메뉴 건너뛰기




Volumn 63, Issue 13, 2011, Pages 1118-1159

Protein-excipient interactions: Mechanisms and biophysical characterization applied to protein formulation development

Author keywords

Biophysical; Excipient; Formulation; High throughput screening; Interaction; Protein; Stability

Indexed keywords

BIOPHYSICAL; EXCIPIENT; FORMULATION; HIGH THROUGHPUT SCREENING; INTERACTION;

EID: 80054717076     PISSN: 0169409X     EISSN: 18728294     Source Type: Journal    
DOI: 10.1016/j.addr.2011.07.006     Document Type: Review
Times cited : (410)

References (559)
  • 1
    • 0036828056 scopus 로고    scopus 로고
    • Excipient-drug interactions in parenteral formulations
    • Akers M.J. Excipient-drug interactions in parenteral formulations. J. Pharm. Sci. 2002, 91:2283-2300.
    • (2002) J. Pharm. Sci. , vol.91 , pp. 2283-2300
    • Akers, M.J.1
  • 4
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization, and formulation of liquid protein pharmaceuticals
    • Wang W. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int. J. Pharm. 1999, 185:129-188.
    • (1999) Int. J. Pharm. , vol.185 , pp. 129-188
    • Wang, W.1
  • 5
    • 75349114023 scopus 로고    scopus 로고
    • Recent trends in stabilising peptides and proteins in pharmaceutical formulation - considerations in the choice of excipients
    • Jorgensen L., Hostrup S., Moeller E.H., Grohganz H. Recent trends in stabilising peptides and proteins in pharmaceutical formulation - considerations in the choice of excipients. Expert Opin. Drug Deliv. 2009, 6:1219-1230.
    • (2009) Expert Opin. Drug Deliv. , vol.6 , pp. 1219-1230
    • Jorgensen, L.1    Hostrup, S.2    Moeller, E.H.3    Grohganz, H.4
  • 9
    • 80052268214 scopus 로고    scopus 로고
    • Multidimensional methods for the formulation of biopharmaceuticals and vaccines
    • Maddux N.R., Josh S.B., Volkin D.B., Ralston J., Middaugh C.R. Multidimensional methods for the formulation of biopharmaceuticals and vaccines. J. Pharm. Sci. 2011, 100:4171-4179.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 4171-4179
    • Maddux, N.R.1    Josh, S.B.2    Volkin, D.B.3    Ralston, J.4    Middaugh, C.R.5
  • 11
    • 79251581274 scopus 로고    scopus 로고
    • Application of a high-throughput screening procedure with PEG-induced precipitation to compare relative protein solubility during formulation development with IgG1 monoclonal antibodies
    • Gibson T.J., McCarty K., McFadyen I.J., Cash E., Dalmonte P., Hinds K.D., Dinerman A.A., Alvarez J.C., Volkin D.B. Application of a high-throughput screening procedure with PEG-induced precipitation to compare relative protein solubility during formulation development with IgG1 monoclonal antibodies. J. Pharm. Sci. 2011, 100:1009-1021.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 1009-1021
    • Gibson, T.J.1    McCarty, K.2    McFadyen, I.J.3    Cash, E.4    Dalmonte, P.5    Hinds, K.D.6    Dinerman, A.A.7    Alvarez, J.C.8    Volkin, D.B.9
  • 12
    • 79951895571 scopus 로고    scopus 로고
    • Formulation development of therapeutic monoclonal antibodies using high-throughput fluorescence and static light scattering techniques: role of conformational and colloidal stability
    • Goldberg D.S., Bishop S.M., Shah A.U., Sathish H.A. Formulation development of therapeutic monoclonal antibodies using high-throughput fluorescence and static light scattering techniques: role of conformational and colloidal stability. J. Pharm. Sci. 2011, 100:1306-1315.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 1306-1315
    • Goldberg, D.S.1    Bishop, S.M.2    Shah, A.U.3    Sathish, H.A.4
  • 13
  • 14
    • 79954498279 scopus 로고    scopus 로고
    • High throughput formulation screening for global aggregation behaviors of three monoclonal antibodies
    • Li Y., Mach H., Blue J.T. High throughput formulation screening for global aggregation behaviors of three monoclonal antibodies. J. Pharm. Sci. 2011, 100:2120-2135.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2120-2135
    • Li, Y.1    Mach, H.2    Blue, J.T.3
  • 15
    • 79955601001 scopus 로고    scopus 로고
    • The degradation of polysorbates 20 and 80 and its potential impact on the stability of biotherapeutics
    • Kishore R.S., Kiese S., Fischer S., Pappenberger A., Grauschopf U., Mahler H.C. The degradation of polysorbates 20 and 80 and its potential impact on the stability of biotherapeutics. Pharm. Res. 2011, 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
  • 19
    • 49249105174 scopus 로고    scopus 로고
    • Endotoxin limits in formulations for preclinical research
    • Malyala P., Singh M. Endotoxin limits in formulations for preclinical research. J. Pharm. Sci. 2008, 97:2041-2044.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 2041-2044
    • Malyala, P.1    Singh, M.2
  • 21
    • 0032940406 scopus 로고    scopus 로고
    • Quality and functionality of excipients
    • Pifferi G., Santoro P., Pedrani M. Quality and functionality of excipients. Farmaco 1999, 54:1-14.
    • (1999) Farmaco , vol.54 , pp. 1-14
    • Pifferi, G.1    Santoro, P.2    Pedrani, M.3
  • 22
    • 0033527272 scopus 로고    scopus 로고
    • Regulatory issues with excipients
    • Robertson M.I. Regulatory issues with excipients. Int. J. Pharm. 1999, 187:273-276.
    • (1999) Int. J. Pharm. , vol.187 , pp. 273-276
    • Robertson, M.I.1
  • 25
    • 79851492106 scopus 로고    scopus 로고
    • Effect of protein and solution properties on the Donnan effect during the ultrafiltration of proteins
    • Bolton G.R., Boesch A.W., Basha J., Lacasse D.P., Kelley B.D., Acharya H. Effect of protein and solution properties on the Donnan effect during the ultrafiltration of proteins. Biotechnol. Prog. 2011, 27:140-152.
    • (2011) Biotechnol. Prog. , vol.27 , pp. 140-152
    • Bolton, G.R.1    Boesch, A.W.2    Basha, J.3    Lacasse, D.P.4    Kelley, B.D.5    Acharya, H.6
  • 27
    • 79954466263 scopus 로고    scopus 로고
    • Predicting diafiltration solution compositions for final ultrafiltration/diafiltration steps of monoclonal antibodies
    • Teeters M., Bezila D., Benner T., Alfonso P., Alred P. Predicting diafiltration solution compositions for final ultrafiltration/diafiltration steps of monoclonal antibodies. Biotechnol. Bioeng. 2011, 108:1338-1346.
    • (2011) Biotechnol. Bioeng. , vol.108 , pp. 1338-1346
    • Teeters, M.1    Bezila, D.2    Benner, T.3    Alfonso, P.4    Alred, P.5
  • 28
    • 78649448511 scopus 로고    scopus 로고
    • Excipient exchange in the comparison of preparations of the same biologic made by different manufacturing processes: an exploratory study with recombinant human growth hormone (rhGH)
    • Cauchy M., Hefford M.A. Excipient exchange in the comparison of preparations of the same biologic made by different manufacturing processes: an exploratory study with recombinant human growth hormone (rhGH). Biologicals 2010, 38:637-643.
    • (2010) Biologicals , vol.38 , pp. 637-643
    • Cauchy, M.1    Hefford, M.A.2
  • 31
    • 39149124830 scopus 로고    scopus 로고
    • Lipid excipients and delivery systems for pharmaceutical development: a regulatory perspective
    • Chen M.L. Lipid excipients and delivery systems for pharmaceutical development: a regulatory perspective. Adv. Drug Deliv. Rev. 2008, 60:768-777.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 768-777
    • Chen, M.L.1
  • 33
    • 84857503859 scopus 로고    scopus 로고
    • GRAS Substances Database http://www.fda.gov/Food/FoodIngredientsPackaging/GenerallyRecognizedasSafeGRAS/GRASSubstancesSCOGSDatabase/default.htm.
    • GRAS Substances Database
  • 34
    • 84857502312 scopus 로고    scopus 로고
    • Inactive Ingredient Search for Approved Drug Products
    • Inactive Ingredient Search for Approved Drug Products, http://www.accessdata.fda.gov/scripts/cder/iig/index.cfm.
  • 36
    • 0036784648 scopus 로고    scopus 로고
    • Stabilization of proteins by low molecular weight multi-ions
    • Maclean D.S., Qian Q., Middaugh C.R. Stabilization of proteins by low molecular weight multi-ions. J. Pharm. Sci. 2002, 91:2220-2229.
    • (2002) J. Pharm. Sci. , vol.91 , pp. 2220-2229
    • Maclean, D.S.1    Qian, Q.2    Middaugh, C.R.3
  • 37
    • 0042320719 scopus 로고    scopus 로고
    • A review and classification of emerging excipients in parenteral medications
    • March
    • Apte S.P., Ugwu S.O. A review and classification of emerging excipients in parenteral medications. Pharm. Technol. March 2003, 46-60.
    • (2003) Pharm. Technol. , pp. 46-60
    • Apte, S.P.1    Ugwu, S.O.2
  • 38
    • 33749031257 scopus 로고    scopus 로고
    • Extremolytes: natural compounds from extremophiles for versatile applications
    • Lentzen G., Schwarz T. Extremolytes: natural compounds from extremophiles for versatile applications. Appl. Microbiol. Biotechnol. 2006, 72:623-634.
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 623-634
    • Lentzen, G.1    Schwarz, T.2
  • 40
    • 30744439811 scopus 로고    scopus 로고
    • Influence of pH, buffer species, and storage temperature on physicochemical stability of a humanized monoclonal antibody LA298
    • Zheng J.Y., Janis L.J. Influence of pH, buffer species, and storage temperature on physicochemical stability of a humanized monoclonal antibody LA298. Int. J. Pharm. 2006, 308:46-51.
    • (2006) Int. J. Pharm. , vol.308 , pp. 46-51
    • Zheng, J.Y.1    Janis, L.J.2
  • 43
    • 70350223665 scopus 로고    scopus 로고
    • Carboxylate-dependent gelation of a monoclonal antibody
    • Esue O., Kanai S., Liu J., Patapoff T.W., Shire S.J. Carboxylate-dependent gelation of a monoclonal antibody. Pharm. Res. 2009, 26:2478-2485.
    • (2009) Pharm. Res. , vol.26 , pp. 2478-2485
    • Esue, O.1    Kanai, S.2    Liu, J.3    Patapoff, T.W.4    Shire, S.J.5
  • 44
    • 0035054119 scopus 로고    scopus 로고
    • Effect of initial buffer composition on pH changes during far-from-equilibrium freezing of sodium phosphate buffer solutions
    • Gomez G., Pikal M.J., Rodriguez-Hornedo N. Effect of initial buffer composition on pH changes during far-from-equilibrium freezing of sodium phosphate buffer solutions. Pharm. Res. 2001, 18:90-97.
    • (2001) Pharm. Res. , vol.18 , pp. 90-97
    • Gomez, G.1    Pikal, M.J.2    Rodriguez-Hornedo, N.3
  • 45
    • 0036771258 scopus 로고    scopus 로고
    • Effect of glycine on pH changes and protein stability during freeze-thawing in phosphate buffer systems
    • Pikal-Cleland K.A., Cleland J.L., Anchordoquy T.J., Carpenter J.F. Effect of glycine on pH changes and protein stability during freeze-thawing in phosphate buffer systems. J. Pharm. Sci. 2002, 91:1969-1979.
    • (2002) J. Pharm. Sci. , vol.91 , pp. 1969-1979
    • Pikal-Cleland, K.A.1    Cleland, J.L.2    Anchordoquy, T.J.3    Carpenter, J.F.4
  • 46
    • 0034671999 scopus 로고    scopus 로고
    • Protein denaturation during freezing and thawing in phosphate buffer systems: monomeric and tetrameric beta-galactosidase
    • Pikal-Cleland K.A., Rodriguez-Hornedo N., Amidon G.L., Carpenter J.F. Protein denaturation during freezing and thawing in phosphate buffer systems: monomeric and tetrameric beta-galactosidase. Arch. Biochem. Biophys. 2000, 384:398-406.
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 398-406
    • Pikal-Cleland, K.A.1    Rodriguez-Hornedo, N.2    Amidon, G.L.3    Carpenter, J.F.4
  • 47
    • 77954700033 scopus 로고    scopus 로고
    • Impact of freezing on pH of buffered solutions and consequences for monoclonal antibody aggregation
    • Kolhe P., Amend E., Singh S.K. Impact of freezing on pH of buffered solutions and consequences for monoclonal antibody aggregation. Biotechnol. Prog. 2010, 26:727-733.
    • (2010) Biotechnol. Prog. , vol.26 , pp. 727-733
    • Kolhe, P.1    Amend, E.2    Singh, S.K.3
  • 48
    • 0032703669 scopus 로고    scopus 로고
    • Effects of buffer composition and processing conditions on aggregation of bovine IgG during freeze-drying
    • Sarciaux J.M., Mansour S., Hageman M.J., Nail S.L. Effects of buffer composition and processing conditions on aggregation of bovine IgG during freeze-drying. J. Pharm. Sci. 1999, 88:1354-1361.
    • (1999) J. Pharm. Sci. , vol.88 , pp. 1354-1361
    • Sarciaux, J.M.1    Mansour, S.2    Hageman, M.J.3    Nail, S.L.4
  • 49
    • 79957597346 scopus 로고    scopus 로고
    • Thermophysical properties of carboxylic and amino acid buffers at subzero temperatures: relevance to frozen state stabilization
    • Sundaramurthi P., Suryanarayanan R. Thermophysical properties of carboxylic and amino acid buffers at subzero temperatures: relevance to frozen state stabilization. J. Phys. Chem. B 2011, 115:7154-7164.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 7154-7164
    • Sundaramurthi, P.1    Suryanarayanan, R.2
  • 50
    • 79951916297 scopus 로고    scopus 로고
    • Predicting the crystallization propensity of carboxylic acid buffers in frozen systems-relevance to freeze-drying
    • Sundaramurthi P., Suryanarayanan R. Predicting the crystallization propensity of carboxylic acid buffers in frozen systems-relevance to freeze-drying. J. Pharm. Sci. 2011, 100:1288-1293.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 1288-1293
    • Sundaramurthi, P.1    Suryanarayanan, R.2
  • 51
    • 79952488362 scopus 로고    scopus 로고
    • The effect of crystallizing and non-crystallizing cosolutes on succinate buffer crystallization and the consequent pH shift in frozen solutions
    • Sundaramurthi P., Suryanarayanan R. The effect of crystallizing and non-crystallizing cosolutes on succinate buffer crystallization and the consequent pH shift in frozen solutions. Pharm. Res. 2011, 28:374-385.
    • (2011) Pharm. Res. , vol.28 , pp. 374-385
    • Sundaramurthi, P.1    Suryanarayanan, R.2
  • 53
    • 0034888365 scopus 로고    scopus 로고
    • Formaldehyde production by Tris buffer in peptide formulations at elevated temperature
    • Song Y., Schowen R.L., Borchardt R.T., Topp E.M. Formaldehyde production by Tris buffer in peptide formulations at elevated temperature. J. Pharm. Sci. 2001, 90:1198-1203.
    • (2001) J. Pharm. Sci. , vol.90 , pp. 1198-1203
    • Song, Y.1    Schowen, R.L.2    Borchardt, R.T.3    Topp, E.M.4
  • 56
    • 35448968555 scopus 로고    scopus 로고
    • Biotechnology applications of amino acids in protein purification and formulations
    • Arakawa T., Tsumoto K., Kita Y., Chang B., Ejima D. Biotechnology applications of amino acids in protein purification and formulations. Amino Acids 2007, 33:587-605.
    • (2007) Amino Acids , vol.33 , pp. 587-605
    • Arakawa, T.1    Tsumoto, K.2    Kita, Y.3    Chang, B.4    Ejima, D.5
  • 57
    • 0346846691 scopus 로고    scopus 로고
    • Influence of histidine on the stability and physical properties of a fully human antibody in aqueous and solid forms
    • Chen B., Bautista R., Yu K., Zapata G.A., Mulkerrin M.G., Chamow S.M. Influence of histidine on the stability and physical properties of a fully human antibody in aqueous and solid forms. Pharm. Res. 2003, 20:1952-1960.
    • (2003) Pharm. Res. , vol.20 , pp. 1952-1960
    • Chen, B.1    Bautista, R.2    Yu, K.3    Zapata, G.A.4    Mulkerrin, M.G.5    Chamow, S.M.6
  • 58
    • 33947716232 scopus 로고    scopus 로고
    • Spectroscopic evaluation of the stabilization of humanized monoclonal antibodies in amino acid formulations
    • Tian F., Middaugh C.R., Offerdahl T., Munson E., Sane S., Rytting J.H. Spectroscopic evaluation of the stabilization of humanized monoclonal antibodies in amino acid formulations. Int. J. Pharm. 2007, 335:20-31.
    • (2007) Int. J. Pharm. , vol.335 , pp. 20-31
    • Tian, F.1    Middaugh, C.R.2    Offerdahl, T.3    Munson, E.4    Sane, S.5    Rytting, J.H.6
  • 59
    • 0032104360 scopus 로고    scopus 로고
    • Antioxidant characteristics of l-histidine
    • Wade A.M., Tucker H.N. Antioxidant characteristics of l-histidine. J. Nutr. Biochem. 1998, 9:308-315.
    • (1998) J. Nutr. Biochem. , vol.9 , pp. 308-315
    • Wade, A.M.1    Tucker, H.N.2
  • 61
    • 69249216709 scopus 로고    scopus 로고
    • Suppression of protein aggregation by l-arginine
    • Lange C., Rudolph R. Suppression of protein aggregation by l-arginine. Curr. Pharm. Biotechnol. 2009, 10:408-414.
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , pp. 408-414
    • Lange, C.1    Rudolph, R.2
  • 62
    • 69249215476 scopus 로고    scopus 로고
    • To be excluded or to bind, that is the question: arginine effects on proteins
    • Nakakido M., Kudou M., Arakawa T., Tsumoto K. To be excluded or to bind, that is the question: arginine effects on proteins. Curr. Pharm. Biotechnol. 2009, 10:415-420.
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , pp. 415-420
    • Nakakido, M.1    Kudou, M.2    Arakawa, T.3    Tsumoto, K.4
  • 63
    • 77958451843 scopus 로고    scopus 로고
    • Interaction of arginine with proteins and the mechanism by which it inhibits aggregation
    • Shukla D., Trout B.L. Interaction of arginine with proteins and the mechanism by which it inhibits aggregation. J. Phys. Chem. B 2010, 114:13426-13438.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 13426-13438
    • Shukla, D.1    Trout, B.L.2
  • 64
    • 0034776736 scopus 로고    scopus 로고
    • Phase transitions of glycine in frozen aqueous solutions and during freeze-drying
    • Pyne A., Suryanarayanan R. Phase transitions of glycine in frozen aqueous solutions and during freeze-drying. Pharm. Res. 2001, 18:1448-1454.
    • (2001) Pharm. Res. , vol.18 , pp. 1448-1454
    • Pyne, A.1    Suryanarayanan, R.2
  • 65
    • 0030724407 scopus 로고    scopus 로고
    • Antioxidants for prevention of methionine oxidation in recombinant monoclonal antibody HER2
    • Lam X.M., Yang J.Y., Cleland J.L. Antioxidants for prevention of methionine oxidation in recombinant monoclonal antibody HER2. J. Pharm. Sci. 1997, 86:1250-1255.
    • (1997) J. Pharm. Sci. , vol.86 , pp. 1250-1255
    • Lam, X.M.1    Yang, J.Y.2    Cleland, J.L.3
  • 66
    • 79551518817 scopus 로고    scopus 로고
    • Local tolerance and stability up to 24months of a new 20% proline-stabilized polyclonal immunoglobulin for subcutaneous administration
    • Maeder W., Lieby P., Sebald A., Spycher M., Pedrussio R., Bolli R. Local tolerance and stability up to 24months of a new 20% proline-stabilized polyclonal immunoglobulin for subcutaneous administration. Biologicals 2011, 39:43-49.
    • (2011) Biologicals , vol.39 , pp. 43-49
    • Maeder, W.1    Lieby, P.2    Sebald, A.3    Spycher, M.4    Pedrussio, R.5    Bolli, R.6
  • 68
    • 3242798849 scopus 로고    scopus 로고
    • A simple method for improving protein solubility and long-term stability
    • Golovanov A.P., Hautbergue G.M., Wilson S.A., Lian L.Y. A simple method for improving protein solubility and long-term stability. J. Am. Chem. Soc. 2004, 126:8933-8939.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8933-8939
    • Golovanov, A.P.1    Hautbergue, G.M.2    Wilson, S.A.3    Lian, L.Y.4
  • 69
    • 70350337659 scopus 로고    scopus 로고
    • Role of naturally occurring osmolytes in protein folding and stability
    • Kumar R. Role of naturally occurring osmolytes in protein folding and stability. Arch. Biochem. Biophys. 2009, 491:1-6.
    • (2009) Arch. Biochem. Biophys. , vol.491 , pp. 1-6
    • Kumar, R.1
  • 70
    • 0022032982 scopus 로고
    • The stabilization of proteins by osmolytes
    • Arakawa T., Timasheff S.N. The stabilization of proteins by osmolytes. Biophys. J. 1985, 47:411-414.
    • (1985) Biophys. J. , vol.47 , pp. 411-414
    • Arakawa, T.1    Timasheff, S.N.2
  • 71
    • 57049105810 scopus 로고    scopus 로고
    • Structural thermodynamics of protein preferential solvation: osmolyte solvation of proteins, aminoacids, and peptides
    • Auton M., Bolen D.W., Rosgen J. Structural thermodynamics of protein preferential solvation: osmolyte solvation of proteins, aminoacids, and peptides. Proteins 2008, 73:802-813.
    • (2008) Proteins , vol.73 , pp. 802-813
    • Auton, M.1    Bolen, D.W.2    Rosgen, J.3
  • 72
    • 4344614677 scopus 로고    scopus 로고
    • Effects of naturally occurring osmolytes on protein stability and solubility: issues important in protein crystallization
    • Bolen D.W. Effects of naturally occurring osmolytes on protein stability and solubility: issues important in protein crystallization. Methods 2004, 34:312-322.
    • (2004) Methods , vol.34 , pp. 312-322
    • Bolen, D.W.1
  • 73
    • 0037137253 scopus 로고    scopus 로고
    • Protein hydration, thermodynamic binding, and preferential hydration
    • Timasheff S.N. Protein hydration, thermodynamic binding, and preferential hydration. Biochemistry 2002, 41:13473-13482.
    • (2002) Biochemistry , vol.41 , pp. 13473-13482
    • Timasheff, S.N.1
  • 76
    • 72749102457 scopus 로고    scopus 로고
    • Mechanisms of protein stabilization and prevention of protein aggregation by glycerol
    • Vagenende V., Yap M.G., Trout B.L. Mechanisms of protein stabilization and prevention of protein aggregation by glycerol. Biochemistry 2009, 48:11084-11096.
    • (2009) Biochemistry , vol.48 , pp. 11084-11096
    • Vagenende, V.1    Yap, M.G.2    Trout, B.L.3
  • 77
    • 79251618192 scopus 로고    scopus 로고
    • Protein and DNA destabilization by osmolytes: the other side of the coin
    • Singh L.R., Poddar N.K., Dar T.A., Kumar R., Ahmad F. Protein and DNA destabilization by osmolytes: the other side of the coin. Life Sci. 2011, 88:117-125.
