메뉴 건너뛰기




Volumn 102, Issue 12, 2013, Pages 4315-4329

Investigating monoclonal antibody aggregation using a combination of H/DX-MS and other biophysical measurements

Author keywords

Antibody dimerization; Calorimetry (DSC); Chromatography; Domain swapping; Electrophoresis; Hydrogen deuterium exchange mass spectrometry (H DX MS); Protein aggregation; Protein structure; Small angle X ray solution scattering (SAXS)

Indexed keywords

DIMER; MAB 1 PROTEIN; MAB 2 PROTEIN; MONOCLONAL ANTIBODY; MONOMER; UNCLASSIFIED DRUG;

EID: 84888198342     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23754     Document Type: Article
Times cited : (83)

References (72)
  • 1
    • 77951586447 scopus 로고    scopus 로고
    • Strategies and challenges for the next generation of therapeutic antibodies
    • Beck A, Wurch T, Bailly C, Corvaia N,. 2010. Strategies and challenges for the next generation of therapeutic antibodies. Nat Rev Immunol 10 (5): 345-352.
    • (2010) Nat Rev Immunol , vol.10 , Issue.5 , pp. 345-352
    • Beck, A.1    Wurch, T.2    Bailly, C.3    Corvaia, N.4
  • 2
    • 84860896956 scopus 로고    scopus 로고
    • Marketed therapeutic antibodies compendium
    • Reichert JM,. 2012. Marketed therapeutic antibodies compendium. mAbs 4 (3): 413-415.
    • (2012) MAbs , vol.4 , Issue.3 , pp. 413-415
    • Reichert, J.M.1
  • 3
    • 84856800190 scopus 로고    scopus 로고
    • Which are the antibodies to watch in 2012?
    • Reichert JM,. 2012. Which are the antibodies to watch in 2012? mAbs 4 (1): 1-3.
    • (2012) MAbs , vol.4 , Issue.1 , pp. 1-3
    • Reichert, J.M.1
  • 4
    • 37549036732 scopus 로고    scopus 로고
    • Fc gamma receptors as regulators of immune responses
    • Nimmerjahn F, Ravetch, JV,. 2008. Fc gamma receptors as regulators of immune responses. Nat Rev Immunol 8: 34-47.
    • (2008) Nat Rev Immunol , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 6
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: An immunologic perspective
    • Rosenberg AS,. 2006. Effects of protein aggregates: An immunologic perspective. AAPS J 8 (3): E501-E507.
    • (2006) AAPS J , vol.8 , Issue.3
    • Rosenberg, A.S.1
  • 7
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang W,. 2005. Protein aggregation and its inhibition in biopharmaceutics. Int J Pharm 289 (1-2): 1-30.
    • (2005) Int J Pharm , vol.289 , Issue.12 , pp. 1-30
    • Wang, W.1
  • 9
    • 0034711745 scopus 로고    scopus 로고
    • Aggregation events occur prior to stable intermediate formation during refolding of interleukin 1beta
    • Finke JM, Roy M, Zimm BH, Jennings PA,. 2000. Aggregation events occur prior to stable intermediate formation during refolding of interleukin 1beta. Biochemistry 39 (3): 575-583.
    • (2000) Biochemistry , vol.39 , Issue.3 , pp. 575-583
    • Finke, J.M.1    Roy, M.2    Zimm, B.H.3    Jennings, P.A.4
  • 10
    • 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
    • 0028559724 scopus 로고
    • Solid-phase aggregation of proteins under pharmaceutically relevant conditions
    • Costantino HR, Langer R, Klibanov AM,. 1994. Solid-phase aggregation of proteins under pharmaceutically relevant conditions. J Pharm Sci 83 (12): 1662-1669.
