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Volumn 418, Issue 2, 2011, Pages 318-333

Predicting solution aggregation rates for therapeutic proteins: Approaches and challenges

Author keywords

Biotechnology; Modeling; Non native aggregation; Protein stability

Indexed keywords

ACCURACY; ARTICLE; BIOTECHNOLOGY; CONFORMATION; MOLECULAR MODEL; OSMOSIS; PREDICTION; PRIORITY JOURNAL; PRODUCT DEVELOPMENT; PROTEIN INTERACTION; PROTEIN STABILITY; QUANTITATIVE ANALYSIS; THERMODYNAMICS;

EID: 80052976278     PISSN: 03785173     EISSN: 18733476     Source Type: Journal    
DOI: 10.1016/j.ijpharm.2011.03.064     Document Type: Article
Times cited : (118)

References (113)
  • 1
    • 43049095653 scopus 로고    scopus 로고
    • Measurement of the second osmotic virial coefficient for protein solutions exhibiting monomer-dimer equilibrium
    • J.R. Alford, B.S. Kendrick, J.F. Carpenter, and T.W. Randolph Measurement of the second osmotic virial coefficient for protein solutions exhibiting monomer-dimer equilibrium Anal. Biochem. 377 2008 128 133
    • (2008) Anal. Biochem. , vol.377 , pp. 128-133
    • Alford, J.R.1    Kendrick, B.S.2    Carpenter, J.F.3    Randolph, T.W.4
  • 2
    • 34250834054 scopus 로고    scopus 로고
    • A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding
    • DOI 10.1021/jp070212j
    • J.M. Andrews, and C.J. Roberts A Lumry-Eyring nucleated polymerization model of protein aggregation kinetics: 1. Aggregation with pre-equilibrated unfolding J. Phys. Chem. B 111 2007 7897 7913 (Pubitemid 47169702)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.27 , pp. 7897-7913
    • Andrews, J.M.1    Roberts, C.J.2
  • 3
    • 0035823520 scopus 로고    scopus 로고
    • Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide
    • R. Azriel, and E. Gazit Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide J. Biol. Chem. 276 2001 34156 34161
    • (2001) J. Biol. Chem. , vol.276 , pp. 34156-34161
    • Azriel, R.1    Gazit, E.2
  • 5
    • 33745413982 scopus 로고    scopus 로고
    • Protein structural conformation and not second virial coefficient relates to long-term irreversible aggregation of a monoclonal antibody and ovalbumin in solution
    • DOI 10.1007/s11095-006-0018-y
    • H. Bajaj, V.K. Sharma, A. Badkar, D. Zeng, S. Nema, and D.S. Kalonia Protein structural conformation and not second virial coefficient relates to long-term irreversible aggregation of a monoclonal antibody and ovalbumin in solution Pharm. Res. 23 2006 1382 1394 (Pubitemid 43946160)
    • (2006) Pharmaceutical Research , vol.23 , Issue.6 , pp. 1382-1394
    • Bajaj, H.1    Sharma, V.K.2    Badkar, A.3    Zeng, D.4    Nema, S.5    Kalonia, D.S.6
  • 9
    • 35348827271 scopus 로고    scopus 로고
    • Determining antibody stability: Creation of solid - Liquid interfacial effects within a high shear environment
    • DOI 10.1021/bp0701261
    • J.G. Biddlecombe, A.V. Craig, H. Zhang, S. Uddin, S. Mulot, B.C. Fish, and D.G. Bracewell Determining antibody stability: creation of solid-liquid interfacial effects within a high shear environment Biotechnol. Prog. 23 2007 1218 1222 (Pubitemid 47587097)
    • (2007) Biotechnology Progress , vol.23 , Issue.5 , pp. 1218-1222
    • Biddlecombe, J.G.1    Craig, A.V.2    Zhang, H.3    Uddin, S.4    Mulot, S.5    Fish, B.C.6    Bracewell, D.G.7
  • 10
    • 79954531753 scopus 로고    scopus 로고
    • Non-native aggregation of an IgG1 antibody in acidic conditions: 1. Unfolding, colloidal interactions, and formation of high molecular weight aggregates
    • (Early View)
    • R.K. Brummitt, D.P. Nesta, L. Chang, S.F. Chase, T.M. Laue, and C.J. Roberts Non-native aggregation of an IgG1 antibody in acidic conditions: 1. Unfolding, colloidal interactions, and formation of high molecular weight aggregates J. Pharm. Sci. 100 2011 2087 2103 (Early View)
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2087-2103
    • Brummitt, R.K.1    Nesta, D.P.2    Chang, L.3    Chase, S.F.4    Laue, T.M.5    Roberts, C.J.6
  • 11
    • 79954494833 scopus 로고    scopus 로고
    • Non-native aggregation of an igg1 antibody in acidic conditions: 2. Nucleation-and-growth kinetics with competing growth mechanisms
    • (Early View)
    • R.K. Brummitt, D.P. Nesta, L. Chang, A.M. Kroetsch, and C.J. Roberts Non-native aggregation of an igg1 antibody in acidic conditions: 2. Nucleation-and-growth kinetics with competing growth mechanisms J. Pharm. Sci. 100 2011 2104 2119 (Early View)
    • (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
  • 12
    • 33748525884 scopus 로고    scopus 로고
    • Computational models for the prediction of polypeptide aggregation propensity
    • DOI 10.1016/j.cbpa.2006.07.009, PII S1367593106001104, Analytical Techniques/Mechanisms
    • A. Caflisch Computational models for the prediction of polypeptide aggregation propensity Curr. Opin. Chem. Biol. 10 2006 437 444 (Pubitemid 44375058)
    • (2006) Current Opinion in Chemical Biology , vol.10 , Issue.5 , pp. 437-444
    • Caflisch, A.1
  • 13
  • 14
    • 79954565890 scopus 로고    scopus 로고
    • The determination of protein valence by capillary electrophoresis
