, Narhi LO,. 2011. Classification and characterization of therapeutic antibody aggregates. J Biol Chem 286 (28): 25118-25133.
    • (2011) J Biol Chem , vol.286 , Issue.28 , pp. 25118-25133
    • Joubert, M.K.1    Luo, Q.2    Nashed-Samuel, Y.3    Wypych, J.4    Narhi, L.O.5
  • 4
    • 84869838281 scopus 로고    scopus 로고
    • Immunogenicity of different stressed IgG monoclonal antibody formulations in immune tolerant transgenic mice
    • Filipe V, Jiskoot W, Basmeleh AH, Halim A, Schellekens H, Filipe V,. 2012. Immunogenicity of different stressed IgG monoclonal antibody formulations in immune tolerant transgenic mice. mAbs 4 (6): 740-752.
    • (2012) MAbs , vol.4 , Issue.6 , pp. 740-752
    • Filipe, V.1    Jiskoot, W.2    Basmeleh, A.H.3    Halim, A.4    Schellekens, H.5    Filipe, V.6
  • 5
    • 84860784107 scopus 로고    scopus 로고
    • Issues and challenges of subvisible and submicron particulate analysis in protein solutions
    • Scherer TM, Leung S, Owyang L, Shire SJ,. 2012. Issues and challenges of subvisible and submicron particulate analysis in protein solutions. AAPS J 14 (2): 236-243.
    • (2012) AAPS J , vol.14 , Issue.2 , pp. 236-243
    • Scherer, T.M.1    Leung, S.2    Owyang, L.3    Shire, S.J.4
  • 6
    • 84862872600 scopus 로고    scopus 로고
    • Particles shed from syringe filters and their effects on agitation-induced protein aggregation
    • Liu L, Randolph TW, Carpenter JF,. 2012. Particles shed from syringe filters and their effects on agitation-induced protein aggregation. J Pharm Sci 101 (8): 2952-2959.
    • (2012) J Pharm Sci , vol.101 , Issue.8 , pp. 2952-2959
    • Liu, L.1    Randolph, T.W.2    Carpenter, J.F.3
  • 7
    • 84865378494 scopus 로고    scopus 로고
    • Protein particles: What we know and what we do not know
    • Ripple DC, Dimitrova MN,. 2012. Protein particles: What we know and what we do not know. J Pharm Sci 101 (10): 3568-3579.
    • (2012) J Pharm Sci , vol.101 , Issue.10 , pp. 3568-3579
    • Ripple, D.C.1    Dimitrova, M.N.2
  • 8
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi EY, Krishnan S, Randolph TW, Carpenter JF,. 2003. Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation. Pharm Res 20 (9): 1325-1336.
    • (2003) Pharm Res , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 9
    • 69249208825 scopus 로고    scopus 로고
    • Mechanisms of protein aggregation
    • Philo JS, Arakawa T,. 2009. Mechanisms of protein aggregation. Curr Pharm Biotechnol 10 (4): 348-351.
    • (2009) Curr Pharm Biotechnol , vol.10 , Issue.4 , pp. 348-351
    • Philo, J.S.1    Arakawa, T.2
  • 11
    • 79954531753 scopus 로고    scopus 로고
    • Nonnative aggregation of an IgG1 antibody in acidic conditions: Part 1. Unfolding, colloidal interactions, and formation of high-molecular-weight aggregates
    • Brummitt RK, Nesta DP, Chang L, Chase SF, Laue TM, Roberts CJ,. 2011. Nonnative aggregation of an IgG1 antibody in acidic conditions: Part 1. Unfolding, colloidal interactions, and formation of high-molecular-weight aggregates. J Pharm Sci 100 (6): 2087-2103.
    • (2011) J Pharm Sci , vol.100 , Issue.6 , pp. 2087-2103
    • Brummitt, R.K.1    Nesta, D.P.2    Chang, L.3    Chase, S.F.4    Laue, T.M.5    Roberts, C.J.6
  • 12
    • 84878893050 scopus 로고    scopus 로고
    • Aggregation mechanism of an IgG2 and two IgG1 monoclonal antibodies at low pH: From oligomers to larger aggregates
    • Arosio P, Rima S, Morbidelli M,. 2013. Aggregation mechanism of an IgG2 and two IgG1 monoclonal antibodies at low pH: From oligomers to larger aggregates. Pharm Res 30 (3): 641-654.