    • (1994) J Pharm Sci , vol.83 , Issue.12 , pp. 1662-1669
    • Costantino, H.R.1    Langer, R.2    Klibanov, A.M.3
  • 12
    • 36749078792 scopus 로고    scopus 로고
    • Folding versus aggregation: Polypeptide conformations on competing pathways
    • Jahn TR, Radford SE,. 2008. Folding versus aggregation: Polypeptide conformations on competing pathways. Arch Biochem Biophys 469 (1): 100-117.
    • (2008) Arch Biochem Biophys , vol.469 , Issue.1 , pp. 100-117
    • Jahn, T.R.1    Radford, S.E.2
  • 13
    • 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 (5): 903-913.
    • (2003) Protein Sci , vol.12 , Issue.5 , 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
  • 14
    • 77953655331 scopus 로고    scopus 로고
    • Potential aggregation prone regions in biotherapeutics: A survey of commercial monoclonal antibodies
    • Wang X, Das TK, Singh SK, Kumar S,. 2009. Potential aggregation prone regions in biotherapeutics: A survey of commercial monoclonal antibodies. mAbs 1 (3): 254-267.
    • (2009) MAbs , vol.1 , Issue.3 , pp. 254-267
    • Wang, X.1    Das, T.K.2    Singh, S.K.3    Kumar, S.4
  • 17
    • 67649394336 scopus 로고    scopus 로고
    • Recombinant antibody therapeutics: The impact of glycosylation on mechanisms of action
    • Jefferis R,. 2009. Recombinant antibody therapeutics: The impact of glycosylation on mechanisms of action. Trends Pharmacol Sci 30 (7): 356-362.
    • (2009) Trends Pharmacol Sci , vol.30 , Issue.7 , pp. 356-362
    • Jefferis, R.1
  • 18
    • 60549114878 scopus 로고    scopus 로고
    • Glycosylation of antibody therapeutics: Optimisation for purpose
    • Jefferis R,. 2009. Glycosylation of antibody therapeutics: Optimisation for purpose. Methods Mol Biol 483: 223-238.
    • (2009) Methods Mol Biol , vol.483 , pp. 223-238
    • Jefferis, R.1
  • 19
    • 64849114588 scopus 로고    scopus 로고
    • Characterization of IgG1 conformation and conformational dynamics by hydrogen/deuterium exchange mass spectrometry
    • Houde D, Arndt J, Domeier W, Berkowitz S, Engen JR,. 2009. Characterization of IgG1 conformation and conformational dynamics by hydrogen/deuterium exchange mass spectrometry. Anal Chem 81 (7): 2644-2651.
    • (2009) Anal Chem , vol.81 , Issue.7 , pp. 2644-2651
    • Houde, D.1    Arndt, J.2    Domeier, W.3    Berkowitz, S.4    Engen, J.R.5
  • 20
    • 77955412238 scopus 로고    scopus 로고
    • Post-translational modifications differentially affect IgG1 conformation and receptor binding
    • Houde D, Peng Y, Berkowitz SA, Engen JR,. 2010. Post-translational modifications differentially affect IgG1 conformation and receptor binding. Mol Cell Proteomics 9 (8): 1716-1728.
    • (2010) Mol Cell Proteomics , vol.9 , Issue.8 , pp. 1716-1728
    • Houde, D.1    Peng, Y.2    Berkowitz, S.A.3    Engen, J.R.4
  • 22
    • 0035081693 scopus 로고    scopus 로고
    • The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: Properties of a series of truncated glycoforms
    • Mimura Y, Church S, Ghirlando R, Ashton PR, Dong S, Goodall M, Lund J, Jefferis R,. 2000. The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: Properties of a series of truncated glycoforms. Mol Immunol 37 (12-13): 697-706.
    • (2000) Mol Immunol , vol.37 , Issue.1213 , pp. 697-706
    • Mimura, Y.1    Church, S.2    Ghirlando, R.3    Ashton, P.R.4    Dong, S.5    Goodall, M.6    Lund, J.7    Jefferis, R.8
  • 24
    • 78650656603 scopus 로고    scopus 로고
    • Biomolecular solution X-ray scattering at the National Synchrotron Light Source
    • Allaire M, Yang L,. 2011. Biomolecular solution X-ray scattering at the National Synchrotron Light Source. J Synchrotron Radiat 18: 41-44.