    • S.F. Chase, and T.M. Laue The determination of protein valence by capillary electrophoresis Beckman Coulter P/ACE Setter 12 1 2008
    • (2008) Beckman Coulter P/ACE Setter , vol.12 , Issue.1
    • Chase, S.F.1    Laue, T.M.2
  • 17
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • DOI 10.1023/A:1025771421906
    • E.Y. Chi, S. Krishnan, T.W. Randolph, and J.F. Carpenter Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation Pharm. Res. 20 2003 1325 1336 (Pubitemid 37164039)
    • (2003) Pharmaceutical Research , vol.20 , Issue.9 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 18
    • 0242515822 scopus 로고    scopus 로고
    • Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor
    • DOI 10.1110/ps.0235703
    • E.Y. Chi, S. Krishnan, B.S. Kendrick, B.S. Chang, J.F. Carpenter, and T.W. Randolph Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor Protein Sci. 12 2003 903 913 (Pubitemid 36505425)
    • (2003) Protein Science , 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
  • 19
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 20
    • 79151485620 scopus 로고    scopus 로고
    • Membrane protein dynamics in different environments: Simulation study of the outer membrane protein X in a lipid bilayer and in a micelle
    • A. Choutko, A. Glattli, C. Fernandez, C. Hilty, K. Wuthrich, and W.F. Gunsteren Membrane protein dynamics in different environments: simulation study of the outer membrane protein X in a lipid bilayer and in a micelle Eur. Biophys. J. 40 2011 39 58
    • (2011) Eur. Biophys. J. , vol.40 , pp. 39-58
    • Choutko, A.1    Glattli, A.2    Fernandez, C.3    Hilty, C.4    Wuthrich, K.5    Gunsteren, W.F.6
  • 21
    • 0027729733 scopus 로고
    • The development of stable protein formulations: A close look at protein aggregation, deamidation, and oxidation
    • J.L. Cleland, M.F. Powell, and S.J. Shire The development of stable protein formulations: a close look at protein aggregation, deamidation, and oxidation Crit. Rev. Ther. Drug Carrier Syst. 10 1993 307 377 (Pubitemid 24021947)
    • (1993) Critical Reviews in Therapeutic Drug Carrier Systems , vol.10 , Issue.4 , pp. 307-377
    • Cleland, J.L.1    Powell, M.F.2    Shire, S.J.3
  • 22
    • 33947517558 scopus 로고    scopus 로고
    • AGGRESCAN: A server for the prediction and evaluation of "hot spots" of aggregation in polypeptides
    • O. Conchillo-Sole, G. de, F.X. Aviles, J. Vendrell, X. Daura, and S. Ventura AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides BMC Bioinf. 8 2007
    • (2007) BMC Bioinf. , vol.8
    • Conchillo-Sole, O.1    De, G.2    Aviles, F.X.3    Vendrell, J.4    Daura, X.5    Ventura, S.6
  • 23
    • 55849153131 scopus 로고    scopus 로고
    • Protein particulate issues in biologics development
    • T. Das, and S. Nema Protein particulate issues in biologics development Am. Pharm. Rev. 11 52 2008 54 57
    • (2008) Am. Pharm. Rev. , vol.11 , Issue.52 , pp. 54-57
    • Das, T.1    Nema, S.2
  • 24
    • 77953655013 scopus 로고    scopus 로고
    • New methods allowing the detection of protein aggregates: A case study on trastuzumab
    • B. Demeule, C. Palais, G. Machaidze, R. Gurny, and T. Arvinte New methods allowing the detection of protein aggregates: a case study on trastuzumab MAbs 1 2009 142 150
    • (2009) MAbs , vol.1 , pp. 142-150
    • Demeule, B.1    Palais, C.2    MacHaidze, G.3    Gurny, R.4    Arvinte, T.5
  • 26
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • M. Fändrich, M.A. Fletcher, and C.M. Dobson Amyloid fibrils from muscle myoglobin Nature 410 2001 165 166
    • (2001) Nature , vol.410 , pp. 165-166
    • Fändrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 27
    • 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
    • C. Fernandez, and A.P. Minton Static light scattering from concentrated protein solutions II: experimental test of theory for protein mixtures and weakly self-associating proteins Biophys. J. 96 2009 1992 1998
    • (2009) Biophys. J. , vol.96 , pp. 1992-1998
    • Fernandez, C.1    Minton, A.P.2
  • 28
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • DOI 10.1038/nbt1012
    • A. Fernandez-Escamilla, F. Rousseau, J. Schymkowitz, and L. Serrano Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins Nat. Biotechnol. 22 2004 1302 1306 (Pubitemid 39336784)
    • (2004) Nature Biotechnology , vol.22 , Issue.10 , pp. 1302-1306
    • Fernandez-Escamilla, A.-M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 29
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • DOI 10.1016/S0076-6879(99)09019-9
    • F. Ferrone Analysis of protein aggregation kinetics Methods Enzymol. 309 1999 256 274 (Pubitemid 29446454)
    • (1999) Methods in Enzymology , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 30
    • 77957365624 scopus 로고    scopus 로고
    • Aggregation and immunogenicity of therapeutic proteins
    • John Wiley & Sons, Inc. plate
    • Filipe, V.; Hawe, A.; Schellekens, H.; Jiskoot, W.; 2010. Aggregation and immunogenicity of therapeutic proteins. In: Aggregation Ther. Proteins. John Wiley & Sons, Inc.; pp. 403-433, 1 plate.
