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Volumn 100, Issue 5, 2011, Pages 1679-1689

Mechanisms of m-cresol-induced protein aggregation studied using a model protein cytochrome c

Author keywords

Antimicrobial preservative; Cresol; Cytochrome c; Formulation; Physical stability; Protein aggregation; Protein structure; Protein unfolding; Proteins; Spectroscopy

Indexed keywords

CYTOCHROME C; META CRESOL; METHIONINE;

EID: 79952239062     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.22426     Document Type: Article
Times cited : (34)

References (59)
  • 1
    • 38149120374 scopus 로고    scopus 로고
    • Antimicrobial preservative use in parenteral products: Past and present
    • Meyer BK, Ni A, Hu B, Shi L. 2007. Antimicrobial preservative use in parenteral products: Past and present. J Pharm Sci 96:3155-3167.
    • (2007) J Pharm Sci , vol.96 , pp. 3155-3167
    • Meyer, B.1    Ni, A.2    Hu, B.3    Shi, L.4
  • 2
    • 0027729733 scopus 로고
    • The development of stable protein formulations-A close look at protein aggregation, deamidation and oxidation
    • Cleland JL, Powell MF, Shire SJ. 1993. The development of stable protein formulations-A close look at protein aggregation, deamidation and oxidation. Crit Rev Ther Drug Carrier Syst 10:307-377
    • (1993) Crit Rev Ther Drug Carrier Syst , vol.10 , pp. 307-377
    • Cleland, J.1    Powell, M.2    Shire, S.3
  • 3
    • 0021630221 scopus 로고
    • Considerations in selecting antimicrobial agents for parental product development
    • Akers MJ. 1984. Considerations in selecting antimicrobial agents for parental product development. Pharm Technol 8:36-46.
    • (1984) Pharm Technol , vol.8 , pp. 36-46
    • Akers, M.1
  • 4
    • 0036828056 scopus 로고    scopus 로고
    • Excipient-drug interactions in parental formulations
    • Akers MJ. 2002. Excipient-drug interactions in parental formulations. J Pharm Sci 91:2283-2300.
    • (2002) J Pharm Sci , vol.91 , pp. 2283-2300
    • Akers, M.1
  • 5
    • 0025870619 scopus 로고
    • Patient acceptance of Nordiject: A new drug delivery system for growth hormone
    • Jorgensen JT, Mortensen HB, Jorgensen JO. 1991. Patient acceptance of Nordiject: A new drug delivery system for growth hormone. DICP: Annals Pharmacother 25:585-588.
    • (1991) DICP: Annals Pharmacother , vol.25 , pp. 585-588
    • Jorgensen, J.1    Mortensen, H.2    Jorgensen, J.3
  • 6
    • 0036588780 scopus 로고    scopus 로고
    • Continuous infusion of coagulation factors
    • Batorova A, Martinowitz U. 2002. Continuous infusion of coagulation factors. Haemophilia 8:170-177.
    • (2002) Haemophilia , vol.8 , pp. 170-177
    • Batorova, A.1    Martinowitz, U.2
  • 7
    • 0027181266 scopus 로고
    • Transforming growth factor-alpha (TGF-alpha) in a semisolid dosage form: Preservative and vehicle selection
    • Tan EL, Shah HS, Leister KJ, Kozick LM, Pasciak P, Vanderlaan RK, Yu CD, Patel B. 1993. Transforming growth factor-alpha (TGF-alpha) in a semisolid dosage form: Preservative and vehicle selection. Pharm Res 10:1238-1242.
    • (1993) Pharm Res , vol.10 , pp. 1238-1242
    • Tan, E.1    Shah, H.2    Leister, K.3    Kozick, L.4    Pasciak, P.5    Vanderlaan, R.6    Yu, C.7    Patel, B.8
  • 8
    • 2342627492 scopus 로고    scopus 로고
    • Development and manufacture of protein pharmaceuticals
    • In; Nail SL, Akers MJ, Eds. New York: Kluwer Academic/ Plenum Publishers.
    • Akers MJ, Vasudevan V, Stickelmeyer M. 2002. Formulation development of protein dosage forms. In Development and manufacture of protein pharmaceuticals; Nail SL, Akers MJ, Eds. New York: Kluwer Academic/ Plenum Publishers, pp 47-127.
    • (2002) Formulation development of protein dosage forms , pp. 47-127
    • Akers, M.1    Vasudevan, V.2    Stickelmeyer, M.3
  • 9
    • 0030606850 scopus 로고    scopus 로고
    • Aggregation of recombinant human growth hormone induced by phenolic compounds
    • Maa YF, Hsu CC. 1996. Aggregation of recombinant human growth hormone induced by phenolic compounds. Int J Pharm 140:155-168.