    • (2011) J Synchrotron Radiat , vol.18 , pp. 41-44
    • Allaire, M.1    Yang, L.2
  • 25
    • 51549121010 scopus 로고    scopus 로고
    • High-speed and high-resolution UPLC separation at zero degrees Celsius
    • Wales TE, Fadgen KE, Gerhardt GC, Engen JR,. 2008. High-speed and high-resolution UPLC separation at zero degrees Celsius. Anal Chem 80 (17): 6815-6820.
    • (2008) Anal Chem , vol.80 , Issue.17 , pp. 6815-6820
    • Wales, T.E.1    Fadgen, K.E.2    Gerhardt, G.C.3    Engen, J.R.4
  • 26
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales TE, Engen JR,. 2006. Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom Rev 25 (1): 158-170.
    • (2006) Mass Spectrom Rev , vol.25 , Issue.1 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 27
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander SW, Kallenbach NR,. 1983. Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q Rev Biophys 16 (4): 521-655.
    • (1983) Q Rev Biophys , vol.16 , Issue.4 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 28
    • 60149083122 scopus 로고    scopus 로고
    • Assessment of the repeatability and reproducibility of hydrogen/deuterium exchange mass spectrometry measurements
    • Burkitt W, O'Connor G,. 2008. Assessment of the repeatability and reproducibility of hydrogen/deuterium exchange mass spectrometry measurements. Rapid Commun Mass Spectrom 22 (23): 3893-3901.
    • (2008) Rapid Commun Mass Spectrom , vol.22 , Issue.23 , pp. 3893-3901
    • Burkitt, W.1    O'Connor, G.2
  • 30
    • 79954629044 scopus 로고    scopus 로고
    • MSTools-Web based application for visualization and presentation of HXMS data
    • Kavan D, Man P,. 2011. MSTools-Web based application for visualization and presentation of HXMS data. Int J Mass Spectrom 302 (1-3): 53-58.
    • (2011) Int J Mass Spectrom , vol.302 , Issue.13 , pp. 53-58
    • Kavan, D.1    Man, P.2
  • 31
    • 77953325845 scopus 로고    scopus 로고
    • Ligand docking and binding site analysis with PyMOL and Autodock/Vina
    • Seeliger D, de Groot BL,. 2010. Ligand docking and binding site analysis with PyMOL and Autodock/Vina. J Comput Aided Mol Des 24 (5): 417-422.
    • (2010) J Comput Aided Mol des , vol.24 , Issue.5 , pp. 417-422
    • Seeliger, D.1    De Groot, B.L.2
  • 32
    • 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 (1): 394-404.
    • (2000) Biophys J , vol.78 , Issue.1 , pp. 394-404
    • Vermeer, A.W.1    Norde, W.2
  • 33
    • 33847416982 scopus 로고    scopus 로고
    • A broad range of Fab stabilities within a host of therapeutic IgGs
    • Garber E, Demarest SJ,. 2007. A broad range of Fab stabilities within a host of therapeutic IgGs. Biochem Biophys Res Commun 355 (3): 751-757.
    • (2007) Biochem Biophys Res Commun , vol.355 , Issue.3 , pp. 751-757
    • Garber, E.1    Demarest, S.J.2
  • 34
    • 43249105327 scopus 로고    scopus 로고
    • Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies
    • Ionescu RM, Vlasak J, Price C, Kirchmeier M,. 2008. Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies. J Pharm Sci 97 (4): 1414-1426.