    • (2010) Aggregation Ther. Proteins , vol.1 , pp. 403-433
    • Filipe, V.1    Hawe, A.2    Schellekens, H.3    Jiskoot, W.4
  • 31
    • 23644457960 scopus 로고    scopus 로고
    • Interdomain side-chain interactions in human γD crystallin influencing folding and stability
    • DOI 10.1110/ps.051460505
    • S.L. Flaugh, M.S. Kosinski-Collins, and J. King Interdomain side-chain interactions in human γD crystallin influencing folding and stability Protein Sci. 14 2005 2030 2043 (Pubitemid 41132368)
    • (2005) Protein Science , vol.14 , Issue.8 , pp. 2030-2043
    • Flaugh, S.L.1    Kosinski-Collins, M.S.2    King, J.3
  • 32
    • 14144250992 scopus 로고    scopus 로고
    • Contributions of hydrophobic domain interface interactions to the folding and stability of human γD-crystallin
    • DOI 10.1110/ps.041111405
    • S.L. Flaugh, M.S. Kosinski-Collins, and J. King Contributions of hydrophobic domain interface interactions to the folding and stability of human γD-crystallin Protein Sci. 14 2005 569 581 (Pubitemid 40283895)
    • (2005) Protein Science , vol.14 , Issue.3 , pp. 569-581
    • Flaugh, S.L.1    Kosinski-Collins, M.S.2    King, J.3
  • 33
    • 0026567099 scopus 로고
    • The molecular basis of cooperativity in protein folding. Thermodynamic dissection of interdomain interactions in phosphoglycerate kinase
    • E. Freire, K.P. Murphy, J.M. Sanchez-Ruiz, M.L. Galisteo, and P.L. Privalov The molecular basis of cooperativity in protein folding. Thermodynamic dissection of interdomain interactions in phosphoglycerate kinase Biochemistry 31 1992 250 256
    • (1992) Biochemistry , vol.31 , pp. 250-256
    • Freire, E.1    Murphy, K.P.2    Sanchez-Ruiz, J.M.3    Galisteo, M.L.4    Privalov, P.L.5
  • 34
    • 33646159747 scopus 로고    scopus 로고
    • ANS fluorescence detects widespread perturbations of protein tertiary structure in ice
    • E. Gabellieri, and G.B. Strambini ANS fluorescence detects widespread perturbations of protein tertiary structure in ice Biophys. J. 90 2006 3239 3245
    • (2006) Biophys. J. , vol.90 , pp. 3239-3245
    • Gabellieri, E.1    Strambini, G.B.2
  • 35
    • 33847683955 scopus 로고    scopus 로고
    • Quantitation of aggregate levels in a recombinant humanized monoclonal antibody formulation by size-exclusion chromatography, asymmetrical flow field flow fractionation, and sedimentation velocity
    • DOI 10.1002/jps.20760
    • J.P. Gabrielson, M.L. Brader, A.H. Pekar, K.B. Mathis, G. Winter, J.F. Carpenter, and T.W. Randolph Quantitation of aggregate levels in a recombinant humanized monoclonal antibody formulation by size-exclusion chromatography, asymmetrical flow field flow fractionation, and sedimentation velocity J. Pharm. Sci. 96 2006 268 279 (Pubitemid 46363558)
    • (2007) Journal of Pharmaceutical Sciences , vol.96 , Issue.2 , pp. 268-279
    • Gabrielson, J.P.1    Brader, M.L.2    Pekar, A.H.3    Mathis, K.B.4    Winter, G.5    Carpenter, J.F.6    Randolph, T.W.7
  • 36
    • 4444231656 scopus 로고    scopus 로고
    • Comparison of selected analytical techniques for protein sizing, quantitation and molecular weight determination
    • DOI 10.1016/j.jbbm.2004.01.007, PII S0165022X04000107
    • H. Goetz, M. Kuschel, T. Wulff, C. Sauber, C. Miller, S. Fisher, and C. Woodward Comparison of selected analytical techniques for protein sizing, quantitation and molecular weight determination J. Biochem. Biophys. Methods 60 2004 281 293 (Pubitemid 39179383)
    • (2004) Journal of Biochemical and Biophysical Methods , vol.60 , Issue.3 , pp. 281-293
    • Goetz, H.1    Kuschel, M.2    Wulff, T.3    Sauber, C.4    Miller, C.5    Fisher, S.6    Woodward, C.7
  • 38
    • 77951589043 scopus 로고    scopus 로고
    • Detection of IgG aggregation by a high throughput method based on extrinsic fluorescence
    • F. He, D.H. Phan, S. Hogan, R. Bailey, G.W. Becker, L.O. Narhi, and V.I. Razinkov Detection of IgG aggregation by a high throughput method based on extrinsic fluorescence J. Pharm. Sci. 99 2010 2598 2608
    • (2010) J. Pharm. Sci. , vol.99 , pp. 2598-2608
    • He, F.1    Phan, D.H.2    Hogan, S.3    Bailey, R.4    Becker, G.W.5    Narhi, L.O.6    Razinkov, V.I.7
  • 39
    • 33646922285 scopus 로고    scopus 로고
    • A statistical thermodynamic model of the protein ensemble
    • DOI 10.1021/cr040423+
    • V.J. Hilser, E. Garcia-Moreno, T.G. Oas, G. Kapp, and S.T. Whitten A statistical thermodynamic model of the protein ensemble Chem. Rev. (Washington, DC, USA) 106 2006 1545 1558 (Pubitemid 43792771)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1545-1558
    • Hilser, V.J.1    Garcia-Moreno, E.B.2    Oas, T.G.3    Kapp, G.4    Whitten, S.T.5
  • 40
    • 37549011420 scopus 로고    scopus 로고
    • In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence
    • Z. Ignatova, A.K. Thakur, R. Wetzel, and L.M. Gierasch In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence J. Biol. Chem. 282 2007 36736 36743
    • (2007) J. Biol. Chem. , vol.282 , pp. 36736-36743
    • Ignatova, Z.1    Thakur, A.K.2    Wetzel, R.3    Gierasch, L.M.4
  • 41
    • 43249105327 scopus 로고    scopus 로고
    • Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies
    • R.M. Ionescu, J. Vlasak, C. Price, and M. Kirchmeier Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies J. Pharm. Sci. 97 2008 1414 1426
    • (2008) J. Pharm. Sci. , vol.97 , pp. 1414-1426
    • Ionescu, R.M.1    Vlasak, J.2    Price, C.3    Kirchmeier, M.4
  • 43
    • 33645240208 scopus 로고    scopus 로고
    • A systematic screen of β2-microglobulin and insulin for amyloid-like segments
    • M.I. Ivanova, M.J. Thompson, and D. Eisenberg A systematic screen of β2-microglobulin and insulin for amyloid-like segments Proc. Natl. Acad. Sci. U.S.A. 103 2006 4079 4082
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 4079-4082
    • Ivanova, M.I.1    Thompson, M.J.2    Eisenberg, D.3
  • 46
    • 33750170831 scopus 로고    scopus 로고
    • A molecular-thermodynamic model for the interactions between globular proteins in aqueous solutions: Applications to bovine serum albumin (BSA), lysozyme, α-chymotrypsin, and immuno-gamma-globulins (IgG) solutions
    • DOI 10.1016/j.jcis.2006.08.046, PII S0021979706007740
    • L. Jin, Y. Yu, and G. Gao A molecular-thermodynamic model for the interactions between globular proteins in aqueous solutions: applications to bovine serum albumin (BSA), lysozyme, α-chymotrypsin, and immuno-gamma-globulins (IgG) solutions J. Colloid Interface Sci. 304 2006 77 83 (Pubitemid 44602115)
    • (2006) Journal of Colloid and Interface Science , vol.304 , Issue.1 , pp. 77-83
    • Jin, L.1    Yu, Y.-X.2    Gao, G.-H.3
  • 47
    • 0037227173 scopus 로고    scopus 로고
    • 2-microglobulin - Insights into the mechanism of fibril formation in vitro
    • DOI 10.1016/S0022-2836(02)01227-5
    • S. Jones, J. Manning, N.M. Kad, and S.E. Radford Amyloid-forming peptides from β2-microglobulin-insights into the mechanism of fibril formation in vitro J. Mol. Biol. 325 2003 249 257 (Pubitemid 36062686)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.2 , pp. 249-257
    • Jones, S.1    Manning, J.2    Kad, N.M.3    Radford, S.E.4
  • 49
    • 55749109195 scopus 로고    scopus 로고
    • Shaken, not stirred: Mechanical stress testing of an IgG1 antibody
    • S. Kiese, A. Papppenberger, W. Friess, and H. Mahler Shaken, not stirred: mechanical stress testing of an IgG1 antibody J. Pharm. Sci. 97 2008 4347 4366
    • (2008) J. Pharm. Sci. , vol.97 , pp. 4347-4366
    • Kiese, S.1    Papppenberger, A.2    Friess, W.3    Mahler, H.4
  • 50
    • 79955581681 scopus 로고    scopus 로고
    • Fundamental structures and behaviors of proteins
    • John Wiley & Sons, Inc. plates
    • Laurence, J.S.; Middaugh, C.R.; 2010. Fundamental structures and behaviors of proteins. In: Aggregation Ther. Proteins. John Wiley & Sons, Inc.; pp. 1-61, 2 plates.
