메뉴 건너뛰기




Volumn 104, Issue 6, 2015, Pages 1885-1898

Developability assessment during the selection of novel therapeutic antibodies

Author keywords

analytical biochemistry; bioinformatics; biotechnology; deamidation; degradation products; immune response; in silico modeling; monoclonal antibody; oxidation; pharmacokinetics

Indexed keywords

ANTIBODY; ASPARAGINE; ASPARTIC ACID; BIOLOGICAL PRODUCT; CYSTEINE; FC RECEPTOR; LYSINE; METHIONINE; THERAPEUTIC ANTIBODY; TRYPTOPHAN; UNCLASSIFIED DRUG; MONOCLONAL ANTIBODY;

EID: 84929179769     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.24430     Document Type: Article
Times cited : (191)

References (137)
  • 1
    • 14844285410 scopus 로고    scopus 로고
    • The therapeutic antibodies market to 2008
    • Pavlou AK, Belsey MJ,. 2005. The therapeutic antibodies market to 2008. Eur J Pharm Biopharm 59: 389-396.
    • (2005) Eur J Pharm Biopharm , vol.59 , pp. 389-396
    • Pavlou, A.K.1    Belsey, M.J.2
  • 2
    • 84871622500 scopus 로고    scopus 로고
    • Therapeutic antibodies: Market considerations, disease targets and bioprocessing
    • Elvin JG, Couston RG, van der Walle CF,. 2013. Therapeutic antibodies: Market considerations, disease targets and bioprocessing. Int J Pharm 440: 83-98.
    • (2013) Int J Pharm , vol.440 , pp. 83-98
    • Elvin, J.G.1    Couston, R.G.2    Van Der Walle, C.F.3
  • 3
    • 33646352962 scopus 로고    scopus 로고
    • Potent antibody therapeutics by design
    • Carter PJ., 2006. Potent antibody therapeutics by design. Nat Rev Immunol 6: 343-357.
    • (2006) Nat Rev Immunol , vol.6 , pp. 343-357
    • Carter, P.J.1
  • 4
    • 33747855481 scopus 로고    scopus 로고
    • Comparing antibody and small-molecule therapies for cancer
    • Imai K, Takaoka A,. 2006. Comparing antibody and small-molecule therapies for cancer. Nat Rev Cancer 6: 714-727.
    • (2006) Nat Rev Cancer , vol.6 , pp. 714-727
    • Imai, K.1    Takaoka, A.2
  • 8
    • 0013473694 scopus 로고    scopus 로고
    • In Monoclonal antibodies: Principles and practice. London, United Kingdom, Academic Press.
    • Goding JW., 1996. Production of monoclonal antibodies. In Monoclonal antibodies: Principles and practice. London, United Kingdom, Academic Press. pp 141-191.
    • (1996) Production of Monoclonal Antibodies , pp. 141-191
    • Goding, J.W.1
  • 10
    • 0036367094 scopus 로고    scopus 로고
    • Rational design of stable lyophilized protein formulations: Theory and practice
    • In; Carpenter J.F. Manning M.C. Eds. 1st ed. New York: Springer Science+Business Media
    • Carpenter J, Chang B, Garzon-Rodriguez W, Randolph T,. 2002. Rational design of stable lyophilized protein formulations: Theory and practice. In Rational design of stable protein formulations: Theory and practice;, Carpenter JF, Manning MC, Eds. 1st ed. New York: Springer Science+Business Media, pp 109-134.
    • (2002) Rational Design of Stable Protein Formulations: Theory and Practice , pp. 109-134
    • Carpenter, J.1    Chang, B.2    Garzon-Rodriguez, W.3    Randolph, T.4
  • 11
    • 84880545300 scopus 로고    scopus 로고
    • Replacing antibodies: Engineering new binding proteins
    • Banta S, Dooley K, Shur O,. 2013. Replacing antibodies: Engineering new binding proteins. Annu Rev Biomed Eng 15: 93-113.
    • (2013) Annu Rev Biomed Eng , vol.15 , pp. 93-113
    • Banta, S.1    Dooley, K.2    Shur, O.3
  • 12
    • 84907904595 scopus 로고    scopus 로고
    • Next-generation optimized biotherapeutics - A review and preclinical study
    • Ueda T., 2014. Next-generation optimized biotherapeutics-A review and preclinical study. Biochim Biophys Acta 1844 (11): 2053-2057.
    • (2014) Biochim Biophys Acta , vol.1844 , Issue.11 , pp. 2053-2057
    • Ueda, T.1
  • 13
    • 60849102193 scopus 로고    scopus 로고
    • Development of novel protein scaffolds as alternatives to whole antibodies for imaging and therapy: Status on discovery research and clinical validation
    • Wurch T, Lowe P, Caussanel V, Bes C, Beck A, Corvaia N,. 2008. Development of novel protein scaffolds as alternatives to whole antibodies for imaging and therapy: Status on discovery research and clinical validation. Curr Pharm Biotechnol 9: 502-509.
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 502-509
    • Wurch, T.1    Lowe, P.2    Caussanel, V.3    Bes, C.4    Beck, A.5    Corvaia, N.6
  • 16
    • 84878370686 scopus 로고    scopus 로고
    • Monoclonal antibody self-association, cluster formation, and rheology at high concentrations
    • Lilyestrom WG, Yadav S, Shire SJ, Scherer TM,. 2013. Monoclonal antibody self-association, cluster formation, and rheology at high concentrations. J Phys Chem B 117: 6373-6384.
    • (2013) J Phys Chem B , vol.117 , pp. 6373-6384
    • Lilyestrom, W.G.1    Yadav, S.2    Shire, S.J.3    Scherer, T.M.4
  • 17
    • 33947688082 scopus 로고    scopus 로고
    • Structural characterization of N-linked oligosaccharides on monoclonal antibody cetuximab by the combination of orthogonal matrix-assisted laser desorption/ionization hybrid quadrupole-quadrupole time-of-flight tandem mass spectrometry and sequential enzymatic digestion
    • Qian J, Liu T, Yang L, Daus A, Crowley R, Zhou Q,. 2007. Structural characterization of N-linked oligosaccharides on monoclonal antibody cetuximab by the combination of orthogonal matrix-assisted laser desorption/ionization hybrid quadrupole-quadrupole time-of-flight tandem mass spectrometry and sequential enzymatic digestion. Anal Biochem 364: 8-18.
    • (2007) Anal Biochem , vol.364 , pp. 8-18
    • Qian, J.1    Liu, T.2    Yang, L.3    Daus, A.4    Crowley, R.5    Zhou, Q.6
  • 19
    • 0033558335 scopus 로고    scopus 로고
    • Position effects of variable region carbohydrate on the affinity and in vivo behavior of an anti-(1->6) dextran antibody
    • Coloma MJ, Trinh RK, Martinez AR, Morrison SL,. 1999. Position effects of variable region carbohydrate on the affinity and in vivo behavior of an anti-(1->6) dextran antibody. J Immunol 162: 2162-2170.
