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Volumn 118, Issue 1, 2014, Pages 26-36

Exploration of pH-dependent behavior of the anion receptor pocket of subdomain IIA of HSA: Determination of effective pocket charge using the Debye-Hückel limiting law

Author keywords

[No Author keywords available]

Indexed keywords

DYES; ELECTROSTATIC SEPARATORS; IONIC STRENGTH; PROTEINS;

EID: 84892618823     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp407057f     Document Type: Article
Times cited : (22)

References (73)
  • 1
    • 84858759719 scopus 로고    scopus 로고
    • Mechanical Modulation of Receptor-Ligand Interactions at Cell-Cell Interfaces
    • Allard, J. F.; Dushek, O.; Coombs, D.; van der Merwe, P. A. Mechanical Modulation of Receptor-Ligand Interactions at Cell-Cell Interfaces Biophys. J. 2012, 102, 1265-1273
    • (2012) Biophys. J. , vol.102 , pp. 1265-1273
    • Allard, J.F.1    Dushek, O.2    Coombs, D.3    Van Der Merwe, P.A.4
  • 3
    • 0000682461 scopus 로고
    • Supramolecular Photochemistry and Photophysics. A Cylindrical Macrotricyclic Receptor and Its Adducts with Protons, Ammonium Ions, and a Pt (II) Complex
    • Ballardini, R.; Balzani, V.; Credi, A.; Gandolfi, M. T.; Hibert, F. K.; Lehn, J. M.; Prodi, L. Supramolecular Photochemistry and Photophysics. A Cylindrical Macrotricyclic Receptor and Its Adducts with Protons, Ammonium Ions, and a Pt (II) Complex J. Am. Chem. Soc. 1994, 116, 5741-5746
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 5741-5746
    • Ballardini, R.1    Balzani, V.2    Credi, A.3    Gandolfi, M.T.4    Hibert, F.K.5    Lehn, J.M.6    Prodi, L.7
  • 5
    • 0000686383 scopus 로고    scopus 로고
    • Introduction: Molecular Recognition
    • Gellman, S. H. Introduction: Molecular Recognition Chem. Rev. 1997, 97, 1231-1232
    • (1997) Chem. Rev. , vol.97 , pp. 1231-1232
    • Gellman, S.H.1
  • 6
    • 0018413926 scopus 로고
    • Human Serum Albumin. Spectroscopic Studies of Binding and Proximity Relationships for Fatty Acids and Bilirubin
    • Berde, C. B.; Hudson, B. S.; Simon, R. D.; Sklar, L. A. Human Serum Albumin. Spectroscopic Studies of Binding and Proximity Relationships for Fatty Acids and Bilirubin J. Biol. Chem. 1979, 254, 391-400
    • (1979) J. Biol. Chem. , vol.254 , pp. 391-400
    • Berde, C.B.1    Hudson, B.S.2    Simon, R.D.3    Sklar, L.A.4
  • 7
    • 38149032895 scopus 로고    scopus 로고
    • Selectivity in Supramolecular Host-Guest Complexes
    • Schneider, H.-J.; Yatsimirsky, A. K. Selectivity in Supramolecular Host-Guest Complexes Chem. Soc. Rev. 2008, 37, 263-277
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 263-277
    • Schneider, H.-J.1    Yatsimirsky, A.K.2
  • 8
    • 0034310780 scopus 로고    scopus 로고
    • Binding of 5-(2 ′-Carboxyphenyl)Azoquinolin-8-Ol to Bovine Serum Albumin: A Spectroscopic Study
    • Pal, B.; Bajpai, P. K.; Baul, T. S. B. Binding of 5-(2 ′-Carboxyphenyl)Azoquinolin-8-Ol to Bovine Serum Albumin: A Spectroscopic Study Spectrochim. Acta, Part A 2000, 56, 2453-2458