    • (2010) Aggregation Ther. Proteins , vol.2 , pp. 1-61
    • Laurence J., .S.1    Middaugh C., .R.2
  • 51
    • 35848945494 scopus 로고    scopus 로고
    • Reconsidering the mechanism of polyglutamine peptide aggregation
    • DOI 10.1021/bi700806c
    • C.C. Lee, R.H. Walters, and R.M. Murphy Reconsidering the mechanism of polyglutamine peptide aggregation Biochemistry 46 2007 12810 12820 (Pubitemid 350060102)
    • (2007) Biochemistry , vol.46 , Issue.44 , pp. 12810-12820
    • Lee, C.C.1    Walters, R.H.2    Murphy, R.M.3
  • 52
    • 34247862247 scopus 로고    scopus 로고
    • A three-stage kinetic model of amyloid fibrillation
    • DOI 10.1529/biophysj.106.098608
    • C. Lee, A. Nayak, A. Sethuraman, G. Belfort, and G.J. McRae A three-stage kinetic model of amyloid fibrillation Biophys. J. 92 2007 3448 3458 (Pubitemid 46698637)
    • (2007) Biophysical Journal , vol.92 , Issue.10 , pp. 3448-3458
    • Lee, C.-C.1    Nayak, A.2    Sethuraman, A.3    Belfort, G.4    McRae, G.J.5
  • 53
    • 0027080869 scopus 로고
    • Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation
    • DOI 10.1021/bi00165a023
    • J.R. Lepock, K.P. Ritchie, M.C. Kolios, A.M. Rodahl, K.A. Heinz, and J. Kruuv Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation Biochemistry 31 1992 12706 12712 (Pubitemid 23016540)
    • (1992) Biochemistry , vol.31 , Issue.50 , pp. 12706-12712
    • Lepock, J.R.1    Ritchie, K.P.2    Kolios, M.C.3    Rodahl, A.M.4    Heinz, K.A.5    Kruuv, J.6
  • 54
    • 0036830506 scopus 로고    scopus 로고
    • Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis
    • DOI 10.1074/jbc.M206334200
    • L. Li, B. von, E. Mandelkow, and E. Mandelkow Structure, stability, and aggregation of paired helical filaments from tau protein and FTDP-17 mutants probed by tryptophan scanning mutagenesis J. Biol. Chem. 277 2002 41390 41400 (Pubitemid 35257439)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.44 , pp. 41390-41400
    • Li, L.1    Von Bergen, M.2    Mandelkow, E.-M.3    Mandelkow, E.4
  • 55
    • 67650072650 scopus 로고    scopus 로고
    • Lumry-Eyring nucleated-polymerization model of protein aggregation kinetics. 2. Competing growth via condensation and chain polymerization
    • Y. Li, and C.J. Roberts Lumry-Eyring nucleated-polymerization model of protein aggregation kinetics. 2. Competing growth via condensation and chain polymerization J. Phys. Chem. B 113 2009 7020 7032
    • (2009) J. Phys. Chem. B , vol.113 , pp. 7020-7032
    • Li, Y.1    Roberts, C.J.2
  • 56
    • 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
    • Y. Li, B.A. Ogunnaike, and C.J. Roberts Multi-variate approach to global protein aggregation behavior and kinetics: effects of pH, NaCl, and temperature for α-chymotrypsinogen A J. Pharm. Sci. 99 2010 645 662
    • (2010) J. Pharm. Sci. , vol.99 , pp. 645-662
    • Li, Y.1    Ogunnaike, B.A.2    Roberts, C.J.3
  • 57
    • 33749452453 scopus 로고    scopus 로고
    • A critical review of analytical ultracentrifugation and field flow fractionation methods for measuring protein aggregation
    • J. Liu, J.D. Andya, and S.J. Shire A critical review of analytical ultracentrifugation and field flow fractionation methods for measuring protein aggregation AAPS J. 8 2006 E580 E589
    • (2006) AAPS J. , vol.8
    • Liu, J.1    Andya, J.D.2    Shire, S.J.3
  • 59
    • 68949085124 scopus 로고    scopus 로고
    • Protein aggregation: Pathways, induction factors and analysis
    • H. Mahler, W. Friess, U. Grauschopf, and S. Kiese Protein aggregation: pathways, induction factors and analysis J. Pharm. Sci. 98 2009 2909 2934
    • (2009) J. Pharm. Sci. , vol.98 , pp. 2909-2934
    • Mahler, H.1    Friess, W.2    Grauschopf, U.3    Kiese, S.4
  • 60
    • 0023406843 scopus 로고
    • Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves
    • L.A. Marky, and K.J. Breslauer Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves Biopolymers 26 1987 1601 1620
    • (1987) Biopolymers , vol.26 , pp. 1601-1620
    • Marky, L.A.1    Breslauer, K.J.2
  • 62
    • 65249121837 scopus 로고    scopus 로고
    • Surface activity of amphiphilic helical β-peptides from molecular dynamics simulation
    • C.A. Miller, N.L. Abbott, and J.J. de Pablo Surface activity of amphiphilic helical β-peptides from molecular dynamics simulation Langmuir 25 2009 2811 2823
    • (2009) Langmuir , vol.25 , pp. 2811-2823
    • Miller, C.A.1    Abbott, N.L.2    De Pablo, J.J.3
  • 63
    • 41649094226 scopus 로고    scopus 로고
    • Effective hard particle model for the osmotic pressure of highly concentrated binary protein solutions
    • A.P. Minton Effective hard particle model for the osmotic pressure of highly concentrated binary protein solutions Biophys. J. 94 2008 L57 L59
    • (2008) Biophys. J. , vol.94
    • Minton, A.P.1
  • 64
    • 34447504216 scopus 로고    scopus 로고
    • Static light scattering from concentrated protein solutions, I: General theory for protein mixtures and application to self-associating proteins
    • DOI 10.1529/biophysj.107.103895
    • A.P. Minton Static light scattering from concentrated protein solutions. I: general theory for protein mixtures and application to self-associating proteins Biophys. J. 93 2007 1321 1328 (Pubitemid 47330911)