    • (1999) J Immunol , vol.162 , pp. 2162-2170
    • Coloma, M.J.1    Trinh, R.K.2    Martinez, A.R.3    Morrison, S.L.4
  • 20
    • 31844447560 scopus 로고    scopus 로고
    • Impact of variable domain glycosylation on antibody clearance: An LC/MS characterization
    • Huang L, Biolsi S, Bales KR, Kuchibhotla U,. 2006. Impact of variable domain glycosylation on antibody clearance: An LC/MS characterization. Anal Biochem 349: 197-207.
    • (2006) Anal Biochem , vol.349 , pp. 197-207
    • Huang, L.1    Biolsi, S.2    Bales, K.R.3    Kuchibhotla, U.4
  • 22
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • Jefferis R., 2005. Glycosylation of recombinant antibody therapeutics. Biotechnol Prog 21: 11-16.
    • (2005) Biotechnol Prog , vol.21 , pp. 11-16
    • Jefferis, R.1
  • 23
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Gavel Y, von HG,. 1990. Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering. Protein Eng 3: 433-442.
    • (1990) Protein Eng , vol.3 , pp. 433-442
    • Gavel, Y.1    Von, H.G.2
  • 24
    • 1342327544 scopus 로고    scopus 로고
    • Statistical analysis of the protein environment of N-glycosylation sites: Implications for occupancy, structure, and folding
    • Petrescu AJ, Milac AL, Petrescu SM, Dwek RA, Wormald MR,. 2004. Statistical analysis of the protein environment of N-glycosylation sites: Implications for occupancy, structure, and folding. Glycobiology 14: 103-114.
    • (2004) Glycobiology , vol.14 , pp. 103-114
    • Petrescu, A.J.1    Milac, A.L.2    Petrescu, S.M.3    Dwek, R.A.4    Wormald, M.R.5
  • 25
    • 73149121904 scopus 로고    scopus 로고
    • Impact of molecular processing in the hinge region of therapeutic IgG4 antibodies on disposition profiles in cynomolgus monkeys
    • Stubenrauch K, Wessels U, Regula JT, Kettenberger H, Schleypen J, Kohnert U,. 2010. Impact of molecular processing in the hinge region of therapeutic IgG4 antibodies on disposition profiles in cynomolgus monkeys. Drug Metab Dispos 38: 84-91.
    • (2010) Drug Metab Dispos , vol.38 , pp. 84-91
    • Stubenrauch, K.1    Wessels, U.2    Regula, J.T.3    Kettenberger, H.4    Schleypen, J.5    Kohnert, U.6
  • 26
    • 79954492422 scopus 로고    scopus 로고
    • Characterization and comparison of disulfide linkages and scrambling patterns in therapeutic monoclonal antibodies: Using LC-MS with electron transfer dissociation
    • Wang Y, Lu Q, Wu SL, Karger BL, Hancock WS,. 2011. Characterization and comparison of disulfide linkages and scrambling patterns in therapeutic monoclonal antibodies: Using LC-MS with electron transfer dissociation. Anal Chem 83: 3133-3140.
    • (2011) Anal Chem , vol.83 , pp. 3133-3140
    • Wang, Y.1    Lu, Q.2    Wu, S.L.3    Karger, B.L.4    Hancock, W.S.5
  • 29
    • 79955577669 scopus 로고    scopus 로고
    • Characterization of site-specific glycation during process development of a human therapeutic monoclonal antibody
    • Miller AK, Hambly DM, Kerwin BA, Treuheit MJ, Gadgil HS,. 2011. Characterization of site-specific glycation during process development of a human therapeutic monoclonal antibody. J Pharm Sci 100: 2543-2550.
    • (2011) J Pharm Sci , vol.100 , pp. 2543-2550
    • Miller, A.K.1    Hambly, D.M.2    Kerwin, B.A.3    Treuheit, M.J.4    Gadgil, H.S.5
  • 30
    • 37749041309 scopus 로고    scopus 로고
    • A study in glycation of a therapeutic recombinant humanized monoclonal antibody: Where it is, how it got there, and how it affects charge-based behavior
    • Quan C, Alcala E, Petkovska I, Matthews D, Canova-Davis E, Taticek R, Ma S,. 2008. A study in glycation of a therapeutic recombinant humanized monoclonal antibody: Where it is, how it got there, and how it affects charge-based behavior. Anal Biochem 373: 179-191.
    • (2008) Anal Biochem , vol.373 , pp. 179-191
    • Quan, C.1    Alcala, E.2    Petkovska, I.3    Matthews, D.4    Canova-Davis, E.5    Taticek, R.6    Ma, S.7
  • 34
    • 50349097199 scopus 로고    scopus 로고
    • Glycation during storage and administration of monoclonal antibody formulations
    • Fischer S, Hoernschemeyer J, Mahler HC,. 2008. Glycation during storage and administration of monoclonal antibody formulations. Eur J Pharm Biopharm 70: 42-50.
    • (2008) Eur J Pharm Biopharm , vol.70 , pp. 42-50
    • Fischer, S.1    Hoernschemeyer, J.2    Mahler, H.C.3
  • 35
    • 77958589701 scopus 로고    scopus 로고
    • Recovery and purification process development for monoclonal antibody production
    • Liu HF, Ma J, Winter C, Bayer R,. 2010. Recovery and purification process development for monoclonal antibody production. MAbs 2: 480-499.
    • (2010) MAbs , vol.2 , pp. 480-499
    • Liu, H.F.1    Ma, J.2    Winter, C.3    Bayer, R.4
  • 42
    • 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 Sci 20: 580-587.
    • (2011) Protein Sci , vol.20 , 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
  • 43
    • 84855901823 scopus 로고    scopus 로고
    • Antibody solubility behavior in monovalent salt solutions reveals specific anion effects at low ionic strength
    • Zhang L, Tan H, Fesinmeyer RM, Li C, Catrone D, Le D, Remmele RL Jr, Zhang J,. 2012. Antibody solubility behavior in monovalent salt solutions reveals specific anion effects at low ionic strength. J Pharm Sci 101: 965-977.
    • (2012) J Pharm Sci , vol.101 , pp. 965-977
    • Zhang, L.1    Tan, H.2    Fesinmeyer, R.M.3    Li, C.4    Catrone, D.5    Le, D.6    Remmele, Jr.R.L.7    Zhang, J.8
  • 44
    • 84896059845 scopus 로고    scopus 로고
    • Dipole-dipole interaction in antibody solutions: Correlation with viscosity behavior at high concentration
    • Singh SN, Yadav S, Shire SJ, Kalonia DS,. 2014. Dipole-dipole interaction in antibody solutions: Correlation with viscosity behavior at high concentration. Pharm Res 31: 2549-2558.