    • (2000) Spectrochim. Acta, Part A , vol.56 , pp. 2453-2458
    • Pal, B.1    Bajpai, P.K.2    Baul, T.S.B.3
  • 9
    • 0037032294 scopus 로고    scopus 로고
    • Probing the Exposure of Tyrosine and Tryptophan Residues in Partially Folded Proteins and Folding Intermediates by Cidnp Pulse-Labeling
    • Lyon, C. E.; Suh, E. S.; Dobson, C. M.; Hore, P. J. Probing the Exposure of Tyrosine and Tryptophan Residues in Partially Folded Proteins and Folding Intermediates by Cidnp Pulse-Labeling J. Am. Chem. Soc. 2002, 124, 13018-13024
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 13018-13024
    • Lyon, C.E.1    Suh, E.S.2    Dobson, C.M.3    Hore, P.J.4
  • 10
    • 70350482625 scopus 로고    scopus 로고
    • Interfaces and Hydrophobic Interactions in Receptor-Ligand Systems: A Level-Set Variational Implicit Solvent Approach
    • Cheng, L. T.; Wang, Z.; Setny, P.; Dzubiella, J.; Li, B.; McCammon, J. A. Interfaces and Hydrophobic Interactions in Receptor-Ligand Systems: A Level-Set Variational Implicit Solvent Approach J. Chem. Phys. 2009, 131, 144102-144111
    • (2009) J. Chem. Phys. , vol.131 , pp. 144102-144111
    • Cheng, L.T.1    Wang, Z.2    Setny, P.3    Dzubiella, J.4    Li, B.5    McCammon, J.A.6
  • 11
    • 55549087599 scopus 로고    scopus 로고
    • Intra- and Intermembrane Pairwise Molecular Recognition between Synthetic Hydrogen Bonding Phospholipids
    • Ma, M.; Paredes, A.; Bong, D. Intra- and Intermembrane Pairwise Molecular Recognition between Synthetic Hydrogen Bonding Phospholipids J. Am. Chem. Soc. 2008, 130, 14456-14458
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14456-14458
    • Ma, M.1    Paredes, A.2    Bong, D.3
  • 12
    • 25444458906 scopus 로고    scopus 로고
    • The Chemical Interaction between the Estrogen Receptor and Monohydroxybenzo[a]Pyrene Derivatives Studied by Fluorescence Line-Narrowing Spectroscopy
    • Bader, A. N.; Van Dongen, M. M.; Van Lipzig, M. M. H.; Kool, J.; Meerman, J. H. N.; Ariese, F.; Gooijer, C. The Chemical Interaction between the Estrogen Receptor and Monohydroxybenzo[a]Pyrene Derivatives Studied by Fluorescence Line-Narrowing Spectroscopy Chem. Res. Toxicol. 2005, 18, 1405-1412
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 1405-1412
    • Bader, A.N.1    Van Dongen, M.M.2    Van Lipzig, M.M.H.3    Kool, J.4    Meerman, J.H.N.5    Ariese, F.6    Gooijer, C.7
  • 13
    • 0345603480 scopus 로고    scopus 로고
    • Extreme Complementarity in a Macrocycle Tweezer Complex
    • Colquhoun, H. M.; Zhu, Z.; Williams, D. J. Extreme Complementarity in a Macrocycle Tweezer Complex Org. Lett. 2003, 5, 4353-4356
    • (2003) Org. Lett. , vol.5 , pp. 4353-4356
    • Colquhoun, H.M.1    Zhu, Z.2    Williams, D.J.3
  • 15
    • 0037332510 scopus 로고    scopus 로고
    • Investigation of Host-Guest Stability Constants of Calix[n]Arenes Complexes with Aromatic Molecules by RP-HPLC Method