    • (2013) Pharm Res , vol.30 , Issue.3 , pp. 641-654
    • Arosio, P.1    Rima, S.2    Morbidelli, M.3
  • 13
    • 84865369923 scopus 로고    scopus 로고
    • Relating particle formation to salt- and pH-dependent phase separation of non-native aggregates of alpha-chymotrypsinogen A
    • Kroetsch AM, Sahin E, Wang HY, Krizman S, Roberts CJ,. 2012. Relating particle formation to salt- and pH-dependent phase separation of non-native aggregates of alpha-chymotrypsinogen A. J Pharm Sci 101 (10): 3651-3660.
    • (2012) J Pharm Sci , vol.101 , Issue.10 , pp. 3651-3660
    • Kroetsch, A.M.1    Sahin, E.2    Wang, H.Y.3    Krizman, S.4    Roberts, C.J.5
  • 14
    • 84873886259 scopus 로고    scopus 로고
    • Aggregation of anti-streptavidin immunoglobulin gamma-1 involves Fab unfolding and competing growth pathways mediated by pH and salt concentration
    • Kim N, Remmele RL, Jr., Liu D, Razinkov VI, Fernandez EJ, Roberts CJ,. 2013. Aggregation of anti-streptavidin immunoglobulin gamma-1 involves Fab unfolding and competing growth pathways mediated by pH and salt concentration. Biophys Chem 172: 26-36.
    • (2013) Biophys Chem , vol.172 , pp. 26-36
    • Kim, N.1    Remmele, Jr.R.L.2    Liu, D.3    Razinkov, V.I.4    Fernandez, E.J.5    Roberts, C.J.6
  • 15
    • 79952125250 scopus 로고    scopus 로고
    • Effective charge measurements reveal selective and preferential accumulation of anions, but not cations, at the protein surface in dilute salt solutions
    • Gokarn YR, Fesinmeyer RM, Saluja A, Razinkov V, Chase SF, Laue TM, Brems DN,. 2011. Effective charge measurements reveal selective and preferential accumulation of anions, but not cations, at the protein surface in dilute salt solutions. Protein Sc 20 (3): 580-587.
    • (2011) Protein Sc , vol.20 , Issue.3 , pp. 580-587
    • Gokarn, Y.R.1    Fesinmeyer, R.M.2    Saluja, A.3    Razinkov, V.4    Chase, S.F.5    Laue, T.M.6    Brems, D.N.7
  • 17
    • 84862849131 scopus 로고    scopus 로고
    • Protein particulate detection issues in biotherapeutics development-current status
    • Das TK., 2012. Protein particulate detection issues in biotherapeutics development-current status. AAPS Pharm Sci Tech 13 (2): 732-746.
    • (2012) AAPS Pharm Sci Tech , vol.13 , Issue.2 , pp. 732-746
    • Das, T.K.1
  • 18
    • 69249215475 scopus 로고    scopus 로고
    • A critical review of analytical methods for subvisible and visible particles
    • Narhi LO, Jiang Y, Cao S, Benedek K, Shnek D,. 2009. A critical review of analytical methods for subvisible and visible particles. Curr Pharm Biotechnol 10 (4): 373-381.
    • (2009) Curr Pharm Biotechnol , vol.10 , Issue.4 , pp. 373-381
    • Narhi, L.O.1    Jiang, Y.2    Cao, S.3    Benedek, K.4    Shnek, D.5
  • 19
    • 78649661342 scopus 로고    scopus 로고
    • Characterization of particles in protein solutions: Reaching the limits of current technologies
    • Demeule B, Messick S, Shire SJ, Liu J,. 2010. Characterization of particles in protein solutions: Reaching the limits of current technologies. AAPS J 12 (4): 708-715.
    • (2010) AAPS J , vol.12 , Issue.4 , pp. 708-715
    • Demeule, B.1    Messick, S.2    Shire, S.J.3    Liu, J.4
  • 21
    • 84865393469 scopus 로고    scopus 로고
    • Compatibility, physical stability, and characterization of an IgG4 monoclonal antibody after dilution into different intravenous administration bags
    • Kumru OS, Liu J, Ji JA, Cheng W, Wang YJ, Wang T, Joshi SB, Middaugh CR, Volkin DB,. 2012. Compatibility, physical stability, and characterization of an IgG4 monoclonal antibody after dilution into different intravenous administration bags. J Pharm Sci 101 (10): 3636-3650.