    • (2014) Pharm Res , vol.31 , pp. 2549-2558
    • Singh, S.N.1    Yadav, S.2    Shire, S.J.3    Kalonia, D.S.4
  • 45
    • 84859327683 scopus 로고    scopus 로고
    • The influence of charge distribution on self-association and viscosity behavior of monoclonal antibody solutions
    • Yadav S, Laue TM, Kalonia DS, Singh SN, Shire SJ,. 2012. The influence of charge distribution on self-association and viscosity behavior of monoclonal antibody solutions. Mol Pharm 9: 791-802.
    • (2012) Mol Pharm , vol.9 , pp. 791-802
    • Yadav, S.1    Laue, T.M.2    Kalonia, D.S.3    Singh, S.N.4    Shire, S.J.5
  • 46
    • 79959871746 scopus 로고    scopus 로고
    • Establishing a link between amino acid sequences and self-associating and viscoelastic behavior of two closely related monoclonal antibodies
    • Yadav S, Sreedhara A, Kanai S, Liu J, Lien S, Lowman H, Kalonia DS, Shire SJ,. 2011. Establishing a link between amino acid sequences and self-associating and viscoelastic behavior of two closely related monoclonal antibodies. Pharm Res 28: 1750-1764.
    • (2011) Pharm Res , vol.28 , pp. 1750-1764
    • Yadav, S.1    Sreedhara, A.2    Kanai, S.3    Liu, J.4    Lien, S.5    Lowman, H.6    Kalonia, D.S.7    Shire, S.J.8
  • 47
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation
    • Geiger T, Clarke S,. 1987. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. J Biol Chem 262: 785-794.
    • (1987) J Biol Chem , vol.262 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 48
    • 27644506040 scopus 로고    scopus 로고
    • Studies on the mechanism of aspartic acid cleavage and glutamine deamidation in the acidic degradation of glucagon
    • Joshi AB, Sawai M, Kearney WR, Kirsch LE,. 2005. Studies on the mechanism of aspartic acid cleavage and glutamine deamidation in the acidic degradation of glucagon. J Pharm Sci 94: 1912-1927.
    • (2005) J Pharm Sci , vol.94 , pp. 1912-1927
    • Joshi, A.B.1    Sawai, M.2    Kearney, W.R.3    Kirsch, L.E.4
  • 49
    • 0023464863 scopus 로고
    • Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins
    • Clarke S., 1987. Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins. Int J Pept Protein Res 30: 808-821.
    • (1987) Int J Pept Protein Res , vol.30 , pp. 808-821
    • Clarke, S.1
  • 50
    • 69649088633 scopus 로고    scopus 로고
    • Human antibody Fc deamidation in vivo
    • Liu YD, van Enk JZ, Flynn GC,. 2009. Human antibody Fc deamidation in vivo. Biologicals 37: 313-322.
    • (2009) Biologicals , vol.37 , pp. 313-322
    • Liu, Y.D.1    Van Enk, J.Z.2    Flynn, G.C.3
  • 51
    • 14744268457 scopus 로고    scopus 로고
    • In vivo deamidation characterization of monoclonal antibody by LC/MS/MS
    • Huang L, Lu J, Wroblewski VJ, Beals JM, Riggin RM,. 2005. In vivo deamidation characterization of monoclonal antibody by LC/MS/MS. Anal Chem 77: 1432-1439.
    • (2005) Anal Chem , vol.77 , pp. 1432-1439
    • Huang, L.1    Lu, J.2    Wroblewski, V.J.3    Beals, J.M.4    Riggin, R.M.5
  • 52
    • 33749860977 scopus 로고    scopus 로고
    • Post-translational modifications in the context of therapeutic proteins
    • Walsh G, Jefferis R,. 2006. Post-translational modifications in the context of therapeutic proteins. Nat Biotech 24: 1241-1252.
    • (2006) Nat Biotech , vol.24 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 55
    • 0030022071 scopus 로고    scopus 로고
    • Isomerization of an aspartic acid residue in the complementarity-determining regions of a recombinant antibody to human IgE: Identification and effect on binding affinity
    • Cacia J, Keck R, Presta LG, Frenz J,. 1996. Isomerization of an aspartic acid residue in the complementarity-determining regions of a recombinant antibody to human IgE: Identification and effect on binding affinity. Biochemistry 35: 1897-1903.
    • (1996) Biochemistry , vol.35 , pp. 1897-1903
    • Cacia, J.1    Keck, R.2    Presta, L.G.3    Frenz, J.4
  • 58
    • 84860567341 scopus 로고    scopus 로고
    • Characterization of the isomerization products of aspartate residues at two different sites in a monoclonal antibody
    • Sreedhara A, Cordoba A, Zhu Q, Kwong J, Liu J,. 2012. Characterization of the isomerization products of aspartate residues at two different sites in a monoclonal antibody. Pharm Res 29: 187-197.
    • (2012) Pharm Res , vol.29 , pp. 187-197
    • Sreedhara, A.1    Cordoba, A.2    Zhu, Q.3    Kwong, J.4    Liu, J.5
  • 59
    • 33846967443 scopus 로고    scopus 로고
    • Aspartate isomerization in the complementarity-determining regions of two closely related monoclonal antibodies
    • Wakankar AA, Borchardt RT, Eigenbrot C, Shia S, Wang YJ, Shire SJ, Liu JL,. 2007. Aspartate isomerization in the complementarity-determining regions of two closely related monoclonal antibodies. Biochemistry 46: 1534-1544.
    • (2007) Biochemistry , vol.46 , pp. 1534-1544
    • Wakankar, A.A.1    Borchardt, R.T.2    Eigenbrot, C.3    Shia, S.4    Wang, Y.J.5    Shire, S.J.6    Liu, J.L.7
  • 60
    • 34249059679 scopus 로고    scopus 로고
    • Accumulation of succinimide in a recombinant monoclonal antibody in mildly acidic buffers under elevated temperatures
    • Chu GC, Chelius D, Xiao G, Khor HK, Coulibaly S, Bondarenko PV,. 2007. Accumulation of succinimide in a recombinant monoclonal antibody in mildly acidic buffers under elevated temperatures. Pharm Res 24: 1145-1156.