    • (2011) Life Sci. , vol.88 , pp. 117-125
    • Singh, L.R.1    Poddar, N.K.2    Dar, T.A.3    Kumar, R.4    Ahmad, F.5
  • 78
    • 0038374325 scopus 로고    scopus 로고
    • Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose
    • Kaushik J.K., Bhat R. Why is trehalose an exceptional protein stabilizer? An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose. J. Biol. Chem. 2003, 278:26458-26465.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26458-26465
    • Kaushik, J.K.1    Bhat, R.2
  • 79
    • 0030725266 scopus 로고    scopus 로고
    • Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: role in restricted conformational mobility and compaction of native state
    • Kendrick B.S., Chang B.S., Arakawa T., Peterson B., Randolph T.W., Manning M.C., Carpenter J.F. Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: role in restricted conformational mobility and compaction of native state. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:11917-11922.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11917-11922
    • Kendrick, B.S.1    Chang, B.S.2    Arakawa, T.3    Peterson, B.4    Randolph, T.W.5    Manning, M.C.6    Carpenter, J.F.7
  • 81
    • 79954514686 scopus 로고    scopus 로고
    • Trehalose: current use and future applications
    • Ohtake S., Wang Y.J. Trehalose: current use and future applications. J. Pharm. Sci. 2011, 100:2020-2053.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2020-2053
    • Ohtake, S.1    Wang, Y.J.2
  • 82
    • 35748979712 scopus 로고    scopus 로고
    • Protein stability during freezing: separation of stresses and mechanisms of protein stabilization
    • Bhatnagar B.S., Bogner R.H., Pikal M.J. Protein stability during freezing: separation of stresses and mechanisms of protein stabilization. Pharm. Dev. Technol. 2007, 12:505-523.
    • (2007) Pharm. Dev. Technol. , vol.12 , pp. 505-523
    • Bhatnagar, B.S.1    Bogner, R.H.2    Pikal, M.J.3
  • 83
    • 68949085125 scopus 로고    scopus 로고
    • Mechanisms of protein stabilization in the solid state
    • Chang L.L., Pikal M.J. Mechanisms of protein stabilization in the solid state. J. Pharm. Sci. 2009, 98:2886-2908.
    • (2009) J. Pharm. Sci. , vol.98 , pp. 2886-2908
    • Chang, L.L.1    Pikal, M.J.2
  • 84
    • 23844447975 scopus 로고    scopus 로고
    • Mechanism of protein stabilization by sugars during freeze-drying and storage: native structure preservation, specific interaction, and/or immobilization in a glassy matrix?
    • Chang L.L., Shepherd D., Sun J., Ouellette D., Grant K.L., Tang X.C., Pikal M.J. Mechanism of protein stabilization by sugars during freeze-drying and storage: native structure preservation, specific interaction, and/or immobilization in a glassy matrix?. J. Pharm. Sci. 2005, 94:1427-1444.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1427-1444
    • Chang, L.L.1    Shepherd, D.2    Sun, J.3    Ouellette, D.4    Grant, K.L.5    Tang, X.C.6    Pikal, M.J.7
  • 85
    • 23844461800 scopus 로고    scopus 로고
    • Effect of sorbitol and residual moisture on the stability of lyophilized antibodies: implications for the mechanism of protein stabilization in the solid state
    • Chang L.L., Shepherd D., Sun J., Tang X.C., Pikal M.J. Effect of sorbitol and residual moisture on the stability of lyophilized antibodies: implications for the mechanism of protein stabilization in the solid state. J. Pharm. Sci. 2005, 94:1445-1455.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1445-1455
    • Chang, L.L.1    Shepherd, D.2    Sun, J.3    Tang, X.C.4    Pikal, M.J.5
  • 88
    • 33845410077 scopus 로고    scopus 로고
    • Sorbitol crystallization can lead to protein aggregation in frozen protein formulations
    • Piedmonte D.M., Summers C., McAuley A., Karamujic L., Ratnaswamy G. Sorbitol crystallization can lead to protein aggregation in frozen protein formulations. Pharm. Res. 2007, 24:136-146.
    • (2007) Pharm. Res. , vol.24 , pp. 136-146
    • Piedmonte, D.M.1    Summers, C.2    McAuley, A.3    Karamujic, L.4    Ratnaswamy, G.5
  • 89
    • 67650257183 scopus 로고    scopus 로고
    • Impact of bulking agents on the stability of a lyophilized monoclonal antibody
    • Meyer J.D., Nayar R., Manning M.C. Impact of bulking agents on the stability of a lyophilized monoclonal antibody. Eur. J. Pharm. Sci. 2009, 38:29-38.
    • (2009) Eur. J. Pharm. Sci. , vol.38 , pp. 29-38
    • Meyer, J.D.1    Nayar, R.2    Manning, M.C.3
  • 90
    • 0036285548 scopus 로고    scopus 로고
    • Mannitol-sucrose mixtures-versatile formulations for protein lyophilization
    • Johnson R.E., Kirchhoff C.F., Gaud H.T. Mannitol-sucrose mixtures-versatile formulations for protein lyophilization. J. Pharm. Sci. 2002, 91:914-922.
    • (2002) J. Pharm. Sci. , vol.91 , pp. 914-922
    • Johnson, R.E.1    Kirchhoff, C.F.2    Gaud, H.T.3
  • 91
    • 72149126106 scopus 로고    scopus 로고
    • Development of inhalable dry powder formulation of basic fibroblast growth factor
    • Ibrahim B.M., Jun S.W., Lee M.Y., Kang S.H., Yeo Y. Development of inhalable dry powder formulation of basic fibroblast growth factor. Int. J. Pharm. 2010, 385:66-72.
    • (2010) Int. J. Pharm. , vol.385 , pp. 66-72
    • Ibrahim, B.M.1    Jun, S.W.2    Lee, M.Y.3    Kang, S.H.4    Yeo, Y.5
  • 92
    • 0035936969 scopus 로고    scopus 로고
    • Influence of formulation excipients and physical characteristics of inhalation dry powders on their aerosolization performance
    • Bosquillon C., Lombry C., Preat V., Vanbever R. Influence of formulation excipients and physical characteristics of inhalation dry powders on their aerosolization performance. J. Control. Release 2001, 70:329-339.
    • (2001) J. Control. Release , vol.70 , pp. 329-339
    • Bosquillon, C.1    Lombry, C.2    Preat, V.3    Vanbever, R.4
  • 93
    • 33845906339 scopus 로고    scopus 로고
    • Inhaling medicines: delivering drugs to the body through the lungs
    • Patton J.S., Byron P.R. Inhaling medicines: delivering drugs to the body through the lungs. Nat. Rev. Drug Discov. 2007, 6:67-74.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 67-74
    • Patton, J.S.1    Byron, P.R.2
  • 94
    • 76649084526 scopus 로고    scopus 로고
    • Inhibition of agitation-induced aggregation of an IgG-antibody by hydroxypropyl-beta-cyclodextrin
    • Serno T., Carpenter J.F., Randolph T.W., Winter G. Inhibition of agitation-induced aggregation of an IgG-antibody by hydroxypropyl-beta-cyclodextrin. J. Pharm. Sci. 2010, 99:1193-1206.
    • (2010) J. Pharm. Sci. , vol.99 , pp. 1193-1206
    • Serno, T.1    Carpenter, J.F.2    Randolph, T.W.3    Winter, G.4
  • 95
    • 77951605340 scopus 로고    scopus 로고
    • The effects of substituted cyclodextrins on the colloidal and conformational stability of selected proteins
    • Samra H.S., He F., Bhambhani A., Pipkin J.D., Zimmerer R., Joshi S.B., Middaugh C.R. The effects of substituted cyclodextrins on the colloidal and conformational stability of selected proteins. J. Pharm. Sci. 2010, 99:2800-2818.
    • (2010) J. Pharm. Sci. , vol.99 , pp. 2800-2818
    • Samra, H.S.1    He, F.2    Bhambhani, A.3    Pipkin, J.D.4    Zimmerer, R.5    Joshi, S.B.6    Middaugh, C.R.7
  • 96
    • 0025905723 scopus 로고
    • Use of 2-hydroxypropyl-beta-cyclodextrin as a solubilizing and stabilizing excipient for protein drugs
    • Brewster M.E., Hora M.S., Simpkins J.W., Bodor N. Use of 2-hydroxypropyl-beta-cyclodextrin as a solubilizing and stabilizing excipient for protein drugs. Pharm. Res. 1991, 8:792-795.
    • (1991) Pharm. Res. , vol.8 , pp. 792-795
    • Brewster, M.E.1    Hora, M.S.2    Simpkins, J.W.3    Bodor, N.4
  • 97
    • 0142217495 scopus 로고    scopus 로고
    • Quantification of 5-HMF and dextrose in commercial aqueous dextrose solutions
    • Xu H., Templeton A.C., Reed R.A. Quantification of 5-HMF and dextrose in commercial aqueous dextrose solutions. J. Pharm. Biomed. Anal. 2003, 32:451-459.
    • (2003) J. Pharm. Biomed. Anal. , vol.32 , pp. 451-459
    • Xu, H.1    Templeton, A.C.2    Reed, R.A.3
  • 98
    • 71649111437 scopus 로고    scopus 로고
    • The effect of sucrose hydrolysis on the stability of protein therapeutics during accelerated formulation studies
    • Banks D.D., Hambly D.M., Scavezze J.L., Siska C.C., Stackhouse N.L., Gadgil H.S. The effect of sucrose hydrolysis on the stability of protein therapeutics during accelerated formulation studies. J. Pharm. Sci. 2009, 98:4501-4510.
    • (2009) J. Pharm. Sci. , vol.98 , pp. 4501-4510
    • Banks, D.D.1    Hambly, D.M.2    Scavezze, J.L.3    Siska, C.C.4    Stackhouse, N.L.5    Gadgil, H.S.6
  • 99
    • 0037021791 scopus 로고    scopus 로고
    • Protein modification during anti-viral heat-treatment bioprocessing of factor VIII concentrates, factor IX concentrates, and model proteins in the presence of sucrose
    • Smales C.M., Pepper D.S., James D.C. Protein modification during anti-viral heat-treatment bioprocessing of factor VIII concentrates, factor IX concentrates, and model proteins in the presence of sucrose. Biotechnol. Bioeng. 2002, 77:37-48.
    • (2002) Biotechnol. Bioeng. , vol.77 , pp. 37-48
    • Smales, C.M.1    Pepper, D.S.2    James, D.C.3
  • 100
    • 0029781099 scopus 로고    scopus 로고
    • Effects of reducing sugars on the chemical stability of human relaxin in the lyophilized state
    • Li S., Patapoff T.W., Overcashier D., Hsu C., Nguyen T.H., Borchardt R.T. Effects of reducing sugars on the chemical stability of human relaxin in the lyophilized state. J. Pharm. Sci. 1996, 85:873-877.
    • (1996) J. Pharm. Sci. , vol.85 , pp. 873-877
    • Li, S.1    Patapoff, T.W.2    Overcashier, D.3    Hsu, C.4    Nguyen, T.H.5    Borchardt, R.T.6
  • 101
    • 0036001387 scopus 로고    scopus 로고
    • Pharmaceutical strategies utilizing recombinant human serum albumin
    • Chuang V.T., Kragh-Hansen U., Otagiri M. Pharmaceutical strategies utilizing recombinant human serum albumin. Pharm. Res. 2002, 19:569-577.
    • (2002) Pharm. Res. , vol.19 , pp. 569-577
    • Chuang, V.T.1    Kragh-Hansen, U.2    Otagiri, M.3
  • 102
    • 0029071504 scopus 로고
    • Aggregation of a lyophilized pharmaceutical protein, recombinant human albumin: effect of moisture and stabilization by excipients
    • Costantino H.R., Langer R., Klibanov A.M. Aggregation of a lyophilized pharmaceutical protein, recombinant human albumin: effect of moisture and stabilization by excipients. Biotechnology (N Y) 1995, 13:493-496.
    • (1995) Biotechnology (N Y) , vol.13 , pp. 493-496
    • Costantino, H.R.1    Langer, R.2    Klibanov, A.M.3
  • 103
    • 34347395337 scopus 로고    scopus 로고
    • Formulation development for hydrophobic therapeutic proteins
    • Hawe A., Friess W. Formulation development for hydrophobic therapeutic proteins. Pharm. Dev. Technol. 2007, 12:223-237.
    • (2007) Pharm. Dev. Technol. , vol.12 , pp. 223-237
    • Hawe, A.1    Friess, W.2
  • 104
    • 0033066393 scopus 로고    scopus 로고
    • Stability study of human serum albumin pharmaceutical preparations
    • Oliva A., Santovena A., Llabres M., Farina J.B. Stability study of human serum albumin pharmaceutical preparations. J. Pharm. Pharmacol. 1999, 51:385-392.
    • (1999) J. Pharm. Pharmacol. , vol.51 , pp. 385-392
    • Oliva, A.1    Santovena, A.2    Llabres, M.3    Farina, J.B.4
  • 105
    • 38149029101 scopus 로고    scopus 로고
    • The structure, stability, and complex behavior of recombinant human gelatins
    • Thyagarajapuram N., Olsen D., Middaugh C.R. The structure, stability, and complex behavior of recombinant human gelatins. J. Pharm. Sci. 2007, 96:3363-3378.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 3363-3378
    • Thyagarajapuram, N.1    Olsen, D.2    Middaugh, C.R.3
  • 106
    • 0030929864 scopus 로고    scopus 로고
    • Dependence of the molecular mobility and protein stability of freeze-dried gamma-globulin formulations on the molecular weight of dextran
    • Yoshioka S., Aso Y., Kojima S. Dependence of the molecular mobility and protein stability of freeze-dried gamma-globulin formulations on the molecular weight of dextran. Pharm. Res. 1997, 14:736-741.
    • (1997) Pharm. Res. , vol.14 , pp. 736-741
    • Yoshioka, S.1    Aso, Y.2    Kojima, S.3
  • 108
    • 0031940141 scopus 로고    scopus 로고
    • Effect of high molecular mobility of poly(vinyl alcohol) on protein stability of lyophilized gamma-globulin formulations
    • Yoshioka S., Aso Y., Nakai Y., Kojima S. Effect of high molecular mobility of poly(vinyl alcohol) on protein stability of lyophilized gamma-globulin formulations. J. Pharm. Sci. 1998, 87:147-151.
    • (1998) J. Pharm. Sci. , vol.87 , pp. 147-151
    • Yoshioka, S.1    Aso, Y.2    Nakai, Y.3    Kojima, S.4
  • 110
    • 0033637883 scopus 로고    scopus 로고
    • Freeze-concentration separates proteins and polymer excipients into different amorphous phases
    • Izutsu K., Kojima S. Freeze-concentration separates proteins and polymer excipients into different amorphous phases. Pharm. Res. 2000, 17:1316-1322.
    • (2000) Pharm. Res. , vol.17 , pp. 1316-1322
    • Izutsu, K.1    Kojima, S.2
  • 112
    • 77957742088 scopus 로고    scopus 로고
    • Carrier mediated protein and peptide stabilization
    • Tiwari A.K., Gajbhiye V., Sharma R., Jain N.K. Carrier mediated protein and peptide stabilization. Drug Deliv. 2010, 17:605-616.
    • (2010) Drug Deliv. , vol.17 , pp. 605-616
    • Tiwari, A.K.1    Gajbhiye, V.2    Sharma, R.3    Jain, N.K.4
  • 115
    • 0030338236 scopus 로고    scopus 로고
    • The characterization, stabilization, and formulation of acidic fibroblast growth factor
    • Volkin D.B., Middaugh C.R. The characterization, stabilization, and formulation of acidic fibroblast growth factor. Pharm. Biotechnol. 1996, 9:181-217.
    • (1996) Pharm. Biotechnol. , vol.9 , pp. 181-217
    • Volkin, D.B.1    Middaugh, C.R.2
  • 116
    • 77951669557 scopus 로고    scopus 로고
    • Chemistry of Hofmeister anions and osmolytes
    • Zhang Y., Cremer P.S. Chemistry of Hofmeister anions and osmolytes. Annu. Rev. Phys. Chem. 2010, 61:63-83.
    • (2010) Annu. Rev. Phys. Chem. , vol.61 , pp. 63-83
    • Zhang, Y.1    Cremer, P.S.2
  • 117
    • 33751408436 scopus 로고    scopus 로고
    • Interactions between macromolecules and ions: the Hofmeister series
    • Zhang Y., Cremer P.S. Interactions between macromolecules and ions: the Hofmeister series. Curr. Opin. Chem. Biol. 2006, 10:658-663.
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 658-663
    • Zhang, Y.1    Cremer, P.S.2
  • 118
    • 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 Y.R., Fesinmeyer R.M., Saluja A., Razinkov V., Chase S.F., Laue T.M., Brems D.N. Effective charge measurements reveal selective and preferential accumulation of anions, but not cations, at the protein surface in dilute salt solutions. Protein Sci. 2011, 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
  • 121
    • 27644477360 scopus 로고    scopus 로고
    • Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution
    • Liu J., Nguyen M.D., Andya J.D., Shire S.J. Reversible self-association increases the viscosity of a concentrated monoclonal antibody in aqueous solution. J. Pharm. Sci. 2005, 94:1928-1940.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1928-1940
    • Liu, J.1    Nguyen, M.D.2    Andya, J.D.3    Shire, S.J.4
  • 122
    • 66349132473 scopus 로고    scopus 로고
    • Increasing IgG concentration modulates the conformational heterogeneity and bonding network that influence solution properties
    • Kamerzell T.J., Kanai S., Liu J., Shire S.J., Wang Y.J. Increasing IgG concentration modulates the conformational heterogeneity and bonding network that influence solution properties. J. Phys. Chem. B 2009, 113:6109-6118.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 6109-6118
    • Kamerzell, T.J.1    Kanai, S.2    Liu, J.3    Shire, S.J.4    Wang, Y.J.5
  • 123
    • 34347393658 scopus 로고    scopus 로고
    • Effect of cations and anions on glass transition temperatures in excipient solutions
    • Nesarikar V.V., Nassar M.N. Effect of cations and anions on glass transition temperatures in excipient solutions. Pharm. Dev. Technol. 2007, 12:259-264.
    • (2007) Pharm. Dev. Technol. , vol.12 , pp. 259-264
    • Nesarikar, V.V.1    Nassar, M.N.2
  • 124
    • 27144483813 scopus 로고    scopus 로고
    • Displacement of adsorbed insulin by Tween 80 monitored using total internal reflection fluorescence and ellipsometry
    • Mollmann S.H., Elofsson U., Bukrinsky J.T., Frokjaer S. Displacement of adsorbed insulin by Tween 80 monitored using total internal reflection fluorescence and ellipsometry. Pharm. Res. 2005, 22:1931-1941.
    • (2005) Pharm. Res. , vol.22 , pp. 1931-1941
    • Mollmann, S.H.1    Elofsson, U.2    Bukrinsky, J.T.3    Frokjaer, S.4
  • 128
    • 52449090177 scopus 로고    scopus 로고
    • Polysorbates 20 and 80 used in the formulation of protein biotherapeutics: structure and degradation pathways
    • Kerwin B.A. Polysorbates 20 and 80 used in the formulation of protein biotherapeutics: structure and degradation pathways. J. Pharm. Sci. 2008, 97:2924-2935.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 2924-2935
    • Kerwin, B.A.1
  • 129
    • 0031742802 scopus 로고    scopus 로고
    • Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions
    • Bam N.B., Cleland J.L., Yang J., Manning M.C., Carpenter J.F., Kelley R.F., Randolph T.W. Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions. J. Pharm. Sci. 1998, 87:1554-1559.
    • (1998) J. Pharm. Sci. , vol.87 , pp. 1554-1559
    • Bam, N.B.1    Cleland, J.L.2    Yang, J.3    Manning, M.C.4    Carpenter, J.F.5    Kelley, R.F.6    Randolph, T.W.7
  • 131
    • 36549040103 scopus 로고    scopus 로고
    • Dual effects of Tween 80 on protein stability
    • Wang W., Wang Y.J., Wang D.Q. Dual effects of Tween 80 on protein stability. Int. J. Pharm. 2008, 347:31-38.
    • (2008) Int. J. Pharm. , vol.347 , pp. 31-38
    • Wang, W.1    Wang, Y.J.2    Wang, D.Q.3
  • 132
    • 0030443567 scopus 로고    scopus 로고
    • Surface-induced denaturation of proteins during freezing and its inhibition by surfactants
    • Chang B.S., Kendrick B.S., Carpenter J.F. Surface-induced denaturation of proteins during freezing and its inhibition by surfactants. J. Pharm. Sci. 1996, 85:1325-1330.
    • (1996) J. Pharm. Sci. , vol.85 , pp. 1325-1330
    • Chang, B.S.1    Kendrick, B.S.2    Carpenter, J.F.3
  • 133
    • 0036167323 scopus 로고    scopus 로고
    • A new mechanism for decreasing aggregation of recombinant human interferon-gamma by a surfactant: slowed dissolution of lyophilized formulations in a solution containing 0.03% polysorbate 20
    • Webb S.D., Cleland J.L., Carpenter J.F., Randolph T.W. A new mechanism for decreasing aggregation of recombinant human interferon-gamma by a surfactant: slowed dissolution of lyophilized formulations in a solution containing 0.03% polysorbate 20. J. Pharm. Sci. 2002, 91:543-558.
    • (2002) J. Pharm. Sci. , vol.91 , pp. 543-558
    • Webb, S.D.1    Cleland, J.L.2    Carpenter, J.F.3    Randolph, T.W.4
  • 134
    • 0036784668 scopus 로고    scopus 로고
    • Peroxide formation in polysorbate 80 and protein stability
    • Ha E., Wang W., Wang Y.J. Peroxide formation in polysorbate 80 and protein stability. J. Pharm. Sci. 2002, 91:2252-2264.
    • (2002) J. Pharm. Sci. , vol.91 , pp. 2252-2264
    • Ha, E.1    Wang, W.2    Wang, Y.J.3
  • 135
    • 39749100132 scopus 로고    scopus 로고
    • Behaviour of polysorbate 20 during dialysis, concentration and filtration using membrane separation techniques
    • Mahler H.C., Printz M., Kopf R., Schuller R., Muller R. Behaviour of polysorbate 20 during dialysis, concentration and filtration using membrane separation techniques. J. Pharm. Sci. 2008, 97:764-774.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 764-774
    • Mahler, H.C.1    Printz, M.2    Kopf, R.3    Schuller, R.4    Muller, R.5
  • 136
    • 0035093096 scopus 로고    scopus 로고
    • Oxidative degradation of pharmaceuticals: theory, mechanisms and inhibition
    • Hovorka S., Schoneich C. Oxidative degradation of pharmaceuticals: theory, mechanisms and inhibition. J. Pharm. Sci. 2001, 90:253-269.
    • (2001) J. Pharm. Sci. , vol.90 , pp. 253-269
    • Hovorka, S.1    Schoneich, C.2
  • 137
    • 70349648767 scopus 로고    scopus 로고
    • Measurement and decomposition kinetics of residual hydrogen peroxide in the presence of commonly used excipients and preservatives
    • Towne V., Oswald C.B., Mogg R., Antonello J., Will M., Gimenez J., Washabaugh M., Sitrin R., Zhao Q. Measurement and decomposition kinetics of residual hydrogen peroxide in the presence of commonly used excipients and preservatives. J. Pharm. Sci. 2009, 98:3987-3996.
    • (2009) J. Pharm. Sci. , vol.98 , pp. 3987-3996
    • Towne, V.1    Oswald, C.B.2    Mogg, R.3    Antonello, J.4    Will, M.5    Gimenez, J.6    Washabaugh, M.7    Sitrin, R.8    Zhao, Q.9
  • 138
    • 0029939394 scopus 로고    scopus 로고
    • Catalytic metals, ascorbate and free radicals: combinations to avoid
    • Buettner G.R., Jurkiewicz B.A. Catalytic metals, ascorbate and free radicals: combinations to avoid. Radiat. Res. 1996, 145:532-541.
    • (1996) Radiat. Res. , vol.145 , pp. 532-541
    • Buettner, G.R.1    Jurkiewicz, B.A.2
  • 139
    • 77957338970 scopus 로고    scopus 로고
    • Comparative evaluation of disodium edetate and diethylenetriaminepentaacetic acid as iron chelators to prevent metal-catalyzed destabilization of a therapeutic monoclonal antibody
    • Zhou S., Zhang B., Sturm E., Teagarden D.L., Schoneich C., Kolhe P., Lewis L.M., Muralidhara B.K., Singh S.K. Comparative evaluation of disodium edetate and diethylenetriaminepentaacetic acid as iron chelators to prevent metal-catalyzed destabilization of a therapeutic monoclonal antibody. J. Pharm. Sci. 2010, 99:4239-4250.