    • (2012) J Pharm Sci , vol.101 , Issue.10 , pp. 3636-3650
    • Kumru, O.S.1    Liu, J.2    Ji, J.A.3    Cheng, W.4    Wang, Y.J.5    Wang, T.6    Joshi, S.B.7    Middaugh, C.R.8    Volkin, D.B.9
  • 22
    • 77955933028 scopus 로고    scopus 로고
    • Micro-flow imaging: Flow microscopy applied to sub-visible particulate analysis in protein formulations
    • Sharma DK, King D, Oma P, Merchant C,. 2010. Micro-flow imaging: Flow microscopy applied to sub-visible particulate analysis in protein formulations. AAPS J 12 (3): 455-464.
    • (2010) AAPS J , vol.12 , Issue.3 , pp. 455-464
    • Sharma, D.K.1    King, D.2    Oma, P.3    Merchant, C.4
  • 23
    • 78650577461 scopus 로고    scopus 로고
    • Subvisible particle counting provides a sensitive method of detecting and quantifying aggregation of monoclonal antibody caused by freeze-thawing: Insights into the roles of particles in the protein aggregation pathway
    • Barnard JG, Singh S, Randolph TW, Carpenter JF,. 2011. Subvisible particle counting provides a sensitive method of detecting and quantifying aggregation of monoclonal antibody caused by freeze-thawing: Insights into the roles of particles in the protein aggregation pathway. J Pharm Sci 100 (2): 492-503.
    • (2011) J Pharm Sci , vol.100 , Issue.2 , pp. 492-503
    • Barnard, J.G.1    Singh, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 24
    • 77955101936 scopus 로고    scopus 로고
    • Development of a microflow digital imaging assay to characterize protein particulates during storage of a high concentration IgG1 monoclonal antibody formulation
    • Wuchner K, Buchler J, Spycher R, Dalmonte P, Volkin DB,. 2010. Development of a microflow digital imaging assay to characterize protein particulates during storage of a high concentration IgG1 monoclonal antibody formulation. J Pharm Sci 99 (8): 3343-3361.
    • (2010) J Pharm Sci , vol.99 , Issue.8 , pp. 3343-3361
    • Wuchner, K.1    Buchler, J.2    Spycher, R.3    Dalmonte, P.4    Volkin, D.B.5
  • 25
    • 84860855378 scopus 로고    scopus 로고
    • Discrimination between silicone oil droplets and protein aggregates in biopharmaceuticals: A novel multiparametric image filter for sub-visible particles in microflow imaging analysis
    • Strehl R, Rombach-Riegraf V, Diez M, Egodage K, Bluemel M, Jeschke M, Koulov A,. 2011. Discrimination between silicone oil droplets and protein aggregates in biopharmaceuticals: A novel multiparametric image filter for sub-visible particles in microflow imaging analysis. J Pharm Res 29 (2): 594-602.
    • (2011) J Pharm Res , vol.29 , Issue.2 , pp. 594-602
    • Strehl, R.1    Rombach-Riegraf, V.2    Diez, M.3    Egodage, K.4    Bluemel, M.5    Jeschke, M.6    Koulov, A.7
  • 26
    • 84876340793 scopus 로고    scopus 로고
    • How subvisible particles become invisible-relevance of the refractive index for protein particle analysis
    • Zolls S, Gregoritza M, Tantipolphan R, Wiggenhorn M, Winter G, Friess W, Hawe A,. 2013. How subvisible particles become invisible-relevance of the refractive index for protein particle analysis. J Pharm Sci 102 (5): 1434-1446.
    • (2013) J Pharm Sci , vol.102 , Issue.5 , pp. 1434-1446
    • Zolls, S.1    Gregoritza, M.2    Tantipolphan, R.3    Wiggenhorn, M.4    Winter, G.5    Friess, W.6    Hawe, A.7
  • 27
    • 77951552352 scopus 로고    scopus 로고
    • Quantification and characterization of subvisible proteinaceous particles in opalescent mAb formulations using micro-flow imaging
    • Sharma DK, Oma P, Pollo MJ, Sukumar M,. 2010. Quantification and characterization of subvisible proteinaceous particles in opalescent mAb formulations using micro-flow imaging. J Pharm Sci 99 (6): 2628-2642.
