메뉴 건너뛰기




Volumn 30, Issue , 2014, Pages 211-217

Protein aggregation and its impact on product quality

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; CHAINS; DRUG PRODUCTS; MONOCLONAL ANTIBODIES; QUALITY CONTROL;

EID: 84907260610     PISSN: 09581669     EISSN: 18790429     Source Type: Journal    
DOI: 10.1016/j.copbio.2014.08.001     Document Type: Review
Times cited : (239)

References (65)
  • 1
    • 84892170718 scopus 로고    scopus 로고
    • What's fueling the biotech engine - 2012 to 2013
    • Rob Aggarwal S. What's fueling the biotech engine - 2012 to 2013. Nat Biotechnol 2014, 32:32-39.
    • (2014) Nat Biotechnol , vol.32 , pp. 32-39
    • Rob Aggarwal, S.1
  • 2
    • 84904636678 scopus 로고    scopus 로고
    • Oral peptide and protein delivery: intestinal obstacles and commercial prospects
    • Smart A.L., Gaisford S., Basit A.W. Oral peptide and protein delivery: intestinal obstacles and commercial prospects. Expert Opin Drug Deliv 2014, 10.1517/17425247.2014.917077.
    • (2014) Expert Opin Drug Deliv
    • Smart, A.L.1    Gaisford, S.2    Basit, A.W.3
  • 3
    • 84906316137 scopus 로고    scopus 로고
    • Orally active-targeted drug delivery systems for proteins and peptides
    • Li X., Yu M., Fan W., Gan Y., Hovgaard L., Yang M. Orally active-targeted drug delivery systems for proteins and peptides. Expert Opin Drug Deliv 2014, 10.1517/17425247.2014.924500.
    • (2014) Expert Opin Drug Deliv
    • Li, X.1    Yu, M.2    Fan, W.3    Gan, Y.4    Hovgaard, L.5    Yang, M.6
  • 5
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang W. Protein aggregation and its inhibition in biopharmaceutics. Int J Pharm 2005, 289:1-30.
    • (2005) Int J Pharm , vol.289 , pp. 1-30
    • Wang, W.1
  • 7
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: folding aggregates, inclusion bodies and amyloid
    • Fink A.L. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold Des 1998, 3:R9-R23.
    • (1998) Fold Des , vol.3
    • Fink, A.L.1
  • 8
    • 61749103757 scopus 로고    scopus 로고
    • Comparative effects of salt, organic, and polymer precipitants on protein phase behavior and implications for vapor diffusion
    • Dumetz A.C., Chockla A.M., Kaler E.W., Lenhoff A.M. Comparative effects of salt, organic, and polymer precipitants on protein phase behavior and implications for vapor diffusion. Cryst Growth Des 2009, 9:682-691.
    • (2009) Cryst Growth Des , vol.9 , pp. 682-691
    • Dumetz, A.C.1    Chockla, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 9
    • 84865369923 scopus 로고    scopus 로고
    • Relating particle formation to salt- and pH-dependent phase separation of non-native aggregates of alpha-chymotrypsinogen A
    • Kroetsch A.M., Sahin E., Wang H.Y., Krizman S., Roberts C.J. Relating particle formation to salt- and pH-dependent phase separation of non-native aggregates of alpha-chymotrypsinogen A. J Pharm Sci 2012, 101:3651-3660.
    • (2012) J Pharm Sci , vol.101 , pp. 3651-3660
    • Kroetsch, A.M.1    Sahin, E.2    Wang, H.Y.3    Krizman, S.4    Roberts, C.J.5
  • 10
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • Chothia C., Janin J. Principles of protein-protein recognition. Nature 1975, 256:705-708.
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia, C.1    Janin, J.2
  • 12
    • 67449132077 scopus 로고    scopus 로고
    • Principles, approaches, and challenges for predicting protein aggregation rates and shelf life
    • Weiss W.F., Young T.M., Roberts C.J. Principles, approaches, and challenges for predicting protein aggregation rates and shelf life. J Pharm Sci 2009, 98:1246-1277.