    • (2010) J. Pharm. Sci. , vol.99 , pp. 4239-4250
    • Zhou, S.1    Zhang, B.2    Sturm, E.3    Teagarden, D.L.4    Schoneich, C.5    Kolhe, P.6    Lewis, L.M.7    Muralidhara, B.K.8    Singh, S.K.9
  • 141
    • 0033960869 scopus 로고    scopus 로고
    • Evaluation of degradation pathways for plasmid DNA in pharmaceutical formulations via accelerated stability studies
    • Evans R.K., Xu Z., Bohannon K.E., Wang B., Bruner M.W., Volkin D.B. Evaluation of degradation pathways for plasmid DNA in pharmaceutical formulations via accelerated stability studies. J. Pharm. Sci. 2000, 89:76-87.
    • (2000) J. Pharm. Sci. , vol.89 , pp. 76-87
    • Evans, R.K.1    Xu, Z.2    Bohannon, K.E.3    Wang, B.4    Bruner, M.W.5    Volkin, D.B.6
  • 145
    • 4844230143 scopus 로고    scopus 로고
    • Effect of metal cations on the conformation and inactivation of recombinant human factor VIII
    • Derrick T.S., Kashi R.S., Durrani M., Jhingan A., Middaugh C.R. Effect of metal cations on the conformation and inactivation of recombinant human factor VIII. J. Pharm. Sci. 2004, 93:2549-2557.
    • (2004) J. Pharm. Sci. , vol.93 , pp. 2549-2557
    • Derrick, T.S.1    Kashi, R.S.2    Durrani, M.3    Jhingan, A.4    Middaugh, C.R.5
  • 148
    • 38149120374 scopus 로고    scopus 로고
    • Antimicrobial preservative use in parenteral products: past and present
    • Meyer B.K., Ni A., Hu B., Shi L. Antimicrobial preservative use in parenteral products: past and present. J. Pharm. Sci. 2007, 96:3155-3167.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 3155-3167
    • Meyer, B.K.1    Ni, A.2    Hu, B.3    Shi, L.4
  • 149
    • 0347300798 scopus 로고    scopus 로고
    • Development of a multidose formulation for a humanized monoclonal antibody using experimental design techniques
    • Gupta S., Kaisheva E. Development of a multidose formulation for a humanized monoclonal antibody using experimental design techniques. AAPS PharmSci 2003, 5:E8.
    • (2003) AAPS PharmSci , vol.5
    • Gupta, S.1    Kaisheva, E.2
  • 150
    • 0030606850 scopus 로고    scopus 로고
    • Aggregation of recombinant human growth hormone induced by phenolic compounds
    • Maa Y.-F., Hsu C.C. Aggregation of recombinant human growth hormone induced by phenolic compounds. Int. J. Pharm. 1996, 140:155-168.
    • (1996) Int. J. Pharm. , vol.140 , pp. 155-168
    • Maa, Y.-F.1    Hsu, C.C.2
  • 152
    • 2642579304 scopus 로고    scopus 로고
    • Benzyl alcohol-induced destabilization of interferon-gamma: a study by hydrogen-deuterium isotope exchange
    • Tobler S.A., Holmes B.W., Cromwell M.E., Fernandez E.J. Benzyl alcohol-induced destabilization of interferon-gamma: a study by hydrogen-deuterium isotope exchange. J. Pharm. Sci. 2004, 93:1605-1617.
    • (2004) J. Pharm. Sci. , vol.93 , pp. 1605-1617
    • Tobler, S.A.1    Holmes, B.W.2    Cromwell, M.E.3    Fernandez, E.J.4
  • 153
    • 33745876259 scopus 로고    scopus 로고
    • Effects of pH, temperature, and sucrose on benzyl alcohol-induced aggregation of recombinant human granulocyte colony stimulating factor
    • Thirumangalathu R., Krishnan S., Brems D.N., Randolph T.W., Carpenter J.F. Effects of pH, temperature, and sucrose on benzyl alcohol-induced aggregation of recombinant human granulocyte colony stimulating factor. J. Pharm. Sci. 2006, 95:1480-1497.
    • (2006) J. Pharm. Sci. , vol.95 , pp. 1480-1497
    • Thirumangalathu, R.1    Krishnan, S.2    Brems, D.N.3    Randolph, T.W.4    Carpenter, J.F.5
  • 154
    • 0030990078 scopus 로고    scopus 로고
    • The effect of benzyl alcohol on recombinant human interferon-gamma
    • Lam X.M., Patapoff T.W., Nguyen T.H. The effect of benzyl alcohol on recombinant human interferon-gamma. Pharm. Res. 1997, 14:725-729.
    • (1997) Pharm. Res. , vol.14 , pp. 725-729
    • Lam, X.M.1    Patapoff, T.W.2    Nguyen, T.H.3
  • 155
    • 0030947271 scopus 로고    scopus 로고
    • Solvent effects on the solubility and physical stability of human insulin-like growth factor I
    • Fransson J., Hallen D., Florin-Robertsson E. Solvent effects on the solubility and physical stability of human insulin-like growth factor I. Pharm. Res. 1997, 14:606-612.
    • (1997) Pharm. Res. , vol.14 , pp. 606-612
    • Fransson, J.1    Hallen, D.2    Florin-Robertsson, E.3
  • 156
    • 33645451427 scopus 로고    scopus 로고
    • Temperature dependence of benzyl alcohol- and 8-anilinonaphthalene-1-sulfonate-induced aggregation of recombinant human interleukin-1 receptor antagonist
    • Roy S., Katayama D., Dong A., Kerwin B.A., Randolph T.W., Carpenter J.F. Temperature dependence of benzyl alcohol- and 8-anilinonaphthalene-1-sulfonate-induced aggregation of recombinant human interleukin-1 receptor antagonist. Biochemistry 2006, 45:3898-3911.
    • (2006) Biochemistry , vol.45 , pp. 3898-3911
    • Roy, S.1    Katayama, D.2    Dong, A.3    Kerwin, B.A.4    Randolph, T.W.5    Carpenter, J.F.6
  • 157
    • 0032958279 scopus 로고    scopus 로고
    • Influence of calcium ions on the structure and stability of recombinant human deoxyribonuclease I in the aqueous and lyophilized states
    • Chen B., Costantino H.R., Liu J., Hsu C.C., Shire S.J. Influence of calcium ions on the structure and stability of recombinant human deoxyribonuclease I in the aqueous and lyophilized states. J. Pharm. Sci. 1999, 88:477-482.
    • (1999) J. Pharm. Sci. , vol.88 , pp. 477-482
    • Chen, B.1    Costantino, H.R.2    Liu, J.3    Hsu, C.C.4    Shire, S.J.5
  • 158
    • 0030328893 scopus 로고    scopus 로고
    • Stability characterization and formulation development of recombinant human deoxyribonuclease I [Pulmozyme, (dornase alpha)]
    • Shire S.J. Stability characterization and formulation development of recombinant human deoxyribonuclease I [Pulmozyme, (dornase alpha)]. Pharm. Biotechnol. 1996, 9:393-426.
    • (1996) Pharm. Biotechnol. , vol.9 , pp. 393-426
    • Shire, S.J.1
  • 159
    • 0031011382 scopus 로고    scopus 로고
    • Size and conformational stability of the hepatitis A virus used to prepare VAQTA, a highly purified inactivated vaccine
    • Volkin D.B., Burke C.J., Marfia K.E., Oswald C.B., Wolanski B., Middaugh C.R. Size and conformational stability of the hepatitis A virus used to prepare VAQTA, a highly purified inactivated vaccine. J. Pharm. Sci. 1997, 86:666-673.
    • (1997) J. Pharm. Sci. , vol.86 , pp. 666-673
    • Volkin, D.B.1    Burke, C.J.2    Marfia, K.E.3    Oswald, C.B.4    Wolanski, B.5    Middaugh, C.R.6
  • 160
    • 0025418979 scopus 로고
    • Lysine and other diamines dramatically stabilize poliovirus against thermoinactivation
    • Dorval B.L., Chow M., Klibanov A.M. Lysine and other diamines dramatically stabilize poliovirus against thermoinactivation. Biotechnol. Bioeng. 1990, 35:1051-1054.
    • (1990) Biotechnol. Bioeng. , vol.35 , pp. 1051-1054
    • Dorval, B.L.1    Chow, M.2    Klibanov, A.M.3
  • 161
  • 162
    • 33750610316 scopus 로고    scopus 로고
    • Chemical and thermal stability of insulin: effects of zinc and ligand binding to the insulin zinc-hexamer
    • Huus K., Havelund S., Olsen H.B., van de Weert M., Frokjaer S. Chemical and thermal stability of insulin: effects of zinc and ligand binding to the insulin zinc-hexamer. Pharm. Res. 2006, 23:2611-2620.
    • (2006) Pharm. Res. , vol.23 , pp. 2611-2620
    • Huus, K.1    Havelund, S.2    Olsen, H.B.3    van de Weert, M.4    Frokjaer, S.5
  • 165
    • 0027828715 scopus 로고
    • Stability characterization and formulation development of alteplase, a recombinant tissue plasminogen activator
    • Nguyen T.H., Ward C. Stability characterization and formulation development of alteplase, a recombinant tissue plasminogen activator. Pharm. Biotechnol. 1993, 5:91-134.
    • (1993) Pharm. Biotechnol. , vol.5 , pp. 91-134
    • Nguyen, T.H.1    Ward, C.2
  • 168
    • 79955845844 scopus 로고    scopus 로고
    • Design and implementation of high throughput screening assays
    • Macarron R., Hertzberg R.P. Design and implementation of high throughput screening assays. Mol. Biotechnol. 2011, 47:270-285.
    • (2011) Mol. Biotechnol. , vol.47 , pp. 270-285
    • Macarron, R.1    Hertzberg, R.P.2
  • 169
    • 70349482953 scopus 로고    scopus 로고
    • Novel trends in high-throughput screening
    • Mayr L.M., Bojanic D. Novel trends in high-throughput screening. Curr. Opin. Pharmacol. 2009, 9:580-588.
    • (2009) Curr. Opin. Pharmacol. , vol.9 , pp. 580-588
    • Mayr, L.M.1    Bojanic, D.2
  • 171
    • 46249087945 scopus 로고    scopus 로고
    • High-throughput screening of chromatographic separations: III. Monoclonal antibodies on ceramic hydroxyapatite
    • Wensel D.L., Kelley B.D., Coffman J.L. High-throughput screening of chromatographic separations: III. Monoclonal antibodies on ceramic hydroxyapatite. Biotechnol. Bioeng. 2008, 100:839-854.
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 839-854
    • Wensel, D.L.1    Kelley, B.D.2    Coffman, J.L.3
  • 172
    • 46249099122 scopus 로고    scopus 로고
    • High-throughput screening of chromatographic separations: II. Hydrophobic interaction
    • Kramarczyk J.F., Kelley B.D., Coffman J.L. High-throughput screening of chromatographic separations: II. Hydrophobic interaction. Biotechnol. Bioeng. 2008, 100:707-720.
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 707-720
    • Kramarczyk, J.F.1    Kelley, B.D.2    Coffman, J.L.3
  • 174
    • 46249092863 scopus 로고    scopus 로고
    • High-throughput screening of chromatographic separations: I. Method development and column modeling
    • Coffman J.L., Kramarczyk J.F., Kelley B.D. High-throughput screening of chromatographic separations: I. Method development and column modeling. Biotechnol. Bioeng. 2008, 100:605-618.
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 605-618
    • Coffman, J.L.1    Kramarczyk, J.F.2    Kelley, B.D.3
  • 175
    • 79951892441 scopus 로고    scopus 로고
    • Screening of monoclonal antibody formulations based on high-throughput thermostability and viscosity measurements: design of experiment and statistical analysis
    • He F., Woods C.E., Trilisky E., Bower K.M., Litowski J.R., Kerwin B.A., Becker G.W., Narhi L.O., Razinkov V.I. Screening of monoclonal antibody formulations based on high-throughput thermostability and viscosity measurements: design of experiment and statistical analysis. J. Pharm. Sci. 2011, 100:1330-1340.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 1330-1340
    • He, F.1    Woods, C.E.2    Trilisky, E.3    Bower, K.M.4    Litowski, J.R.5    Kerwin, B.A.6    Becker, G.W.7    Narhi, L.O.8    Razinkov, V.I.9
  • 176
    • 77949789023 scopus 로고    scopus 로고
    • High throughput thermostability screening of monoclonal antibody formulations
    • He F., Hogan S., Latypov R.F., Narhi L.O., Razinkov V.I. High throughput thermostability screening of monoclonal antibody formulations. J. Pharm. Sci. 2010, 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
  • 177
    • 77649185864 scopus 로고    scopus 로고
    • High-throughput dynamic light scattering method for measuring viscosity of concentrated protein solutions
    • He F., Becker G.W., Litowski J.R., Narhi L.O., Brems D.N., Razinkov V.I. High-throughput dynamic light scattering method for measuring viscosity of concentrated protein solutions. Anal. Biochem. 2010, 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
  • 179
    • 33745359812 scopus 로고    scopus 로고
    • A systematic approach to stabilizing EBA-175 RII-NG for use as a malaria vaccine
    • Peek L.J., Brandau D.T., Jones L.S., Joshi S.B., Middaugh C.R. A systematic approach to stabilizing EBA-175 RII-NG for use as a malaria vaccine. Vaccine 2006, 24:5839-5851.
    • (2006) Vaccine , vol.24 , pp. 5839-5851
    • Peek, L.J.1    Brandau, D.T.2    Jones, L.S.3    Joshi, S.B.4    Middaugh, C.R.5
  • 180
    • 70349528139 scopus 로고    scopus 로고
    • Towards development of stable formulations of a live attenuated bacterial vaccine: a preformulation study facilitated by a biophysical approach
    • Zeng Y., Fan H., Chiueh G., Pham B., Martin R., Lechuga-Ballesteros D., Truong V.L., Joshi S.B., Middaugh C.R. Towards development of stable formulations of a live attenuated bacterial vaccine: a preformulation study facilitated by a biophysical approach. Hum. Vaccin. 2009, 5:322-331.
    • (2009) Hum. Vaccin. , vol.5 , pp. 322-331
    • Zeng, Y.1    Fan, H.2    Chiueh, G.3    Pham, B.4    Martin, R.5    Lechuga-Ballesteros, D.6    Truong, V.L.7    Joshi, S.B.8    Middaugh, C.R.9
  • 181
    • 58149213971 scopus 로고    scopus 로고
    • Evaluation of the physical stability of the EC5 domain of E-cadherin: effects of pH, temperature, ionic strength, and disulfide bonds
    • Zheng K., Middaugh C.R., Siahaan T.J. Evaluation of the physical stability of the EC5 domain of E-cadherin: effects of pH, temperature, ionic strength, and disulfide bonds. J. Pharm. Sci. 2009, 98:63-73.
    • (2009) J. Pharm. Sci. , vol.98 , pp. 63-73
    • Zheng, K.1    Middaugh, C.R.2    Siahaan, T.J.3
  • 182
    • 65649124496 scopus 로고    scopus 로고
    • Characterization of multiple stable conformers of the EC5 domain of E-cadherin and the interaction of EC5 with E-cadherin peptides
    • Zheng K., Laurence J.S., Kuczera K., Verkhivker G., Middaugh C.R., Siahaan T.J. Characterization of multiple stable conformers of the EC5 domain of E-cadherin and the interaction of EC5 with E-cadherin peptides. Chem. Biol. Drug Des. 2009, 73:584-598.
    • (2009) Chem. Biol. Drug Des. , vol.73 , pp. 584-598
    • Zheng, K.1    Laurence, J.S.2    Kuczera, K.3    Verkhivker, G.4    Middaugh, C.R.5    Siahaan, T.J.6
  • 184
    • 52449110979 scopus 로고    scopus 로고
    • A biophysical characterization of the peptide drug pramlintide (AC137) using empirical phase diagrams
    • Nonoyama A., Laurence J.S., Garriques L., Qi H., Le T., Middaugh C.R. A biophysical characterization of the peptide drug pramlintide (AC137) using empirical phase diagrams. J. Pharm. Sci. 2008, 97:2552-2567.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 2552-2567
    • Nonoyama, A.1    Laurence, J.S.2    Garriques, L.3    Qi, H.4    Le, T.5    Middaugh, C.R.6
  • 186
    • 38149121440 scopus 로고    scopus 로고
    • Stabilization of proteins by recombinant human gelatins
    • Thyagarajapuram N., Olsen D., Middaugh C.R. Stabilization of proteins by recombinant human gelatins. J. Pharm. Sci. 2007, 96:3304-3315.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 3304-3315
    • Thyagarajapuram, N.1    Olsen, D.2    Middaugh, C.R.3
  • 187
    • 34247330236 scopus 로고    scopus 로고
    • Effects of pH and polyanions on the thermal stability of fibroblast growth factor 20
    • Fan H., Vitharana S.N., Chen T., O'Keefe D., Middaugh C.R. Effects of pH and polyanions on the thermal stability of fibroblast growth factor 20. Mol. Pharm. 2007, 4:232-240.
    • (2007) Mol. Pharm. , vol.4 , pp. 232-240
    • Fan, H.1    Vitharana, S.N.2    Chen, T.3    O'Keefe, D.4    Middaugh, C.R.5
  • 188
    • 34250703143 scopus 로고    scopus 로고
    • Effects of solutes on empirical phase diagrams of human fibroblast growth factor 1
    • Fan H., Li H., Zhang M., Middaugh C.R. Effects of solutes on empirical phase diagrams of human fibroblast growth factor 1. J. Pharm. Sci. 2007, 96:1490-1503.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 1490-1503
    • Fan, H.1    Li, H.2    Zhang, M.3    Middaugh, C.R.4
  • 191
    • 77955101936 scopus 로고    scopus 로고
    • Development of a microflow digital imaging assay to characterize protein particulates during storage of a high concentration IgG1 monoclonal antibody formulation
    • Wuchner K., Buchler J., Spycher R., Dalmonte P., Volkin D.B. Development of a microflow digital imaging assay to characterize protein particulates during storage of a high concentration IgG1 monoclonal antibody formulation. J. Pharm. Sci. 2010, 99:3343-3361.
    • (2010) J. Pharm. Sci. , vol.99 , pp. 3343-3361
    • Wuchner, K.1    Buchler, J.2    Spycher, R.3    Dalmonte, P.4    Volkin, D.B.5
  • 192
    • 79954498279 scopus 로고    scopus 로고
    • High throughput formulation screening for global aggregation behaviors of three monoclonal antibodies
    • Li Y., Mach H., Blue J.T. High throughput formulation screening for global aggregation behaviors of three monoclonal antibodies. J. Pharm. Sci. 2011, 100:2120-2135.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2120-2135
    • Li, Y.1    Mach, H.2    Blue, J.T.3
  • 193
    • 78650581772 scopus 로고    scopus 로고
    • H1N1 influenza virus-like particles: physical degradation pathways and identification of stabilizers
    • Kissmann J., Joshi S.B., Haynes J.R., Dokken L., Richardson C., Middaugh C.R. H1N1 influenza virus-like particles: physical degradation pathways and identification of stabilizers. J. Pharm. Sci. 2011, 100:634-645.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 634-645
    • Kissmann, J.1    Joshi, S.B.2    Haynes, J.R.3    Dokken, L.4    Richardson, C.5    Middaugh, C.R.6
  • 194
    • 77954686777 scopus 로고    scopus 로고
    • Vaccines as physically and chemically well-defined pharmaceutical dosage forms
    • Volkin D.B., Middaugh C.R. Vaccines as physically and chemically well-defined pharmaceutical dosage forms. Expert Rev. Vaccines 2010, 9:689-691.
    • (2010) Expert Rev. Vaccines , vol.9 , pp. 689-691
    • Volkin, D.B.1    Middaugh, C.R.2
  • 196
    • 68949111766 scopus 로고    scopus 로고
    • Structural stability of hepatitis C virus envelope glycoprotein E1: effect of pH and dissociative detergents
    • He F., Joshi S.B., Bosman F., Verhaeghe M., Middaugh C.R. Structural stability of hepatitis C virus envelope glycoprotein E1: effect of pH and dissociative detergents. J. Pharm. Sci. 2009, 98:3340-3357.
    • (2009) J. Pharm. Sci. , vol.98 , pp. 3340-3357
    • He, F.1    Joshi, S.B.2    Bosman, F.3    Verhaeghe, M.4    Middaugh, C.R.5
  • 200
    • 34248214194 scopus 로고    scopus 로고
    • High-throughput screening of stabilizers for respiratory syncytial virus: identification of stabilizers and their effects on the conformational thermostability of viral particles
    • Ausar S.F., Espina M., Brock J., Thyagarayapuran N., Repetto R., Khandke L., Middaugh C.R. High-throughput screening of stabilizers for respiratory syncytial virus: identification of stabilizers and their effects on the conformational thermostability of viral particles. Hum. Vaccin. 2007, 3:94-103.
    • (2007) Hum. Vaccin. , vol.3 , pp. 94-103
    • Ausar, S.F.1    Espina, M.2    Brock, J.3    Thyagarayapuran, N.4    Repetto, R.5    Khandke, L.6    Middaugh, C.R.7
  • 202
    • 32644437409 scopus 로고    scopus 로고
    • Effect of pH and ionic strength on the physical stability of adenovirus type 5
    • Rexroad J., Evans R.K., Middaugh C.R. Effect of pH and ionic strength on the physical stability of adenovirus type 5. J. Pharm. Sci. 2006, 95:237-247.
    • (2006) J. Pharm. Sci. , vol.95 , pp. 237-247
    • Rexroad, J.1    Evans, R.K.2    Middaugh, C.R.3
  • 203
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth A., Zscherp C. What vibrations tell us about proteins. Q. Rev. Biophys. 2002, 35:369-430.
    • (2002) Q. Rev. Biophys. , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 204
    • 53049097130 scopus 로고    scopus 로고
    • Pharmaceutical applications of vibrational chemical imaging and chemometrics: a review
    • Gendrin C., Roggo Y., Collet C. Pharmaceutical applications of vibrational chemical imaging and chemometrics: a review. J. Pharm. Biomed. Anal. 2008, 48:533-553.
    • (2008) J. Pharm. Biomed. Anal. , vol.48 , pp. 533-553
    • Gendrin, C.1    Roggo, Y.2    Collet, C.3
  • 206
    • 0015277452 scopus 로고
    • Normal vibrations of polyglycine II
    • Abe Y., Krimm S. Normal vibrations of polyglycine II. Biopolymers 1972, 11:1841-1853.
    • (1972) Biopolymers , vol.11 , pp. 1841-1853
    • Abe, Y.1    Krimm, S.2
  • 207
    • 0033515091 scopus 로고    scopus 로고
    • The two-dimensional IR nonlinear spectroscopy of a cyclic penta-peptide in relation to its three-dimensional structure
    • Hamm P., Lim M., DeGrado W.F., Hochstrasser R.M. The two-dimensional IR nonlinear spectroscopy of a cyclic penta-peptide in relation to its three-dimensional structure. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:2036-2041.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 2036-2041
    • Hamm, P.1    Lim, M.2    DeGrado, W.F.3    Hochstrasser, R.M.4
  • 208
    • 0015407488 scopus 로고
    • Intermolecular interaction effects in the amide I vibrations of polypeptides
    • Krimm S., Abe Y. Intermolecular interaction effects in the amide I vibrations of polypeptides. Proc. Natl. Acad. Sci. U. S. A. 1972, 69:2788-2792.