    • (2008) J Pharm Sci , vol.97 , Issue.4 , pp. 1414-1426
    • Ionescu, R.M.1    Vlasak, J.2    Price, C.3    Kirchmeier, M.4
  • 35
    • 0032554658 scopus 로고    scopus 로고
    • Investigation of the cooperative structure of Fc fragments from myeloma immunoglobulin G
    • Tischenko VM, Abramov VM, Zav'yalov VP,. 1998. Investigation of the cooperative structure of Fc fragments from myeloma immunoglobulin G. Biochemistry 37 (16): 5576-5581.
    • (1998) Biochemistry , vol.37 , Issue.16 , pp. 5576-5581
    • Tischenko, V.M.1    Abramov, V.M.2    Vp, Z.3
  • 36
    • 84855870882 scopus 로고    scopus 로고
    • SAXS data analysis and modeling of tetravalent neutralizing antibody CD4-IgG2 -/+ HIV-1 gp120 revealed that first two gp120 bind to the same Fab arm
    • Rathore YS, Solanki AK, Dhoke RR, Ashish,. 2011. SAXS data analysis and modeling of tetravalent neutralizing antibody CD4-IgG2 -/+ HIV-1 gp120 revealed that first two gp120 bind to the same Fab arm. Biochem Biophys Res Commun 415 (4): 680-685.
    • (2011) Biochem Biophys Res Commun , vol.415 , Issue.4 , pp. 680-685
    • Rathore, Y.S.1    Solanki, A.K.2    Dhoke, R.R.3    Ashish4
  • 37
    • 72949106692 scopus 로고    scopus 로고
    • Global structure of HIV-1 neutralizing antibody IgG1 b12 is asymmetric
    • Ashish, Solanki AK, Boone CD, Krueger JK,. 2010. Global structure of HIV-1 neutralizing antibody IgG1 b12 is asymmetric. Biochem Biophys Res Commun 391 (1): 947-951.
    • (2010) Biochem Biophys Res Commun , vol.391 , Issue.1 , pp. 947-951
    • Ashish1    Solanki, A.K.2    Boone, C.D.3    Krueger, J.K.4
  • 39
    • 84865130275 scopus 로고    scopus 로고
    • Influence of the cosolute environment on IgG solution structure analyzed by small-angle X-ray scattering
    • Lilyestrom WG, Shire SJ, Scherer TM,. 2012. Influence of the cosolute environment on IgG solution structure analyzed by small-angle X-ray scattering. J Phys Chem B 116 (32): 9611-9618.
    • (2012) J Phys Chem B , vol.116 , Issue.32 , pp. 9611-9618
    • Lilyestrom, W.G.1    Shire, S.J.2    Scherer, T.M.3
  • 40
    • 79958138362 scopus 로고    scopus 로고
    • Fine details of IGF-1R activation, inhibition, and asymmetry determined by associated hydrogen /deuterium-exchange and peptide mass mapping
    • Houde D, Demarest SJ,. 2011. Fine details of IGF-1R activation, inhibition, and asymmetry determined by associated hydrogen /deuterium-exchange and peptide mass mapping. Structure 19 (6): 890-900.
    • (2011) Structure , vol.19 , Issue.6 , pp. 890-900
    • Houde, D.1    Demarest, S.J.2
  • 41
    • 79954547968 scopus 로고    scopus 로고
    • The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studies
    • Houde D, Berkowitz SA, Engen JR,. 2011. The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studies. J Pharm Sci 100 (6): 2071-2086.
    • (2011) J Pharm Sci , vol.100 , Issue.6 , pp. 2071-2086
    • Houde, D.1    Berkowitz, S.A.2    Engen, J.R.3
  • 42
    • 54749126668 scopus 로고    scopus 로고
    • Detection and characterization of altered conformations of protein pharmaceuticals using complementary mass spectrometry-based approaches
    • Bobst CE, Abzalimov RR, Houde D, Kloczewiak M, Mhatre R, Berkowitz SA, Kaltashov IA,. 2008. Detection and characterization of altered conformations of protein pharmaceuticals using complementary mass spectrometry-based approaches. Anal Chem 80 (19): 7473-7481.