    • Baudry, R.; Kalchenko, O.; Dumazet-Bonnamour, I.; Vocanson, F.; Lamartine, R. Investigation of Host-Guest Stability Constants of Calix[n]Arenes Complexes with Aromatic Molecules by RP-HPLC Method J. Chromatogr. Sci. 2003, 41, 157-163
    • (2003) J. Chromatogr. Sci. , vol.41 , pp. 157-163
    • Baudry, R.1    Kalchenko, O.2    Dumazet-Bonnamour, I.3    Vocanson, F.4    Lamartine, R.5
  • 16
    • 84878977296 scopus 로고    scopus 로고
    • Highly Elastic Supramolecular Hydrogels Using Host-Guest Inclusion Complexes with Cyclodextrins
    • Kakuta, T.; Takashima, Y.; Harada, A. Highly Elastic Supramolecular Hydrogels Using Host-Guest Inclusion Complexes with Cyclodextrins Macromolecules 2013, 46, 4575-4579
    • (2013) Macromolecules , vol.46 , pp. 4575-4579
    • Kakuta, T.1    Takashima, Y.2    Harada, A.3
  • 17
    • 0032843983 scopus 로고    scopus 로고
    • Molecular Recognition of Nucleotide Pairs by a Cyclo-Bis-Intercaland-Type Receptor Molecule: A Spectrophotometric and Electrospray Mass Spectrometry Study
    • Baudoin, O.; Gonnet, F.; Teulade-Fichou, M. P.; Vigneron, J. P.; Tabet, J. C.; Lehn, J. M. Molecular Recognition of Nucleotide Pairs by a Cyclo-Bis-Intercaland-Type Receptor Molecule: A Spectrophotometric and Electrospray Mass Spectrometry Study Chem.-Eur. J. 1999, 5, 2762-2771
    • (1999) Chem. - Eur. J. , vol.5 , pp. 2762-2771
    • Baudoin, O.1    Gonnet, F.2    Teulade-Fichou, M.P.3    Vigneron, J.P.4    Tabet, J.C.5    Lehn, J.M.6
  • 18
    • 77953452882 scopus 로고    scopus 로고
    • Electrostatics in Proteins and Protein-Ligand Complexes
    • Kukić, P.; Nielsen, J. E. Electrostatics in Proteins and Protein-Ligand Complexes Future Med. Chem. 2010, 2, 647-666
    • (2010) Future Med. Chem. , vol.2 , pp. 647-666
    • Kukić, P.1    Nielsen, J.E.2
  • 19
    • 0027536858 scopus 로고
    • Ligand Protein Electrostatic Interactions Govern the Specificity of Retinol-Binding and Fatty Acid-Binding Proteins
    • Jakoby, M. G.; Miller, K. R.; Toner, J. J.; Bauman, A.; Cheng, L.; Li, E.; Cistola, D. P. Ligand Protein Electrostatic Interactions Govern the Specificity of Retinol-Binding and Fatty Acid-Binding Proteins Biochemistry 1993, 32, 872-878
    • (1993) Biochemistry , vol.32 , pp. 872-878
    • Jakoby, M.G.1    Miller, K.R.2    Toner, J.J.3    Bauman, A.4    Cheng, L.5    Li, E.6    Cistola, D.P.7
  • 22
    • 65249136509 scopus 로고    scopus 로고
    • Interaction of Bovine Serum Albumin with Dipolar Molecules: Fluorescence and Molecular Docking Studies
    • Bhattacharya, B.; Nakka, S.; Guruprasad, L.; Samanta, A. Interaction of Bovine Serum Albumin with Dipolar Molecules: Fluorescence and Molecular Docking Studies J. Phys. Chem. B 2009, 113, 2143-2150
    • (2009) J. Phys. Chem. B , vol.113 , pp. 2143-2150
    • Bhattacharya, B.1    Nakka, S.2    Guruprasad, L.3    Samanta, A.4
  • 23
    • 0035997013 scopus 로고    scopus 로고
    • Protein Folding Pathways and Kinetics: Molecular Dynamics Simulations of Beta-Strand Motifs