    • (2007) Biophysical Journal , vol.93 , Issue.4 , pp. 1321-1328
    • Minton, A.P.1
  • 65
    • 42049106418 scopus 로고    scopus 로고
    • Molecular dynamics simulations of proteins and peptides: From folding to drug design
    • DOI 10.2174/138920308783955234
    • G. Morra, M. Meli, and G. Colombo Molecular dynamics simulations of proteins and peptides: from folding to drug design Curr. Protein Pept. Sci. 9 2008 181 196 (Pubitemid 351516887)
    • (2008) Current Protein and Peptide Science , vol.9 , Issue.2 , pp. 181-196
    • Morra, G.1    Meli, M.2    Colombo, G.3
  • 66
    • 39749112546 scopus 로고    scopus 로고
    • Fitting neurological protein aggregation kinetic data via a 2-step, minimal/"Ockham's razor" model: The Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth
    • DOI 10.1021/bi701899y
    • A.M. Morris, M.A. Watzky, J.N. Agar, and R.G. Finke Fitting neurological protein aggregation kinetic data via a 2-step, Minimal/"Ockham's Razor" Model: the Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth Biochemistry 47 2008 2413 2427 (Pubitemid 351304547)
    • (2008) Biochemistry , vol.47 , Issue.8 , pp. 2413-2427
    • Morris, A.M.1    Watzky, M.A.2    Agar, J.N.3    Finke, R.G.4
  • 67
    • 0031723926 scopus 로고    scopus 로고
    • Molecular origins of osmotic second virial coefficients of proteins
    • B.L. Neal, D. Asthagiri, and A.M. Lenhoff Molecular origins of osmotic second virial coefficients of proteins Biophys. J. 75 1998 2469 2477 (Pubitemid 28492130)
    • (1998) Biophysical Journal , vol.75 , Issue.5 , pp. 2469-2477
    • Neal, B.L.1    Asthagiri, D.2    Lenhoff, A.M.3
  • 68
    • 20444440728 scopus 로고    scopus 로고
    • Structure of the cross-β spine of amyloid-like fibrils
    • DOI 10.1038/nature03680
    • R. Nelson, M.R. Sawaya, M. Balbirnie, A.O. Madsen, C. Riekel, R. Grothe, and D. Eisenberg Structure of the cross-β spine of amyloid-like fibrils Nature (London, UK) 435 2005 773 778 (Pubitemid 40839722)
    • (2005) Nature , vol.435 , Issue.7043 , pp. 773-778
    • Nelson, R.1    Sawaya, M.R.2    Balbirnie, M.3    Madsen, A.O.4    Riekel, C.5    Grothe, R.6    Eisenberg, D.7
  • 69
    • 51349136571 scopus 로고    scopus 로고
    • Structural insight into pH-induced conformational changes within the native human transthyretin tetramer
    • S.K. Palaninathan, N.N. Mohamedmohaideen, W.C. Snee, J.W. Kelly, and J.C. Sacchettini Structural insight into pH-induced conformational changes within the native human transthyretin tetramer J. Mol. Biol. 382 2008 1157 1167
    • (2008) J. Mol. Biol. , vol.382 , pp. 1157-1167
    • Palaninathan, S.K.1    Mohamedmohaideen, N.N.2    Snee, W.C.3    Kelly, J.W.4    Sacchettini, J.C.5
  • 70
    • 0034875603 scopus 로고    scopus 로고
    • A mathematical model of the kinetics of β-amyloid fibril growth from the denatured state
    • M.M. Pallitto, and R.M. Murphy A mathematical model of the kinetics of β-amyloid fibril growth from the denatured state Biophys. J. 81 2001 1805 1822 (Pubitemid 32783616)
    • (2001) Biophysical Journal , vol.81 , Issue.3 , pp. 1805-1822
    • Pallitto, M.M.1    Murphy, R.M.2
  • 71
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
    • S18349/1-S18349/14
    • A.K. Paravastu, R.D. Leapman, W. Yau, and R. Tycko Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils Proc. Natl. Acad. Sci. U.S.A. 105 2008 18349 18354 S18349/1-S18349/14
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Yau, W.3    Tycko, R.4
  • 72
    • 68949105477 scopus 로고    scopus 로고
    • Conformational implications of an inversed pH-dependent antibody aggregation
    • N. Perico, J. Purtell, T.M. Dillon, and M.S. Ricci Conformational implications of an inversed pH-dependent antibody aggregation J. Pharm. Sci. 98 2009 3031 3042
    • (2009) J. Pharm. Sci. , vol.98 , pp. 3031-3042
    • Perico, N.1    Purtell, J.2    Dillon, T.M.3    Ricci, M.S.4
  • 74
    • 33947103491 scopus 로고    scopus 로고
    • Amyloid Fibril Formation and Disaggregation of Fragment 1-29 of Apomyoglobin: Insights into the Effect of pH on Protein Fibrillogenesis
    • DOI 10.1016/j.jmb.2007.01.072, PII S0022283607001374
    • P. Picotti, G. De Franceschi, E. Frare, B. Spolaore, M. Zambonin, F. Chiti, P.P. de Laureto, and A. Fontana Amyloid fibril formation and disaggregation of fragment 1-29 of apomyoglobin: insights into the effect of pH on protein fibrillogenesis J. Mol. Biol. 367 2007 1237 1245 (Pubitemid 46413274)
    • (2007) Journal of Molecular Biology , vol.367 , Issue.5 , pp. 1237-1245
    • Picotti, P.1    De Franceschi, G.2    Frare, E.3    Spolaore, B.4    Zambonin, M.5    Chiti, F.6    De Laureto, P.P.7    Fontana, A.8
  • 75
    • 0018588511 scopus 로고
    • Stability of proteins. Small globular proteins
    • P.L. Privalov Stability of proteins. Small globular proteins Adv. Protein Chem. 33 1979 167 241
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 76
    • 0020348367 scopus 로고
    • Stability of proteins. Proteins which do not present a single cooperative system
    • P.L. Privalov Stability of proteins. Proteins which do not present a single cooperative system Adv. Protein Chem. 35 1982 1 104
    • (1982) Adv. Protein Chem. , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 77