    • (2008) Anal Chem , vol.80 , Issue.19 , pp. 7473-7481
    • Bobst, C.E.1    Abzalimov, R.R.2    Houde, D.3    Kloczewiak, M.4    Mhatre, R.5    Berkowitz, S.A.6    Kaltashov, I.A.7
  • 43
    • 70349613463 scopus 로고    scopus 로고
    • Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS
    • Engen JR., 2009. Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS. Anal Chem 81 (19): 7870-7875.
    • (2009) Anal Chem , vol.81 , Issue.19 , pp. 7870-7875
    • Engen, J.R.1
  • 44
    • 0035326304 scopus 로고    scopus 로고
    • Investigating protein structure and dynamics by hydrogen exchange MS
    • Engen JR, Smith DL,. 2001. Investigating protein structure and dynamics by hydrogen exchange MS. Anal Chem 73 (9): 256A-265A.
    • (2001) Anal Chem , vol.73 , Issue.9
    • Engen, J.R.1    Smith, D.L.2
  • 45
    • 0031018084 scopus 로고    scopus 로고
    • Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry
    • Smith DL, Deng Y, Zhang Z,. 1997. Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry. J Mass Spectrom 32 (2): 135-146.
    • (1997) J Mass Spectrom , vol.32 , Issue.2 , pp. 135-146
    • Smith, D.L.1    Deng, Y.2    Zhang, Z.3
  • 46
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Zhang Z, Smith DL,. 1993. Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation. Protein Sci 2 (4): 522-531.
    • (1993) Protein Sci , vol.2 , Issue.4 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 47
    • 0026134908 scopus 로고
    • Conformational changes in proteins probed by hydrogen-exchange electrospray-ionization mass spectrometry
    • Katta V, Chait BT,. 1991. Conformational changes in proteins probed by hydrogen-exchange electrospray-ionization mass spectrometry. Rapid Commun Mass Spectrom 5 (4): 214-217.
    • (1991) Rapid Commun Mass Spectrom , vol.5 , Issue.4 , pp. 214-217
    • Katta, V.1    Chait, B.T.2
  • 50
    • 79954631167 scopus 로고    scopus 로고
    • False EX1 signatures caused by sample carryover during HX MS analyses
    • Fang J, Rand KD, Beuning PJ, Engen JR,. 2011. False EX1 signatures caused by sample carryover during HX MS analyses. Int J Mass Spectrom 302 (1-3): 19-25.
    • (2011) Int J Mass Spectrom , vol.302 , Issue.13 , pp. 19-25
    • Fang, J.1    Rand, K.D.2    Beuning, P.J.3    Engen, J.R.4
  • 51
    • 55749109195 scopus 로고    scopus 로고
    • Shaken, not stirred: Mechanical stress testing of an IgG1 antibody
    • Kiese S, Papppenberger A, Friess W, Mahler HC,. 2008. Shaken, not stirred: Mechanical stress testing of an IgG1 antibody. J Pharm Sci 97 (10): 4347-4366.
    • (2008) J Pharm Sci , vol.97 , Issue.10 , pp. 4347-4366
    • Kiese, S.1    Papppenberger, A.2    Friess, W.3    Mahler, H.C.4
  • 55
    • 84877922131 scopus 로고    scopus 로고
    • The identification of free cysteine residues within antibodies and a potential role for free cysteine residues in covalent aggregation because of agitation stress
    • Huh JH, White AJ, Brych SR, Franey H,. 2013. The identification of free cysteine residues within antibodies and a potential role for free cysteine residues in covalent aggregation because of agitation stress. J Pharm Sci 102 (6): 1701-1711.
    • (2013) J Pharm Sci , vol.102 , Issue.6 , pp. 1701-1711
    • Huh, J.H.1    White, A.J.2    Brych, S.R.3    Franey, H.4
  • 56
    • 78049249356 scopus 로고    scopus 로고
    • Comparative effects of pH and ionic strength on protein-protein interactions, unfolding, and aggregation for IgG1 antibodies
    • Sahin E, Grillo AO, Perkins MD, Roberts CJ,. 2010. Comparative effects of pH and ionic strength on protein-protein interactions, unfolding, and aggregation for IgG1 antibodies. J Pharm Sci 99 (12): 4830-4848.