    • (2009) J Pharm Sci , vol.98 , pp. 1246-1277
    • Weiss, W.F.1    Young, T.M.2    Roberts, C.J.3
  • 13
    • 65549164345 scopus 로고    scopus 로고
    • Static light scattering from concentrated protein solutions. II: Experimental test of theory for protein mixtures and weakly self-associating proteins
    • Fernandez C., Minton A.P. Static light scattering from concentrated protein solutions. II: Experimental test of theory for protein mixtures and weakly self-associating proteins. Biophys J 2009, 96:1992-1998.
    • (2009) Biophys J , vol.96 , pp. 1992-1998
    • Fernandez, C.1    Minton, A.P.2
  • 14
    • 84863491050 scopus 로고    scopus 로고
    • Weak interactions govern the viscosity of concentrated antibody solutions: high-throughput analysis using the diffusion interaction parameter
    • Connolly B.D., Petry C., Yadav S., Demeule B., Ciaccio N., Moore J.M.R., Shire S.J., Gokarn Y.R. Weak interactions govern the viscosity of concentrated antibody solutions: high-throughput analysis using the diffusion interaction parameter. Biophys J 2012, 103:69-78.
    • (2012) Biophys J , vol.103 , pp. 69-78
    • Connolly, B.D.1    Petry, C.2    Yadav, S.3    Demeule, B.4    Ciaccio, N.5    Moore, J.M.R.6    Shire, S.J.7    Gokarn, Y.R.8
  • 16
    • 84881463459 scopus 로고    scopus 로고
    • Small-angle neutron scattering characterization of monoclonal antibody conformations and interactions at high concentrations
    • Yearley E.J., Zarraga I.E., Shire S.J., Scherer T.M., Gokarn Y., Wagner N.J., Liu Y. Small-angle neutron scattering characterization of monoclonal antibody conformations and interactions at high concentrations. Biophys J 2013, 105:720-731.
    • (2013) Biophys J , vol.105 , pp. 720-731
    • Yearley, E.J.1    Zarraga, I.E.2    Shire, S.J.3    Scherer, T.M.4    Gokarn, Y.5    Wagner, N.J.6    Liu, Y.7
  • 17
    • 84886476769 scopus 로고    scopus 로고
    • Intermediate range order and structure in colloidal dispersions with competing interactions
    • Godfrin P.D., Castañeda-Priego R., Liu Y., Wagner N.J. Intermediate range order and structure in colloidal dispersions with competing interactions. J Chem Phys 2013, 139:154904.
    • (2013) J Chem Phys , vol.139 , pp. 154904
    • Godfrin, P.D.1    Castañeda-Priego, R.2    Liu, Y.3    Wagner, N.J.4
  • 18
    • 84863012551 scopus 로고    scopus 로고
    • Distinguishing the monomer to cluster phase transition in concentrated lysozyme solutions by studying the temperature dependence of the short-time dynamics
    • Falus P., Porcar L., Fratini E., Chen W.-R., Faraone A., Hong K., Baglioni P., Liu Y. Distinguishing the monomer to cluster phase transition in concentrated lysozyme solutions by studying the temperature dependence of the short-time dynamics. J Phys Condens Matter: Inst Phys J 2012, 24:064114.
    • (2012) J Phys Condens Matter: Inst Phys J , vol.24 , pp. 064114
    • Falus, P.1    Porcar, L.2    Fratini, E.3    Chen, W.-R.4    Faraone, A.5    Hong, K.6    Baglioni, P.7    Liu, Y.8
  • 19
    • 33751283870 scopus 로고    scopus 로고
    • A small-angle scattering study on equilibrium clusters in lysozyme solutions
    • Stradner A., Cardinaux F., Schurtenberger P. A small-angle scattering study on equilibrium clusters in lysozyme solutions. J Phys Chem B 2006, 110:21222-21231.
    • (2006) J Phys Chem B , vol.110 , pp. 21222-21231
    • Stradner, A.1    Cardinaux, F.2    Schurtenberger, P.3
  • 20
    • 2142700029 scopus 로고    scopus 로고
    • Protein interactions and association: an open challenge for colloid science
    • Piazza R. Protein interactions and association: an open challenge for colloid science. Curr Opin Colloid Interface Sci 2004, 8:515-522.