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • P.L. Privalov, and S.A. Potekhin Scanning microcalorimetry in studying temperature-induced changes in proteins Methods Enzymol. 131 1986 4 51 (Pubitemid 16002194)
    • (1986) Methods in Enzymology , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 78
    • 80052973341 scopus 로고    scopus 로고
    • Case studies involving protein aggregation
    • John Wiley & Sons, Inc.
    • R.S. Rajan, T. Li, and T. Arakawa Case studies involving protein aggregation Aggregation Ther. Proteins 2010 John Wiley & Sons, Inc. pp. 367-401
    • (2010) Aggregation Ther. Proteins , pp. 367-401
    • Rajan, R.S.1    Li, T.2    Arakawa, T.3
  • 79
    • 24344497281 scopus 로고    scopus 로고
    • Aggregation of granulocyte-colony stimulating factor in vitro involves a conformationally altered monomeric state
    • DOI 10.1110/ps.051489405
    • S.W. Raso, J. Abel, J.M. Barnes, K.M. Maloney, G. Pipes, M.J. Treuheit, J. King, and D.N. Brems Aggregation of granulocyte-colony stimulating factor in vitro involves a conformationally altered monomeric state Protein Sci. 14 2005 2246 2257 (Pubitemid 41252793)
    • (2005) Protein Science , vol.14 , Issue.9 , pp. 2246-2257
    • Raso, S.W.1    Abel, J.2    Barnes, J.M.3    Maloney, K.M.4    Pipes, G.5    Treuheit, M.J.6    King, J.7    Brems, D.N.8
  • 80
    • 0035000257 scopus 로고    scopus 로고
    • Some thermodynamic implications for the thermostability of proteins
    • DOI 10.1110/ps.180101
    • D.C. Rees, and A.D. Robertson Some thermodynamic implications for the thermostability of proteins Protein Sci. 10 2001 1187 1194 (Pubitemid 32476479)
    • (2001) Protein Science , vol.10 , Issue.6 , pp. 1187-1194
    • Rees, D.C.1    Robertson, A.D.2
  • 81
    • 27144457667 scopus 로고    scopus 로고
    • Monoclonal antibody successes in the clinic
    • DOI 10.1038/nbt0905-1073, PII N09051073
    • J.M. Reichert, C.J. Rosensweig, L.B. Faden, and M.C. Dewitz Monoclonal antibody successes in the clinic Nat. Biotechnol. 23 2005 1073 1078 (Pubitemid 41486385)
    • (2005) Nature Biotechnology , vol.23 , Issue.9 , pp. 1073-1078
    • Reichert, J.M.1    Rosensweig, C.J.2    Faden, L.B.3    Dewitz, M.C.4
  • 82
    • 14444277713 scopus 로고    scopus 로고
    • Interleukin-1 receptor (IL-1R) liquid formulation development using differential scanning calorimetry
    • DOI 10.1023/A:1011902215383
    • R.L. Remmele, N.S. Nightlinger, S. Srinivasan, and W.R. Gombotz Interleukin-1 receptor (IL-1R) liquid formulation development using differential scanning calorimetry Pharm. Res. 15 1998 200 208 (Pubitemid 28144230)
    • (1998) Pharmaceutical Research , vol.15 , Issue.2 , pp. 200-208
    • Remmele Jr., R.L.1    Nightlinger, N.S.2    Srinivasan, S.3    Gombotz, W.R.4
  • 83
    • 0039723136 scopus 로고    scopus 로고
    • Minimization of recombinant human Flt3 ligand aggregation at the Tm plateau: A matter of thermal reversibility
    • R.L. Remmele, S.D. Bhat, D.H. Phan, and W.R. Gombotz Minimization of recombinant human Flt3 ligand aggregation at the Tm plateau: a matter of thermal reversibility Biochemistry 38 1999 5241 5247
    • (1999) Biochemistry , vol.38 , pp. 5241-5247
    • Remmele, R.L.1    Bhat, S.D.2    Phan, D.H.3    Gombotz, W.R.4
  • 85
    • 0242684664 scopus 로고    scopus 로고
    • Irreversible aggregation of recombinant bovine granulocyte-colony stimulating factor (bG-CSF) and implications for predicting protein shelf life
    • DOI 10.1002/jps.10377
    • C.J. Roberts, R.T. Darrington, and M.B. Whitley Irreversible aggregation of recombinant bovine granulocyte-colony stimulating factor (bG-CSF) and implications for predicting protein shelf life J. Pharm. Sci. 92 2003 1095 1111 (Pubitemid 36523456)
    • (2003) Journal of Pharmaceutical Sciences , vol.92 , Issue.5 , pp. 1095-1111
    • Roberts, C.J.1    Darrington, R.T.2    Whitley, M.B.3
  • 86
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • DOI 10.1002/bit.21627
    • C.J. Roberts Non-native protein aggregation kinetics Biotechnol. Bioeng. 98 2007 927 938 (Pubitemid 350205571)
    • (2007) Biotechnology and Bioengineering , vol.98 , Issue.5 , pp. 927-938
    • Roberts, C.J.1
  • 87
    • 0031592933 scopus 로고    scopus 로고
    • Formation of a denatured dimer limits the thermal stability of Arc repressor
    • DOI 10.1006/jmbi.1997.1342
    • C.R. Robinson, D. Rentzeperis, J.L. Silva, and R.T. Sauer Formation of a denatured dimer limits the thermal stability of Arc repressor J. Mol. Biol. 273 1997 692 700 (Pubitemid 27488810)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.3 , pp. 692-700
    • Robinson, C.R.1    Rentzeperis, D.2    Silva, J.L.3    Sauer, R.T.4
  • 88
    • 0037337270 scopus 로고    scopus 로고
    • The unfolding story of three-dimensional domain swapping
    • DOI 10.1016/S0969-2126(03)00029-7, PII S0969212603000297
    • F. Rousseau, J.W.H. Schymkowitz, and L.S. Itzhaki The unfolding story of three-dimensional domain swapping Structure (Cambridge, MA, USA) 11 2003 243 251 (Pubitemid 36287689)
    • (2003) Structure , vol.11 , Issue.3 , pp. 243-251
    • Rousseau, F.1    Schymkowitz, J.W.H.2    Itzhaki, L.S.3
  • 89
    • 78049249356 scopus 로고    scopus 로고
    • Comparative effects of pH and ionic strength on protein-protein interactions, unfolding, and aggregation for IgG1 antibodies