    • (2010) J Pharm Sci , vol.99 , Issue.12 , pp. 4830-4848
    • Sahin, E.1    Grillo, A.O.2    Perkins, M.D.3    Roberts, C.J.4
  • 58
    • 79959417321 scopus 로고    scopus 로고
    • 3D domain swapping-implications for conformational disorders and ways of control
    • Jaskolski M., 2011. 3D domain swapping-implications for conformational disorders and ways of control. Bio Technologia 92: 34-44.
    • (2011) Bio Technologia , vol.92 , pp. 34-44
    • Jaskolski, M.1
  • 60
    • 7044247460 scopus 로고    scopus 로고
    • Folding mechanism of the CH2 antibody domain
    • Feige MJ, Walter S, Buchner J,. 2004. Folding mechanism of the CH2 antibody domain. J Mol Biol 344 (1): 107-118.
    • (2004) J Mol Biol , vol.344 , Issue.1 , pp. 107-118
    • Feige, M.J.1    Walter, S.2    Buchner, J.3
  • 61
    • 81255197729 scopus 로고    scopus 로고
    • The impact of glycosylation on monoclonal antibody conformation and stability
    • Zheng K, Bantog C, Bayer R,. 2011. The impact of glycosylation on monoclonal antibody conformation and stability. mAbs 3 (6): 568-576.
    • (2011) MAbs , vol.3 , Issue.6 , pp. 568-576
    • Zheng, K.1    Bantog, C.2    Bayer, R.3
  • 62
    • 84860581906 scopus 로고    scopus 로고
    • Distinct aggregation mechanisms of monoclonal antibody under thermal and freeze-thaw stresses revealed by hydrogen exchange
    • Zhang A, Singh SK, Shirts MR, Kumar S, Fernandez EJ,. 2012. Distinct aggregation mechanisms of monoclonal antibody under thermal and freeze-thaw stresses revealed by hydrogen exchange. Pharm Res 29 (1): 236-250.
    • (2012) Pharm Res , vol.29 , Issue.1 , pp. 236-250
    • Zhang, A.1    Singh, S.K.2    Shirts, M.R.3    Kumar, S.4    Fernandez, E.J.5
  • 63
    • 33745823893 scopus 로고    scopus 로고
    • Modulation of the effector functions of a human IgG1 through engineering of its hinge region
    • Dall'Acqua WF, Cook KE, Damschroder MM, Woods RM, Wu H,. 2006. Modulation of the effector functions of a human IgG1 through engineering of its hinge region. J Immunol 177 (2): 1129-1138.
    • (2006) J Immunol , vol.177 , Issue.2 , pp. 1129-1138
    • Wf, D.1    Cook, K.E.2    Damschroder, M.M.3    Woods, R.M.4    Wu, H.5
  • 64
    • 0021277712 scopus 로고
    • Correlation between segmental flexibility and effector function of antibodies
    • Oi VT, Vuong TM, Hardy R, Reidler J, Dangle J, Herzenberg LA, Stryer L,. 1984. Correlation between segmental flexibility and effector function of antibodies. Nature 307 (5947): 136-140.
    • (1984) Nature , vol.307 , Issue.5947 , pp. 136-140
    • Oi, V.T.1    Vuong, T.M.2    Hardy, R.3    Reidler, J.4    Dangle, J.5    Herzenberg, L.A.6    Stryer, L.7
  • 65
    • 0025145337 scopus 로고
    • Enhancement of complement activation and cytolysis of human IgG3 by deletion of hinge exons
    • Michaelsen TE, Aase A, Westby C, Sandlie I,. 1990. Enhancement of complement activation and cytolysis of human IgG3 by deletion of hinge exons. Scand J Immunol 32 (5): 517-528.