    • Jang, H.; Hall, C. K.; Zhou, Y. Q. Protein Folding Pathways and Kinetics: Molecular Dynamics Simulations of Beta-Strand Motifs Biophys. J. 2002, 83, 819-835
    • (2002) Biophys. J. , vol.83 , pp. 819-835
    • Jang, H.1    Hall, C.K.2    Zhou, Y.Q.3
  • 24
    • 0042420691 scopus 로고    scopus 로고
    • Investigation of the Induced-Fit Mechanism and Catalytic Activity of the Human Cytomegalovirus Protease Homodimer Via Molecular Dynamics Simulations
    • de Oliveira, C. A. F.; Guimaraes, C. R. W.; Barreiro, G.; de Alencastro, R. B. Investigation of the Induced-Fit Mechanism and Catalytic Activity of the Human Cytomegalovirus Protease Homodimer Via Molecular Dynamics Simulations Proteins: Struct., Funct., Genet. 2003, 52, 483-491
    • (2003) Proteins: Struct., Funct., Genet. , vol.52 , pp. 483-491
    • De Oliveira, C.A.F.1    Guimaraes, C.R.W.2    Barreiro, G.3    De Alencastro, R.B.4
  • 25
    • 0033618249 scopus 로고    scopus 로고
    • Interaction of 7-Hydroxy-8-(Phenylazo) 1,3-Naphthalenedisulfonate with Bovine Plasma Albumin - Spectroscopic Studies
    • Patel, A. B.; Srivastava, S.; Phadke, R. S. Interaction of 7-Hydroxy-8-(Phenylazo) 1,3-Naphthalenedisulfonate with Bovine Plasma Albumin-Spectroscopic Studies J. Biol. Chem. 1999, 274, 21755-21762
    • (1999) J. Biol. Chem. , vol.274 , pp. 21755-21762
    • Patel, A.B.1    Srivastava, S.2    Phadke, R.S.3
  • 26
    • 55349105837 scopus 로고    scopus 로고
    • Interaction of Serum Albumin with Vinyl Sulfonate Azo Dye
    • Sereikaite, J.; Bumelis, V. A. Interaction of Serum Albumin with Vinyl Sulfonate Azo Dye Cent. Eur. J. Chem. 2008, 6, 509-512
    • (2008) Cent. Eur. J. Chem. , vol.6 , pp. 509-512
    • Sereikaite, J.1    Bumelis, V.A.2
  • 28
    • 0022386437 scopus 로고
    • Tailoring the pH-Dependence of Enzyme Catalysis Using Protein Engineering
    • Thomas, P. G.; Russell, A. J.; Fersht, A. R. Tailoring the pH-Dependence of Enzyme Catalysis Using Protein Engineering Nature 1985, 318, 375-376
    • (1985) Nature , vol.318 , pp. 375-376
    • Thomas, P.G.1    Russell, A.J.2    Fersht, A.R.3
  • 29
    • 0031552366 scopus 로고    scopus 로고
    • Thermodynamics of the Interaction of Barnase and Barstar: Changes in Free Energy Versus Changes in Enthalpy on Mutation
    • Frisch, C.; Schreiber, G.; Johnson, C. M.; Fersht, A. R. Thermodynamics of the Interaction of Barnase and Barstar: Changes in Free Energy Versus Changes in Enthalpy on Mutation J. Mol. Biol. 1997, 267, 696-706
    • (1997) J. Mol. Biol. , vol.267 , pp. 696-706
    • Frisch, C.1    Schreiber, G.2    Johnson, C.M.3    Fersht, A.R.4
  • 30
    • 33749669289 scopus 로고    scopus 로고
    • In Vitro Study on the Binding of Neutral Red to Bovine Serum Albumin by Molecular Spectroscopy
    • Shang, L.; Jiang, X. U.; Dong, S. J. In Vitro Study on the Binding of Neutral Red to Bovine Serum Albumin by Molecular Spectroscopy J. Photochem. Photobiol., A 2006, 184, 93-97
    • (2006) J. Photochem. Photobiol., A , vol.184 , pp. 93-97
    • Shang, L.1    Jiang, X.U.2    Dong, S.J.3
  • 31