    • (1972) Proc. Natl. Acad. Sci. U. S. A. , vol.69 , pp. 2788-2792
    • Krimm, S.1    Abe, Y.2
  • 209
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm S., Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 1986, 38:181-364.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 210
    • 0031648837 scopus 로고    scopus 로고
    • Effects of intermolecular hydrogen-bonding interactions on the amide I mode of N-methylacetamide: matrix-isolation infrared studies and ab initio molecular orbital calculations
    • Torii H., Tatsumi T., Kanazawa T., Tasumi M. Effects of intermolecular hydrogen-bonding interactions on the amide I mode of N-methylacetamide: matrix-isolation infrared studies and ab initio molecular orbital calculations. J. Phys. Chem. B 1998, 102:309-314.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 309-314
    • Torii, H.1    Tatsumi, T.2    Kanazawa, T.3    Tasumi, M.4
  • 211
    • 0001443463 scopus 로고    scopus 로고
    • Effects of hydration on the structure, vibration wavenumbers, vibrational force field and resonance Raman intensities of N-methylacetamide
    • Torii H., Tatsumi T., Tatsumi M. Effects of hydration on the structure, vibration wavenumbers, vibrational force field and resonance Raman intensities of N-methylacetamide. J. Raman Spectrosc. 1998, 29:537-546.
    • (1998) J. Raman Spectrosc. , vol.29 , pp. 537-546
    • Torii, H.1    Tatsumi, T.2    Tatsumi, M.3
  • 212
    • 0001324390 scopus 로고
    • Protein secondary structure from FT-IR spectroscopy: correlation with dihedral angles from three dimensional Ramachandran plots
    • Jackson M., Mantsch H.H. Protein secondary structure from FT-IR spectroscopy: correlation with dihedral angles from three dimensional Ramachandran plots. Can. J. Chem. 1991, 69:1639-1642.
    • (1991) Can. J. Chem. , vol.69 , pp. 1639-1642
    • Jackson, M.1    Mantsch, H.H.2
  • 213
    • 0017250407 scopus 로고
    • Infrared spectra and resonance interaction of amide-I vibration of the parallel-chain pleated sheets
    • Chirgadze Y.N., Nevskaya N.A. Infrared spectra and resonance interaction of amide-I vibration of the parallel-chain pleated sheets. Biopolymers 1976, 15:627-636.
    • (1976) Biopolymers , vol.15 , pp. 627-636
    • Chirgadze, Y.N.1    Nevskaya, N.A.2
  • 214
    • 0017288712 scopus 로고
    • Infrared spectra and resonance interaction of amide-I vibration of the antiparallel-chain pleated sheet
    • Chirgadze Y.N., Nevskaya N.A. Infrared spectra and resonance interaction of amide-I vibration of the antiparallel-chain pleated sheet. Biopolymers 1976, 15:607-625.
    • (1976) Biopolymers , vol.15 , pp. 607-625
    • Chirgadze, Y.N.1    Nevskaya, N.A.2
  • 215
    • 0017250408 scopus 로고
    • Infrared spectra and resonance interactions of amide-I and II vibration of alpha-helix
    • Nevskaya N.A., Chirgadze Y.N. Infrared spectra and resonance interactions of amide-I and II vibration of alpha-helix. Biopolymers 1976, 15:637-648.
    • (1976) Biopolymers , vol.15 , pp. 637-648
    • Nevskaya, N.A.1    Chirgadze, Y.N.2
  • 216
    • 33646196840 scopus 로고    scopus 로고
    • Evaluation of the information content in infrared spectra for protein secondary structure determination
    • Goormaghtigh E., Ruysschaert J.M., Raussens V. Evaluation of the information content in infrared spectra for protein secondary structure determination. Biophys. J. 2006, 90:2946-2957.
    • (2006) Biophys. J. , vol.90 , pp. 2946-2957
    • Goormaghtigh, E.1    Ruysschaert, J.M.2    Raussens, V.3
  • 217
    • 0032986173 scopus 로고    scopus 로고
    • Raman spectroscopy of protein and nucleic acid assemblies
    • Thomas G.J. Raman spectroscopy of protein and nucleic acid assemblies. Annu. Rev. Biophys. Biomol. Struct. 1999, 28:1-27.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 1-27
    • Thomas, G.J.1
  • 218
    • 36849073223 scopus 로고    scopus 로고
    • Raman spectroscopy of protein pharmaceuticals
    • Wen Z.Q. Raman spectroscopy of protein pharmaceuticals. J. Pharm. Sci. 2007, 96:2861-2878.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 2861-2878
    • Wen, Z.Q.1
  • 219
    • 0344004860 scopus 로고    scopus 로고
    • A holistic approach to protein secondary structure characterization using amide I band Raman spectroscopy
    • Sane S.U., Cramer S.M., Przybycien T.M. A holistic approach to protein secondary structure characterization using amide I band Raman spectroscopy. Anal. Biochem. 1999, 269:255-272.
    • (1999) Anal. Biochem. , vol.269 , pp. 255-272
    • Sane, S.U.1    Cramer, S.M.2    Przybycien, T.M.3
  • 221
    • 47749137757 scopus 로고    scopus 로고
    • Measurement of the distribution of site enhancements in surface-enhanced Raman scattering
    • Fang Y., Seong N.H., Dlott D.D. Measurement of the distribution of site enhancements in surface-enhanced Raman scattering. Science 2008, 321:388-392.
    • (2008) Science , vol.321 , pp. 388-392
    • Fang, Y.1    Seong, N.H.2    Dlott, D.D.3
  • 223
    • 43049122134 scopus 로고    scopus 로고
    • Single-molecule and single-nanoparticle SERS: from fundamental mechanisms to biomedical applications
    • Qian X.M., Nie S.M. Single-molecule and single-nanoparticle SERS: from fundamental mechanisms to biomedical applications. Chem. Soc. Rev. 2008, 37:912-920.
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 912-920
    • Qian, X.M.1    Nie, S.M.2
  • 224
    • 67649200157 scopus 로고    scopus 로고
    • A unified view of surface-enhanced Raman scattering
    • Lombardi J.R., Birke R.L. A unified view of surface-enhanced Raman scattering. Acc. Chem. Res. 2009, 42:734-742.
    • (2009) Acc. Chem. Res. , vol.42 , pp. 734-742
    • Lombardi, J.R.1    Birke, R.L.2
  • 225
    • 0036802313 scopus 로고    scopus 로고
    • Protein and peptide secondary structure and conformational determination with vibrational circular dichroism
    • Keiderling T.A. Protein and peptide secondary structure and conformational determination with vibrational circular dichroism. Curr. Opin. Chem. Biol. 2002, 6:682-688.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 682-688
    • Keiderling, T.A.1
  • 226
    • 0022230575 scopus 로고
    • Vibrational circular dichroism
    • Stephens P.J. Vibrational circular dichroism. Annu. Rev. Phys. Chem. 1985, 36:213-241.
    • (1985) Annu. Rev. Phys. Chem. , vol.36 , pp. 213-241
    • Stephens, P.J.1
  • 228
    • 77954000803 scopus 로고    scopus 로고
    • Applications of vibrational optical activity in the pharmaceutical industry
    • John Wiley and Sons, D. Pivonka, J. Chalmers, P. Griffiths (Eds.)
    • Nafie L.A., Dukor R.K. Applications of vibrational optical activity in the pharmaceutical industry. The Handbook of Vibrational Spectroscopy 2007, John Wiley and Sons. D. Pivonka, J. Chalmers, P. Griffiths (Eds.).
    • (2007) The Handbook of Vibrational Spectroscopy
    • Nafie, L.A.1    Dukor, R.K.2
  • 229
    • 80054757301 scopus 로고    scopus 로고
    • Dynamics of water interacting with interfaces, molecules, and ions
    • (in press), doi:doi:10.1021/ar2000088
    • M.D. Fayer, Dynamics of water interacting with interfaces, molecules, and ions, Acc. Chem. Res. (in press), doi:. doi:10.1021/ar2000088.
    • Acc. Chem. Res.
    • Fayer, M.D.1
  • 230
    • 79952751402 scopus 로고    scopus 로고
    • Conformational switching between protein substates studied with 2D IR vibrational echo spectroscopy and molecular dynamics simulations
    • Bagchi S., Thorpe D.G., Thorpe I.F., Voth G.A., Fayer M.D. Conformational switching between protein substates studied with 2D IR vibrational echo spectroscopy and molecular dynamics simulations. J. Phys. Chem. B 2010, 114:17187-17193.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 17187-17193
    • Bagchi, S.1    Thorpe, D.G.2    Thorpe, I.F.3    Voth, G.A.4    Fayer, M.D.5
  • 231
    • 58849154044 scopus 로고    scopus 로고
    • Ion-water hydrogen-bond switching observed with 2D IR vibrational echo chemical exchange spectroscopy
    • Moilanen D.E., Wong D., Rosenfeld D.E., Fenn E.E., Fayer M.D. Ion-water hydrogen-bond switching observed with 2D IR vibrational echo chemical exchange spectroscopy. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:375-380.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 375-380
    • Moilanen, D.E.1    Wong, D.2    Rosenfeld, D.E.3    Fenn, E.E.4    Fayer, M.D.5
  • 232
    • 70350484725 scopus 로고    scopus 로고
    • Water dynamics in salt solutions studied with ultrafast two-dimensional infrared (2D IR) vibrational echo spectroscopy
    • Fayer M.D., Moilanen D.E., Wong D., Rosenfeld D.E., Fenn E.E., Park S. Water dynamics in salt solutions studied with ultrafast two-dimensional infrared (2D IR) vibrational echo spectroscopy. Acc. Chem. Res. 2009, 42:1210-1219.
    • (2009) Acc. Chem. Res. , vol.42 , pp. 1210-1219
    • Fayer, M.D.1    Moilanen, D.E.2    Wong, D.3    Rosenfeld, D.E.4    Fenn, E.E.5    Park, S.6
  • 233
    • 67449091507 scopus 로고    scopus 로고
    • Dynamics of liquids, molecules, and proteins measured with ultrafast 2D IR vibrational echo chemical exchange spectroscopy
    • Fayer M.D. Dynamics of liquids, molecules, and proteins measured with ultrafast 2D IR vibrational echo chemical exchange spectroscopy. Annu. Rev. Phys. Chem. 2009, 60:21-38.
    • (2009) Annu. Rev. Phys. Chem. , vol.60 , pp. 21-38
    • Fayer, M.D.1
  • 234
    • 33846476186 scopus 로고    scopus 로고
    • Ultrafast 2D IR vibrational echo spectroscopy
    • Zheng J., Kwak K., Fayer M.D. Ultrafast 2D IR vibrational echo spectroscopy. Acc. Chem. Res. 2007, 40:75-83.
    • (2007) Acc. Chem. Res. , vol.40 , pp. 75-83
    • Zheng, J.1    Kwak, K.2    Fayer, M.D.3
  • 236
    • 33644767320 scopus 로고    scopus 로고
    • Visualization and characterization of the infrared active amide I vibrations of proteins
    • Chung H.S., Tokmakoff A. Visualization and characterization of the infrared active amide I vibrations of proteins. J. Phys. Chem. B 2006, 110:2888-2898.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 2888-2898
    • Chung, H.S.1    Tokmakoff, A.2
  • 237
    • 80052193169 scopus 로고    scopus 로고
    • Identification of arginine residues in peptides by 2D-IR echo spectroscopy
    • Ghosh A., Tucker M.J., Hochstrasser R.M. Identification of arginine residues in peptides by 2D-IR echo spectroscopy. J. Phys. Chem. A 2011, 115:9731-9738.
    • (2011) J. Phys. Chem. A , vol.115 , pp. 9731-9738
    • Ghosh, A.1    Tucker, M.J.2    Hochstrasser, R.M.3
  • 240
    • 35548952683 scopus 로고    scopus 로고
    • Multidimensional ultrafast spectroscopy special feature: multidimensional ultrafast spectroscopy
    • Hochstrasser R.M. Multidimensional ultrafast spectroscopy special feature: multidimensional ultrafast spectroscopy. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:14189.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 14189
    • Hochstrasser, R.M.1
  • 241
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody R.W. Circular dichroism. Methods Enzymol. 1995, 246:34-71.
    • (1995) Methods Enzymol. , vol.246 , pp. 34-71
    • Woody, R.W.1
  • 242
    • 1642546383 scopus 로고    scopus 로고
    • Computation and analysis of protein circular dichroism spectra
    • Sreerama N., Woody R.W. Computation and analysis of protein circular dichroism spectra. Methods Enzymol. 2004, 383:318-351.
    • (2004) Methods Enzymol. , vol.383 , pp. 318-351
    • Sreerama, N.1    Woody, R.W.2
  • 243
    • 0347994116 scopus 로고    scopus 로고
    • On the analysis of membrane protein circular dichroism spectra
    • Sreerama N., Woody R.W. On the analysis of membrane protein circular dichroism spectra. Protein Sci. 2004, 13:100-112.
    • (2004) Protein Sci. , vol.13 , pp. 100-112
    • Sreerama, N.1    Woody, R.W.2
  • 244
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: a practical guide
    • Johnson C.W. Protein secondary structure and circular dichroism: a practical guide. Proteins: Struct. Funct. Genet. 1990, 7:205-214.
    • (1990) Proteins: Struct. Funct. Genet. , vol.7 , pp. 205-214
    • Johnson, C.W.1
  • 245
    • 33646569374 scopus 로고    scopus 로고
    • Ultraviolet absorption spectroscopy
    • American Association of Pharmaceutical Scientists, Arlington, VA, W. Jiskoot, D.J. Crommelin (Eds.)
    • Kueltzo L.A., Middaugh C.R. Ultraviolet absorption spectroscopy. Methods for Structural Analysis of Protein Pharmaceuticals 2005, American Association of Pharmaceutical Scientists, Arlington, VA. W. Jiskoot, D.J. Crommelin (Eds.).
    • (2005) Methods for Structural Analysis of Protein Pharmaceuticals
    • Kueltzo, L.A.1    Middaugh, C.R.2
  • 247
    • 79951862242 scopus 로고    scopus 로고
    • Ultraviolet spectroscopy as a tool in therapeutic protein development
    • Mach H., Middaugh C.R. Ultraviolet spectroscopy as a tool in therapeutic protein development. J. Pharm. Sci. 2011, 100:1214-1227.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 1214-1227
    • Mach, H.1    Middaugh, C.R.2
  • 248
    • 0041336626 scopus 로고    scopus 로고
    • Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: a bGCSF case study
    • Kueltzo L.A., Ersoy B., Ralston J.P., Middaugh C.R. Derivative absorbance spectroscopy and protein phase diagrams as tools for comprehensive protein characterization: a bGCSF case study. J. Pharm. Sci. 2003, 92:1805-1820.
    • (2003) J. Pharm. Sci. , vol.92 , pp. 1805-1820
    • Kueltzo, L.A.1    Ersoy, B.2    Ralston, J.P.3    Middaugh, C.R.4
  • 249
    • 73149083990 scopus 로고    scopus 로고
    • Temperature dependent 2nd derivative absorbance spectroscopy of aromatic amino acids as a probe of protein dynamics
    • Esfandiary R., Hunjan J.S., Lushington G.H., Joshi S.B., Middaugh C.R. Temperature dependent 2nd derivative absorbance spectroscopy of aromatic amino acids as a probe of protein dynamics. Protein Sci. 2009, 18:2603-2614.
    • (2009) Protein Sci. , vol.18 , pp. 2603-2614
    • Esfandiary, R.1    Hunjan, J.S.2    Lushington, G.H.3    Joshi, S.B.4    Middaugh, C.R.5
  • 252
    • 0024352110 scopus 로고
    • Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • Klunk W.E., Pettegrew J.W., Abraham D.J. Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. J. Histochem. Cytochem. 1989, 37:1273-1281.
    • (1989) J. Histochem. Cytochem. , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 253
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of beta-sheet amyloid fibril structures with thioflavin T
    • LeVine H. Quantification of beta-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 1999, 309:274-284.
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • LeVine, H.1
  • 254
    • 33846022722 scopus 로고    scopus 로고
    • Conformational flexibility, hydration and state parameter fluctuations of fibroblast growth factor-10: effects of ligand binding
    • Kamerzell T.J., Unruh J.R., Johnson C.K., Middaugh C.R. Conformational flexibility, hydration and state parameter fluctuations of fibroblast growth factor-10: effects of ligand binding. Biochemistry 2006, 45:15288-15300.
    • (2006) Biochemistry , vol.45 , pp. 15288-15300
    • Kamerzell, T.J.1    Unruh, J.R.2    Johnson, C.K.3    Middaugh, C.R.4
  • 255
    • 33947538420 scopus 로고    scopus 로고
    • Effects of stabilizers on the destabilization of proteins upon adsorption to aluminum salt adjuvants
    • Peek L.J., Martin T.T., Elk Nation C., Pegram S.A., Middaugh C.R. Effects of stabilizers on the destabilization of proteins upon adsorption to aluminum salt adjuvants. J. Pharm. Sci. 2007, 96:547-557.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 547-557
    • Peek, L.J.1    Martin, T.T.2    Elk Nation, C.3    Pegram, S.A.4    Middaugh, C.R.5
  • 257
    • 0029091385 scopus 로고
    • Dielectric relaxation spectroscopy and some applications in the pharmaceutical sciences
    • Smith G., Duffy A.P., Shen J., Olliff C.J. Dielectric relaxation spectroscopy and some applications in the pharmaceutical sciences. J. Pharm. Sci. 1995, 84:1029-1044.
    • (1995) J. Pharm. Sci. , vol.84 , pp. 1029-1044
    • Smith, G.1    Duffy, A.P.2    Shen, J.3    Olliff, C.J.4
  • 258
    • 42449118010 scopus 로고    scopus 로고
    • Immunoglobulin dynamics, conformational fluctuations, and nonlinear elasticity and their effects on stability
    • Kamerzell T.J., Ramsey J.D., Middaugh C.R. Immunoglobulin dynamics, conformational fluctuations, and nonlinear elasticity and their effects on stability. J. Phys. Chem. B 2008, 112:3240-3250.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 3240-3250
    • Kamerzell, T.J.1    Ramsey, J.D.2    Middaugh, C.R.3
  • 259
    • 0027535729 scopus 로고
    • Hydrational and intrinsic compressibilities of globular proteins
    • Kharakoz D.P., Sarvazyan A.P. Hydrational and intrinsic compressibilities of globular proteins. Biopolymers 1993, 33:11-26.
    • (1993) Biopolymers , vol.33 , pp. 11-26
    • Kharakoz, D.P.1    Sarvazyan, A.P.2
  • 260
    • 0025855018 scopus 로고
    • Ultrasonic velocimetry of biological compounds
    • Sarvazyan A.P. Ultrasonic velocimetry of biological compounds. Annu. Rev. Biophys. Biophys. Chem. 1991, 20:321-342.
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 321-342
    • Sarvazyan, A.P.1
  • 261
    • 33845923185 scopus 로고    scopus 로고
    • The effects of cosolutes on protein dynamics: the reversal of denaturant-induced protein fluctuations by trimethylamine N-oxide
    • Doan-Nguyen V., Loria J.P. The effects of cosolutes on protein dynamics: the reversal of denaturant-induced protein fluctuations by trimethylamine N-oxide. Protein Sci. 2007, 16:20-29.
    • (2007) Protein Sci. , vol.16 , pp. 20-29
    • Doan-Nguyen, V.1    Loria, J.P.2
  • 262
    • 0028787226 scopus 로고
    • Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy
    • Frank M.K., Clore G.M., Gronenborn A.M. Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy. Protein Sci. 1995, 4:2605-2615.
    • (1995) Protein Sci. , vol.4 , pp. 2605-2615
    • Frank, M.K.1    Clore, G.M.2    Gronenborn, A.M.3
  • 264
    • 33645834303 scopus 로고    scopus 로고
    • New tools provide new insights in NMR studies of protein dynamics
    • Mittermaier A., Kay L.E. New tools provide new insights in NMR studies of protein dynamics. Science 2006, 312:224-228.
    • (2006) Science , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 265
    • 55749115080 scopus 로고    scopus 로고
    • High-field solution NMR spectroscopy as a tool for assessing protein interactions with small molecule ligands
    • Skinner A.L., Laurence J.S. High-field solution NMR spectroscopy as a tool for assessing protein interactions with small molecule ligands. J. Pharm. Sci. 2008, 97:4670-4695.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 4670-4695
    • Skinner, A.L.1    Laurence, J.S.2
  • 266
    • 77951518291 scopus 로고    scopus 로고
    • Probing residue-specific interactions in the stabilization of proteins using high-resolution NMR: a study of disulfide bond compensation
    • Skinner A.L., Laurence J.S. Probing residue-specific interactions in the stabilization of proteins using high-resolution NMR: a study of disulfide bond compensation. J. Pharm. Sci. 2010, 99:2643-2654.
    • (2010) J. Pharm. Sci. , vol.99 , pp. 2643-2654
    • Skinner, A.L.1    Laurence, J.S.2
  • 267
    • 0019011405 scopus 로고
    • Fluctuations of protein structure as expressed in the distribution of hydrogen exchange rate constants
    • Knox D.G., Rosenberg A. Fluctuations of protein structure as expressed in the distribution of hydrogen exchange rate constants. Biopolymers 1980, 19:1049-1068.
    • (1980) Biopolymers , vol.19 , pp. 1049-1068
    • Knox, D.G.1    Rosenberg, A.2
  • 268
    • 33646925084 scopus 로고    scopus 로고
    • Protein folding pathways studied by pulsed- and native-state hydrogen exchange
    • Bai Y. Protein folding pathways studied by pulsed- and native-state hydrogen exchange. Chem. Rev. 2006, 106:1757-1768.
    • (2006) Chem. Rev. , vol.106 , pp. 1757-1768
    • Bai, Y.1
  • 269
    • 0029643523 scopus 로고
    • Protein folding intermediates: native-state hydrogen exchange
    • Bai Y., Sosnick T.R., Mayne L., Englander S.W. Protein folding intermediates: native-state hydrogen exchange. Science 1995, 269:192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 270
    • 0030612609 scopus 로고    scopus 로고
    • Hydrogen exchange: the modern legacy of Linderstrom-Lang
    • Englander S.W., Mayne L., Bai Y., Sosnick T.R. Hydrogen exchange: the modern legacy of Linderstrom-Lang. Protein Sci. 1997, 6:1101-1109.
    • (1997) Protein Sci. , vol.6 , pp. 1101-1109
    • Englander, S.W.1    Mayne, L.2    Bai, Y.3    Sosnick, T.R.4
  • 272
    • 34548230395 scopus 로고    scopus 로고
    • Two-dimensional correlation spectroscopy reveals coupled immunoglobulin regions of differential flexibility that influence stability
    • Kamerzell T.J., Middaugh C.R. Two-dimensional correlation spectroscopy reveals coupled immunoglobulin regions of differential flexibility that influence stability. Biochemistry 2007, 46:9762-9773.
    • (2007) Biochemistry , vol.46 , pp. 9762-9773
    • Kamerzell, T.J.1    Middaugh, C.R.2
  • 273
    • 4143121255 scopus 로고    scopus 로고
    • Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
    • Lo M.C., Aulabaugh A., Jin G., Cowling R., Bard J., Malamas M., Ellestad G. Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery. Anal. Biochem. 2004, 332:153-159.
    • (2004) Anal. Biochem. , vol.332 , pp. 153-159
    • Lo, M.C.1    Aulabaugh, A.2    Jin, G.3    Cowling, R.4    Bard, J.5    Malamas, M.6    Ellestad, G.7
  • 275
    • 53549116738 scopus 로고    scopus 로고
    • The complex inter-relationships between protein flexibility and stability
    • Kamerzell T.J., Middaugh C.R. The complex inter-relationships between protein flexibility and stability. J. Pharm. Sci. 2008, 97:3494-3517.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 3494-3517
    • Kamerzell, T.J.1    Middaugh, C.R.2
  • 276
    • 0036363969 scopus 로고    scopus 로고
    • The red-edge effects: 30years of exploration
    • Demchenko A.P. The red-edge effects: 30years of exploration. Luminescence 2002, 17:19-42.
    • (2002) Luminescence , vol.17 , pp. 19-42
    • Demchenko, A.P.1
  • 277
    • 0021766889 scopus 로고
    • Red-edge excitation of fluorescence and dynamic properties of proteins and membranes
    • Lakowicz J.R., Keating-Nakamoto S. Red-edge excitation of fluorescence and dynamic properties of proteins and membranes. Biochemistry 1984, 23:3013-3021.
    • (1984) Biochemistry , vol.23 , pp. 3013-3021
    • Lakowicz, J.R.1    Keating-Nakamoto, S.2
  • 278
    • 79955963495 scopus 로고    scopus 로고
    • Applications of pressure perturbation calorimetry in biophysical studies
    • Zhai Y., Okoro L., Cooper A., Winter R. Applications of pressure perturbation calorimetry in biophysical studies. Biophys. Chem. 2011, 156:13-23.