    • (2007) Pharm Res , vol.24 , pp. 1145-1156
    • Chu, G.C.1    Chelius, D.2    Xiao, G.3    Khor, H.K.4    Coulibaly, S.5    Bondarenko, P.V.6
  • 63
    • 78149352601 scopus 로고    scopus 로고
    • State of the art and challenges in sequence based T-cell epitope prediction
    • Lundegaard C, Hoof I, Lund O, Nielsen M,. 2010. State of the art and challenges in sequence based T-cell epitope prediction. Immunome Res 6 (Suppl 2): S3.
    • (2010) Immunome Res , vol.6 , pp. S3
    • Lundegaard, C.1    Hoof, I.2    Lund, O.3    Nielsen, M.4
  • 65
    • 7944224384 scopus 로고    scopus 로고
    • Discovery of promiscuous HLA-II-restricted T cell epitopes with TEPITOPE
    • Bian H, Hammer J,. 2004. Discovery of promiscuous HLA-II-restricted T cell epitopes with TEPITOPE. Methods 34: 468-475.
    • (2004) Methods , vol.34 , pp. 468-475
    • Bian, H.1    Hammer, J.2
  • 66
    • 44649167715 scopus 로고    scopus 로고
    • Application of machine learning techniques in predicting MHC binders
    • Lata S, Bhasin M, Raghava GP,. 2007. Application of machine learning techniques in predicting MHC binders. Methods Mol Biol 409: 201-215.
    • (2007) Methods Mol Biol , vol.409 , pp. 201-215
    • Lata, S.1    Bhasin, M.2    Raghava, G.P.3
  • 68
    • 0033849945 scopus 로고    scopus 로고
    • A kinetic model of vertebrate 20S proteasome accounting for the generation of major proteolytic fragments from oligomeric peptide substrates
    • Holzhutter HG, Kloetzel PM,. 2000. A kinetic model of vertebrate 20S proteasome accounting for the generation of major proteolytic fragments from oligomeric peptide substrates. Biophys J 79: 1196-1205.
    • (2000) Biophys J , vol.79 , pp. 1196-1205
    • Holzhutter, H.G.1    Kloetzel, P.M.2
  • 69
    • 3042697402 scopus 로고    scopus 로고
    • A novel predictive technique for the MHC class II peptide-binding interaction
    • Davies MN, Sansom CE, Beazley C, Moss DS,. 2003. A novel predictive technique for the MHC class II peptide-binding interaction. Mol Med 9: 220-225.
    • (2003) Mol Med , vol.9 , pp. 220-225
    • Davies, M.N.1    Sansom, C.E.2    Beazley, C.3    Moss, D.S.4
  • 70
    • 0030890660 scopus 로고    scopus 로고
    • An interactive web site providing major histocompatibility ligand predictions: Application to HIV research
    • De Groot AS, Jesdale BM, Szu E, Schafer JR, Chicz RM, Deocampo G,. 1997. An interactive web site providing major histocompatibility ligand predictions: Application to HIV research. AIDS Res Hum Retroviruses 13: 529-531.
    • (1997) AIDS Res Hum Retroviruses , vol.13 , pp. 529-531
    • Groot As, D.1    Jesdale, B.M.2    Szu, E.3    Schafer, J.R.4    Chicz, R.M.5    Deocampo, G.6
  • 71
    • 33747839161 scopus 로고    scopus 로고
    • SVMHC: A server for prediction of MHC-binding peptides
    • Donnes P, Kohlbacher O,. 2006. SVMHC: A server for prediction of MHC-binding peptides. Nucleic Acids Res 34: W194-W197.
    • (2006) Nucleic Acids Res , vol.34 , pp. W194-W197
    • Donnes, P.1    Kohlbacher, O.2
  • 73
    • 0037163034 scopus 로고    scopus 로고
    • The influence of protein structure on the products emerging from succinimide hydrolysis
    • Athmer L, Kindrachuk J, Georges F, Napper S,. 2002. The influence of protein structure on the products emerging from succinimide hydrolysis. J Biol Chem 277: 30502-30507.
    • (2002) J Biol Chem , vol.277 , pp. 30502-30507
    • Athmer, L.1    Kindrachuk, J.2    Georges, F.3    Napper, S.4
  • 74
    • 67749109890 scopus 로고    scopus 로고
    • Effect of protein structure on deamidation rate in the Fc fragment of an IgG1 monoclonal antibody
    • Sinha S, Zhang L, Duan S, Williams TD, Vlasak J, Ionescu R, Topp EM,. 2009. Effect of protein structure on deamidation rate in the Fc fragment of an IgG1 monoclonal antibody. Protein Sci 18: 1573-1584.
    • (2009) Protein Sci , vol.18 , pp. 1573-1584
    • Sinha, S.1    Zhang, L.2    Duan, S.3    Williams, T.D.4    Vlasak, J.5    Ionescu, R.6    Topp, E.M.7
  • 75
    • 61649094568 scopus 로고    scopus 로고
    • Deamidation of asparagine residues: Direct hydrolysis versus succinimide-mediated deamidation mechanisms
    • Catak S, Monard G, Aviyente V, Ruiz-Lopez MF,. 2009. Deamidation of asparagine residues: Direct hydrolysis versus succinimide-mediated deamidation mechanisms. J Phys Chem A 113: 1111-1120.
    • (2009) J Phys Chem A , vol.113 , pp. 1111-1120
    • Catak, S.1    Monard, G.2    Aviyente, V.3    Mf, R.-L.4
  • 76
    • 84903711520 scopus 로고    scopus 로고
    • Characterization of asparagine 330 deamidation in an Fc-fragment of IgG1 using cation exchange chromatography and peptide mapping
    • Zhang YT, Hu J, Pace AL, Wong R, Wang YJ, Kao YH,. 2014. Characterization of asparagine 330 deamidation in an Fc-fragment of IgG1 using cation exchange chromatography and peptide mapping. J Chromatogr B Analyt Technol Biomed Life Sci 965C: 65-71.
    • (2014) J Chromatogr B Analyt Technol Biomed Life Sci , vol.965 C , pp. 65-71
    • Zhang, Y.T.1    Hu, J.2    Pace, A.L.3    Wong, R.4    Wang, Y.J.5    Kao, Y.H.6
  • 77
    • 84896793782 scopus 로고    scopus 로고
    • Hexyl glucoside and hexyl maltoside inhibit light-induced oxidation of tryptophan
    • Adem YT, Molina P, Liu H, Patapoff TW, Sreedhara A, Esue O,. 2014. Hexyl glucoside and hexyl maltoside inhibit light-induced oxidation of tryptophan. J Pharm Sci 103: 409-416.