    • (2004) Curr Opin Colloid Interface Sci , vol.8 , pp. 515-522
    • Piazza, R.1
  • 25
    • 78649892101 scopus 로고    scopus 로고
    • Liquid-liquid phase separation of a monoclonal antibody and nonmonotonic influence of hofmeister anions
    • Mason B.D., Zhang-van Enk J., Zhang L., Remmele R.L., Zhang J. Liquid-liquid phase separation of a monoclonal antibody and nonmonotonic influence of hofmeister anions. Biophys J 2010, 99:3792-3800.
    • (2010) Biophys J , vol.99 , pp. 3792-3800
    • Mason, B.D.1    Zhang-van Enk, J.2    Zhang, L.3    Remmele, R.L.4    Zhang, J.5
  • 26
    • 3242670796 scopus 로고    scopus 로고
    • Opalescent appearance of an IgG1 antibody at high concentrations and its relationship to noncovalent association
    • Sukumar M., Doyle B.L., Combs J.L., Pekar A.H. Opalescent appearance of an IgG1 antibody at high concentrations and its relationship to noncovalent association. Pharm Res 2004, 21:1087-1093.
    • (2004) Pharm Res , vol.21 , pp. 1087-1093
    • Sukumar, M.1    Doyle, B.L.2    Combs, J.L.3    Pekar, A.H.4
  • 28
    • 84862994155 scopus 로고    scopus 로고
    • Thermodynamics of amyloid dissociation provide insights into aggregate stability regimes
    • Brummitt R.K., Andrews J.M., Jordan J.L., Fernandez E.J., Roberts C.J. Thermodynamics of amyloid dissociation provide insights into aggregate stability regimes. Biophys Chem 2012, 168-169:10-18.
    • (2012) Biophys Chem , pp. 10-18
    • Brummitt, R.K.1    Andrews, J.M.2    Jordan, J.L.3    Fernandez, E.J.4    Roberts, C.J.5
  • 29
    • 84894282128 scopus 로고    scopus 로고
    • Aggregates of α-chymotrypsinogen anneal to access more stable states
    • Maurer R.W., Hunter A.K., Robinson A.S., Roberts C.J. Aggregates of α-chymotrypsinogen anneal to access more stable states. Biotechnol Bioeng 2014, 111:782-791.
    • (2014) Biotechnol Bioeng , vol.111 , pp. 782-791
    • Maurer, R.W.1    Hunter, A.K.2    Robinson, A.S.3    Roberts, C.J.4
  • 30
    • 0037420910 scopus 로고    scopus 로고
    • Pressure treatment of tailspike aggregates rapidly produces on-pathway folding intermediates
    • Lefebvre B.G., Robinson A.S. Pressure treatment of tailspike aggregates rapidly produces on-pathway folding intermediates. Biotechnol Bioeng 2003, 82:595-604.
    • (2003) Biotechnol Bioeng , vol.82 , pp. 595-604
    • Lefebvre, B.G.1    Robinson, A.S.2
  • 33
    • 74049123780 scopus 로고    scopus 로고
    • Multi-variate approach to global protein aggregation behavior and kinetics: effects of pH, NaCl, and temperature for α-chymotrypsinogen A
    • Li Y., Ogunnaike B.A., Roberts C.J. Multi-variate approach to global protein aggregation behavior and kinetics: effects of pH, NaCl, and temperature for α-chymotrypsinogen A. J Pharm Sci 2010, 99:645-662.
    • (2010) J Pharm Sci , vol.99 , pp. 645-662
    • Li, Y.1    Ogunnaike, B.A.2    Roberts, C.J.3
  • 34
    • 79954494833 scopus 로고    scopus 로고
    • Nonnative aggregation of an IgG1 antibody in acidic conditions. Part 2: Nucleation and growth kinetics with competing growth mechanisms
    • Brummitt R.K., Nesta D.P., Chang L., Kroetsch A.M., Roberts C.J. Nonnative aggregation of an IgG1 antibody in acidic conditions. Part 2: Nucleation and growth kinetics with competing growth mechanisms. J Pharm Sci 2011, 100:2104-2119.