    • (2011) Biophys. Chem. , vol.156 , pp. 13-23
    • Zhai, Y.1    Okoro, L.2    Cooper, A.3    Winter, R.4
  • 279
    • 78650350863 scopus 로고    scopus 로고
    • Volume changes associated with guanidine hydrochloride, temperature, and ethanol induced unfolding of lysozyme
    • Sirotkin V.A., Winter R. Volume changes associated with guanidine hydrochloride, temperature, and ethanol induced unfolding of lysozyme. J. Phys. Chem. B 2010, 114:16881-16886.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 16881-16886
    • Sirotkin, V.A.1    Winter, R.2
  • 280
    • 2442419632 scopus 로고    scopus 로고
    • Pressure perturbation calorimetry: a new technique provides surprising results on the effects of co-solvents on protein solvation and unfolding behaviour
    • Ravindra R., Winter R. Pressure perturbation calorimetry: a new technique provides surprising results on the effects of co-solvents on protein solvation and unfolding behaviour. Chemphyschem 2004, 5:566-571.
    • (2004) Chemphyschem , vol.5 , pp. 566-571
    • Ravindra, R.1    Winter, R.2
  • 281
    • 79953762890 scopus 로고    scopus 로고
    • Probing free-energy surfaces with differential scanning calorimetry
    • Sanchez-Ruiz J.M. Probing free-energy surfaces with differential scanning calorimetry. Annu. Rev. Phys. Chem. 2011, 62:231-255.
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 231-255
    • Sanchez-Ruiz, J.M.1
  • 283
    • 0032850996 scopus 로고    scopus 로고
    • Thermodynamic analysis of biomolecular interactions
    • Cooper A. Thermodynamic analysis of biomolecular interactions. Curr. Opin. Chem. Biol. 1999, 3:557-563.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 557-563
    • Cooper, A.1
  • 285
    • 34250641961 scopus 로고    scopus 로고
    • Isothermal titration calorimetry to determine association constants for high-affinity ligands
    • Velazquez-Campoy A., Freire E. Isothermal titration calorimetry to determine association constants for high-affinity ligands. Nat. Protoc. 2006, 1:186-191.
    • (2006) Nat. Protoc. , vol.1 , pp. 186-191
    • Velazquez-Campoy, A.1    Freire, E.2
  • 286
    • 61849095281 scopus 로고    scopus 로고
    • Isothermal titration calorimetry: general formalism using binding polynomials
    • Freire E., Schon A., Velazquez-Campoy A. Isothermal titration calorimetry: general formalism using binding polynomials. Methods Enzymol. 2009, 455:127-155.
    • (2009) Methods Enzymol. , vol.455 , pp. 127-155
    • Freire, E.1    Schon, A.2    Velazquez-Campoy, A.3
  • 287
    • 43249095250 scopus 로고    scopus 로고
    • The interaction of heparin/polyanions with bovine, porcine, and human growth hormone
    • Joshi S.B., Kamerzell T.J., McNown C., Middaugh C.R. The interaction of heparin/polyanions with bovine, porcine, and human growth hormone. J. Pharm. Sci. 2008, 97:1368-1385.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 1368-1385
    • Joshi, S.B.1    Kamerzell, T.J.2    McNown, C.3    Middaugh, C.R.4
  • 289
    • 33947544337 scopus 로고    scopus 로고
    • Highly concentrated monoclonal antibody solutions: direct analysis of physical structure and thermal stability
    • Harn N., Allan C., Oliver C., Middaugh C.R. Highly concentrated monoclonal antibody solutions: direct analysis of physical structure and thermal stability. J. Pharm. Sci. 2007, 96:532-546.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 532-546
    • Harn, N.1    Allan, C.2    Oliver, C.3    Middaugh, C.R.4
  • 290
    • 0030835825 scopus 로고    scopus 로고
    • Preferential solvation changes upon lysozyme heat denaturation in mixed solvents
    • Kovrigin E.L., Potekhin S.A. Preferential solvation changes upon lysozyme heat denaturation in mixed solvents. Biochemistry 1997, 36:9195-9199.
    • (1997) Biochemistry , vol.36 , pp. 9195-9199
    • Kovrigin, E.L.1    Potekhin, S.A.2
  • 291
    • 0029034433 scopus 로고
    • An osmolyte effect on the heat capacity change for protein folding
    • Plaza del Pino I.M., Sanchez-Ruiz J.M. An osmolyte effect on the heat capacity change for protein folding. Biochemistry 1995, 34:8621-8630.
    • (1995) Biochemistry , vol.34 , pp. 8621-8630
    • Plaza del Pino, I.M.1    Sanchez-Ruiz, J.M.2
  • 292
    • 0016699207 scopus 로고
    • Macromolecular binding
    • Schellman J.A. Macromolecular binding. Biopolymers 1975, 14:999-1018.
    • (1975) Biopolymers , vol.14 , pp. 999-1018
    • Schellman, J.A.1
  • 293
    • 0025030410 scopus 로고
    • A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures
    • Schellman J.A. A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures. Biophys. Chem. 1990, 37:121-140.
    • (1990) Biophys. Chem. , vol.37 , pp. 121-140
    • Schellman, J.A.1
  • 294
    • 1542502033 scopus 로고    scopus 로고
    • Microcalorimetric study of the effect of dimethylsulfoxide on the heat denaturation of lysozyme
    • Kovrigin E.L., Potekhin S.A. Microcalorimetric study of the effect of dimethylsulfoxide on the heat denaturation of lysozyme. Biofizika 1996, 41:1201-1206.
    • (1996) Biofizika , vol.41 , pp. 1201-1206
    • Kovrigin, E.L.1    Potekhin, S.A.2
  • 295
    • 0033992112 scopus 로고    scopus 로고
    • On the stabilizing action of protein denaturants: acetonitrile effect on stability of lysozyme in aqueous solutions
    • Kovrigin E.L., Potekhin S.A. On the stabilizing action of protein denaturants: acetonitrile effect on stability of lysozyme in aqueous solutions. Biophys. Chem. 2000, 83:45-59.
    • (2000) Biophys. Chem. , vol.83 , pp. 45-59
    • Kovrigin, E.L.1    Potekhin, S.A.2
  • 296
    • 1642409882 scopus 로고    scopus 로고
    • Effects of chaotropic and kosmotropic cosolvents on the pressure-induced unfolding and denaturation of proteins: an FT-IR study on staphylococcal nuclease
    • Herberhold H., Royer C.A., Winter R. Effects of chaotropic and kosmotropic cosolvents on the pressure-induced unfolding and denaturation of proteins: an FT-IR study on staphylococcal nuclease. Biochemistry 2004, 43:3336-3345.
    • (2004) Biochemistry , vol.43 , pp. 3336-3345
    • Herberhold, H.1    Royer, C.A.2    Winter, R.3
  • 297
    • 77950802384 scopus 로고    scopus 로고
    • Four-dimensional electron microscopy
    • Zewail A.H. Four-dimensional electron microscopy. Science 2010, 328:187-193.
    • (2010) Science , vol.328 , pp. 187-193
    • Zewail, A.H.1
  • 298
    • 34547202026 scopus 로고    scopus 로고
    • Target-locking acquisition with real-time confocal (TARC) microscopy
    • Lu P.J., Sims P.A., Oki H., Macarthur J.B., Weitz D.A. Target-locking acquisition with real-time confocal (TARC) microscopy. Opt. Express 2007, 15:8702-8712.
    • (2007) Opt. Express , vol.15 , pp. 8702-8712
    • Lu, P.J.1    Sims, P.A.2    Oki, H.3    Macarthur, J.B.4    Weitz, D.A.5
  • 301
    • 0033593012 scopus 로고    scopus 로고
    • Varieties of imaging with scanning probe microscopes
    • Hansma H.G. Varieties of imaging with scanning probe microscopes. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:14678-14680.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 14678-14680
    • Hansma, H.G.1
  • 302
    • 69549111335 scopus 로고    scopus 로고
    • The chemical structure of a molecule resolved by atomic force microscopy
    • Gross L., Mohn F., Moll N., Liljeroth P., Meyer G. The chemical structure of a molecule resolved by atomic force microscopy. Science 2009, 325:1110-1114.
    • (2009) Science , vol.325 , pp. 1110-1114
    • Gross, L.1    Mohn, F.2    Moll, N.3    Liljeroth, P.4    Meyer, G.5
  • 303
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • Hinterdorfer P., Dufrene Y.F. Detection and localization of single molecular recognition events using atomic force microscopy. Nat. Methods 2006, 3:347-355.
    • (2006) Nat. Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrene, Y.F.2
  • 304
    • 0027263959 scopus 로고
    • Imaging viscoelasticity by force modulation with the atomic force microscope
    • Radmacher M., Tillmann R.W., Gaub H.E. Imaging viscoelasticity by force modulation with the atomic force microscope. Biophys. J. 1993, 64:735-742.
    • (1993) Biophys. J. , vol.64 , pp. 735-742
    • Radmacher, M.1    Tillmann, R.W.2    Gaub, H.E.3
  • 305
    • 70349885458 scopus 로고    scopus 로고
    • Force and function: probing proteins with AFM-based force spectroscopy
    • Puchner E.M., Gaub H.E. Force and function: probing proteins with AFM-based force spectroscopy. Curr. Opin. Struct. Biol. 2009, 19:605-614.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 605-614
    • Puchner, E.M.1    Gaub, H.E.2
  • 306
    • 34249889315 scopus 로고    scopus 로고
    • Nanoscale compositional mapping with gentle forces
    • Garcia R., Magerle R., Perez R. Nanoscale compositional mapping with gentle forces. Nat. Mater. 2007, 6:405-411.
    • (2007) Nat. Mater. , vol.6 , pp. 405-411
    • Garcia, R.1    Magerle, R.2    Perez, R.3
  • 307
    • 34547698856 scopus 로고    scopus 로고
    • An atomic force microscope tip designed to measure time-varying nanomechanical forces
    • Sahin O., Magonov S., Su C., Quate C.F., Solgaard O. An atomic force microscope tip designed to measure time-varying nanomechanical forces. Nat. Nanotechnol. 2007, 2:507-514.
    • (2007) Nat. Nanotechnol. , vol.2 , pp. 507-514
    • Sahin, O.1    Magonov, S.2    Su, C.3    Quate, C.F.4    Solgaard, O.5
  • 308
    • 79959964603 scopus 로고    scopus 로고
    • Probing osmolyte participation in the unfolding transition state of a protein
    • Dougan L., Genchev G.Z., Lu H., Fernandez J.M. Probing osmolyte participation in the unfolding transition state of a protein. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:9759-9764.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 9759-9764
    • Dougan, L.1    Genchev, G.Z.2    Lu, H.3    Fernandez, J.M.4
  • 309
    • 67649774601 scopus 로고    scopus 로고
    • Osmolyte-induced separation of the mechanical folding phases of ubiquitin
    • Garcia-Manyes S., Dougan L., Fernandez J.M. Osmolyte-induced separation of the mechanical folding phases of ubiquitin. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:10540-10545.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 10540-10545
    • Garcia-Manyes, S.1    Dougan, L.2    Fernandez, J.M.3
  • 310
    • 42149186359 scopus 로고    scopus 로고
    • Solvent molecules bridge the mechanical unfolding transition state of a protein
    • Dougan L., Feng G., Lu H., Fernandez J.M. Solvent molecules bridge the mechanical unfolding transition state of a protein. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:3185-3190.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 3185-3190
    • Dougan, L.1    Feng, G.2    Lu, H.3    Fernandez, J.M.4
  • 311
    • 56749155582 scopus 로고    scopus 로고
    • The effects of macromolecular crowding on the mechanical stability of protein molecules
    • Yuan J.M., Chyan C.L., Zhou H.X., Chung T.Y., Peng H., Ping G., Yang G. The effects of macromolecular crowding on the mechanical stability of protein molecules. Protein Sci. 2008, 17:2156-2166.
    • (2008) Protein Sci. , vol.17 , pp. 2156-2166
    • Yuan, J.M.1    Chyan, C.L.2    Zhou, H.X.3    Chung, T.Y.4    Peng, H.5    Ping, G.6    Yang, G.7
  • 312
    • 36348998132 scopus 로고    scopus 로고
    • How do chemical denaturants affect the mechanical folding and unfolding of proteins?
    • Cao Y., Li H. How do chemical denaturants affect the mechanical folding and unfolding of proteins?. J. Mol. Biol. 2008, 375:316-324.
    • (2008) J. Mol. Biol. , vol.375 , pp. 316-324
    • Cao, Y.1    Li, H.2
  • 313
    • 78649677842 scopus 로고    scopus 로고
    • Naturally occurring osmolytes modulate the nanomechanical properties of polycystic kidney disease domains
    • Ma L., Xu M., Oberhauser A.F. Naturally occurring osmolytes modulate the nanomechanical properties of polycystic kidney disease domains. J. Biol. Chem. 2010, 285:38438-38443.
    • (2010) J. Biol. Chem. , vol.285 , pp. 38438-38443
    • Ma, L.1    Xu, M.2    Oberhauser, A.F.3
  • 315
    • 0028816796 scopus 로고
    • Stability of protein formulations: investigation of surfactant effects by a novel EPR spectroscopic technique
    • Bam N.B., Randolph T.W., Cleland J.L. Stability of protein formulations: investigation of surfactant effects by a novel EPR spectroscopic technique. Pharm. Res. 1995, 12:2-11.
    • (1995) Pharm. Res. , vol.12 , pp. 2-11
    • Bam, N.B.1    Randolph, T.W.2    Cleland, J.L.3
  • 316
    • 0033047039 scopus 로고    scopus 로고
    • Investigation of protein-surfactant interactions by analytical ultracentrifugation and electron paramagnetic resonance: the use of recombinant human tissue factor as an example
    • Jones L.S., Cipolla D., Liu J., Shire S.J., Randolph T.W. Investigation of protein-surfactant interactions by analytical ultracentrifugation and electron paramagnetic resonance: the use of recombinant human tissue factor as an example. Pharm. Res. 1999, 16:808-812.
    • (1999) Pharm. Res. , vol.16 , pp. 808-812
    • Jones, L.S.1    Cipolla, D.2    Liu, J.3    Shire, S.J.4    Randolph, T.W.5
  • 317
    • 67650119674 scopus 로고    scopus 로고
    • The fate of free radicals in a cellulose based hydrogel: detection by electron paramagnetic resonance spectroscopy
    • Basumallick L., Ji J.A., Naber N., Wang Y.J. The fate of free radicals in a cellulose based hydrogel: detection by electron paramagnetic resonance spectroscopy. J. Pharm. Sci. 2009, 98:2464-2471.
    • (2009) J. Pharm. Sci. , vol.98 , pp. 2464-2471
    • Basumallick, L.1    Ji, J.A.2    Naber, N.3    Wang, Y.J.4
  • 318
    • 0034737261 scopus 로고    scopus 로고
    • Dynamic surface tension and adsorption mechanisms of surfactants at the air-water interface
    • Eastoe J., Dalton J.S. Dynamic surface tension and adsorption mechanisms of surfactants at the air-water interface. Adv. Colloid Interface Sci. 2000, 85:103-144.
    • (2000) Adv. Colloid Interface Sci. , vol.85 , pp. 103-144
    • Eastoe, J.1    Dalton, J.S.2
  • 319
    • 79952112477 scopus 로고    scopus 로고
    • Interfacial activity and interfacial shear rheology of native beta-lactoglobulin monomers and their heat-induced fibers
    • Jung J.M., Gunes D.Z., Mezzenga R. Interfacial activity and interfacial shear rheology of native beta-lactoglobulin monomers and their heat-induced fibers. Langmuir 2010, 26:15366-15375.
    • (2010) Langmuir , vol.26 , pp. 15366-15375
    • Jung, J.M.1    Gunes, D.Z.2    Mezzenga, R.3
  • 321
    • 0017858702 scopus 로고
    • Ellipsometry as a tool to study the adsorption behavior of synthetic and biopolymers at the air-water interface
    • De Feijter J., Benjamins J.A., Veer F. Ellipsometry as a tool to study the adsorption behavior of synthetic and biopolymers at the air-water interface. Biopolymers 1978, 17:1759-1772.
    • (1978) Biopolymers , vol.17 , pp. 1759-1772
    • De Feijter, J.1    Benjamins, J.A.2    Veer, F.3
  • 322
    • 14644442352 scopus 로고    scopus 로고
    • Interfacial dynamics and structure of surfactant layers
    • Zhmud B., Tiberg F. Interfacial dynamics and structure of surfactant layers. Adv. Colloid Interface Sci. 2005, 113:21-42.
    • (2005) Adv. Colloid Interface Sci. , vol.113 , pp. 21-42
    • Zhmud, B.1    Tiberg, F.2
  • 323
    • 57249093642 scopus 로고    scopus 로고
    • Neutron reflection studies of interactions between surfactants and proteins at interfaces
    • Lu J.R. Neutron reflection studies of interactions between surfactants and proteins at interfaces. Annu. Rep. Prog. Chem. C: Phys. Chem. 2002, 98:2-32.
    • (2002) Annu. Rep. Prog. Chem. C: Phys. Chem. , vol.98 , pp. 2-32
    • Lu, J.R.1
  • 324
    • 0033883969 scopus 로고    scopus 로고
    • Surfactant layers at the air/water interface: structure and composition
    • Lu J.R., Thomas R.K., Penfold J. Surfactant layers at the air/water interface: structure and composition. Adv. Colloid Interface Sci. 2000, 84:143-304.
    • (2000) Adv. Colloid Interface Sci. , vol.84 , pp. 143-304
    • Lu, J.R.1    Thomas, R.K.2    Penfold, J.3
  • 329
    • 0020794259 scopus 로고
    • Immunoglobulin surface-binding kinetics studied by total internal reflection with fluorescence correlation spectroscopy
    • Thompson N.L., Axelrod D. Immunoglobulin surface-binding kinetics studied by total internal reflection with fluorescence correlation spectroscopy. Biophys. J. 1983, 43:103-114.
    • (1983) Biophys. J. , vol.43 , pp. 103-114
    • Thompson, N.L.1    Axelrod, D.2
  • 330
    • 0019366933 scopus 로고
    • Measuring surface dynamics of biomolecules by total internal reflection fluorescence with photobleaching recovery or correlation spectroscopy
    • Thompson N.L., Burghardt T.P., Axelrod D. Measuring surface dynamics of biomolecules by total internal reflection fluorescence with photobleaching recovery or correlation spectroscopy. Biophys. J. 1981, 33:435-454.
    • (1981) Biophys. J. , vol.33 , pp. 435-454
    • Thompson, N.L.1    Burghardt, T.P.2    Axelrod, D.3
  • 331
    • 36148937163 scopus 로고    scopus 로고
    • Protein-surfactant interactions at hydrophobic interfaces studied with total internal reflection fluorescence correlation spectroscopy (TIR-FCS)
    • Sonesson A.W., Blom H., Hassler K., Elofsson U.M., Callisen T.H., Widengren J., Brismar H. Protein-surfactant interactions at hydrophobic interfaces studied with total internal reflection fluorescence correlation spectroscopy (TIR-FCS). J. Colloid Interface Sci. 2008, 317:449-457.
    • (2008) J. Colloid Interface Sci. , vol.317 , pp. 449-457
    • Sonesson, A.W.1    Blom, H.2    Hassler, K.3    Elofsson, U.M.4    Callisen, T.H.5    Widengren, J.6    Brismar, H.7
  • 332
    • 0037948870 scopus 로고    scopus 로고
    • Hessian eigenmaps: locally linear embedding techniques for high-dimensional data
    • Donoho D.L., Grimes C. Hessian eigenmaps: locally linear embedding techniques for high-dimensional data. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:5591-5596.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5591-5596
    • Donoho, D.L.1    Grimes, C.2
  • 333
    • 37349039375 scopus 로고    scopus 로고
    • Multidimensional scaling: a brief overview
    • Mugavin M.E. Multidimensional scaling: a brief overview. Nurs. Res. 2008, 57:64-68.
    • (2008) Nurs. Res. , vol.57 , pp. 64-68
    • Mugavin, M.E.1
  • 335
    • 0034704222 scopus 로고    scopus 로고
    • Nonlinear dimensionality reduction by locally linear embedding
    • Roweis S.T., Saul L.K. Nonlinear dimensionality reduction by locally linear embedding. Science 2000, 290:2323-2326.
    • (2000) Science , vol.290 , pp. 2323-2326
    • Roweis, S.T.1    Saul, L.K.2
  • 336
    • 0036790769 scopus 로고    scopus 로고
    • How to make large self-organizing maps for nonvectorial data
    • Kohonen T., Somervuo P. How to make large self-organizing maps for nonvectorial data. Neural Netw. 2002, 15:945-952.
    • (2002) Neural Netw. , vol.15 , pp. 945-952
    • Kohonen, T.1    Somervuo, P.2
  • 337
    • 0023646242 scopus 로고
    • Computing with neural networks
    • Kohonen T., Oja E. Computing with neural networks. Science 1987, 235:1227a.
    • (1987) Science , vol.235
    • Kohonen, T.1    Oja, E.2
  • 340
    • 0025434356 scopus 로고
    • Two-dimensional infrared (2D IR) spectroscopy: theory and applications
    • Noda I. Two-dimensional infrared (2D IR) spectroscopy: theory and applications. Appl. Spectrosc. 1990, 44:550-561.
    • (1990) Appl. Spectrosc. , vol.44 , pp. 550-561
    • Noda, I.1
  • 342
    • 79951939606 scopus 로고    scopus 로고
    • The relative rate of immunoglobulin gamma 1 fragmentation
    • Kamerzell T.J., Li M., Arora S., Ji J.A., Wang Y.J. The relative rate of immunoglobulin gamma 1 fragmentation. J. Pharm. Sci. 2011, 100:1341-1349.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 1341-1349
    • Kamerzell, T.J.1    Li, M.2    Arora, S.3    Ji, J.A.4    Wang, Y.J.5
  • 344
    • 0026317248 scopus 로고
    • Measuring electrostatic, van der Waals, and hydration forces in electrolyte solutions with an atomic force microscope
    • Butt H.J. Measuring electrostatic, van der Waals, and hydration forces in electrolyte solutions with an atomic force microscope. Biophys. J. 1991, 60:1438-1444.
    • (1991) Biophys. J. , vol.60 , pp. 1438-1444
    • Butt, H.J.1
  • 345
    • 0026038548 scopus 로고
    • Electrostatic interaction in atomic force microscopy
    • Butt H.J. Electrostatic interaction in atomic force microscopy. Biophys. J. 1991, 60:777-785.
    • (1991) Biophys. J. , vol.60 , pp. 777-785
    • Butt, H.J.1
  • 346
  • 347
    • 20544452788 scopus 로고    scopus 로고
    • Amide I vibrational dynamics of N-methylacetamide in polar solvents: the role of electrostatic interactions
    • DeCamp M.F., DeFlores L., McCracken J.M., Tokmakoff A., Kwac K., Cho M. Amide I vibrational dynamics of N-methylacetamide in polar solvents: the role of electrostatic interactions. J. Phys. Chem. B 2005, 109:11016-11026.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 11016-11026
    • DeCamp, M.F.1    DeFlores, L.2    McCracken, J.M.3    Tokmakoff, A.4    Kwac, K.5    Cho, M.6
  • 348
    • 34948833721 scopus 로고    scopus 로고
    • Label-free and high-resolution protein/DNA nanoarray analysis using Kelvin probe force microscopy
    • Sinensky A.K., Belcher A.M. Label-free and high-resolution protein/DNA nanoarray analysis using Kelvin probe force microscopy. Nat. Nanotechnol. 2007, 2:653-659.