    • (2010) J Pharm Sci , vol.99 , Issue.6 , pp. 2628-2642
    • Sharma, D.K.1    Oma, P.2    Pollo, M.J.3    Sukumar, M.4
  • 28
    • 84864625506 scopus 로고    scopus 로고
    • Quantification and characterization of micrometer and submicrometer subvisible particles in protein therapeutics by use of a suspended microchannel resonator
    • Patel AR, Lau D, Liu J,. 2012. Quantification and characterization of micrometer and submicrometer subvisible particles in protein therapeutics by use of a suspended microchannel resonator. Anal Chem 84 (15): 6833-6840.
    • (2012) Anal Chem , vol.84 , Issue.15 , pp. 6833-6840
    • Patel, A.R.1    Lau, D.2    Liu, J.3
  • 29
    • 84879025305 scopus 로고    scopus 로고
    • Micro-flow imaging and resonant mass measurement (archimedes) - Complementary methods to quantitatively differentiate protein particles and silicone oil droplets
    • Weinbuch D, Zolls S, Wiggenhorn M, Friess W, Winter G, Jiskoot W, Hawe A,. 2013. Micro-flow imaging and resonant mass measurement (archimedes)- Complementary methods to quantitatively differentiate protein particles and silicone oil droplets. J Pharm Sci 102 (7): 2152-2165.
    • (2013) J Pharm Sci , vol.102 , Issue.7 , pp. 2152-2165
    • Weinbuch, D.1    Zolls, S.2    Wiggenhorn, M.3    Friess, W.4    Winter, G.5    Jiskoot, W.6    Hawe, A.7
  • 30
    • 80052268214 scopus 로고    scopus 로고
    • Multidimensional methods for the formulation of biopharmaceuticals and vaccines
    • 100
    • Maddux NR, Joshi SB, Volkin DB, Ralston JP, Middaugh CR,. 2011. Multidimensional methods for the formulation of biopharmaceuticals and vaccines. J Pharm Sci 100 (10): 4171-4197.
    • (2011) J Pharm Sci , vol.10 , pp. 4171-4197
    • Maddux, N.R.1    Joshi, S.B.2    Volkin, D.B.3    Ralston, J.P.4    Middaugh, C.R.5
  • 31
    • 80052946330 scopus 로고    scopus 로고
    • Introduction to statistical methods to analyze large data sets: Principal components analysis
    • tr3
    • Clark NR, Ma'ayan A,. 2011. Introduction to statistical methods to analyze large data sets: Principal components analysis. Sci Signal 4 (190):tr3.
    • (2011) Sci Signal , vol.4 , Issue.190
    • Clark, N.R.1    Ma'ayan, A.2
  • 32
    • 84864319122 scopus 로고    scopus 로고
    • Comparison of high-throughput biophysical methods to identify stabilizing excipients for a model IgG2 monoclonal antibody: Conformational stability and kinetic aggregation measurements
    • Cheng W, Joshi SB, He F, Brems DN, He B, Kerwin BA, Volkin DB, Middaugh CR,. 2012. Comparison of high-throughput biophysical methods to identify stabilizing excipients for a model IgG2 monoclonal antibody: Conformational stability and kinetic aggregation measurements. J Pharm Sci 101 (5): 1701-1720.
    • (2012) J Pharm Sci , vol.101 , Issue.5 , pp. 1701-1720
    • Cheng, W.1    Joshi, S.B.2    He, F.3    Brems, D.N.4    He, B.5    Kerwin, B.A.6    Volkin, D.B.7    Middaugh, C.R.8
  • 33
    • 84855877977 scopus 로고    scopus 로고
    • Formulation design and high-throughput excipient selection based on structural integrity and conformational stability of dilute and highly concentrated IgG1 monoclonal antibody solutions
    • Bhambhani A, Kissmann JM, Joshi SB, Volkin DB, Kashi RS, Middaugh CR,. 2012. Formulation design and high-throughput excipient selection based on structural integrity and conformational stability of dilute and highly concentrated IgG1 monoclonal antibody solutions. J Pharm Sci 101 (3): 1120-1135.