    • 0036787578 scopus 로고    scopus 로고
    • Protein Unfolding in Detergents: Effect of Micelle Structure, Ionic Strength, pH and Temperature
    • Otzen, D. E. Protein Unfolding in Detergents: Effect of Micelle Structure, Ionic Strength, pH and Temperature Biophys. J. 2002, 83, 2219-2230
    • (2002) Biophys. J. , vol.83 , pp. 2219-2230
    • Otzen, D.E.1
  • 32
    • 55749089574 scopus 로고    scopus 로고
    • Study on the Interaction between Bovine Serum Albumin and Cdte Quantum Dots with Spectroscopic Techniques
    • Liang, J. G.; Cheng, Y. P.; Han, H. Y. Study on the Interaction between Bovine Serum Albumin and Cdte Quantum Dots with Spectroscopic Techniques J. Mol. Struct. 2008, 892, 116-120
    • (2008) J. Mol. Struct. , vol.892 , pp. 116-120
    • Liang, J.G.1    Cheng, Y.P.2    Han, H.Y.3
  • 33
    • 0035930019 scopus 로고    scopus 로고
    • Quantitative Analysis of the Effect of Salt Concentration on Enzymatic Catalysis
    • Park, C.; Raines, R. T. Quantitative Analysis of the Effect of Salt Concentration on Enzymatic Catalysis J. Am. Chem. Soc. 2001, 123, 11472-11479
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11472-11479
    • Park, C.1    Raines, R.T.2
  • 34
    • 58549119543 scopus 로고    scopus 로고
    • Poisson-Boltzmann Model Analysis of Binding mRNA Cap Analogues to the Translation Initiation Factor Eif4e
    • Szklarczyk, O.; Zuberek, J.; Antosiewicz, J. M. Poisson-Boltzmann Model Analysis of Binding mRNA Cap Analogues to the Translation Initiation Factor Eif4e Biophys. Chem. 2009, 140, 16-23
    • (2009) Biophys. Chem. , vol.140 , pp. 16-23
    • Szklarczyk, O.1    Zuberek, J.2    Antosiewicz, J.M.3
  • 35
    • 33646477010 scopus 로고    scopus 로고
    • Salt-Dependent Binding of Iron(II) Mixed-Ligand Complexes Containing 1,10-Phenanthroline and Dipyrido[3,2-A: 2 ′,3 ′-C] Phenazine to Calf Thymus DNA
    • Mudasir; Wijaya, K.; Wahyuni, E. T.; Yoshioka, N.; Inoue, H. Salt-Dependent Binding of Iron(II) Mixed-Ligand Complexes Containing 1,10-Phenanthroline and Dipyrido[3,2-A: 2 ′,3 ′-C] Phenazine to Calf Thymus DNA Biophys. Chem. 2006, 121, 44-50
    • (2006) Biophys. Chem. , vol.121 , pp. 44-50
    • Mudasir1    Wijaya, K.2    Wahyuni, E.T.3    Yoshioka, N.4    Inoue, H.5
  • 36
    • 79955888291 scopus 로고    scopus 로고
    • Understanding the Physical Basis of the Salt Dependence of the Electrostatic Binding Free Energy of Mutated Charged Ligand-Nucleic Acid Complexes
    • Harris, R. C.; Bredenberg, J. H.; Silalahi, A. R. J.; Boschitsch, A. H.; Fenley, M. O. Understanding the Physical Basis of the Salt Dependence of the Electrostatic Binding Free Energy of Mutated Charged Ligand-Nucleic Acid Complexes Biophys. Chem. 2011, 156, 79-87
    • (2011) Biophys. Chem. , vol.156 , pp. 79-87
    • Harris, R.C.1    Bredenberg, J.H.2    Silalahi, A.R.J.3    Boschitsch, A.H.4    Fenley, M.O.5
  • 37
    • 59849124286 scopus 로고    scopus 로고
    • Interaction of Malachite Green with Bovine Serum Albumin: Determination of the Binding Mechanism and Binding Site by Spectroscopic Methods