    • (2007) Nat. Nanotechnol. , vol.2 , pp. 653-659
    • Sinensky, A.K.1    Belcher, A.M.2
  • 350
    • 0034598941 scopus 로고    scopus 로고
    • Thermodynamics of DNA binding and condensation: isothermal titration calorimetry and electrostatic mechanism
    • Matulis D., Rouzina I., Bloomfield V.A. Thermodynamics of DNA binding and condensation: isothermal titration calorimetry and electrostatic mechanism. J. Mol. Biol. 2000, 296:1053-1063.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1053-1063
    • Matulis, D.1    Rouzina, I.2    Bloomfield, V.A.3
  • 351
    • 4444270626 scopus 로고    scopus 로고
    • Influence of salts on rhodopsin photoproduct equilibria and protein stability
    • Vogel R. Influence of salts on rhodopsin photoproduct equilibria and protein stability. Curr. Opin. Colloid Interface Sci. 2004, 9:133-138.
    • (2004) Curr. Opin. Colloid Interface Sci. , vol.9 , pp. 133-138
    • Vogel, R.1
  • 352
  • 353
    • 34248222222 scopus 로고    scopus 로고
    • Ultrafast dynamics in complex fluids observed through the ultrafast optically-heterodyne-detected optical-Kerr-effect (OHD-OKE)
    • Hunt N.T., Jaye A.A., Meech S.R. Ultrafast dynamics in complex fluids observed through the ultrafast optically-heterodyne-detected optical-Kerr-effect (OHD-OKE). Phys. Chem. Chem. Phys. 2007, 9:2167-2180.
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 2167-2180
    • Hunt, N.T.1    Jaye, A.A.2    Meech, S.R.3
  • 354
    • 65249172623 scopus 로고    scopus 로고
    • Stark realities
    • Boxer S.G. Stark realities. J. Phys. Chem. B 2009, 113:2972-2983.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 2972-2983
    • Boxer, S.G.1
  • 355
    • 33746702555 scopus 로고
    • Electric-field level-crossing spectroscopy
    • Khadjavi A. Electric-field level-crossing spectroscopy. Phys. Rev. Lett. 1966, 17:463-465.
    • (1966) Phys. Rev. Lett. , vol.17 , pp. 463-465
    • Khadjavi, A.1
  • 356
    • 0001684206 scopus 로고
    • Molecular level-crossing spectroscopy
    • Zare R.N. Molecular level-crossing spectroscopy. J. Chem. Phys. 1966, 45:4510-4518.
    • (1966) J. Chem. Phys. , vol.45 , pp. 4510-4518
    • Zare, R.N.1
  • 357
    • 0036667303 scopus 로고    scopus 로고
    • Molecular bonding and interactions at aqueous surfaces as probed by vibrational sum frequency spectroscopy
    • Richmond G.L. Molecular bonding and interactions at aqueous surfaces as probed by vibrational sum frequency spectroscopy. Chem. Rev. 2002, 102:2693-2724.
    • (2002) Chem. Rev. , vol.102 , pp. 2693-2724
    • Richmond, G.L.1
  • 358
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin R.L. How Hofmeister ion interactions affect protein stability. Biophys. J. 1996, 71:2056-2063.
    • (1996) Biophys. J. , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 359
    • 67849115884 scopus 로고    scopus 로고
    • Water dynamics: ion-ing out the details
    • Bakker H.J. Water dynamics: ion-ing out the details. Nat. Chem. 2009, 1:24-25.
    • (2009) Nat. Chem. , vol.1 , pp. 24-25
    • Bakker, H.J.1
  • 360
    • 0038115064 scopus 로고    scopus 로고
    • Negligible effect of ions on the hydrogen-bond structure in liquid water
    • Omta A.W., Kropman M.F., Woutersen S., Bakker H.J. Negligible effect of ions on the hydrogen-bond structure in liquid water. Science 2003, 301:347-349.
    • (2003) Science , vol.301 , pp. 347-349
    • Omta, A.W.1    Kropman, M.F.2    Woutersen, S.3    Bakker, H.J.4
  • 364
    • 0027197880 scopus 로고
    • Effect of polyanions on the unfolding of acidic fibroblast growth factor
    • Burke C.J., Volkin D.B., Mach H., Middaugh C.R. Effect of polyanions on the unfolding of acidic fibroblast growth factor. Biochemistry 1993, 32:6419-6426.
    • (1993) Biochemistry , vol.32 , pp. 6419-6426
    • Burke, C.J.1    Volkin, D.B.2    Mach, H.3    Middaugh, C.R.4
  • 365
    • 79952753113 scopus 로고    scopus 로고
    • Preferential interaction coefficients of proteins in aqueous arginine solutions and their molecular origins
    • Shukla D., Trout B.L. Preferential interaction coefficients of proteins in aqueous arginine solutions and their molecular origins. J. Phys. Chem. B 2011, 115:1243-1253.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 1243-1253
    • Shukla, D.1    Trout, B.L.2
  • 366
    • 4243468938 scopus 로고    scopus 로고
    • The cation-pi interaction
    • Ma J.C., Dougherty D.A. The cation-pi interaction. Chem. Rev. 1997, 97:1303-1324.
    • (1997) Chem. Rev. , vol.97 , pp. 1303-1324
    • Ma, J.C.1    Dougherty, D.A.2
  • 367
    • 0030033588 scopus 로고    scopus 로고
    • Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp
    • Dougherty D.A. Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science 1996, 271:163-168.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 369
    • 13644272606 scopus 로고    scopus 로고
    • Structural and thermodynamic studies on cation-pi interactions in lectin-ligand complexes: high-affinity galectin-3 inhibitors through fine-tuning of an arginine-arene interaction
    • Sorme P., Arnoux P., Kahl-Knutsson B., Leffler H., Rini J.M., Nilsson U.J. Structural and thermodynamic studies on cation-pi interactions in lectin-ligand complexes: high-affinity galectin-3 inhibitors through fine-tuning of an arginine-arene interaction. J. Am. Chem. Soc. 2005, 127:1737-1743.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 1737-1743
    • Sorme, P.1    Arnoux, P.2    Kahl-Knutsson, B.3    Leffler, H.4    Rini, J.M.5    Nilsson, U.J.6
  • 371
    • 15444374846 scopus 로고    scopus 로고
    • Role of arginine in the stabilization of proteins against aggregation
    • Baynes B.M., Wang D.I., Trout B.L. Role of arginine in the stabilization of proteins against aggregation. Biochemistry 2005, 44:4919-4925.
    • (2005) Biochemistry , vol.44 , pp. 4919-4925
    • Baynes, B.M.1    Wang, D.I.2    Trout, B.L.3
  • 372
    • 16344389701 scopus 로고    scopus 로고
    • Cation-pi interactions in protein-protein interfaces
    • Crowley P.B., Golovin A. Cation-pi interactions in protein-protein interfaces. Proteins 2005, 59:231-239.
    • (2005) Proteins , vol.59 , pp. 231-239
    • Crowley, P.B.1    Golovin, A.2
  • 373
    • 0018400776 scopus 로고
    • Measurements of preferential solvent interactions by densimetric techniques
    • Lee J.C., Gekko K., Timasheff S.N. Measurements of preferential solvent interactions by densimetric techniques. Methods Enzymol. 1979, 61:26-49.
    • (1979) Methods Enzymol. , vol.61 , pp. 26-49
    • Lee, J.C.1    Gekko, K.2    Timasheff, S.N.3
  • 374
    • 0015950174 scopus 로고
    • Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride
    • Lee J.C., Timasheff S.N. Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride. Biochemistry 1974, 13:257-265.
    • (1974) Biochemistry , vol.13 , pp. 257-265
    • Lee, J.C.1    Timasheff, S.N.2
  • 375
    • 33746679254 scopus 로고    scopus 로고
    • Chemical potential derivatives and preferential interaction parameters in biological systems from Kirkwood-Buff theory
    • Smith P.E. Chemical potential derivatives and preferential interaction parameters in biological systems from Kirkwood-Buff theory. Biophys. J. 2006, 91:849-856.
    • (2006) Biophys. J. , vol.91 , pp. 849-856
    • Smith, P.E.1
  • 376
    • 0038311869 scopus 로고    scopus 로고
    • Protein stability in mixed solvents: a balance of contact interaction and excluded volume
    • Schellman J.A. Protein stability in mixed solvents: a balance of contact interaction and excluded volume. Biophys. J. 2003, 85:108-125.
    • (2003) Biophys. J. , vol.85 , pp. 108-125
    • Schellman, J.A.1
  • 377
    • 0037162456 scopus 로고    scopus 로고
    • Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components
    • Timasheff S.N. Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:9721-9726.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 9721-9726
    • Timasheff, S.N.1
  • 378
    • 0034635965 scopus 로고    scopus 로고
    • Osmotic stress, crowding, preferential hydration, and binding: a comparison of perspectives
    • Parsegian V.A., Rand R.P., Rau D.C. Osmotic stress, crowding, preferential hydration, and binding: a comparison of perspectives. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:3987-3992.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3987-3992
    • Parsegian, V.A.1    Rand, R.P.2    Rau, D.C.3
  • 379
    • 0014604482 scopus 로고
    • Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. II. Dependence on denaturant concentration at 25 degrees
    • Aune K.C., Tanford C. Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. II. Dependence on denaturant concentration at 25 degrees. Biochemistry 1969, 8:4586-4590.
    • (1969) Biochemistry , vol.8 , pp. 4586-4590
    • Aune, K.C.1    Tanford, C.2
  • 380
    • 79958243356 scopus 로고    scopus 로고
    • Arginine and the hofmeister series: the role of ion-ion interactions in protein aggregation suppression
    • Schneider C.P., Shukla D., Trout B.L. Arginine and the hofmeister series: the role of ion-ion interactions in protein aggregation suppression. J. Phys. Chem. B 2011, 115:7447-7458.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 7447-7458
    • Schneider, C.P.1    Shukla, D.2    Trout, B.L.3
  • 381
    • 65349138458 scopus 로고    scopus 로고
    • Investigation of cosolute-protein preferential interaction coefficients: new insight into the mechanism by which arginine inhibits aggregation
    • Schneider C.P., Trout B.L. Investigation of cosolute-protein preferential interaction coefficients: new insight into the mechanism by which arginine inhibits aggregation. J. Phys. Chem. B 2009, 113:2050-2058.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 2050-2058
    • Schneider, C.P.1    Trout, B.L.2
  • 382
    • 78751687015 scopus 로고    scopus 로고
    • An effective solvent theory connecting the underlying mechanisms of osmolytes and denaturants for protein stability
    • Linhananta A., Hadizadeh S., Plotkin S.S. An effective solvent theory connecting the underlying mechanisms of osmolytes and denaturants for protein stability. Biophys. J. 2011, 100:459-468.
    • (2011) Biophys. J. , vol.100 , pp. 459-468
    • Linhananta, A.1    Hadizadeh, S.2    Plotkin, S.S.3
  • 383
    • 33749365298 scopus 로고    scopus 로고
    • A molecular mechanism for osmolyte-induced protein stability
    • Street T.O., Bolen D.W., Rose G.D. A molecular mechanism for osmolyte-induced protein stability. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:13997-14002.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 13997-14002
    • Street, T.O.1    Bolen, D.W.2    Rose, G.D.3
  • 384
    • 0037138672 scopus 로고    scopus 로고
    • The molecular mechanism of stabilization of proteins by TMAO and its ability to counteract the effects of urea
    • Zou Q., Bennion B.J., Daggett V., Murphy K.P. The molecular mechanism of stabilization of proteins by TMAO and its ability to counteract the effects of urea. J. Am. Chem. Soc. 2002, 124:1192-1202.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1192-1202
    • Zou, Q.1    Bennion, B.J.2    Daggett, V.3    Murphy, K.P.4
  • 385
    • 65249176368 scopus 로고    scopus 로고
    • Destabilization of the hydrogen-bond structure of water by the osmolyte trimethylamine N-oxide
    • Rezus Y.L., Bakker H.J. Destabilization of the hydrogen-bond structure of water by the osmolyte trimethylamine N-oxide. J. Phys. Chem. B 2009, 113:4038-4044.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 4038-4044
    • Rezus, Y.L.1    Bakker, H.J.2
  • 386
    • 72449131449 scopus 로고    scopus 로고
    • Effects of urea and trimethylamine-N-oxide on the properties of water and the secondary structure of hen egg white lysozyme
    • Panuszko A., Bruzdziak P., Zielkiewicz J., Wyrzykowski D., Stangret J. Effects of urea and trimethylamine-N-oxide on the properties of water and the secondary structure of hen egg white lysozyme. J. Phys. Chem. B 2009, 113:14797-14809.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 14797-14809
    • Panuszko, A.1    Bruzdziak, P.2    Zielkiewicz, J.3    Wyrzykowski, D.4    Stangret, J.5
  • 387
    • 70349257327 scopus 로고    scopus 로고
    • Molecular anatomy of preferential interaction coefficients by elucidating protein solvation in mixed solvents: methodology and application for lysozyme in aqueous glycerol
    • Vagenende V., Yap M.G., Trout B.L. Molecular anatomy of preferential interaction coefficients by elucidating protein solvation in mixed solvents: methodology and application for lysozyme in aqueous glycerol. J. Phys. Chem. B 2009, 113:11743-11753.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 11743-11753
    • Vagenende, V.1    Yap, M.G.2    Trout, B.L.3
  • 388
    • 0042845844 scopus 로고    scopus 로고
    • Specific ion effects: why the properties of lysozyme in salt solutions follow a Hofmeister series
    • Bostrom M., Williams D.R., Ninham B.W. Specific ion effects: why the properties of lysozyme in salt solutions follow a Hofmeister series. Biophys. J. 2003, 85:686-694.
    • (2003) Biophys. J. , vol.85 , pp. 686-694
    • Bostrom, M.1    Williams, D.R.2    Ninham, B.W.3
  • 389
    • 55949131241 scopus 로고    scopus 로고
    • Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding
    • Hua L., Zhou R., Thirumalai D., Berne B.J. Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:16928-16933.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 16928-16933
    • Hua, L.1    Zhou, R.2    Thirumalai, D.3    Berne, B.J.4
  • 390
    • 19744371399 scopus 로고    scopus 로고
    • Molecular recognition of saccharides by proteins. Insights on the origin of the carbohydrate-aromatic interactions
    • del Carmen Fernandez-Alonso M., Canada F.J., Jimenez-Barbero J., Cuevas G. Molecular recognition of saccharides by proteins. Insights on the origin of the carbohydrate-aromatic interactions. J. Am. Chem. Soc. 2005, 127:7379-7386.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 7379-7386
    • del Carmen Fernandez-Alonso, M.1    Canada, F.J.2    Jimenez-Barbero, J.3    Cuevas, G.4
  • 391
    • 0030031382 scopus 로고    scopus 로고
    • Van der Waals interactions involving proteins
    • Roth C.M., Neal B.L., Lenhoff A.M. Van der Waals interactions involving proteins. Biophys. J. 1996, 70:977-987.
    • (1996) Biophys. J. , vol.70 , pp. 977-987
    • Roth, C.M.1    Neal, B.L.2    Lenhoff, A.M.3
  • 392
    • 0000355678 scopus 로고
    • Additivity of intermolecular forces at interfaces. I. Determination of the contribution to surface and interfacial tensions of dispersion forces in various liquids
    • Fowkes F.M. Additivity of intermolecular forces at interfaces. I. Determination of the contribution to surface and interfacial tensions of dispersion forces in various liquids. J. Phys. Chem. 1963, 67:2538-2541.
    • (1963) J. Phys. Chem. , vol.67 , pp. 2538-2541
    • Fowkes, F.M.1
  • 393
    • 0034274898 scopus 로고    scopus 로고
    • Origins and applications of London dispersion forces and hamaker constants in ceramics
    • French R.H. Origins and applications of London dispersion forces and hamaker constants in ceramics. J. Am. Ceram. Soc. 2000, 83:2117-2146.
    • (2000) J. Am. Ceram. Soc. , vol.83 , pp. 2117-2146
    • French, R.H.1
  • 394
    • 0000250129 scopus 로고
    • Electrostatic and van der Waals contributions to protein adsorption: comparison of theory and experiment
    • Roth C.M., Lenhoff A.M. Electrostatic and van der Waals contributions to protein adsorption: comparison of theory and experiment. Langmuir 1995, 11:3500-3509.
    • (1995) Langmuir , vol.11 , pp. 3500-3509
    • Roth, C.M.1    Lenhoff, A.M.2
  • 395
    • 0012115003 scopus 로고
    • Structure and properties of van der Waals molecules
    • Ewing G.E. Structure and properties of van der Waals molecules. Acc. Chem. Res. 1975, 8:185-192.
    • (1975) Acc. Chem. Res. , vol.8 , pp. 185-192
    • Ewing, G.E.1
  • 397
    • 75649108542 scopus 로고    scopus 로고
    • Effects of urea, tetramethyl urea, and trimethylamine N-oxide on aqueous solution structure and solvation of protein backbones: a molecular dynamics simulation study
    • Wei H., Fan Y., Gao Y.Q. Effects of urea, tetramethyl urea, and trimethylamine N-oxide on aqueous solution structure and solvation of protein backbones: a molecular dynamics simulation study. J. Phys. Chem. B 2010, 114:557-568.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 557-568
    • Wei, H.1    Fan, Y.2    Gao, Y.Q.3
  • 398
    • 63149153986 scopus 로고    scopus 로고
    • Urea's action on hydrophobic interactions
    • Zangi R., Zhou R., Berne B.J. Urea's action on hydrophobic interactions. J. Am. Chem. Soc. 2009, 131:1535-1541.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1535-1541
    • Zangi, R.1    Zhou, R.2    Berne, B.J.3
  • 399
    • 77749255800 scopus 로고    scopus 로고
    • Why direct or reversed Hofmeister series? Interplay of hydration, non-electrostatic potentials, and ion size
    • Parsons D.F., Bostrom M., Maceina T.J., Salis A., Ninham B.W. Why direct or reversed Hofmeister series? Interplay of hydration, non-electrostatic potentials, and ion size. Langmuir 2010, 26:3323-3328.
    • (2010) Langmuir , vol.26 , pp. 3323-3328
    • Parsons, D.F.1    Bostrom, M.2    Maceina, T.J.3    Salis, A.4    Ninham, B.W.5
  • 401
    • 30344438534 scopus 로고    scopus 로고
    • Specific ion effects in solutions of globular proteins: comparison between analytical models and simulation
    • Bostrom M., Tavares F.W., Bratko D., Ninham B.W. Specific ion effects in solutions of globular proteins: comparison between analytical models and simulation. J. Phys. Chem. B 2005, 109:24489-24494.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 24489-24494
    • Bostrom, M.1    Tavares, F.W.2    Bratko, D.3    Ninham, B.W.4
  • 402
    • 15844387737 scopus 로고    scopus 로고
    • Hofmeister effects in surface tension of aqueous electrolyte solution
    • Bostrom M., Kunz W., Ninham B.W. Hofmeister effects in surface tension of aqueous electrolyte solution. Langmuir 2005, 21:2619-2623.
    • (2005) Langmuir , vol.21 , pp. 2619-2623
    • Bostrom, M.1    Kunz, W.2    Ninham, B.W.3
  • 403
    • 4344662387 scopus 로고    scopus 로고
    • Energetics of galactose- and glucose-aromatic amino acid interactions: implications for binding in galactose-specific proteins
    • Sujatha M.S., Sasidhar Y.U., Balaji P.V. Energetics of galactose- and glucose-aromatic amino acid interactions: implications for binding in galactose-specific proteins. Protein Sci. 2004, 13:2502-2514.
    • (2004) Protein Sci. , vol.13 , pp. 2502-2514
    • Sujatha, M.S.1    Sasidhar, Y.U.2    Balaji, P.V.3
  • 404
    • 20444429796 scopus 로고    scopus 로고
    • Insights into the role of the aromatic residue in galactose-binding sites: MP2/6-311G++** study on galactose- and glucose-aromatic residue analogue complexes
    • Sujatha M.S., Sasidhar Y.U., Balaji P.V. Insights into the role of the aromatic residue in galactose-binding sites: MP2/6-311G++** study on galactose- and glucose-aromatic residue analogue complexes. Biochemistry 2005, 44:8554-8562.
    • (2005) Biochemistry , vol.44 , pp. 8554-8562
    • Sujatha, M.S.1    Sasidhar, Y.U.2    Balaji, P.V.3
  • 407
    • 0027996135 scopus 로고
    • Structure and energetics of protein-carbohydrate complexes
    • Toone E.J. Structure and energetics of protein-carbohydrate complexes. Curr. Opin. Struct. Biol. 1994, 4:719-728.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 719-728
    • Toone, E.J.1
  • 408
    • 0030666313 scopus 로고    scopus 로고
    • Lectin-carbohydrate interactions: different folds, common recognition principles
    • Elgavish S., Shaanan B. Lectin-carbohydrate interactions: different folds, common recognition principles. Trends Biochem. Sci. 1997, 22:462-467.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 462-467
    • Elgavish, S.1    Shaanan, B.2
  • 410
    • 33750999581 scopus 로고    scopus 로고
    • The nature of the hydrogen bond: a synthesis from the interacting quantum atoms picture
    • Martin Pendas A., Blanco M.A., Francisco E. The nature of the hydrogen bond: a synthesis from the interacting quantum atoms picture. J. Chem. Phys. 2006, 125:184112.
    • (2006) J. Chem. Phys. , vol.125 , pp. 184112
    • Martin Pendas, A.1    Blanco, M.A.2    Francisco, E.3
  • 411
    • 33744811377 scopus 로고
    • The theory of the hydrogen bond
    • Kollman P.A., Allen L.C. The theory of the hydrogen bond. Chem. Rev. 1972, 72:283-303.
    • (1972) Chem. Rev. , vol.72 , pp. 283-303
    • Kollman, P.A.1    Allen, L.C.2
  • 412
    • 0002351307 scopus 로고
    • Low frequency Raman scattering from water and aqueous solution: a direct measure of hydrogen bonding
    • Walrafen G.E., Fisher M. Low frequency Raman scattering from water and aqueous solution: a direct measure of hydrogen bonding. Methods Enzymol. 1986, 127:91-105.
    • (1986) Methods Enzymol. , vol.127 , pp. 91-105
    • Walrafen, G.E.1    Fisher, M.2
  • 413
    • 0022485951 scopus 로고
    • Determination of water structure around biomolecules using X-ray and neutron diffraction methods
    • Savage H., Wlodawer A. Determination of water structure around biomolecules using X-ray and neutron diffraction methods. Methods Enzymol. 1986, 127:162-183.
    • (1986) Methods Enzymol. , vol.127 , pp. 162-183
    • Savage, H.1    Wlodawer, A.2
  • 416
    • 0024549238 scopus 로고
    • An infrared spectroscopic study of the interactions of carbohydrates with dried proteins
    • Carpenter J.F., Crowe J.H. An infrared spectroscopic study of the interactions of carbohydrates with dried proteins. Biochemistry 1989, 28:3916-3922.
    • (1989) Biochemistry , vol.28 , pp. 3916-3922
    • Carpenter, J.F.1    Crowe, J.H.2
  • 417
    • 0023905575 scopus 로고
    • The mechanism of cryoprotection of proteins by solutes
    • Carpenter J.F., Crowe J.H. The mechanism of cryoprotection of proteins by solutes. Cryobiology 1988, 25:244-255.
    • (1988) Cryobiology , vol.25 , pp. 244-255
    • Carpenter, J.F.1    Crowe, J.H.2
  • 418
    • 0023659990 scopus 로고
    • Stabilization of phosphofructokinase with sugars during freeze-drying: characterization of enhanced protection in the presence of divalent cations
    • Carpenter J.F., Crowe L.M., Crowe J.H. Stabilization of phosphofructokinase with sugars during freeze-drying: characterization of enhanced protection in the presence of divalent cations. Biochim. Biophys. Acta 1987, 923:109-115.
    • (1987) Biochim. Biophys. Acta , vol.923 , pp. 109-115
    • Carpenter, J.F.1    Crowe, L.M.2    Crowe, J.H.3
  • 419
    • 0023428513 scopus 로고
    • Stabilization of phosphofructokinase during air-drying with sugars and sugar/transition metal mixtures
    • Carpenter J.F., Martin B., Crowe L.M., Crowe J.H. Stabilization of phosphofructokinase during air-drying with sugars and sugar/transition metal mixtures. Cryobiology 1987, 24:455-464.