    • (2012) J Pharm Sci , vol.101 , Issue.3 , pp. 1120-1135
    • Bhambhani, A.1    Kissmann, J.M.2    Joshi, S.B.3    Volkin, D.B.4    Kashi, R.S.5    Middaugh, C.R.6
  • 34
    • 84864055322 scopus 로고    scopus 로고
    • Excipients differentially influence the conformational stability and pretransition dynamics of two IgG1 monoclonal antibodies
    • Thakkar SV, Joshi SB, Jones ME, Sathish HA, Bishop SM, Volkin DB, Middaugh CR,. 2012. Excipients differentially influence the conformational stability and pretransition dynamics of two IgG1 monoclonal antibodies. J Pharm Sci 101 (9): 3062-3077.
    • (2012) J Pharm Sci , vol.101 , Issue.9 , pp. 3062-3077
    • Thakkar, S.V.1    Joshi, S.B.2    Jones, M.E.3    Sathish, H.A.4    Bishop, S.M.5    Volkin, D.B.6    Middaugh, C.R.7
  • 35
    • 84870690077 scopus 로고    scopus 로고
    • Comparative signature diagrams to evaluate biophysical data for differences in protein structure across various formulations
    • Iyer V, Maddux N, Hu L, Cheng W, Youssef AK, Winter G, Joshi SB, Volkin DB, Middaugh CR,. 2013. Comparative signature diagrams to evaluate biophysical data for differences in protein structure across various formulations. J Pharm Sci 102 (1): 43-51.
    • (2013) J Pharm Sci , vol.102 , Issue.1 , pp. 43-51
    • Iyer, V.1    Maddux, N.2    Hu, L.3    Cheng, W.4    Youssef, A.K.5    Winter, G.6    Joshi, S.B.7    Volkin, D.B.8    Middaugh, C.R.9
  • 36
    • 84866612452 scopus 로고    scopus 로고
    • Improved data visualization techniques for analyzing macromolecule structural changes
    • Kim JH, Iyer V, Joshi SB, Volkin DB, Middaugh CR,. 2012. Improved data visualization techniques for analyzing macromolecule structural changes. Protein Sci 21 (10): 1540-1553.
    • (2012) Protein Sci , vol.21 , Issue.10 , pp. 1540-1553
    • Kim, J.H.1    Iyer, V.2    Joshi, S.B.3    Volkin, D.B.4    Middaugh, C.R.5
  • 37
    • 84879009285 scopus 로고    scopus 로고
    • Correlating excipient effects on conformational and storage stability of an IgG1 monoclonal antibody with local dynamics as measured by hydrogen/deuterium-exchange mass spectrometry
    • Manikwar P, Majumdar R, Hickey JM, Thakkar SV, Samra HS, Sathish HA, Bishop SM, Middaugh CR, Weis DD, Volkin DB,. 2013. Correlating excipient effects on conformational and storage stability of an IgG1 monoclonal antibody with local dynamics as measured by hydrogen/deuterium-exchange mass spectrometry. J Pharm Sci 102 (7): 2136-2151.
    • (2013) J Pharm Sci , vol.102 , Issue.7 , pp. 2136-2151
    • Manikwar, P.1    Majumdar, R.2    Hickey, J.M.3    Thakkar, S.V.4    Samra, H.S.5    Sathish, H.A.6    Bishop, S.M.7    Middaugh, C.R.8    Weis, D.D.9    Volkin, D.B.10
  • 38
    • 77951587964 scopus 로고    scopus 로고
    • Evaluation of a dual-wavelength size exclusion HPLC method with improved sensitivity to detect protein aggregates and its use to better characterize degradation pathways of an IgG1 monoclonal antibody
    • Bond MD, Panek ME, Zhang Z, Wang D, Mehndiratta P, Zhao H, Gunton K, Ni A, Nedved ML, Burman S, Volkin DB,. 2010. Evaluation of a dual-wavelength size exclusion HPLC method with improved sensitivity to detect protein aggregates and its use to better characterize degradation pathways of an IgG1 monoclonal antibody. J Pharm Sci 99 (6): 2582-2597.