    • (1996) Int J Pharm , vol.140 , pp. 155-168
    • Maa, Y.1    Hsu, C.2
  • 10
    • 0031391073 scopus 로고    scopus 로고
    • Use of poloxamer polymers to stabilize recombinant human growth hormone against various processing stresses
    • Katakam M, Banga AK. 1997. Use of poloxamer polymers to stabilize recombinant human growth hormone against various processing stresses. Pharm Dev Technol 2:143-149.
    • (1997) Pharm Dev Technol , vol.2 , pp. 143-149
    • Katakam, M.1    Banga, A.2
  • 11
    • 14444277713 scopus 로고    scopus 로고
    • Interleukin-1 receptor (IL-1RA) liquid formulation development using differential scanning calorimetry
    • Remmele Jr. RL, Nightlinger NS, Srinivasan S, Gombotz WR. 1998. Interleukin-1 receptor (IL-1RA) liquid formulation development using differential scanning calorimetry. Pharm Res 15:200-208.
    • (1998) Pharm Res , vol.15 , pp. 200-208
    • Remmele Jr, R.1    Nightlinger, N.2    Srinivasan, S.3    Gombotz, W.4
  • 12
    • 0347300798 scopus 로고    scopus 로고
    • Development of a multidose formulation for a humanized monoclonal antibody using experimental design techniques
    • Gupta S, Kaisheva E. 2003. Development of a multidose formulation for a humanized monoclonal antibody using experimental design techniques. AAPS Pharm Sci 5:1-9.
    • (2003) AAPS Pharm Sci , vol.5 , pp. 1-9
    • Gupta, S.1    Kaisheva, E.2
  • 13
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
    • Chi EY, Krishnan S, Randolph TW, Carpenter JF. 2003. Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation. Pharm Res 20:1325-1336.
    • (2003) Pharm Res , vol.20 , pp. 1325-1336
    • Chi, E.1    Krishnan, S.2    Randolph, T.3    Carpenter, J.4
  • 14
    • 0018974918 scopus 로고
    • Role of aggregated human growth hormone (Hgh) in development of antibodies to Hgh
    • Moore WV, Leppert P. 1980. Role of aggregated human growth hormone (Hgh) in development of antibodies to Hgh. J Clin Endocrin Metab 51:691-697.
    • (1980) J Clin Endocrin Metab , vol.51 , pp. 691-697
    • Moore, W.1    Leppert, P.2
  • 15
    • 0025286235 scopus 로고
    • Persistent cutaneous insulin allergy resulting from high molecular weight insulin aggregates
    • Ratner RE, Phillips TM, Steiner M. 1990. Persistent cutaneous insulin allergy resulting from high molecular weight insulin aggregates. Diabetes 39:728-733.
    • (1990) Diabetes , vol.39 , pp. 728-733
    • Ratner, R.1    Phillips, T.2    Steiner, M.3
  • 16
    • 0027475961 scopus 로고
    • Safety of intravenous immunoglobulin
    • Thornton CA, Ballow M. 1993. Safety of intravenous immunoglobulin. Arch Neurol 50:135-136.
    • (1993) Arch Neurol , vol.50 , pp. 135-136
    • Thornton, C.1    Ballow, M.2
  • 17
    • 68949135230 scopus 로고    scopus 로고
    • Immunogenicity of aggregates of recombinant human growth hormone in mouse models
    • Fradkin AH, Carpenter JF, Randolph TW. 2009. Immunogenicity of aggregates of recombinant human growth hormone in mouse models. J Pharm Sci 98:3247-3264.
    • (2009) J Pharm Sci , vol.98 , pp. 3247-3264
    • Fradkin, A.1    Carpenter, J.2    Randolph, T.3
  • 18
    • 0030990078 scopus 로고    scopus 로고
    • The effect of benzyl alcohol on recombinant human interferon-γ
    • Lam XM, Patapoff TW, Nguyen TH. 1997. The effect of benzyl alcohol on recombinant human interferon-γ. Pharm Res 14:725-729.
    • (1997) Pharm Res , vol.14 , pp. 725-729
    • Lam, X.1    Patapoff, T.2    Nguyen, T.3
  • 19
    • 10644283956 scopus 로고    scopus 로고
    • Mechanism for benzyl alcohol-induced aggregation of recombinant human interleukin-1-receptor antagonist in aqueous solution
    • Zhang Y, Roy S, Jones LS, Krishnan S, Kerwin BA, Chang BS, Manning MC, Randolph TW, Carpenter JF. 2004. Mechanism for benzyl alcohol-induced aggregation of recombinant human interleukin-1-receptor antagonist in aqueous solution. J Pharm Sci 93:3076-3089.