    • (2011) J Pharm Sci , vol.100 , pp. 2104-2119
    • Brummitt, R.K.1    Nesta, D.P.2    Chang, L.3    Kroetsch, A.M.4    Roberts, C.J.5
  • 35
    • 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 R.L., Liu D., Razinkov V.I., Fernandez E.J., Roberts C.J. Aggregation of anti-streptavidin immunoglobulin gamma-1 involves Fab unfolding and competing growth pathways mediated by pH and salt concentration. Biophys Chem 2013, 172:26-36.
    • (2013) Biophys Chem , vol.172 , pp. 26-36
    • Kim, N.1    Remmele, R.L.2    Liu, D.3    Razinkov, V.I.4    Fernandez, E.J.5    Roberts, C.J.6
  • 37
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • Roberts C.J. Non-native protein aggregation kinetics. Biotechnol Bioeng 2007, 98:927-938.
    • (2007) Biotechnol Bioeng , vol.98 , pp. 927-938
    • Roberts, C.J.1
  • 38
    • 84862876623 scopus 로고    scopus 로고
    • Native-state solubility and transfer free energy as predictive tools for selecting excipients to include in protein formulation development studies
    • Banks D.D., Latypov R.F., Ketchem R.R., Woodard J., Scavezze J.L., Siska C.C., Razinkov V.I. Native-state solubility and transfer free energy as predictive tools for selecting excipients to include in protein formulation development studies. J Pharm Sci 2012, 101:2720-2732.
    • (2012) J Pharm Sci , vol.101 , pp. 2720-2732
    • Banks, D.D.1    Latypov, R.F.2    Ketchem, R.R.3    Woodard, J.4    Scavezze, J.L.5    Siska, C.C.6    Razinkov, V.I.7
  • 39
    • 84902805802 scopus 로고    scopus 로고
    • Therapeutic protein aggregation: mechanisms, design, and control
    • Roberts C.J. Therapeutic protein aggregation: mechanisms, design, and control. Trends Biotechnol 2014, 32:372-380.
    • (2014) Trends Biotechnol , vol.32 , pp. 372-380
    • Roberts, C.J.1
  • 40
    • 37349050368 scopus 로고    scopus 로고
    • A.M. Nonnative protein polymers: structure, morphology, and relation to nucleation and growth
    • Weiss W.F., Hodgdon I.V., Kaler T.K., Lenhoff E.W., Roberts CJ: A.M. Nonnative protein polymers: structure, morphology, and relation to nucleation and growth. Biophys J 2007, 93:4392-4403.
    • (2007) Biophys J , vol.93 , pp. 4392-4403
    • Weiss, W.F.1    Hodgdon, I.V.2    Kaler, T.K.3    Lenhoff, E.W.4    Roberts, C.J.5
  • 41
    • 84874152071 scopus 로고    scopus 로고
    • Do clustering monoclonal antibody solutions really have a concentration dependence of viscosity?
    • Pathak J.A., Sologuren R.R., Narwal R. Do clustering monoclonal antibody solutions really have a concentration dependence of viscosity?. Biophys J 2013, 104:913-923.
    • (2013) Biophys J , vol.104 , pp. 913-923
    • Pathak, J.A.1    Sologuren, R.R.2    Narwal, R.3
  • 43
    • 84890413359 scopus 로고    scopus 로고
    • Renewal of the air-water interface as a critical system parameter of protein stability: aggregation of the human growth hormone and its prevention by surface-active compounds
    • Wiesbauer J., Prassl R., Nidetzky B. Renewal of the air-water interface as a critical system parameter of protein stability: aggregation of the human growth hormone and its prevention by surface-active compounds. Langmuir ACS J Surf Colloids 2013, 29:15240-15250.
    • (2013) Langmuir ACS J Surf Colloids , vol.29 , pp. 15240-15250
    • Wiesbauer, J.1    Prassl, R.2    Nidetzky, B.3
  • 44
    • 84866977081 scopus 로고    scopus 로고
    • Production of particles of therapeutic proteins at the air-water interface during compression/dilation cycles
    • Bee J.S., Schwartz D.K., Trabelsi S., Freund E., Stevenson J.L., Carpenter J.F., Randolph T.W. Production of particles of therapeutic proteins at the air-water interface during compression/dilation cycles. Soft Matter 2012, 8:10329-10335.