    • (2014) J Pharm Sci , vol.103 , pp. 409-416
    • Adem, Y.T.1    Molina, P.2    Liu, H.3    Patapoff, T.W.4    Sreedhara, A.5    Esue, O.6
  • 78
    • 79955601001 scopus 로고    scopus 로고
    • The degradation of polysorbates 20 and 80 and its potential impact on the stability of biotherapeutics
    • Kishore RS, Kiese S, Fischer S, Pappenberger A, Grauschopf U, Mahler HC,. 2011. The degradation of polysorbates 20 and 80 and its potential impact on the stability of biotherapeutics. Pharm Res 28: 1194-1210.
    • (2011) Pharm Res , vol.28 , pp. 1194-1210
    • Kishore, R.S.1    Kiese, S.2    Fischer, S.3    Pappenberger, A.4    Grauschopf, U.5    Mahler, H.C.6
  • 79
    • 80054773616 scopus 로고    scopus 로고
    • Site-specific tryptophan oxidation induced by autocatalytic reaction of polysorbate 20 in protein formulation
    • Lam XM, Lai WG, Chan EK, Ling V, Hsu CC,. 2011. Site-specific tryptophan oxidation induced by autocatalytic reaction of polysorbate 20 in protein formulation. Pharm Res 28: 2543-2555.
    • (2011) Pharm Res , vol.28 , pp. 2543-2555
    • Lam, X.M.1    Lai, W.G.2    Chan, E.K.3    Ling, V.4    Hsu, C.C.5
  • 80
    • 84895502551 scopus 로고    scopus 로고
    • Oxidation of therapeutic proteins and peptides: Structural and biological consequences
    • Torosantucci R, Schoneich C, Jiskoot W,. 2014. Oxidation of therapeutic proteins and peptides: Structural and biological consequences. Pharm Res 31: 541-553.
    • (2014) Pharm Res , vol.31 , pp. 541-553
    • Torosantucci, R.1    Schoneich, C.2    Jiskoot, W.3
  • 81
    • 84864485477 scopus 로고    scopus 로고
    • Chemical modifications in aggregates of recombinant human insulin induced by metal-catalyzed oxidation: Covalent cross-linking via michael addition to tyrosine oxidation products
    • Torosantucci R, Mozziconacci O, Sharov V, Schoneich C, Jiskoot W,. 2012. Chemical modifications in aggregates of recombinant human insulin induced by metal-catalyzed oxidation: Covalent cross-linking via michael addition to tyrosine oxidation products. Pharm Res 29: 2276-2293.
    • (2012) Pharm Res , vol.29 , pp. 2276-2293
    • Torosantucci, R.1    Mozziconacci, O.2    Sharov, V.3    Schoneich, C.4    Jiskoot, W.5
  • 82
    • 84878643485 scopus 로고    scopus 로고
    • Identification of oxidation sites and covalent cross-links in metal catalyzed oxidized interferon beta-1a: Potential implications for protein aggregation and immunogenicity
    • Torosantucci R, Sharov VS, van BM, Brinks V, Schoneich C, Jiskoot W,. 2013. Identification of oxidation sites and covalent cross-links in metal catalyzed oxidized interferon beta-1a: Potential implications for protein aggregation and immunogenicity. Mol Pharm 10: 2311-2322.
    • (2013) Mol Pharm , vol.10 , pp. 2311-2322
    • Torosantucci, R.1    Sharov, V.S.2    Van, B.M.3    Brinks, V.4    Schoneich, C.5    Jiskoot, W.6
  • 83
    • 84904357557 scopus 로고    scopus 로고
    • Characterization of the degradation products of a color-changed monoclonal antibody: Tryptophan-derived chromophores
    • Li Y, Polozova A, Gruia F, Feng J,. 2014. Characterization of the degradation products of a color-changed monoclonal antibody: Tryptophan-derived chromophores. Anal Chem 86: 6850-6857.
    • (2014) Anal Chem , vol.86 , pp. 6850-6857
    • Li, Y.1    Polozova, A.2    Gruia, F.3    Feng, J.4
  • 84
    • 0030965970 scopus 로고    scopus 로고
    • Disrupting the hydrophobic patches at the antibody variable/constant domain interface: Improved in vivo folding and physical characterization of an engineered scFv fragment
    • Nieba L, Honegger A, Krebber C, Pluckthun A,. 1997. Disrupting the hydrophobic patches at the antibody variable/constant domain interface: Improved in vivo folding and physical characterization of an engineered scFv fragment. Protein Eng 10: 435-444.
    • (1997) Protein Eng , vol.10 , pp. 435-444
    • Nieba, L.1    Honegger, A.2    Krebber, C.3    Pluckthun, A.4
  • 85
    • 8344287523 scopus 로고    scopus 로고
    • A structural and mechanistic study of the oxidation of methionine residues in hPTH(1-34) via experiments and simulations
    • Chu JW, Yin J, Wang DI, Trout BL,. 2004. A structural and mechanistic study of the oxidation of methionine residues in hPTH(1-34) via experiments and simulations. Biochemistry 43: 14139-14148.
    • (2004) Biochemistry , vol.43 , pp. 14139-14148
    • Chu, J.W.1    Yin, J.2    Wang, D.I.3    Trout, B.L.4
  • 86
    • 71649111656 scopus 로고    scopus 로고
    • Methionine, tryptophan, and histidine oxidation in a model protein, PTH: Mechanisms and stabilization
    • Ji JA, Zhang B, Cheng W, Wang YJ,. 2009. Methionine, tryptophan, and histidine oxidation in a model protein, PTH: Mechanisms and stabilization. J Pharm Sci 98: 4485-4500.
    • (2009) J Pharm Sci , vol.98 , pp. 4485-4500
    • Ji, J.A.1    Zhang, B.2    Cheng, W.3    Wang, Y.J.4
  • 88
    • 4644319116 scopus 로고    scopus 로고
    • Stabilizing mechanisms in commercial albumin preparations: Octanoate and N-acetyl-L-tryptophanate protect human serum albumin against heat and oxidative stress
    • Anraku M, Tsurusaki Y, Watanabe H, Maruyama T, Kragh-Hansen U, Otagiri M,. 2004. Stabilizing mechanisms in commercial albumin preparations: Octanoate and N-acetyl-L-tryptophanate protect human serum albumin against heat and oxidative stress. Biochim Biophys Acta 1702: 9-17.
    • (2004) Biochim Biophys Acta , vol.1702 , pp. 9-17
    • Anraku, M.1    Tsurusaki, Y.2    Watanabe, H.3    Maruyama, T.4    Kragh-Hansen, U.5    Otagiri, M.6
  • 89
    • 34250797997 scopus 로고    scopus 로고
    • Enrichment and analysis of nonenzymatically glycated peptides: Boronate affinity chromatography coupled with electron-transfer dissociation mass spectrometry
    • Zhang Q, Tang N, Brock JW, Mottaz HM, Ames JM, Baynes JW, Smith RD, Metz TO,. 2007. Enrichment and analysis of nonenzymatically glycated peptides: Boronate affinity chromatography coupled with electron-transfer dissociation mass spectrometry. J Proteome Res 6: 2323-2330.