    • (1987) Cryobiology , vol.24 , pp. 455-464
    • Carpenter, J.F.1    Martin, B.2    Crowe, L.M.3    Crowe, J.H.4
  • 420
    • 0023696310 scopus 로고
    • Long-term preservation of dried phosphofructokinase by sugars and sugar/zinc mixtures
    • Carpenter J.F., Martin B., Loomis S.H., Crowe J.H. Long-term preservation of dried phosphofructokinase by sugars and sugar/zinc mixtures. Cryobiology 1988, 25:372-376.
    • (1988) Cryobiology , vol.25 , pp. 372-376
    • Carpenter, J.F.1    Martin, B.2    Loomis, S.H.3    Crowe, J.H.4
  • 421
    • 0027163348 scopus 로고
    • Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers
    • Prestrelski S.J., Tedeschi N., Arakawa T., Carpenter J.F. Dehydration-induced conformational transitions in proteins and their inhibition by stabilizers. Biophys. J. 1993, 65:661-671.
    • (1993) Biophys. J. , vol.65 , pp. 661-671
    • Prestrelski, S.J.1    Tedeschi, N.2    Arakawa, T.3    Carpenter, J.F.4
  • 422
    • 0033562141 scopus 로고    scopus 로고
    • Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding
    • Allison S.D., Chang B., Randolph T.W., Carpenter J.F. Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding. Arch. Biochem. Biophys. 1999, 365:289-298.
    • (1999) Arch. Biochem. Biophys. , vol.365 , pp. 289-298
    • Allison, S.D.1    Chang, B.2    Randolph, T.W.3    Carpenter, J.F.4
  • 423
    • 0034001717 scopus 로고    scopus 로고
    • Optimization of storage stability of lyophilized actin using combinations of disaccharides and dextran
    • Allison S.D., Manning M.C., Randolph T.W., Middleton K., Davis A., Carpenter J.F. Optimization of storage stability of lyophilized actin using combinations of disaccharides and dextran. J. Pharm. Sci. 2000, 89:199-214.
    • (2000) J. Pharm. Sci. , vol.89 , pp. 199-214
    • Allison, S.D.1    Manning, M.C.2    Randolph, T.W.3    Middleton, K.4    Davis, A.5    Carpenter, J.F.6
  • 424
    • 0037308304 scopus 로고    scopus 로고
    • Effects of types of sugar on the stabilization of protein in the dried state
    • Imamura K., Ogawa T., Sakiyama T., Nakanishi K. Effects of types of sugar on the stabilization of protein in the dried state. J. Pharm. Sci. 2003, 92:266-274.
    • (2003) J. Pharm. Sci. , vol.92 , pp. 266-274
    • Imamura, K.1    Ogawa, T.2    Sakiyama, T.3    Nakanishi, K.4
  • 425
    • 0028673438 scopus 로고
    • Mapping of hydrogen bonding between saccharides and proteins in solution
    • Glaudemans C.P., Kovac P., Nashed E.M. Mapping of hydrogen bonding between saccharides and proteins in solution. Methods Enzymol. 1994, 247:305-322.
    • (1994) Methods Enzymol. , vol.247 , pp. 305-322
    • Glaudemans, C.P.1    Kovac, P.2    Nashed, E.M.3
  • 426
    • 48749129145 scopus 로고    scopus 로고
    • Thermal signature of hydrophobic hydration dynamics
    • Qvist J., Halle B. Thermal signature of hydrophobic hydration dynamics. J. Am. Chem. Soc. 2008, 130:10345-10353.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 10345-10353
    • Qvist, J.1    Halle, B.2
  • 427
    • 1242319518 scopus 로고    scopus 로고
    • Impact of protein denaturants and stabilizers on water structure
    • Batchelor J.D., Olteanu A., Tripathy A., Pielak G.J. Impact of protein denaturants and stabilizers on water structure. J. Am. Chem. Soc. 2004, 126:1958-1961.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1958-1961
    • Batchelor, J.D.1    Olteanu, A.2    Tripathy, A.3    Pielak, G.J.4
  • 428
    • 35448999589 scopus 로고    scopus 로고
    • A practical guide on how osmolytes modulate macromolecular properties
    • Harries D., Rosgen J. A practical guide on how osmolytes modulate macromolecular properties. Methods Cell Biol. 2008, 84:679-735.
    • (2008) Methods Cell Biol. , vol.84 , pp. 679-735
    • Harries, D.1    Rosgen, J.2
  • 429
    • 58049184362 scopus 로고    scopus 로고
    • Effect of osmolytes on pressure-induced unfolding of proteins: a high-pressure SAXS study
    • Krywka C., Sternemann C., Paulus M., Tolan M., Royer C., Winter R. Effect of osmolytes on pressure-induced unfolding of proteins: a high-pressure SAXS study. Chemphyschem 2008, 9:2809-2815.
    • (2008) Chemphyschem , vol.9 , pp. 2809-2815
    • Krywka, C.1    Sternemann, C.2    Paulus, M.3    Tolan, M.4    Royer, C.5    Winter, R.6
  • 430
    • 27244462333 scopus 로고    scopus 로고
    • Maintenance of quaternary structure in the frozen state stabilizes lactate dehydrogenase during freeze-drying
    • Anchordoquy T.J., Izutsu K.I., Randolph T.W., Carpenter J.F. Maintenance of quaternary structure in the frozen state stabilizes lactate dehydrogenase during freeze-drying. Arch. Biochem. Biophys. 2001, 390:35-41.
    • (2001) Arch. Biochem. Biophys. , vol.390 , pp. 35-41
    • Anchordoquy, T.J.1    Izutsu, K.I.2    Randolph, T.W.3    Carpenter, J.F.4
  • 431
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • Shire S.J., Shahrokh Z., Liu J. Challenges in the development of high protein concentration formulations. J. Pharm. Sci. 2004, 93:1390-1402.
    • (2004) J. Pharm. Sci. , vol.93 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 433
    • 38349042010 scopus 로고    scopus 로고
    • Protein phase behavior in aqueous solutions: crystallization, liquid-liquid phase separation, gels, and aggregates
    • Dumetz A.C., Chockla A.M., Kaler E.W., Lenhoff A.M. Protein phase behavior in aqueous solutions: crystallization, liquid-liquid phase separation, gels, and aggregates. Biophys. J. 2008, 94:570-583.
    • (2008) Biophys. J. , vol.94 , pp. 570-583
    • Dumetz, A.C.1    Chockla, A.M.2    Kaler, E.W.3    Lenhoff, A.M.4
  • 437
    • 67651202371 scopus 로고    scopus 로고
    • Freezing-induced phase separation and spatial microheterogeneity in protein solutions
    • Dong J., Hubel A., Bischof J.C., Aksan A. Freezing-induced phase separation and spatial microheterogeneity in protein solutions. J. Phys. Chem. B 2009, 113:10081-10087.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 10081-10087
    • Dong, J.1    Hubel, A.2    Bischof, J.C.3    Aksan, A.4
  • 439
    • 0021452281 scopus 로고
    • Intrinsic phosphorescence from proteins in the solid state
    • Strambini G.B., Gabellieri E. Intrinsic phosphorescence from proteins in the solid state. Photochem. Photobiol. 1984, 39:725-729.
    • (1984) Photochem. Photobiol. , vol.39 , pp. 725-729
    • Strambini, G.B.1    Gabellieri, E.2
  • 440
    • 0023646714 scopus 로고
    • Phosphorescence anisotropy of liver alcohol dehydrogenase in the crystalline state. Apparent glasslike rigidity of the coenzyme-binding domain
    • Strambini G.B., Gabellieri E. Phosphorescence anisotropy of liver alcohol dehydrogenase in the crystalline state. Apparent glasslike rigidity of the coenzyme-binding domain. Biochemistry 1987, 26:6527-6530.
    • (1987) Biochemistry , vol.26 , pp. 6527-6530
    • Strambini, G.B.1    Gabellieri, E.2
  • 441
    • 33751283870 scopus 로고    scopus 로고
    • A small-angle scattering study on equilibrium clusters in lysozyme solutions
    • Stradner A., Cardinaux F., Schurtenberger P. A small-angle scattering study on equilibrium clusters in lysozyme solutions. J. Phys. Chem. B 2006, 110:21222-21231.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 21222-21231
    • Stradner, A.1    Cardinaux, F.2    Schurtenberger, P.3
  • 443
    • 77649185058 scopus 로고    scopus 로고
    • Vibrational spectroscopy and chemometrics to characterize and quantitate trehalose crystallization
    • Connolly B., Patapoff T.W., Wang Y.J., Moore J.M., Kamerzell T.J. Vibrational spectroscopy and chemometrics to characterize and quantitate trehalose crystallization. Anal. Biochem. 2010, 399:48-57.
    • (2010) Anal. Biochem. , vol.399 , pp. 48-57
    • Connolly, B.1    Patapoff, T.W.2    Wang, Y.J.3    Moore, J.M.4    Kamerzell, T.J.5
  • 448
    • 0032962882 scopus 로고    scopus 로고
    • The effect of formulation excipients on protein stability and aerosol performance of spray-dried powders of a recombinant humanized anti-IgE monoclonal antibody
    • Andya J.D., Maa Y.F., Costantino H.R., Nguyen P.A., Dasovich N., Sweeney T.D., Hsu C.C., Shire S.J. The effect of formulation excipients on protein stability and aerosol performance of spray-dried powders of a recombinant humanized anti-IgE monoclonal antibody. Pharm. Res. 1999, 16:350-358.
    • (1999) Pharm. Res. , vol.16 , pp. 350-358
    • Andya, J.D.1    Maa, Y.F.2    Costantino, H.R.3    Nguyen, P.A.4    Dasovich, N.5    Sweeney, T.D.6    Hsu, C.C.7    Shire, S.J.8
  • 450
    • 23744490027 scopus 로고    scopus 로고
    • The effect of stabilizers and denaturants on the cold denaturation temperatures of proteins and implications for freeze-drying
    • Tang X.C., Pikal M.J. The effect of stabilizers and denaturants on the cold denaturation temperatures of proteins and implications for freeze-drying. Pharm. Res. 2005, 22:1167-1175.
    • (2005) Pharm. Res. , vol.22 , pp. 1167-1175
    • Tang, X.C.1    Pikal, M.J.2
  • 451
    • 0001644688 scopus 로고
    • Comparison of solute-induced protein stabilization in aqueous solution and in the frozen and dried states
    • Carpenter J.F., Crowe J.H., Arakawa T. Comparison of solute-induced protein stabilization in aqueous solution and in the frozen and dried states. J. Dairy Sci. 1990, 73:3627-3636.
    • (1990) J. Dairy Sci. , vol.73 , pp. 3627-3636
    • Carpenter, J.F.1    Crowe, J.H.2    Arakawa, T.3
  • 452
    • 0030443488 scopus 로고    scopus 로고
    • Effects of phase separating systems on lyophilized hemoglobin
    • Heller M.C., Carpenter J.F., Randolph T.W. Effects of phase separating systems on lyophilized hemoglobin. J. Pharm. Sci. 1996, 85:1358-1362.
    • (1996) J. Pharm. Sci. , vol.85 , pp. 1358-1362
    • Heller, M.C.1    Carpenter, J.F.2    Randolph, T.W.3
  • 453
    • 0030712895 scopus 로고    scopus 로고
    • Phase separation of excipients during lyophilization: effects on protein stability
    • Randolph T.W. Phase separation of excipients during lyophilization: effects on protein stability. J. Pharm. Sci. 1997, 86:1198-1203.
    • (1997) J. Pharm. Sci. , vol.86 , pp. 1198-1203
    • Randolph, T.W.1
  • 454
    • 0000740448 scopus 로고
    • 2O on pH and composition during freezing
    • 2O on pH and composition during freezing. Arch. Biochem. Biophys. 1959, 84:305-315.
    • (1959) Arch. Biochem. Biophys. , vol.84 , pp. 305-315
    • Van Den Berg, L.1
  • 456
    • 0027337054 scopus 로고
    • Decreased protein-stabilizing effects of cryoprotectants due to crystallization
    • Izutsu K., Yoshioka S., Terao T. Decreased protein-stabilizing effects of cryoprotectants due to crystallization. Pharm. Res. 1993, 10:1232-1237.
    • (1993) Pharm. Res. , vol.10 , pp. 1232-1237
    • Izutsu, K.1    Yoshioka, S.2    Terao, T.3
  • 458
    • 0030043206 scopus 로고    scopus 로고
    • Proteins in frozen solutions: evidence of ice-induced partial unfolding
    • Strambini G.B., Gabellieri E. Proteins in frozen solutions: evidence of ice-induced partial unfolding. Biophys. J. 1996, 70:971-976.
    • (1996) Biophys. J. , vol.70 , pp. 971-976
    • Strambini, G.B.1    Gabellieri, E.2
  • 459
    • 33947627702 scopus 로고    scopus 로고
    • Protein stability in ice
    • Strambini G.B., Gonnelli M. Protein stability in ice. Biophys. J. 2007, 92:2131-2138.
    • (2007) Biophys. J. , vol.92 , pp. 2131-2138
    • Strambini, G.B.1    Gonnelli, M.2
  • 460
    • 0029820371 scopus 로고    scopus 로고
    • Is trehalose special for preserving dry biomaterials?
    • Crowe L.M., Reid D.S., Crowe J.H. Is trehalose special for preserving dry biomaterials?. Biophys. J. 1996, 71:2087-2093.
    • (1996) Biophys. J. , vol.71 , pp. 2087-2093
    • Crowe, L.M.1    Reid, D.S.2    Crowe, J.H.3
  • 461
    • 85010251846 scopus 로고
    • The effect of lactose crystallization on protein stability in frozen concentrated milk
    • Tumerman L., Fram H., Cornely K.W. The effect of lactose crystallization on protein stability in frozen concentrated milk. J. Dairy Sci. 1954, 37:830-839.
    • (1954) J. Dairy Sci. , vol.37 , pp. 830-839
    • Tumerman, L.1    Fram, H.2    Cornely, K.W.3
  • 462
    • 51049097028 scopus 로고    scopus 로고
    • Specific anions effects of on the stability of azurin in ice
    • Strambini G.B., Gonnelli M. Specific anions effects of on the stability of azurin in ice. J. Phys. Chem. B 2008, 112:10255-10263.
    • (2008) J. Phys. Chem. B , vol.112 , pp. 10255-10263
    • Strambini, G.B.1    Gonnelli, M.2
  • 464
    • 3242670796 scopus 로고    scopus 로고
    • Opalescent appearance of an IgG1 antibody at high concentrations and its relationship to noncovalent association
    • Sukumar M., Doyle B.L., Combs J.L., Pekar A.H. Opalescent appearance of an IgG1 antibody at high concentrations and its relationship to noncovalent association. Pharm. Res. 2004, 21:1087-1093.
    • (2004) Pharm. Res. , vol.21 , pp. 1087-1093
    • Sukumar, M.1    Doyle, B.L.2    Combs, J.L.3    Pekar, A.H.4
  • 465
    • 78649649134 scopus 로고    scopus 로고
    • Formulation effects on opalescence of a high-concentration MAb
    • Woods J., Nesta D. Formulation effects on opalescence of a high-concentration MAb. BioProcess Int. 2010, 8:48-59.
    • (2010) BioProcess Int. , vol.8 , pp. 48-59
    • Woods, J.1    Nesta, D.2
  • 466
    • 80053232304 scopus 로고    scopus 로고
    • Opalescence of an IgG2 monoclonal antibody solution as it relates to liquid-liquid phase separation
    • Mason B.D., Zhang L., Remmele R.L., Zhang J. Opalescence of an IgG2 monoclonal antibody solution as it relates to liquid-liquid phase separation. J. Pharm. Sci. 2011, 100:4587-4596.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 4587-4596
    • Mason, B.D.1    Zhang, L.2    Remmele, R.L.3    Zhang, J.4
  • 467
    • 77951552352 scopus 로고    scopus 로고
    • Quantification and characterization of subvisible proteinaceous particles in opalescent mAb formulations using micro-flow imaging
    • Sharma D.K., Oma P., Pollo M.J., Sukumar M. Quantification and characterization of subvisible proteinaceous particles in opalescent mAb formulations using micro-flow imaging. J. Pharm. Sci. 2010, 99:2628-2642.
    • (2010) J. Pharm. Sci. , vol.99 , pp. 2628-2642
    • Sharma, D.K.1    Oma, P.2    Pollo, M.J.3    Sukumar, M.4
  • 468
    • 0025952279 scopus 로고
    • Effect of freezing on aggregation of human growth hormone
    • Eckhardt B.M., Oeswein J.Q., Bewley T.A. Effect of freezing on aggregation of human growth hormone. Pharm. Res. 1991, 8:1360-1364.
    • (1991) Pharm. Res. , vol.8 , pp. 1360-1364
    • Eckhardt, B.M.1    Oeswein, J.Q.2    Bewley, T.A.3
  • 470
    • 0027828184 scopus 로고
    • Stability and characterization of human growth hormone
    • Pearlman R., Bewley T.A. Stability and characterization of human growth hormone. Pharm. Biotechnol. 1993, 5:1-58.
    • (1993) Pharm. Biotechnol. , vol.5 , pp. 1-58
    • Pearlman, R.1    Bewley, T.A.2
  • 471
    • 0028816797 scopus 로고
    • Surface denaturation at solid-void interface-a possible pathway by which opalescent particulates form during the storage of lyophilized tissue-type plasminogen activator at high temperatures
    • Hsu C.C., Nguyen H.M., Yeung D.A., Brooks D.A., Koe G.S., Bewley T.A., Pearlman R. Surface denaturation at solid-void interface-a possible pathway by which opalescent particulates form during the storage of lyophilized tissue-type plasminogen activator at high temperatures. Pharm. Res. 1995, 12:69-77.
    • (1995) Pharm. Res. , vol.12 , pp. 69-77
    • Hsu, C.C.1    Nguyen, H.M.2    Yeung, D.A.3    Brooks, D.A.4    Koe, G.S.5    Bewley, T.A.6    Pearlman, R.7
  • 472
    • 73949150096 scopus 로고    scopus 로고
    • Opalescence in antibody formulations is a solution critical phenomenon
    • Philadelphia, PA
    • Cromwell M. Opalescence in antibody formulations is a solution critical phenomenon. The 236th ACS National Meeting 2008, Philadelphia, PA.
    • (2008) The 236th ACS National Meeting
    • Cromwell, M.1
  • 474
    • 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. Phase separation of an IgG1 antibody solution under a low ionic strength condition. Pharm. Res. 2010, 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
  • 475
    • 78649892101 scopus 로고    scopus 로고
    • Liquid-liquid phase separation of a monoclonal antibody and nonmonotonic influence of Hofmeister anions
    • Mason B.D., Zhang-van Enk J., Zhang L., Remmele R.L., Zhang J. Liquid-liquid phase separation of a monoclonal antibody and nonmonotonic influence of Hofmeister anions. Biophys. J. 2010, 99:3792-3800.
    • (2010) Biophys. J. , vol.99 , pp. 3792-3800
    • Mason, B.D.1    Zhang-van Enk, J.2    Zhang, L.3    Remmele, R.L.4    Zhang, J.5
  • 479
    • 0034612274 scopus 로고    scopus 로고
    • Control of protein crystal nucleation around the metastable liquid-liquid phase boundary
    • Galkin O., Vekilov P.G. Control of protein crystal nucleation around the metastable liquid-liquid phase boundary. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:6277-6281.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6277-6281
    • Galkin, O.1    Vekilov, P.G.2
  • 480
    • 0019284656 scopus 로고
    • The effects of glycols, aldehydes, and acrylamide on phase separation and opacification in the calf lens
    • Clark J.I., Benedek G.B. The effects of glycols, aldehydes, and acrylamide on phase separation and opacification in the calf lens. Invest. Ophthalmol. Vis. Sci. 1980, 19:771-776.
    • (1980) Invest. Ophthalmol. Vis. Sci. , vol.19 , pp. 771-776
    • Clark, J.I.1    Benedek, G.B.2
  • 481
  • 482
    • 33748752323 scopus 로고    scopus 로고
    • Influence of cosolvent systems on the gelation mechanism of globular protein: thermodynamic, kinetic, and structural aspects of globular protein gelation
    • Baier S., McClements D.J. Influence of cosolvent systems on the gelation mechanism of globular protein: thermodynamic, kinetic, and structural aspects of globular protein gelation. Compr. Rev. Food Sci. Food Saf. 2005, 4:43-54.
    • (2005) Compr. Rev. Food Sci. Food Saf. , vol.4 , pp. 43-54
    • Baier, S.1    McClements, D.J.2
  • 483
    • 0033789735 scopus 로고    scopus 로고
    • Effects of sugars on whey protein isolate gelation
    • Rich L.M., Foegeding E.A. Effects of sugars on whey protein isolate gelation. J. Agric. Food Chem. 2000, 48:5046-5052.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 5046-5052
    • Rich, L.M.1    Foegeding, E.A.2
  • 487
    • 0000027238 scopus 로고    scopus 로고
    • Interactions involved in the gelation of bovine serum albumin
    • Boye J.I., Alli I., Ismail A.A. Interactions involved in the gelation of bovine serum albumin. J. Agric. Food Chem. 1996, 44:996-1004.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 996-1004
    • Boye, J.I.1    Alli, I.2    Ismail, A.A.3
  • 488
    • 0019536747 scopus 로고
    • Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels
    • Clark A.H., Saunderson D.H., Suggett A. Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels. Int. J. Pept. Protein Res. 1981, 17:353-364.
    • (1981) Int. J. Pept. Protein Res. , vol.17 , pp. 353-364
    • Clark, A.H.1    Saunderson, D.H.2    Suggett, A.3
  • 489
    • 0000583890 scopus 로고
    • Effects of various anions on the rheological and gelling behavior of soy proteins: thermodynamic observations
    • Babajimopoulos M., Damodaran S., Rizvi S., Kinsella J.E. Effects of various anions on the rheological and gelling behavior of soy proteins: thermodynamic observations. J. Agric. Food Chem. 1983, 31:1270-1275.
    • (1983) J. Agric. Food Chem. , vol.31 , pp. 1270-1275
    • Babajimopoulos, M.1    Damodaran, S.2    Rizvi, S.3    Kinsella, J.E.4
  • 490
    • 85013793081 scopus 로고
    • Effects of anions on thermally induced whey protein isolate gels
    • Bowland E.L., Foegeding E.A. Effects of anions on thermally induced whey protein isolate gels. Food Hydrocolloids 1995, 9:47-56.
    • (1995) Food Hydrocolloids , vol.9 , pp. 47-56
    • Bowland, E.L.1    Foegeding, E.A.2
  • 491
    • 33645234553 scopus 로고    scopus 로고
    • Effects of sugars on the cross-linking formation and phase separation of high-pressure induced gel of whey protein from bovine milk
    • He J.S., Azuma N., Hagiwara T., Kanno C. Effects of sugars on the cross-linking formation and phase separation of high-pressure induced gel of whey protein from bovine milk. Biosci. Biotechnol. Biochem. 2006, 70:615-625.
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 615-625
    • He, J.S.1    Azuma, N.2    Hagiwara, T.3    Kanno, C.4
  • 492
  • 494
    • 0022781496 scopus 로고
    • Adsorption of proteins from solution at the solid-liquid interface
    • Norde W. Adsorption of proteins from solution at the solid-liquid interface. Adv. Colloid Interface Sci. 1986, 25:267-340.
    • (1986) Adv. Colloid Interface Sci. , vol.25 , pp. 267-340
    • Norde, W.1
  • 496
    • 0342762048 scopus 로고    scopus 로고
    • Protein denaturation by combined effect of shear and air-liquid interface
    • Maa Y.F., Hsu C.C. Protein denaturation by combined effect of shear and air-liquid interface. Biotechnol. Bioeng. 1997, 54:503-512.
    • (1997) Biotechnol. Bioeng. , vol.54 , pp. 503-512
    • Maa, Y.F.1    Hsu, C.C.2
  • 497
    • 21244462685 scopus 로고    scopus 로고
    • Protein structural perturbation and aggregation on homogeneous surfaces
    • Sethuraman A., Belfort G. Protein structural perturbation and aggregation on homogeneous surfaces. Biophys. J. 2005, 88:1322-1333.