    • (2012) Soft Matter , vol.8 , pp. 10329-10335
    • Bee, J.S.1    Schwartz, D.K.2    Trabelsi, S.3    Freund, E.4    Stevenson, J.L.5    Carpenter, J.F.6    Randolph, T.W.7
  • 46
    • 73949093277 scopus 로고    scopus 로고
    • Aggregation of a monoclonal antibody induced by adsorption to stainless steel
    • Bee J.S., Davis M., Freund E., Carpenter J.F., Randolph T.W. Aggregation of a monoclonal antibody induced by adsorption to stainless steel. Biotechnol Bioeng 2009, 105:121-129.
    • (2009) Biotechnol Bioeng , vol.105 , pp. 121-129
    • Bee, J.S.1    Davis, M.2    Freund, E.3    Carpenter, J.F.4    Randolph, T.W.5
  • 50
    • 84866409927 scopus 로고    scopus 로고
    • Differential temperature-dependent multimeric assemblies of replication and repair polymerases on DNA increase processivity
    • Lin H.-K., Chase S.F., Laue T.M., Jen-Jacobson L., Trakselis M.A. Differential temperature-dependent multimeric assemblies of replication and repair polymerases on DNA increase processivity. Biochemistry (Mosc) 2012, 51:7367-7382.
    • (2012) Biochemistry (Mosc) , vol.51 , pp. 7367-7382
    • Lin, H.-K.1    Chase, S.F.2    Laue, T.M.3    Jen-Jacobson, L.4    Trakselis, M.A.5
  • 51
    • 84902214593 scopus 로고    scopus 로고
    • Significance of unfolding thermodynamics for predicting aggregation kinetics: a case study on high concentration solutions of a multi-domain protein
    • Saluja A., Sadineni V., Mungikar A., Nashine V., Kroetsch A., Dahlheim C., Rao V.M. Significance of unfolding thermodynamics for predicting aggregation kinetics: a case study on high concentration solutions of a multi-domain protein. Pharm Res 2014, 10.1007/s11095-013-1263-5.
    • (2014) Pharm Res
    • Saluja, A.1    Sadineni, V.2    Mungikar, A.3    Nashine, V.4    Kroetsch, A.5    Dahlheim, C.6    Rao, V.M.7
  • 52
    • 84879794535 scopus 로고    scopus 로고
    • Non-Arrhenius protein aggregation
    • Wang W., Roberts C.J. Non-Arrhenius protein aggregation. AAPS J 2013, 15:840-851.
    • (2013) AAPS J , vol.15 , pp. 840-851
    • Wang, W.1    Roberts, C.J.2
  • 53
    • 79955591497 scopus 로고    scopus 로고
    • Evaluation of a non-Arrhenius model for therapeutic monoclonal antibody aggregation
    • Kayser V., Chennamsetty N., Voynov V., Helk B., Forrer K., Trout B.L. Evaluation of a non-Arrhenius model for therapeutic monoclonal antibody aggregation. J Pharm Sci 2011, 100:2526-2542.
    • (2011) J Pharm Sci , vol.100 , pp. 2526-2542
    • Kayser, V.1    Chennamsetty, N.2    Voynov, V.3    Helk, B.4    Forrer, K.5    Trout, B.L.6
  • 55
    • 34548427923 scopus 로고    scopus 로고
    • Patterns of protein-protein interactions in salt solutions and implications for protein crystallization
    • Dumetz A.C., Snellinger-O'Brien A.M., Kaler E.W., Lenhoff A.M. Patterns of protein-protein interactions in salt solutions and implications for protein crystallization. Protein Sci 2007, 16:1867-1877.
    • (2007) Protein Sci , vol.16 , pp. 1867-1877
    • Dumetz, A.C.1    Snellinger-O'Brien, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 56
    • 27744488083 scopus 로고    scopus 로고
    • Evaluation of Hofmeister effects on the kinetic stability of proteins
    • Broering J.M., Bommarius A.S. Evaluation of Hofmeister effects on the kinetic stability of proteins. J Phys Chem B 2005, 109:20612-20619.
    • (2005) J Phys Chem B , vol.109 , pp. 20612-20619
    • Broering, J.M.1    Bommarius, A.S.2
  • 57
    • 80052319202 scopus 로고    scopus 로고
    • Osmolyte effects on protein stability and solubility: a balancing act between backbone and side-chains
    • Auton M., Rösgen J., Sinev M., Holthauzen L.M.F., Bolen D.W. Osmolyte effects on protein stability and solubility: a balancing act between backbone and side-chains. Biophys Chem 2011, 159:90-99.