    • (2004) J Pharm Sci , vol.93 , pp. 3076-3089
    • Zhang, Y.1    Roy, S.2    Jones, L.3    Krishnan, S.4    Kerwin, B.5    Chang, B.6    Manning, M.7    Randolph, T.8    Carpenter, J.9
  • 20
    • 2642579304 scopus 로고    scopus 로고
    • Benzyl alcohol-induced destabilization of interferon-γ
    • Tobler SA, Holmes BW, Cromwell MEM, Fernandez EJ. 2004. Benzyl alcohol-induced destabilization of interferon-γ. J Pharm Sci 93:1605-1617
    • (2004) J Pharm Sci , vol.93 , pp. 1605-1617
    • Tobler, S.1    Holmes, B.2    Cromwell, M.3    Fernandez, E.4
  • 21
    • 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 BA, Randolph TW, Carpenter JF. 2006. Temperature dependence of benzyl alcohol-and 8-anilinonaphthalene-1-sulfonate-induced aggregation of recombinant human interleukin-1 receptor antagonist. Biochemistry 45:3898-3911.
    • (2006) Biochemistry , vol.45 , pp. 3898-3911
    • Roy, S.1    Katayama, D.2    Dong, A.3    Kerwin, B.4    Randolph, T.5    Carpenter, J.6
  • 22
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:945-949.
    • (1991) J Appl Crystallogr , vol.24 , pp. 945-949
    • Kraulis, P.1
  • 23
    • 0242578172 scopus 로고    scopus 로고
    • Intimate view of a kinetic protein folding intermediate: Residue-resolved structure, interactions, stability, folding and unfolding rates, homogeneity
    • Krishna MMG, Lin Y, Mayne L, Englander SW. 2003. Intimate view of a kinetic protein folding intermediate: Residue-resolved structure, interactions, stability, folding and unfolding rates, homogeneity. J Mol Biol 334:501-513.
    • (2003) J Mol Biol , vol.334 , pp. 501-513
    • Krishna, M.1    Lin, Y.2    Mayne, L.3    Englander, S.4
  • 24
    • 0033778161 scopus 로고    scopus 로고
    • Two-state vs. multistate protein unfolding studies by optical melting and hydrogen exchange
    • Mayne L, Englander SW. 2000. Two-state vs. multistate protein unfolding studies by optical melting and hydrogen exchange. Protein Sci 9:1873-1877.
    • (2000) Protein Sci , vol.9 , pp. 1873-1877
    • Mayne, L.1    Englander, S.2
  • 25
    • 51249083687 scopus 로고    scopus 로고
    • Förster resonance energy transfer and conformational stability of proteins. An advanced biophysical module for physical chemistry students
    • Sanchez KM, Schlamadinger DE, Gable JE, Kim JE. 2008. Förster resonance energy transfer and conformational stability of proteins. An advanced biophysical module for physical chemistry students. J Chem Ed 85:1253-1256.
    • (2008) J Chem Ed , vol.85 , pp. 1253-1256
    • Sanchez, K.1    Schlamadinger, D.2    Gable, J.3    Kim, J.4
  • 28
    • 70449234614 scopus 로고
    • Spectrum of horse-heart cytochrome c
    • Margoliash E, Frohwirt N. 1959. Spectrum of horse-heart cytochrome c. Biochem J 71:570-572.
    • (1959) Biochem J , vol.71 , pp. 570-572
    • Margoliash, E.1    Frohwirt, N.2
  • 29
    • 0027464611 scopus 로고
    • Destabilizing effects of replacing a surface lysine of cytochrome c with aromatic amino acids: Implications for the denatured state
    • Bowler BE, May K, Zaragoza T, York P, Dong A, Caughey WS. 1993. Destabilizing effects of replacing a surface lysine of cytochrome c with aromatic amino acids: Implications for the denatured state. Biochemistry 32:183-190.
    • (1993) Biochemistry , vol.32 , pp. 183-190
    • Bowler, B.1    May, K.2    Zaragoza, T.3    York, P.4    Dong, A.5    Caughey, W.6
  • 30
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131:266-280.
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.1
  • 31
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro MM, Bolen DW. 1988. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27:8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.1    Bolen, D.2
  • 32
    • 0026754044 scopus 로고
    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • Santoro MM, Bolen DW. 1992. A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. Biochemistry 31:4901-4907.