    • (1990) Scand J Immunol , vol.32 , Issue.5 , pp. 517-528
    • Michaelsen, T.E.1    Aase, A.2    Westby, C.3    Sandlie, I.4
  • 66
    • 0031897048 scopus 로고    scopus 로고
    • Activation of complement by human IgG1 and human IgG3 antibodies against the human leucocyte antigen CD52
    • Redpath S, Michaelsen T, Sandlie I, Clark MR,. 1998. Activation of complement by human IgG1 and human IgG3 antibodies against the human leucocyte antigen CD52. Immunology 93 (4): 595-600.
    • (1998) Immunology , vol.93 , Issue.4 , pp. 595-600
    • Redpath, S.1    Michaelsen, T.2    Sandlie, I.3    Clark, M.R.4
  • 67
    • 84877787093 scopus 로고    scopus 로고
    • Effects of salts from the hofmeister series on the conformational stability, aggregation propensity, and local flexibility of an IgG1 monoclonal antibody
    • Majumdar R, Manikwar P, Hickey JM, Samra HS, Sathish HA, Bishop SM, Middaugh CR, Volkin DB, Weis DD,. 2013. Effects of salts from the hofmeister series on the conformational stability, aggregation propensity, and local flexibility of an IgG1 monoclonal antibody. Biochemistry 52 (19): 3376-3389.
    • (2013) Biochemistry , vol.52 , Issue.19 , pp. 3376-3389
    • Majumdar, R.1    Manikwar, P.2    Hickey, J.M.3    Samra, H.S.4    Sathish, H.A.5    Bishop, S.M.6    Middaugh, C.R.7    Volkin, D.B.8    Weis, D.D.9
  • 68
    • 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
  • 69
    • 0028204771 scopus 로고
    • Domain swapping: Entangling alliances between proteins
    • Bennett MJ, Choe S, Eisenberg D,. 1994. Domain swapping: Entangling alliances between proteins. Proc Natl Acad Sci USA 91 (8): 3127-3131.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.8 , pp. 3127-3131
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 70
    • 78751585161 scopus 로고    scopus 로고
    • Hinge-loop mutation can be used to control 3D domain swapping and amyloidogenesis of human cystatin C
    • Orlikowska M, Jankowska E, Kolodziejczyk R, Jaskolski M, Szymanska A,. 2011. Hinge-loop mutation can be used to control 3D domain swapping and amyloidogenesis of human cystatin C. J Struct Biol 173 (2): 406-413.
    • (2011) J Struct Biol , vol.173 , Issue.2 , pp. 406-413
    • Orlikowska, M.1    Jankowska, E.2    Kolodziejczyk, R.3    Jaskolski, M.4    Szymanska, A.5
  • 71
    • 84866793691 scopus 로고    scopus 로고
    • Implications of 3D domain swapping for protein folding, misfolding and function
    • Rousseau F, Schymkowitz J, Itzhaki LS,. 2012. Implications of 3D domain swapping for protein folding, misfolding and function. Adv Exp Med Biol 747: 137-152.
    • (2012) Adv Exp Med Biol , vol.747 , pp. 137-152
    • Rousseau, F.1    Schymkowitz, J.2    Itzhaki, L.S.3
  • 72
    • 78751585161 scopus 로고    scopus 로고
    • Hinge-loop mutation can be used to control 3D domain swapping and amyloidogenesis of human cystatin C
    • Orlikowska M, Jankowska E, Kolodziejczyk R, Jaskolski M, Szymanska A,. 2011. Hinge-loop mutation can be used to control 3D domain swapping and amyloidogenesis of human cystatin C. J Struct Biol 173 (2): 406-413.
    • (2011) J Struct Biol , vol.173 , Issue.2 , pp. 406-413
    • Orlikowska, M.1    Jankowska, E.2    Kolodziejczyk, R.3    Jaskolski, M.4    Szymanska, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.