    • (2010) J Pharm Sci , vol.99 , Issue.6 , pp. 2582-2597
    • Bond, M.D.1    Panek, M.E.2    Zhang, Z.3    Wang, D.4    Mehndiratta, P.5    Zhao, H.6    Gunton, K.7    Ni, A.8    Nedved, M.L.9    Burman, S.10    Volkin, D.B.11
  • 39
    • 4644311920 scopus 로고    scopus 로고
    • Average protein density is a molecular-weight-dependent function
    • Fischer H, Polikarpov I, Craievich AF,. 2004. Average protein density is a molecular-weight-dependent function. Protein Sci 13 (10): 2825-2828.
    • (2004) Protein Sci , vol.13 , Issue.10 , pp. 2825-2828
    • Fischer, H.1    Polikarpov, I.2    Craievich, A.F.3
  • 40
    • 84866419200 scopus 로고    scopus 로고
    • Mechanistic complexity of subvisible particle formation: Links to protein aggregation are highly specific
    • Simler BR, Hui G, Dahl JE, Perez-Ramirez B,. 2012. Mechanistic complexity of subvisible particle formation: Links to protein aggregation are highly specific. J Pharm Sci 101 (11): 4140-4154.
    • (2012) J Pharm Sci , vol.101 , Issue.11 , pp. 4140-4154
    • Simler, B.R.1    Hui, G.2    Dahl, J.E.3    Perez-Ramirez, B.4
  • 43
    • 84878144842 scopus 로고    scopus 로고
    • Flow imaging: Moving toward best practices for subvisible particle quantitation in protein products
    • Wilson GA, Manning MC,. 2013. Flow imaging: Moving toward best practices for subvisible particle quantitation in protein products. J Pharm Sci 102 (3): 1133-1134.
    • (2013) J Pharm Sci , vol.102 , Issue.3 , pp. 1133-1134
    • Wilson, G.A.1    Manning, M.C.2
  • 45
    • 84877623789 scopus 로고    scopus 로고
    • Analytical lessons learned from selected therapeutic protein drug comparability studies
    • Federici M, Lubiniecki A, Manikwar P, Volkin DB,. 2013. Analytical lessons learned from selected therapeutic protein drug comparability studies. Biologicals 41 (3): 131-147.
    • (2013) Biologicals , vol.41 , Issue.3 , pp. 131-147
    • Federici, M.1    Lubiniecki, A.2    Manikwar, P.3    Volkin, D.B.4
  • 46
    • 84872490861 scopus 로고    scopus 로고
    • Ionic strength affects tertiary structure and aggregation propensity of a monoclonal antibody adsorbed to silicone oil-water interfaces
    • Gerhardt A, Bonam K, Bee JS, Carpenter JF, Randolph TW,. 2013. Ionic strength affects tertiary structure and aggregation propensity of a monoclonal antibody adsorbed to silicone oil-water interfaces. J Pharm Sci 102 (2): 429-440.
    • (2013) J Pharm Sci , vol.102 , Issue.2 , pp. 429-440
    • Gerhardt, A.1    Bonam, K.2    Bee, J.S.3    Carpenter, J.F.4    Randolph, T.W.5
  • 49
    • 84875421347 scopus 로고    scopus 로고
    • Methods of high throughput biophysical characterization in biopharmaceutical development
    • Razinkov VI, Treuheit MJ, Becker GW,. 2013. Methods of high throughput biophysical characterization in biopharmaceutical development. Curr Drug Discov Technol 10 (1): 59-70.
    • (2013) Curr Drug Discov Technol , vol.10 , Issue.1 , pp. 59-70
    • Razinkov, V.I.1    Treuheit, M.J.2    Becker, G.W.3
  • 50
    • 84859319265 scopus 로고    scopus 로고
    • Advancements in high throughput biophysical technologies: Applications for characterization and screening during early formulation development of monoclonal antibodies
    • Samra HS, He F,. 2012. Advancements in high throughput biophysical technologies: Applications for characterization and screening during early formulation development of monoclonal antibodies. Mol Pharm 9 (4): 696-707.
    • (2012) Mol Pharm , vol.9 , Issue.4 , pp. 696-707
    • Samra, H.S.1    He, F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.