    • (1992) Biochemistry , vol.31 , pp. 4901-4907
    • Santoro, M.1    Bolen, D.2
  • 33
  • 34
    • 77953865084 scopus 로고    scopus 로고
    • Principles of fluorescence spectroscopy
    • 3rd ed.New York: Springer Science.
    • Lakowicz JR. 2006. Principles of fluorescence spectroscopy. 3rd ed.New York: Springer Science.
    • (2006)
    • Lakowicz, J.1
  • 35
    • 0032766705 scopus 로고    scopus 로고
    • Experimental study of the protein folding landscape: Unfolding reactions in cytochrome c
    • Milne JS, Xu Y, Mayne LC, Englander SW. 1999. Experimental study of the protein folding landscape: Unfolding reactions in cytochrome c. J Mol Biol 290:811-822.
    • (1999) J Mol Biol , vol.290 , pp. 811-822
    • Milne, J.1    Xu, Y.2    Mayne, L.3    Englander, S.4
  • 37
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • Dong A, Huang P, Caughey WS. 1990. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29:3303-3308.
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.3
  • 38
    • 0034473318 scopus 로고    scopus 로고
    • The infrared absorption of amino acid side chains
    • Barth A. 2000. The infrared absorption of amino acid side chains. Prog Biophys Mol Biol 74:141-173.
    • (2000) Prog Biophys Mol Biol , vol.74 , pp. 141-173
    • Barth, A.1
  • 39
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers JK, Pace CN, Scholtz JM. 1995. Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding. Protein Sci 4:2138-2148.
    • (1995) Protein Sci , vol.4 , pp. 2138-2148
    • Myers, J.1    Pace, C.2    Scholtz, J.3
  • 40
    • 0031662891 scopus 로고    scopus 로고
    • Evidence for an unfolding and refolding pathway in cytochrome c
    • Xu Y, Mayne L, Englander SW. 1998. Evidence for an unfolding and refolding pathway in cytochrome c. Nature Struct Biol 5:774-778.
    • (1998) Nature Struct Biol , vol.5 , pp. 774-778
    • Xu, Y.1    Mayne, L.2    Englander, S.3
  • 41
    • 33745137861 scopus 로고    scopus 로고
    • Order of steps in the cytochrome c folding pathway: Evidence for a sequential stabilization mechanism
    • Krishna MMG, Maity H, Rumbley JN, Lin Y, Englander SW. 2006. Order of steps in the cytochrome c folding pathway: Evidence for a sequential stabilization mechanism. J Mol Biol 359:1411-1420.
    • (2006) J Mol Biol , vol.359 , pp. 1411-1420
    • Krishna, M.1    Maity, H.2    Rumbley, J.3    Lin, Y.4    Englander, S.5
  • 42
    • 0032528558 scopus 로고    scopus 로고
    • Intermolecular β-sheet results from trifluoroethanol-induced nonnative α-helical structure in β-sheet predominant proteins: Infrared and circular dichroism spectroscopic study
    • Dong A, Matsuura J, Manning MC, Carpenter JF. 1998. Intermolecular β-sheet results from trifluoroethanol-induced nonnative α-helical structure in β-sheet predominant proteins: Infrared and circular dichroism spectroscopic study. Arch Biochem Biophys 355:275-281.
    • (1998) Arch Biochem Biophys , vol.355 , pp. 275-281
    • Dong, A.1    Matsuura, J.2    Manning, M.3    Carpenter, J.4
  • 44
    • 0034623286 scopus 로고    scopus 로고
    • Entrapping intermediates of thermal aggregation in α-helical proteins with low concentration of guanidine hydrochloride
    • Dong A, Randolph TW, Carpenter JF. 2000. Entrapping intermediates of thermal aggregation in α-helical proteins with low concentration of guanidine hydrochloride. J Biol Chem 275:27689-27693.
    • (2000) J Biol Chem , vol.275 , pp. 27689-27693
    • Dong, A.1    Randolph, T.2    Carpenter, J.3
  • 45
    • 0001753988 scopus 로고
    • Primary structure and evolution of cytochrome c
    • Margoliash E. 1963. Primary structure and evolution of cytochrome c. Proc Natl Acad Sci USA 50:672-679.
    • (1963) Proc Natl Acad Sci USA , vol.50 , pp. 672-679
    • Margoliash, E.1
  • 46
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai Y, Sosnick TR, Mayne L, Englander SW. 1995. Protein folding intermediates: Native-state hydrogen exchange. Science 269:192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.2    Mayne, L.3    Englander, S.4
  • 48
    • 42449151176 scopus 로고    scopus 로고
    • Protein folding and misfolding: Mechanism and principles
    • Englander SW, Mayne L, Krishna MMG. 2007. Protein folding and misfolding: Mechanism and principles. Q Rev Biophys 40:287-326.