    • (2007) J Proteome Res , vol.6 , pp. 2323-2330
    • Zhang, Q.1    Tang, N.2    Brock, J.W.3    Mottaz, H.M.4    Ames, J.M.5    Baynes, J.W.6    Smith, R.D.7    Metz, T.O.8
  • 90
    • 84922608590 scopus 로고    scopus 로고
    • Modulation of hydrophobic interactions by proximally immobilized ions
    • Ma CD, Wang C, cevedo-Velez C, Gellman SH, Abbott NL,. 2015. Modulation of hydrophobic interactions by proximally immobilized ions. Nature 517: 347-350.
    • (2015) Nature , vol.517 , pp. 347-350
    • Ma, C.D.1    Wang, C.2    Cevedo-Velez, C.3    Gellman, S.H.4    Abbott, N.L.5
  • 92
    • 84867016746 scopus 로고    scopus 로고
    • Aggregation-resistant domain antibodies engineered with charged mutations near the edges of the complementarity-determining regions
    • Perchiacca JM, Ladiwala AR, Bhattacharya M, Tessier PM,. 2012. Aggregation-resistant domain antibodies engineered with charged mutations near the edges of the complementarity-determining regions. Protein Eng Des Sel 25: 591-601.
    • (2012) Protein Eng des Sel , vol.25 , pp. 591-601
    • Perchiacca, J.M.1    Ladiwala, A.R.2    Bhattacharya, M.3    Tessier, P.M.4
  • 93
    • 84903764911 scopus 로고    scopus 로고
    • Separation of mAbs molecular variants by analytical hydrophobic interaction chromatography HPLC: Overview and applications
    • Haverick M, Mengisen S, Shameem M, Ambrogelly A,. 2014. Separation of mAbs molecular variants by analytical hydrophobic interaction chromatography HPLC: Overview and applications. MAbs 6: 852-858.
    • (2014) MAbs , vol.6 , pp. 852-858
    • Haverick, M.1    Mengisen, S.2    Shameem, M.3    Ambrogelly, A.4
  • 94
    • 0035805436 scopus 로고    scopus 로고
    • Hydrophobic interaction chromatography of proteins
    • Queiroz JA, Tomaz CT, Cabral JM,. 2001. Hydrophobic interaction chromatography of proteins. J Biotechnol 87: 143-159.
    • (2001) J Biotechnol , vol.87 , pp. 143-159
    • Queiroz, J.A.1    Tomaz, C.T.2    Cabral, J.M.3
  • 98
    • 0242515822 scopus 로고    scopus 로고
    • Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor
    • Chi EY, Krishnan S, Kendrick BS, Chang BS, Carpenter JF, Randolph TW,. 2003. Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Protein Sci 12: 903-913.
    • (2003) Protein Sci , vol.12 , pp. 903-913
    • Chi, E.Y.1    Krishnan, S.2    Kendrick, B.S.3    Chang, B.S.4    Carpenter, J.F.5    Randolph, T.W.6
  • 99
    • 84897897035 scopus 로고    scopus 로고
    • Gauging colloidal and thermal stability in human IgG1-sugar solutions through diffusivity measurements
    • Rubin J, Sharma A, Linden L, Bommarius AS, Behrens SH,. 2014. Gauging colloidal and thermal stability in human IgG1-sugar solutions through diffusivity measurements. J Phys Chem B 118: 2803-2809.
    • (2014) J Phys Chem B , vol.118 , pp. 2803-2809
    • Rubin, J.1    Sharma, A.2    Linden, L.3    Bommarius, A.S.4    Behrens, S.H.5
  • 100
    • 84892936418 scopus 로고    scopus 로고
    • Understanding the relevance of local conformational stability and dynamics to the aggregation propensity of an IgG1 and IgG2 monoclonal antibodies
    • Thakkar SV, Sahni N, Joshi SB, Kerwin BA, He F, Volkin DB, Middaugh CR,. 2013. Understanding the relevance of local conformational stability and dynamics to the aggregation propensity of an IgG1 and IgG2 monoclonal antibodies. Protein Sci 22: 1295-1305.
    • (2013) Protein Sci , vol.22 , pp. 1295-1305
    • Thakkar, S.V.1    Sahni, N.2    Joshi, S.B.3    Kerwin, B.A.4    He, F.5    Volkin, D.B.6    Middaugh, C.R.7
  • 101
    • 0037227517 scopus 로고    scopus 로고
    • Biophysical properties of human antibody variable domains
    • Ewert S, Huber T, Honegger A, Pluckthun A,. 2003. Biophysical properties of human antibody variable domains. J Mol Biol 325: 531-553.
    • (2003) J Mol Biol , vol.325 , pp. 531-553
    • Ewert, S.1    Huber, T.2    Honegger, A.3    Pluckthun, A.4
  • 102
    • 84855575327 scopus 로고    scopus 로고
    • A screening tool for therapeutic monoclonal antibodies: Identifying the most stable protein and its best formulation based on thioflavin T binding
    • Kayser V, Chennamsetty N, Voynov V, Helk B, Forrer K, Trout BL,. 2012. A screening tool for therapeutic monoclonal antibodies: Identifying the most stable protein and its best formulation based on thioflavin T binding. Biotechnol J 7: 127-132.
    • (2012) Biotechnol J , vol.7 , pp. 127-132
    • Kayser, V.1    Chennamsetty, N.2    Voynov, V.3    Helk, B.4    Forrer, K.5    Trout, B.L.6
  • 103
    • 84880161443 scopus 로고    scopus 로고
    • Frontier of therapeutic antibody discovery: The challenges and how to face them
    • Lu ZJ, Deng SJ, Huang DG, He Y, Lei M, Zhou L, Jin P,. 2012. Frontier of therapeutic antibody discovery: The challenges and how to face them. World J Biol Chem 3: 187-196.
    • (2012) World J Biol Chem , vol.3 , pp. 187-196
    • Lu, Z.J.1    Deng, S.J.2    Huang, D.G.3    He, Y.4    Lei, M.5    Zhou, L.6    Jin, P.7
  • 104
    • 77949789023 scopus 로고    scopus 로고
    • High throughput thermostability screening of monoclonal antibody formulations
    • He F, Hogan S, Latypov RF, Narhi LO, Razinkov VI,. 2010. High throughput thermostability screening of monoclonal antibody formulations. J Pharm Sci 99: 1707-1720.