    • E. Sahin, A.O. Grillo, M.D. Perkins, and C.J. Roberts Comparative effects of pH and ionic strength on protein-protein interactions, unfolding, and aggregation for IgG1 antibodies J. Pharm. Sci. 99 2010 4830 4848
    • (2010) J. Pharm. Sci. , vol.99 , pp. 4830-4848
    • Sahin, E.1    Grillo, A.O.2    Perkins, M.D.3    Roberts, C.J.4
  • 90
    • 79952092133 scopus 로고    scopus 로고
    • Computational design and biophysical characterization of aggregation-resistant point mutations for γd crystallin illustrate a balance of conformational stability and intrinsic aggregation propensity
    • 10.1021/bi100978r (available online)
    • E. Sahin, J.L. Jordan, M.L. Spatara, A. Naranjo, J.A. Costanzo, W.F. Weiss, R. Skaja, E.J. Fernandez, and C.J. Roberts Computational design and biophysical characterization of aggregation-resistant point mutations for γD crystallin illustrate a balance of conformational stability and intrinsic aggregation propensity Biochemistry 2011 10.1021/bi100978r (available online)
    • (2011) Biochemistry
    • Sahin, E.1    Jordan, J.L.2    Spatara, M.L.3    Naranjo, A.4    Costanzo, J.A.5    Weiss, W.F.6    Skaja, R.7    Fernandez, E.J.8    Roberts, C.J.9
  • 92
    • 0024281290 scopus 로고
    • Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin
    • J.M. Sanchez-Ruiz, J.L. Lopez-Lacomba, M. Cortijo, and P.L. Mateo Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin Biochemistry 27 1988 1648 1652
    • (1988) Biochemistry , vol.27 , pp. 1648-1652
    • Sanchez-Ruiz, J.M.1    Lopez-Lacomba, J.L.2    Cortijo, M.3    Mateo, P.L.4
  • 93
    • 0026586591 scopus 로고
    • Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
    • J.M. Sanchez-Ruiz Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry Biophys. J. 61 1992 921 935
    • (1992) Biophys. J. , vol.61 , pp. 921-935
    • Sanchez-Ruiz, J.M.1
  • 94
    • 0030834850 scopus 로고    scopus 로고
    • Temperature, stability, and the hydrophobic interaction
    • J.A. Schellman Temperature, stability, and the hydrophobic interaction Biophys. J. 73 1997 2960 2964 (Pubitemid 27525762)
    • (1997) Biophysical Journal , vol.73 , Issue.6 , pp. 2960-2964
    • Schellman, J.A.1
  • 95
    • 80053039882 scopus 로고    scopus 로고
    • Experimental detection and characterization of protein aggregates
    • John Wiley & Sons, Inc.
    • V.K. Sharma, and D.S. Kalonia Experimental detection and characterization of protein aggregates Aggregation Ther. Proteins 2010 John Wiley & Sons, Inc. pp. 205-256
    • (2010) Aggregation Ther. Proteins , pp. 205-256
    • Sharma, V.K.1    Kalonia, D.S.2
  • 96
    • 0036194842 scopus 로고    scopus 로고
    • Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography
    • P.M. Tessier, A.M. Lenhoff, and S.I. Sandler Rapid measurement of protein osmotic second virial coefficients by self-interaction chromatography Biophys. J. 82 2002 1620 1631 (Pubitemid 34204779)
    • (2002) Biophysical Journal , vol.82 , Issue.3 , pp. 1620-1631
    • Tessier, P.M.1    Lenhoff, A.M.2    Sandler, S.I.3
  • 98
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • S.N. Timasheff The control of protein stability and association by weak interactions with water: How do solvents affect these processes? Annu. Rev. Biophys. Biomol. Struct. 22 1993 67 97 (Pubitemid 23180317)
    • (1993) Annual Review of Biophysics and Biomolecular Structure , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 99
    • 0036109430 scopus 로고    scopus 로고
    • Structural features of interferon-γ aggregation revealed by hydrogen exchange
    • DOI 10.1110/ps.3770102
    • S.A. Tobler, and E.J. Fernandez Structural features of interferon-γ aggregation revealed by hydrogen exchange Protein Sci. 11 2002 1340 1352 (Pubitemid 34547206)
    • (2002) Protein Science , vol.11 , Issue.6 , pp. 1340-1352
    • Tobler, S.A.1    Fernandez, E.J.2
  • 101
    • 0031768735 scopus 로고    scopus 로고
    • Protein interactions in solution characterized by light and neutron scattering: Comparison of lysozyme and chymotrypsinogen
    • O.D. Velev, E.W. Kaler, and A.M. Lenhoff Protein interactions in solution characterized by light and neutron scattering: comparison of lysozyme and chymotrypsinogen Biophys. J. 75 1998 2682 2697 (Pubitemid 28548940)
    • (1998) Biophysical Journal , vol.75 , Issue.6 , pp. 2682-2697
    • Velev, O.D.1    Kaler, E.W.2    Lenhoff, A.M.3
  • 102
    • 77953655331 scopus 로고    scopus 로고
    • Potential aggregation prone regions in biotherapeutics: A survey of commercial monoclonal antibodies
    • X. Wang, T.K. Das, S.K. Singh, and S. Kumar Potential aggregation prone regions in biotherapeutics: a survey of commercial monoclonal antibodies MAbs 1 2009 254 267
    • (2009) MAbs , vol.1 , pp. 254-267
    • Wang, X.1    Das, T.K.2    Singh, S.K.3    Kumar, S.4
  • 103
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • DOI 10.1016/j.ijpharm.2004.11.014, PII S0378517304006908
    • W. Wang Protein aggregation and its inhibition in biopharmaceutics Int. J. Pharm. 289 2005 1 30 (Pubitemid 40093537)
    • (2005) International Journal of Pharmaceutics , vol.289 , Issue.1-2 , pp. 1-30
    • Wang, W.1
  • 105
    • 80053028171 scopus 로고    scopus 로고
    • Regulatory perspective on aggregates as a product quality attribute
    • John Wiley & Sons, Inc.