    • (2007) Q Rev Biophys , vol.40 , pp. 287-326
    • Englander, S.1    Mayne, L.2    Krishna, M.3
  • 50
    • 0038786579 scopus 로고    scopus 로고
    • Cooperative omega loops in cytochrome c: Role in folding and function
    • Krishna MMG, Lin Y, Rumbley JN, Englander SW. 2003. Cooperative omega loops in cytochrome c: Role in folding and function. J Mol Biol 331:29-36.
    • (2003) J Mol Biol , vol.331 , pp. 29-36
    • Krishna, M.1    Lin, Y.2    Rumbley, J.3    Englander, S.4
  • 51
    • 0028346251 scopus 로고
    • Comparison of the conformational stability of the molten globule and native states of horse cytochrome c: Effects of acetylation, urea and guanidine-hydrochloride
    • Hagihara Y, Tan Y, Goto Y. 1994. Comparison of the conformational stability of the molten globule and native states of horse cytochrome c: Effects of acetylation, urea and guanidine-hydrochloride. J Mol Biol 237:336-348.
    • (1994) J Mol Biol , vol.237 , pp. 336-348
    • Hagihara, Y.1    Tan, Y.2    Goto, Y.3
  • 53
    • 0043157689 scopus 로고    scopus 로고
    • Anion concentration modulates the conformation and stability of the molten globule of cytochrome c
    • Sinibaldi F, Howes BD, Smulevich G, Ciaccio C, Coletta M, Santucci R. 2003. Anion concentration modulates the conformation and stability of the molten globule of cytochrome c. J Biol Inorg Chem 8:663-670.
    • (2003) J Biol Inorg Chem , vol.8 , pp. 663-670
    • Sinibaldi, F.1    Howes, B.2    Smulevich, G.3    Ciaccio, C.4    Coletta, M.5    Santucci, R.6
  • 54
    • 17044441821 scopus 로고    scopus 로고
    • Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles
    • Pinheiro TJT, Elove GA, Watts A, Roder H. 1997. Structural and kinetic description of cytochrome c unfolding induced by the interaction with lipid vesicles. Biochemistry 36:13122-13132.
    • (1997) Biochemistry , vol.36 , pp. 13122-13132
    • Pinheiro, T.1    Elove, G.2    Watts, A.3    Roder, H.4
  • 55
    • 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 DN, Randolph TW, Carpenter JF. 2006. Effects of pH, temperature, and sucrose on benzyl alcohol-induced aggregation of recombinant human granulocyte colony stimulating factor. J Pharm Sci 95:1480-1497.
    • (2006) J Pharm Sci , vol.95 , pp. 1480-1497
    • Thirumangalathu, R.1    Krishnan, S.2    Brems, D.3    Randolph, T.4    Carpenter, J.5
  • 57
    • 81255160473 scopus 로고    scopus 로고
    • drugs, and biologicals
    • 14th ed. Merck Sharp & Dohme Corp., Whitehouse Station, New Jersey, USA.
    • O'Neil MJ. The Merck Index - An encyclopedia of chemicals, drugs, and biologicals 14th ed. Merck Sharp & Dohme Corp., Whitehouse Station, New Jersey, USA.
    • The Merck Index - An encyclopedia of chemicals
    • O'Neil, M.1
  • 58
    • 33645459665 scopus 로고    scopus 로고
    • Ligand binding and thermostability of different allosteric states of the insulin zinc-hexamer
    • Huus K, Havelund S, Olsen HB, Sigurskjold BW, van de Weert M, Frokjaer S. 2006. Ligand binding and thermostability of different allosteric states of the insulin zinc-hexamer. Biochemistry 45:4014-4024.
    • (2006) Biochemistry , vol.45 , pp. 4014-4024
    • Huus, K.1    Havelund, S.2    Olsen, H.3    Sigurskjold, B.4    van de Weert, M.5    Frokjaer, S.6
  • 59
    • 77957372324 scopus 로고    scopus 로고
    • Stabilization of lysozyme by benzyl alcohol: Surface tension and thermodynamic parameters
    • Goyal MK, Roy I, Amin A, Banerjee UC, Bansal AK. 2010. Stabilization of lysozyme by benzyl alcohol: Surface tension and thermodynamic parameters. J Pharm Sci 99:4149-4161.
    • (2010) J Pharm Sci , vol.99 , pp. 4149-4161
    • Goyal, M.1    Roy, I.2    Amin, A.3    Banerjee, U.4    Bansal, A.5


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