    • (2005) Biophys. J. , vol.88 , pp. 1322-1333
    • Sethuraman, A.1    Belfort, G.2
  • 498
    • 45149128290 scopus 로고    scopus 로고
    • Current perspectives on stability of protein drug products during formulation, fill and finish operations
    • Rathore N., Rajan R.S. Current perspectives on stability of protein drug products during formulation, fill and finish operations. Biotechnol. Prog. 2008, 24:504-514.
    • (2008) Biotechnol. Prog. , vol.24 , pp. 504-514
    • Rathore, N.1    Rajan, R.S.2
  • 499
    • 33947661498 scopus 로고    scopus 로고
    • Immunogenicity of therapeutic proteins. Part 2: impact of container closures
    • Sharma B. Immunogenicity of therapeutic proteins. Part 2: impact of container closures. Biotechnol. Adv. 2007, 25:318-324.
    • (2007) Biotechnol. Adv. , vol.25 , pp. 318-324
    • Sharma, B.1
  • 500
    • 0026434962 scopus 로고
    • Interfacial protein adsorption and inactivation
    • Sadana A. Interfacial protein adsorption and inactivation. Bioseparation 1992, 3:297-320.
    • (1992) Bioseparation , vol.3 , pp. 297-320
    • Sadana, A.1
  • 501
    • 0035822024 scopus 로고    scopus 로고
    • Lysozyme inactivation under mechanical stirring: effect of physical and molecular interfaces
    • Colombie S., Gaunand A., Lindet B. Lysozyme inactivation under mechanical stirring: effect of physical and molecular interfaces. Enzyme Microb. Technol. 2001, 28:820-826.
    • (2001) Enzyme Microb. Technol. , vol.28 , pp. 820-826
    • Colombie, S.1    Gaunand, A.2    Lindet, B.3
  • 502
    • 0035060814 scopus 로고    scopus 로고
    • On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon
    • Nakanishi K., Sakiyama T., Imamura K. On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon. J. Biosci. Bioeng. 2001, 91:233-244.
    • (2001) J. Biosci. Bioeng. , vol.91 , pp. 233-244
    • Nakanishi, K.1    Sakiyama, T.2    Imamura, K.3
  • 506
    • 0029094884 scopus 로고
    • Adsorption of protein onto stainless-steel surfaces
    • Fukuzaki S., Urano H., Nagata K. Adsorption of protein onto stainless-steel surfaces. J. Ferment. Bioeng. 1995, 80:6-11.
    • (1995) J. Ferment. Bioeng. , vol.80 , pp. 6-11
    • Fukuzaki, S.1    Urano, H.2    Nagata, K.3
  • 507
    • 0026154124 scopus 로고
    • The effect of pH and sodium chloride concentration on adsorption of B-lactoglobulin at hydrophilic and hydrophobic silicon surfaces
    • Luey J., McGuire J., Sproull R. The effect of pH and sodium chloride concentration on adsorption of B-lactoglobulin at hydrophilic and hydrophobic silicon surfaces. J. Colloid Interface Sci. 1991, 143:489-500.
    • (1991) J. Colloid Interface Sci. , vol.143 , pp. 489-500
    • Luey, J.1    McGuire, J.2    Sproull, R.3
  • 509
    • 0026883585 scopus 로고
    • On the adsorption of IgG onto polystyrene particles: electrophoretic mobility and critical coagulation concentration
    • Serra J., Puig J., Martin A., Galisteo F., Galvez M., Hidalgo-Alvarez R. On the adsorption of IgG onto polystyrene particles: electrophoretic mobility and critical coagulation concentration. Colloid Polym. Sci. 1992, 270:574-583.
    • (1992) Colloid Polym. Sci. , vol.270 , pp. 574-583
    • Serra, J.1    Puig, J.2    Martin, A.3    Galisteo, F.4    Galvez, M.5    Hidalgo-Alvarez, R.6
  • 510
    • 0003025269 scopus 로고
    • The adsorption from solutions of beta-lactoblobulin mixed with lactoferrin or lysozyme onto silica and methylated silica surfaces
    • Wahlgren M.C., Arnebrant T., Paulsson M.A. The adsorption from solutions of beta-lactoblobulin mixed with lactoferrin or lysozyme onto silica and methylated silica surfaces. J. Colloid Interface Sci. 1993, 158:46-53.
    • (1993) J. Colloid Interface Sci. , vol.158 , pp. 46-53
    • Wahlgren, M.C.1    Arnebrant, T.2    Paulsson, M.A.3
  • 511
    • 4243766747 scopus 로고    scopus 로고
    • Changes in the secondary structure of adsorbed IgG and F(ab')2 studied by FTIR spectroscopy
    • Buijs J., Norde W., Lichtenbelt J. Changes in the secondary structure of adsorbed IgG and F(ab')2 studied by FTIR spectroscopy. Langmuir 1996, 12:1605-1613.
    • (1996) Langmuir , vol.12 , pp. 1605-1613
    • Buijs, J.1    Norde, W.2    Lichtenbelt, J.3
  • 512
    • 0001289369 scopus 로고
    • Adsorption competition between albumin and monoclonal immunogammaglobulins on polystyrene latexes
    • Elgersma A., Zsom R., Lyklema J., Norde W. Adsorption competition between albumin and monoclonal immunogammaglobulins on polystyrene latexes. J. Colloid Interface Sci. 1992, 152:410-428.
    • (1992) J. Colloid Interface Sci. , vol.152 , pp. 410-428
    • Elgersma, A.1    Zsom, R.2    Lyklema, J.3    Norde, W.4
  • 513
    • 13244284133 scopus 로고
    • Interfacial free energies in protein solution droplets on FEP-teflon by axisymmetric drop shape analysis by profile-IgG versus BSA
    • Van der Vegt W., Van der Mei H.C., Busscher H.J. Interfacial free energies in protein solution droplets on FEP-teflon by axisymmetric drop shape analysis by profile-IgG versus BSA. J. Colloid Interface Sci. 1993, 156:129-136.
    • (1993) J. Colloid Interface Sci. , vol.156 , pp. 129-136
    • Van der Vegt, W.1    Van der Mei, H.C.2    Busscher, H.J.3
  • 514
    • 70449637481 scopus 로고    scopus 로고
    • The role of electrolytes on protein adsorption at a hydrophilic solid-water interface
    • Wendorf J.R., Radke C.J., Blanch H.W. The role of electrolytes on protein adsorption at a hydrophilic solid-water interface. Colloids Surf. B Biointerfaces 2010, 75:100-106.
    • (2010) Colloids Surf. B Biointerfaces , vol.75 , pp. 100-106
    • Wendorf, J.R.1    Radke, C.J.2    Blanch, H.W.3
  • 515
    • 65249164173 scopus 로고    scopus 로고
    • Buffer effect on protein adsorption at liquid/solid interface
    • Wei T., Kaewtathip S., Shing K. Buffer effect on protein adsorption at liquid/solid interface. J. Phys. Chem. C 2009, 113:2053-2062.
    • (2009) J. Phys. Chem. C , vol.113 , pp. 2053-2062
    • Wei, T.1    Kaewtathip, S.2    Shing, K.3
  • 517
    • 0001797840 scopus 로고    scopus 로고
    • Surfactant stabilized protein formulations: a review of protein-surfactant interactions and novel analytical methodologies
    • American Chemical Society
    • Jones L., Bam N.B., Randolph T.W. Surfactant stabilized protein formulations: a review of protein-surfactant interactions and novel analytical methodologies. Therapeutic Protein and Peptide Formulation and Delivery 1997, American Chemical Society.
    • (1997) Therapeutic Protein and Peptide Formulation and Delivery
    • Jones, L.1    Bam, N.B.2    Randolph, T.W.3
  • 520
    • 14344262955 scopus 로고    scopus 로고
    • Heterogeneous nucleation-controlled particulate formation of recombinant human platelet-activating factor acetylhydrolase in pharmaceutical formulation
    • Chi E.Y., Weickmann J., Carpenter J.F., Manning M.C., Randolph T.W. Heterogeneous nucleation-controlled particulate formation of recombinant human platelet-activating factor acetylhydrolase in pharmaceutical formulation. J. Pharm. Sci. 2005, 94:256-274.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 256-274
    • Chi, E.Y.1    Weickmann, J.2    Carpenter, J.F.3    Manning, M.C.4    Randolph, T.W.5
  • 522
    • 0029078173 scopus 로고
    • Influence of surfactants upon protein/peptide adsorption to glass and polypropylene
    • Duncan M.R., Lee J.M., Warchol M.P. Influence of surfactants upon protein/peptide adsorption to glass and polypropylene. Int. J. Pharm. 1995, 120:179-188.
    • (1995) Int. J. Pharm. , vol.120 , pp. 179-188
    • Duncan, M.R.1    Lee, J.M.2    Warchol, M.P.3
  • 523
    • 55749109195 scopus 로고    scopus 로고
    • Shaken, not stirred: mechanical stress testing of an IgG1 antibody
    • Kiese S., Papppenberger A., Friess W., Mahler H.C. Shaken, not stirred: mechanical stress testing of an IgG1 antibody. J. Pharm. Sci. 2008, 97:4347-4366.
    • (2008) J. Pharm. Sci. , vol.97 , pp. 4347-4366
    • Kiese, S.1    Papppenberger, A.2    Friess, W.3    Mahler, H.C.4
  • 525
    • 70449436442 scopus 로고    scopus 로고
    • Polysorbate 20 prevents the precipitation of a monoclonal antibody during shear
    • Patapoff T.W., Esue O. Polysorbate 20 prevents the precipitation of a monoclonal antibody during shear. Pharm. Dev. Technol. 2009, 14:659-664.
    • (2009) Pharm. Dev. Technol. , vol.14 , pp. 659-664
    • Patapoff, T.W.1    Esue, O.2
  • 526
    • 67349139279 scopus 로고    scopus 로고
    • Insights into protein-polysorbate interactions analysed by means of isothermal titration and differential scanning calorimetry
    • Hoffmann C., Blume A., Miller I., Garidel P. Insights into protein-polysorbate interactions analysed by means of isothermal titration and differential scanning calorimetry. Eur. Biophys. J. 2009, 38:557-568.
    • (2009) Eur. Biophys. J. , vol.38 , pp. 557-568
    • Hoffmann, C.1    Blume, A.2    Miller, I.3    Garidel, P.4
  • 527
    • 25144460975 scopus 로고    scopus 로고
    • Analysis of protein-surfactant interactions-a titration calorimetric and fluorescence spectroscopic investigation of interactions between Humicola insolens cutinase and an anionic surfactant
    • Nielsen A.D., Arleth L., Westh P. Analysis of protein-surfactant interactions-a titration calorimetric and fluorescence spectroscopic investigation of interactions between Humicola insolens cutinase and an anionic surfactant. Biochim. Biophys. Acta 2005, 1752:124-132.
    • (2005) Biochim. Biophys. Acta , vol.1752 , pp. 124-132
    • Nielsen, A.D.1    Arleth, L.2    Westh, P.3
  • 528
    • 65949093954 scopus 로고    scopus 로고
    • A thermodynamic analysis of the binding interaction between polysorbate 20 and 80 with human serum albumins and immunoglobulins: a contribution to understand colloidal protein stabilisation
    • Garidel P., Hoffmann C., Blume A. A thermodynamic analysis of the binding interaction between polysorbate 20 and 80 with human serum albumins and immunoglobulins: a contribution to understand colloidal protein stabilisation. Biophys. Chem. 2009, 143:70-78.
    • (2009) Biophys. Chem. , vol.143 , pp. 70-78
    • Garidel, P.1    Hoffmann, C.2    Blume, A.3
  • 529
    • 0033080411 scopus 로고    scopus 로고
    • Orogenic displacement of protein from the air/water interface by competitive adsorption
    • Mackie A., Gunning A.P., Wilde P., Morris V.J. Orogenic displacement of protein from the air/water interface by competitive adsorption. J. Colloid Interface Sci. 1999, 210:157-166.
    • (1999) J. Colloid Interface Sci. , vol.210 , pp. 157-166
    • Mackie, A.1    Gunning, A.P.2    Wilde, P.3    Morris, V.J.4
  • 531
    • 4644335636 scopus 로고    scopus 로고
    • Reduced protein adsorption at solid interfaces by sugar excipients
    • Wendorf J.R., Radke C.J., Blanch H.W. Reduced protein adsorption at solid interfaces by sugar excipients. Biotechnol. Bioeng. 2004, 87:565-573.
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 565-573
    • Wendorf, J.R.1    Radke, C.J.2    Blanch, H.W.3
  • 532
    • 58149216346 scopus 로고    scopus 로고
    • IgG particle formation during filling pump operation: a case study of heterogeneous nucleation on stainless steel nanoparticles
    • Tyagi A.K., Randolph T.W., Dong A., Maloney K.M., Hitscherich C., Carpenter J.F. IgG particle formation during filling pump operation: a case study of heterogeneous nucleation on stainless steel nanoparticles. J. Pharm. Sci. 2009, 98:94-104.
    • (2009) J. Pharm. Sci. , vol.98 , pp. 94-104
    • Tyagi, A.K.1    Randolph, T.W.2    Dong, A.3    Maloney, K.M.4    Hitscherich, C.5    Carpenter, J.F.6
  • 536
    • 17744363305 scopus 로고    scopus 로고
    • Silicone oil induced aggregation of proteins
    • Jones L.S., Kaufmann A., Middaugh C.R. Silicone oil induced aggregation of proteins. J. Pharm. Sci. 2005, 94:918-927.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 918-927
    • Jones, L.S.1    Kaufmann, A.2    Middaugh, C.R.3
  • 537
    • 34250331531 scopus 로고    scopus 로고
    • The perfect mix: recent progress in adjuvant research
    • Guy B. The perfect mix: recent progress in adjuvant research. Nat. Rev. Microbiol. 2007, 5:505-517.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 505-517
    • Guy, B.1
  • 539
    • 0029200884 scopus 로고
    • Structure and properties of aluminum-containing adjuvants
    • Hem S.L., White J.L. Structure and properties of aluminum-containing adjuvants. Pharm. Biotechnol. 1995, 6:249-276.
    • (1995) Pharm. Biotechnol. , vol.6 , pp. 249-276
    • Hem, S.L.1    White, J.L.2
  • 540
    • 0032490610 scopus 로고    scopus 로고
    • Aluminum compounds as vaccine adjuvants
    • Gupta R.K. Aluminum compounds as vaccine adjuvants. Adv. Drug Deliv. Rev. 1998, 32:155-172.
    • (1998) Adv. Drug Deliv. Rev. , vol.32 , pp. 155-172
    • Gupta, R.K.1
  • 541
    • 0037205174 scopus 로고    scopus 로고
    • Mechanisms of stimulation of the immune response by aluminum adjuvants
    • Hogenesch H. Mechanisms of stimulation of the immune response by aluminum adjuvants. Vaccine 2002, 20(Suppl. 3):S34-S39.
    • (2002) Vaccine , vol.20 , Issue.SUPPL. 3
    • Hogenesch, H.1
  • 542
    • 0029200883 scopus 로고
    • A compendium of vaccine adjuvants and excipients
    • Vogel F.R., Powell M.F. A compendium of vaccine adjuvants and excipients. Pharm. Biotechnol. 1995, 6:141-228.
    • (1995) Pharm. Biotechnol. , vol.6 , pp. 141-228
    • Vogel, F.R.1    Powell, M.F.2
  • 543
    • 14244259422 scopus 로고    scopus 로고
    • Immunogenicity in mice of anthrax recombinant protective antigen in the presence of aluminum adjuvants
    • Berthold I., Pombo M.L., Wagner L., Arciniega J.L. Immunogenicity in mice of anthrax recombinant protective antigen in the presence of aluminum adjuvants. Vaccine 2005, 23:1993-1999.
    • (2005) Vaccine , vol.23 , pp. 1993-1999
    • Berthold, I.1    Pombo, M.L.2    Wagner, L.3    Arciniega, J.L.4
  • 544
    • 33845187202 scopus 로고    scopus 로고
    • Potentiation of the immune response to non-adsorbed antigens by aluminum-containing adjuvants
    • Romero Mendez I.Z., Shi Y., HogenEsch H., Hem S.L. Potentiation of the immune response to non-adsorbed antigens by aluminum-containing adjuvants. Vaccine 2007, 25:825-833.
    • (2007) Vaccine , vol.25 , pp. 825-833
    • Romero Mendez, I.Z.1    Shi, Y.2    HogenEsch, H.3    Hem, S.L.4
  • 545
    • 0028836690 scopus 로고
    • Contribution of electrostatic and hydrophobic interactions to the adsorption of proteins by aluminium-containing adjuvants
    • al-Shakhshir R.H., Regnier F.E., White J.L., Hem S.L. Contribution of electrostatic and hydrophobic interactions to the adsorption of proteins by aluminium-containing adjuvants. Vaccine 1995, 13:41-44.
    • (1995) Vaccine , vol.13 , pp. 41-44
    • al-Shakhshir, R.H.1    Regnier, F.E.2    White, J.L.3    Hem, S.L.4
  • 546
    • 35348968868 scopus 로고    scopus 로고
    • Relationship between physical and chemical properties of aluminum-containing adjuvants and immunopotentiation
    • Hem S.L., Hogenesch H. Relationship between physical and chemical properties of aluminum-containing adjuvants and immunopotentiation. Expert Rev. Vaccines 2007, 6:685-698.
    • (2007) Expert Rev. Vaccines , vol.6 , pp. 685-698
    • Hem, S.L.1    Hogenesch, H.2
  • 547
    • 1842561485 scopus 로고    scopus 로고
    • Mechanism of adsorption of hepatitis B surface antigen by aluminum hydroxide adjuvant
    • Iyer S., Robinett R.S., HogenEsch H., Hem S.L. Mechanism of adsorption of hepatitis B surface antigen by aluminum hydroxide adjuvant. Vaccine 2004, 22:1475-1479.
    • (2004) Vaccine , vol.22 , pp. 1475-1479
    • Iyer, S.1    Robinett, R.S.2    HogenEsch, H.3    Hem, S.L.4
  • 548
    • 12844265403 scopus 로고    scopus 로고
    • Effect of phosphorylation of ovalbumin on adsorption by aluminum-containing adjuvants and elution upon exposure to interstitial fluid
    • Morefield G.L., Jiang D., Romero-Mendez I.Z., Geahlen R.L., Hogenesch H., Hem S.L. Effect of phosphorylation of ovalbumin on adsorption by aluminum-containing adjuvants and elution upon exposure to interstitial fluid. Vaccine 2005, 23:1502-1506.
    • (2005) Vaccine , vol.23 , pp. 1502-1506
    • Morefield, G.L.1    Jiang, D.2    Romero-Mendez, I.Z.3    Geahlen, R.L.4    Hogenesch, H.5    Hem, S.L.6
  • 549
    • 0025959504 scopus 로고
    • Predicting the adsorption of proteins by aluminium-containing adjuvants
    • Seeber S.J., White J.L., Hem S.L. Predicting the adsorption of proteins by aluminium-containing adjuvants. Vaccine 1991, 9:201-203.
    • (1991) Vaccine , vol.9 , pp. 201-203
    • Seeber, S.J.1    White, J.L.2    Hem, S.L.3
  • 550
    • 17144427675 scopus 로고    scopus 로고
    • Effects of adsorption to aluminum salt adjuvants on the structure and stability of model protein antigens
    • Jones L.S., Peek L.J., Power J., Markham A., Yazzie B., Middaugh C.R. Effects of adsorption to aluminum salt adjuvants on the structure and stability of model protein antigens. J. Biol. Chem. 2005, 280:13406-13414.
    • (2005) J. Biol. Chem. , vol.280 , pp. 13406-13414
    • Jones, L.S.1    Peek, L.J.2    Power, J.3    Markham, A.4    Yazzie, B.5    Middaugh, C.R.6
  • 551
    • 0032509289 scopus 로고    scopus 로고
    • Evidence for the denaturation of recombinant hepatitis B surface antigen on aluminium hydroxide gel
    • Tleugabulova D., Falcon V., Penton E. Evidence for the denaturation of recombinant hepatitis B surface antigen on aluminium hydroxide gel. J. Chromatogr. B Biomed. Sci. Appl. 1998, 720:153-163.
    • (1998) J. Chromatogr. B Biomed. Sci. Appl. , vol.720 , pp. 153-163
    • Tleugabulova, D.1    Falcon, V.2    Penton, E.3
  • 552
    • 68949113643 scopus 로고    scopus 로고
    • Stability of a trivalent recombinant protein vaccine formulation against botulinum neurotoxin during storage in aqueous solution
    • Vessely C., Estey T., Randolph T.W., Henderson I., Cooper J., Nayar R., Braun L.J., Carpenter J.F. Stability of a trivalent recombinant protein vaccine formulation against botulinum neurotoxin during storage in aqueous solution. J. Pharm. Sci. 2009, 98:2970-2993.
    • (2009) J. Pharm. Sci. , vol.98 , pp. 2970-2993
    • Vessely, C.1    Estey, T.2    Randolph, T.W.3    Henderson, I.4    Cooper, J.5    Nayar, R.6    Braun, L.J.7    Carpenter, J.F.8
  • 553
    • 78650570898 scopus 로고    scopus 로고
    • Application of extrinsic fluorescence spectroscopy for the high throughput formulation screening of aluminum-adjuvanted vaccines
    • Ausar S.F., Chan J., Hoque W., James O., Jayasundara K., Harper K. Application of extrinsic fluorescence spectroscopy for the high throughput formulation screening of aluminum-adjuvanted vaccines. J. Pharm. Sci. 2011, 100:431-440.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 431-440
    • Ausar, S.F.1    Chan, J.2    Hoque, W.3    James, O.4    Jayasundara, K.5    Harper, K.6
  • 554
    • 33846131223 scopus 로고    scopus 로고
    • A rapid, three-step process for the preformulation of a recombinant ricin toxin A-chain vaccine
    • Peek L.J., Brey R.N., Middaugh C.R. A rapid, three-step process for the preformulation of a recombinant ricin toxin A-chain vaccine. J. Pharm. Sci. 2007, 96:44-60.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 44-60
    • Peek, L.J.1    Brey, R.N.2    Middaugh, C.R.3
  • 556
    • 65549121292 scopus 로고    scopus 로고
    • Effects of immobilization onto aluminum hydroxide particles on the thermally induced conformational behavior of three model proteins
    • Bai S., Dong A. Effects of immobilization onto aluminum hydroxide particles on the thermally induced conformational behavior of three model proteins. Int. J. Biol. Macromol. 2009, 45:80-85.
    • (2009) Int. J. Biol. Macromol. , vol.45 , pp. 80-85
    • Bai, S.1    Dong, A.2
  • 557
    • 33645294911 scopus 로고    scopus 로고
    • Secondary structures of proteins adsorbed onto aluminum hydroxide: infrared spectroscopic analysis of proteins from low solution concentrations
    • Dong A., Jones L.S., Kerwin B.A., Krishnan S., Carpenter J.F. Secondary structures of proteins adsorbed onto aluminum hydroxide: infrared spectroscopic analysis of proteins from low solution concentrations. Anal. Biochem. 2006, 351:282-289.
    • (2006) Anal. Biochem. , vol.351 , pp. 282-289
    • Dong, A.1    Jones, L.S.2    Kerwin, B.A.3    Krishnan, S.4    Carpenter, J.F.5
  • 558
    • 1542270987 scopus 로고    scopus 로고
    • Effect of microenvironment pH of aluminum hydroxide adjuvant on the chemical stability of adsorbed antigen
    • Wittayanukulluk A., Jiang D., Regnier F.E., Hem S.L. Effect of microenvironment pH of aluminum hydroxide adjuvant on the chemical stability of adsorbed antigen. Vaccine 2004, 22:1172-1176.
    • (2004) Vaccine , vol.22 , pp. 1172-1176
    • Wittayanukulluk, A.1    Jiang, D.2    Regnier, F.E.3    Hem, S.L.4
  • 559
    • 78650555727 scopus 로고    scopus 로고
    • Vaccines with aluminum-containing adjuvants: optimizing vaccine efficacy and thermal stability
    • Clapp T., Siebert P., Chen D., Jones Braun L. Vaccines with aluminum-containing adjuvants: optimizing vaccine efficacy and thermal stability. J. Pharm. Sci. 2011, 100:388-401.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 388-401
    • Clapp, T.1    Siebert, P.2    Chen, D.3    Jones Braun, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.