    • W.C. Weinberg, L. Ha, S.L. Kirschner, and D.I. Verthelyi Regulatory perspective on aggregates as a product quality attribute Aggregation Ther. Proteins 2010 John Wiley & Sons, Inc. pp. 435-452
    • (2010) Aggregation Ther. Proteins , pp. 435-452
    • Weinberg, W.C.1    Ha, L.2    Kirschner, S.L.3    Verthelyi, D.I.4
  • 106
    • 37349050368 scopus 로고    scopus 로고
    • Nonnative protein polymers: Structure, morphology, and relation to nucleation and growth
    • DOI 10.1529/biophysj.107.112102
    • W.F. Weiss, T.K. Hodgdon, E.W. Kaler, A.M. Lenhoff, and C.J. Roberts Nonnative protein polymers: structure, morphology, and relation to nucleation and growth Biophys. J. 93 2007 4392 4403 (Pubitemid 350294485)
    • (2007) Biophysical Journal , vol.93 , Issue.12 , pp. 4392-4403
    • Weiss IV, W.F.1    Hodgdon, T.K.2    Kaler, E.W.3    Lenhoff, A.M.4    Roberts, C.J.5
  • 107
    • 67449132077 scopus 로고    scopus 로고
    • Principles, approaches, and challenges for predicting protein aggregation rates and shelf life
    • W.F. Weiss IV, T.M. Young, and C.J. Roberts Principles, approaches, and challenges for predicting protein aggregation rates and shelf life J. Pharm. Sci. 98 2009 1246 1277
    • (2009) J. Pharm. Sci. , vol.98 , pp. 1246-1277
    • Weiss, I.V.W.F.1    Young, T.M.2    Roberts, C.J.3
  • 108
    • 0035793208 scopus 로고    scopus 로고
    • Stability engineering of antibody single-chain Fv fragments
    • DOI 10.1006/jmbi.2000.4265
    • A. Worn, and A. Pluckthun Stability engineering of antibody single-chain Fv fragments J. Mol. Biol. 305 2001 989 1010 (Pubitemid 33028934)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.5 , pp. 989-1010
    • Worn, A.1    Pluckthun, A.2
  • 109
    • 76649099495 scopus 로고    scopus 로고
    • Specific interactions in high concentration antibody solutions resulting in high viscosity
    • S. Yadav, J. Liu, S.J. Shire, and D.S. Kalonia Specific interactions in high concentration antibody solutions resulting in high viscosity J. Pharm. Sci. 99 2010 1152 1168
    • (2010) J. Pharm. Sci. , vol.99 , pp. 1152-1168
    • Yadav, S.1    Liu, J.2    Shire, S.J.3    Kalonia, D.S.4
  • 110
    • 0028073866 scopus 로고
    • Is stability prediction possible for protein drugs? Denaturation kinetics of β-galactosidase in solution
    • DOI 10.1023/A:1018955031042
    • S. Yoshioka, Y. Aso, K. Izutsu, and S. Kojima Is stability prediction possible for protein drugs? Denaturation kinetics of β-galactosidase in solution Pharm. Res. 11 1994 1721 1725 (Pubitemid 24377081)
    • (1994) Pharmaceutical Research , vol.11 , Issue.12 , pp. 1721-1725
    • Yoshioka, S.1    Aso, Y.2    Izutsu, K.3    Kojima, S.4
  • 111
    • 0037339326 scopus 로고    scopus 로고
    • Short peptide amyloid organization: Stabilities and conformations of the islet amyloid peptide NFGAIL
    • D. Zanuy, B. Ma, and R. Nussinov Short peptide amyloid organization: stabilities and conformations of the islet amyloid peptide NFGAIL Biophys. J. 84 2003 1884 1894 (Pubitemid 36322950)
    • (2003) Biophysical Journal , vol.84 , Issue.3 , pp. 1884-1894
    • Zanuy, D.1    Ma, B.2    Nussinov, R.3
  • 112
    • 78650154417 scopus 로고    scopus 로고
    • Molecular level insights into thermally induced α-chymotrypsinogen A amyloid aggregation mechanism and semiflexible protofibril morphology
    • A. Zhang, J.L. Jordan, M.I. Ivanova, W.F. Weiss IV, C.J. Roberts, and E.J. Fernandez Molecular level insights into thermally induced α-chymotrypsinogen A amyloid aggregation mechanism and semiflexible protofibril morphology Biochemistry 49 2010 10553 10564
    • (2010) Biochemistry , vol.49 , pp. 10553-10564
    • Zhang, A.1    Jordan, J.L.2    Ivanova, M.I.3    Weiss, I.V.W.F.4    Roberts, C.J.5    Fernandez, E.J.6
  • 113
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences
    • H. Zhou, G. Rivas, and A.P. Minton Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences Annu. Rev. Biophys. 37 2008 375 397
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 375-397
    • Zhou, H.1    Rivas, G.2    Minton, A.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.