    • (2011) Biophys Chem , vol.159 , pp. 90-99
    • Auton, M.1    Rösgen, J.2    Sinev, M.3    Holthauzen, L.M.F.4    Bolen, D.W.5
  • 58
    • 0035912726 scopus 로고    scopus 로고
    • Partial molar volume, surface area, and hydration changes for equilibrium unfolding and formation of aggregation transition state: high-pressure and cosolute studies on recombinant human IFN-γ
    • Webb J.N., Webb S.D., Cleland J.L., Carpenter J.F., Randolph T.W. Partial molar volume, surface area, and hydration changes for equilibrium unfolding and formation of aggregation transition state: high-pressure and cosolute studies on recombinant human IFN-γ. Proc Natl Acad Sci U S A 2001, 98:7259-7264.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 7259-7264
    • Webb, J.N.1    Webb, S.D.2    Cleland, J.L.3    Carpenter, J.F.4    Randolph, T.W.5
  • 59
    • 33751511950 scopus 로고    scopus 로고
    • Effects of additives on surfactant phase behavior relevant to bacteriorhodopsin crystallization
    • Berger B.W., Gendron C.M., Lenhoff A.M., Kaler E.W. Effects of additives on surfactant phase behavior relevant to bacteriorhodopsin crystallization. Protein Sci 2006, 15:2682-2696.
    • (2006) Protein Sci , vol.15 , pp. 2682-2696
    • Berger, B.W.1    Gendron, C.M.2    Lenhoff, A.M.3    Kaler, E.W.4
  • 60
    • 78751683949 scopus 로고    scopus 로고
    • The morphology and composition of cholesterol-rich micellar nanostructures determine transmembrane protein (GPCR) activity
    • O'Malley M.A., Helgeson M.E., Wagner N.J., Robinson A.S. The morphology and composition of cholesterol-rich micellar nanostructures determine transmembrane protein (GPCR) activity. Biophys J 2011, 100:L11-L13.
    • (2011) Biophys J , vol.100
    • O'Malley, M.A.1    Helgeson, M.E.2    Wagner, N.J.3    Robinson, A.S.4
  • 61
    • 80052976278 scopus 로고    scopus 로고
    • Predicting solution aggregation rates for therapeutic proteins: approaches and challenges
    • Roberts C.J., Das T.K., Sahin E. Predicting solution aggregation rates for therapeutic proteins: approaches and challenges. Int J Pharm 2011, 418:318-333.
    • (2011) Int J Pharm , vol.418 , pp. 318-333
    • Roberts, C.J.1    Das, T.K.2    Sahin, E.3
  • 62
    • 33750955290 scopus 로고    scopus 로고
    • Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization
    • Wakankar A.A., Borchardt R.T. Formulation considerations for proteins susceptible to asparagine deamidation and aspartate isomerization. J Pharm Sci 2006, 95:2321-2336.
    • (2006) J Pharm Sci , vol.95 , pp. 2321-2336
    • Wakankar, A.A.1    Borchardt, R.T.2
  • 63
    • 84895502551 scopus 로고    scopus 로고
    • Oxidation of therapeutic proteins and peptides: structural and biological consequences
    • Torosantucci R., Schöneich C., Jiskoot W. Oxidation of therapeutic proteins and peptides: structural and biological consequences. Pharm Res 2014, 31:541-553.
    • (2014) Pharm Res , vol.31 , pp. 541-553
    • Torosantucci, R.1    Schöneich, C.2    Jiskoot, W.3
  • 65
    • 84883788945 scopus 로고    scopus 로고
    • Effects of temperature and osmolytes on competing degradation routes for an IgG1 antibody
    • Roberts C.J., Nesta D.P., Kim N. Effects of temperature and osmolytes on competing degradation routes for an IgG1 antibody. J Pharm Sci 2013, 102:3556-3566.
    • (2013) J Pharm Sci , vol.102 , pp. 3556-3566
    • Roberts, C.J.1    Nesta, D.P.2    Kim, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.