    • (2010) J Pharm Sci , vol.99 , pp. 1707-1720
    • He, F.1    Hogan, S.2    Latypov, R.F.3    Narhi, L.O.4    Razinkov, V.I.5
  • 105
    • 0035933314 scopus 로고    scopus 로고
    • The alternatively folded state of the antibody C(H)3 domain
    • Thies MJ, Kammermeier R, Richter K, Buchner J,. 2001. The alternatively folded state of the antibody C(H)3 domain. J Mol Biol 309: 1077-1085.
    • (2001) J Mol Biol , vol.309 , pp. 1077-1085
    • Thies, M.J.1    Kammermeier, R.2    Richter, K.3    Buchner, J.4
  • 106
    • 0026792807 scopus 로고
    • A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies
    • Buchner J, Pastan I, Brinkmann U,. 1992. A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies. Anal Biochem 205: 263-270.
    • (1992) Anal Biochem , vol.205 , pp. 263-270
    • Buchner, J.1    Pastan, I.2    Brinkmann, U.3
  • 107
    • 0034076282 scopus 로고    scopus 로고
    • The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein
    • Vermeer AW, Norde W,. 2000. The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein. Biophys J 78: 394-404.
    • (2000) Biophys J , vol.78 , pp. 394-404
    • Vermeer, A.W.1    Norde, W.2
  • 108
    • 0006454079 scopus 로고
    • Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • Buchner J, Rudolph R,. 1991. Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Biotechnology (NY) 9: 157-162.
    • (1991) Biotechnology (NY) , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 109
    • 84873743043 scopus 로고    scopus 로고
    • Differential scanning fluorimetry: Rapid screening of formulations that promote the stability of reference preparations
    • Malik K, Matejtschuk P, Thelwell C, Burns CJ,. 2013. Differential scanning fluorimetry: Rapid screening of formulations that promote the stability of reference preparations. J Pharm Biomed Anal 77: 163-166.
    • (2013) J Pharm Biomed Anal , vol.77 , pp. 163-166
    • Malik, K.1    Matejtschuk, P.2    Thelwell, C.3    Burns, C.J.4
  • 110
    • 84921021627 scopus 로고    scopus 로고
    • Concomitant Raman spectroscopy and dynamic light scattering for characterization of therapeutic proteins at high concentrations
    • Zhou C, Qi W, Neil LE, Carpenter JF,. 2015. Concomitant Raman spectroscopy and dynamic light scattering for characterization of therapeutic proteins at high concentrations. Anal Biochem 472: 7-20.
    • (2015) Anal Biochem , vol.472 , pp. 7-20
    • Zhou, C.1    Qi, W.2    Neil, L.E.3    Carpenter, J.F.4
  • 111
    • 84914819810 scopus 로고    scopus 로고
    • Improving monoclonal antibody selection and engineering using measurements of colloidal protein interactions
    • Geng SB, Cheung JK, Narasimhan C, Shameem M, Tessier PM,. 2014. Improving monoclonal antibody selection and engineering using measurements of colloidal protein interactions. J Pharm Sci 103: 3356-3363.
    • (2014) J Pharm Sci , vol.103 , pp. 3356-3363
    • Geng, S.B.1    Cheung, J.K.2    Narasimhan, C.3    Shameem, M.4    Tessier, P.M.5
  • 112
    • 84897894651 scopus 로고    scopus 로고
    • Emerging methods for identifying monoclonal antibodies with low propensity to self-associate during the early discovery process
    • Tessier PM, Wu J, Dickinson CD,. 2014. Emerging methods for identifying monoclonal antibodies with low propensity to self-associate during the early discovery process. Expert Opin Drug Deliv 11: 461-465.
    • (2014) Expert Opin Drug Deliv , vol.11 , pp. 461-465
    • Tessier, P.M.1    Wu, J.2    Dickinson, C.D.3
  • 113
    • 77953617541 scopus 로고    scopus 로고
    • Phase separation of an IgG1 antibody solution under a low ionic strength condition
    • Nishi H, Miyajima M, Nakagami H, Noda M, Uchiyama S, Fukui K,. 2010. Phase separation of an IgG1 antibody solution under a low ionic strength condition. Pharm Res 27: 1348-1360.
    • (2010) Pharm Res , vol.27 , pp. 1348-1360
    • Nishi, H.1    Miyajima, M.2    Nakagami, H.3    Noda, M.4    Uchiyama, S.5    Fukui, K.6
  • 114
    • 79955573442 scopus 로고    scopus 로고
    • Assessment of net charge and protein-protein interactions of different monoclonal antibodies
    • Lehermayr C, Mahler HC, Mader K, Fischer S,. 2011. Assessment of net charge and protein-protein interactions of different monoclonal antibodies. J Pharm Sci 100: 2551-2562.
    • (2011) J Pharm Sci , vol.100 , pp. 2551-2562
    • Lehermayr, C.1    Mahler, H.C.2    Mader, K.3    Fischer, S.4
  • 115
    • 4344565219 scopus 로고    scopus 로고
    • Ions from the Hofmeister series and osmolytes: Effects on proteins in solution and in the crystallization process
    • Collins KD., 2004. Ions from the Hofmeister series and osmolytes: Effects on proteins in solution and in the crystallization process. Methods 34: 300-311.
    • (2004) Methods , vol.34 , pp. 300-311
    • Collins, K.D.1
  • 116
    • 84865959053 scopus 로고    scopus 로고
    • Specific ion-protein interactions dictate solubility behavior of a monoclonal antibody at low salt concentrations
    • Zhang L, Zhang J,. 2012. Specific ion-protein interactions dictate solubility behavior of a monoclonal antibody at low salt concentrations. Mol Pharm 9: 2582-2590.
    • (2012) Mol Pharm , vol.9 , pp. 2582-2590
    • Zhang, L.1    Zhang, J.2
  • 117
    • 84863009479 scopus 로고    scopus 로고
    • On the role of salt type and concentration on the stability behavior of a monoclonal antibody solution
    • Arosio P, Jaquet B, Wu H, Morbidelli M,. 2012. On the role of salt type and concentration on the stability behavior of a monoclonal antibody solution. Biophys Chem 168-169: 19-27.
    • (2012) Biophys Chem , vol.168-169 , pp. 19-27
    • Arosio, P.1    Jaquet, B.2    Wu, H.3    Morbidelli, M.4
  • 118
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • Shire SJ, Shahrokh Z, Liu J,. 2004. Challenges in the development of high protein concentration formulations. J Pharm Sci 93: 1390-1402.
    • (2004) J Pharm Sci , vol.93 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 120
    • 84863491050 scopus 로고    scopus 로고
    • Weak interactions govern the viscosity of concentrated antibody solutions: High-throughput analysis using the diffusion interaction parameter
    • Connolly BD, Petry C, Yadav S, Demeule B, Ciaccio N, Moore JM, Shire SJ, Gokarn YR,. 2012. Weak interactions govern the viscosity of concentrated antibody solutions: High-throughput analysis using the diffusion interaction parameter. Biophys J 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.6    Shire, S.J.7    Gokarn, Y.R.8
  • 121
    • 84876492451 scopus 로고    scopus 로고
    • Effects of ionic strength and sugars on the aggregation propensity of monoclonal antibodies: Influence of colloidal and conformational stabilities
    • Saito S, Hasegawa J, Kobayashi N, Tomitsuka T, Uchiyama S, Fukui K,. 2013. Effects of ionic strength and sugars on the aggregation propensity of monoclonal antibodies: Influence of colloidal and conformational stabilities. Pharm Res 30: 1263-1280.
    • (2013) Pharm Res , vol.30 , pp. 1263-1280
    • Saito, S.1    Hasegawa, J.2    Kobayashi, N.3    Tomitsuka, T.4    Uchiyama, S.5    Fukui, K.6
  • 122
    • 80054935483 scopus 로고    scopus 로고
    • High-throughput assessment of thermal and colloidal stability parameters for monoclonal antibody formulations
    • He F, Woods CE, Becker GW, Narhi LO, Razinkov VI,. 2011. High-throughput assessment of thermal and colloidal stability parameters for monoclonal antibody formulations. J Pharm Sci 100: 5126-5141.
    • (2011) J Pharm Sci , vol.100 , pp. 5126-5141
    • He, F.1    Woods, C.E.2    Becker, G.W.3    Narhi, L.O.4    Razinkov, V.I.5
  • 124
    • 84875763312 scopus 로고    scopus 로고
    • Rapid analysis of antibody self-association in complex mixtures using immunogold conjugates
    • Sule SV, Dickinson CD, Lu J, Chow CK, Tessier PM,. 2013. Rapid analysis of antibody self-association in complex mixtures using immunogold conjugates. Mol Pharm 10: 1322-1331.
    • (2013) Mol Pharm , vol.10 , pp. 1322-1331
    • Sule, S.V.1    Dickinson, C.D.2    Lu, J.3    Chow, C.K.4    Tessier, P.M.5
  • 125
    • 84889816985 scopus 로고    scopus 로고
    • High throughput detection of antibody self-interaction by bio-layer interferometry
    • Sun T, Reid F, Liu Y, Cao Y, Estep P, Nauman C, Xu Y,. 2013. High throughput detection of antibody self-interaction by bio-layer interferometry. MAbs 5: 838-841.
    • (2013) MAbs , vol.5 , pp. 838-841
    • Sun, T.1    Reid, F.2    Liu, Y.3    Cao, Y.4    Estep, P.5    Nauman, C.6    Xu, Y.7
  • 126
    • 84932179752 scopus 로고    scopus 로고
    • Concentration dependent viscosity of monoclonal antibody solutions: Explaining experimental behavior in terms of molecular properties
    • Li L, Kumar S, Buck PM, Burns C, Lavoie J, Singh SK, Warne NW, Nichols P, Luksha N, Boardman D,. 2014. Concentration dependent viscosity of monoclonal antibody solutions: Explaining experimental behavior in terms of molecular properties. Pharm Res 31: 3161-3178.
    • (2014) Pharm Res , vol.31 , pp. 3161-3178
    • Li, L.1    Kumar, S.2    Buck, P.M.3    Burns, C.4    Lavoie, J.5    Singh, S.K.6    Warne, N.W.7    Nichols, P.8    Luksha, N.9    Boardman, D.10
  • 127
    • 84855891967 scopus 로고    scopus 로고
    • Viscosity behavior of high-concentration monoclonal antibody solutions: Correlation with interaction parameter and electroviscous effects
    • Yadav S, Shire SJ, Kalonia DS,. 2012. Viscosity behavior of high-concentration monoclonal antibody solutions: Correlation with interaction parameter and electroviscous effects. J Pharm Sci 101: 998-1011.
    • (2012) J Pharm Sci , vol.101 , pp. 998-1011
    • Yadav, S.1    Shire, S.J.2    Kalonia, D.S.3
  • 128
    • 77649185864 scopus 로고    scopus 로고
    • High-throughput dynamic light scattering method for measuring viscosity of concentrated protein solutions
    • He F, Becker GW, Litowski JR, Narhi LO, Brems DN, Razinkov VI,. 2010. High-throughput dynamic light scattering method for measuring viscosity of concentrated protein solutions. Anal Biochem 399: 141-143.
    • (2010) Anal Biochem , vol.399 , pp. 141-143
    • He, F.1    Becker, G.W.2    Litowski, J.R.3    Narhi, L.O.4    Brems, D.N.5    Razinkov, V.I.6
  • 129
    • 84921367691 scopus 로고    scopus 로고
    • Early developability screen of therapeutic antibody candidates using Taylor dispersion analysis and UV area imaging detection
    • Lavoisier A, Schlaeppi JM,. 2014. Early developability screen of therapeutic antibody candidates using Taylor dispersion analysis and UV area imaging detection. MAbs 7: 77-83.
    • (2014) MAbs , vol.7 , pp. 77-83
    • Lavoisier, A.1    Schlaeppi, J.M.2
  • 130
    • 0345426282 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of dimer formation and dissociation for a recombinant humanized monoclonal antibody to vascular endothelial growth factor
    • Moore JM, Patapoff TW, Cromwell ME,. 1999. Kinetics and thermodynamics of dimer formation and dissociation for a recombinant humanized monoclonal antibody to vascular endothelial growth factor. Biochemistry 38: 13960-13967.
    • (1999) Biochemistry , vol.38 , pp. 13960-13967
    • Moore, J.M.1    Patapoff, T.W.2    Cromwell, M.E.3
  • 132
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: The neonatal Fc receptor comes of age
    • Roopenian DC, Akilesh S,. 2007. FcRn: the neonatal Fc receptor comes of age. Nat Rev Immunol 7: 715-725.
    • (2007) Nat Rev Immunol , vol.7 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 134
    • 80052008224 scopus 로고    scopus 로고
    • Monoclonal antibodies with identical Fc sequences can bind to FcRn differentially with pharmacokinetic consequences
    • Wang W, Lu P, Fang Y, Hamuro L, Pittman T, Carr B, Hochman J, Prueksaritanont T,. 2011. Monoclonal antibodies with identical Fc sequences can bind to FcRn differentially with pharmacokinetic consequences. Drug Metab Dispos 39: 1469-1477.
    • (2011) Drug Metab Dispos , vol.39 , pp. 1469-1477
    • Wang, W.1    Lu, P.2    Fang, Y.3    Hamuro, L.4    Pittman, T.5    Carr, B.6    Hochman, J.7    Prueksaritanont, T.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.