    • Zhang, Y. Z.; Zhou, B.; Zhang, X. P.; Huang, P.; Li, C. H.; Liu, Y. Interaction of Malachite Green with Bovine Serum Albumin: Determination of the Binding Mechanism and Binding Site by Spectroscopic Methods J. Hazard. Mater. 2009, 163, 1345-1352
    • (2009) J. Hazard. Mater. , vol.163 , pp. 1345-1352
    • Zhang, Y.Z.1    Zhou, B.2    Zhang, X.P.3    Huang, P.4    Li, C.H.5    Liu, Y.6
  • 38
    • 84859598351 scopus 로고    scopus 로고
    • Optical Spectroscopic Exploration of Binding of Cochineal Red A with Two Homologous Serum Albumins
    • Bolel, P.; Mahapatra, N.; Halder, M. Optical Spectroscopic Exploration of Binding of Cochineal Red A with Two Homologous Serum Albumins J. Agric. Food Chem. 2012, 60, 3727-3734
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 3727-3734
    • Bolel, P.1    Mahapatra, N.2    Halder, M.3
  • 39
    • 84877099888 scopus 로고    scopus 로고
    • PH-Insensitive Electrostatic Interaction of Carmoisine with Two Serum Proteins: A Possible Caution on Its Uses in Food and Pharmaceutical Industry
    • Datta, S.; Mahapatra, N.; Halder, M. pH-Insensitive Electrostatic Interaction of Carmoisine with Two Serum Proteins: A Possible Caution on Its Uses in Food and Pharmaceutical Industry J. Photochem. Photobiol., B 2013, 124, 50-62
    • (2013) J. Photochem. Photobiol., B , vol.124 , pp. 50-62
    • Datta, S.1    Mahapatra, N.2    Halder, M.3
  • 41
    • 0001471927 scopus 로고
    • Thermodynamic and Kinetic Data for Macrocycle Interaction with Cations, Anions, and Neutral Molecules
    • Izatt, R. M.; Pawlak, K.; Bradshaw, J. S. Thermodynamic and Kinetic Data for Macrocycle Interaction with Cations, Anions, and Neutral Molecules Chem. Rev. 1995, 95, 2529-2586
    • (1995) Chem. Rev. , vol.95 , pp. 2529-2586
    • Izatt, R.M.1    Pawlak, K.2    Bradshaw, J.S.3
  • 42
    • 84877710767 scopus 로고    scopus 로고
    • Interplay of pH and Binding of Multivalent Metal Ions: Charge Inversion and Reentrant Condensation in Protein Solutions
    • Roosen-Runge, F.; Heck, B. S.; Zhang, F. J.; Kohlbacher, O.; Schreiber, F. Interplay of pH and Binding of Multivalent Metal Ions: Charge Inversion and Reentrant Condensation in Protein Solutions J. Phys. Chem. B 2013, 117, 5777-5787
    • (2013) J. Phys. Chem. B , vol.117 , pp. 5777-5787
    • Roosen-Runge, F.1    Heck, B.S.2    Zhang, F.J.3    Kohlbacher, O.4    Schreiber, F.5
  • 43
    • 0001166734 scopus 로고
    • The Theory of Electrolytes.1.Lowering of Freezing Point and Rleated Phenomena
    • Debye, P.; Hückel, E. The Theory of Electrolytes.1.Lowering of Freezing Point and Rleated Phenomena Phys. Z. 1923, 24, 185-206
    • (1923) Phys. Z. , vol.24 , pp. 185-206
    • Debye, P.1    Hückel, E.2
  • 44
    • 0001112223 scopus 로고
    • The Inter-Ionic Attraction Theory of Ionized Solutes. Iv. The Influence of Variation of Dielectric Constant on the Limiting Law for Small Concentrations
    • Debye, P.; Pauling, L. The Inter-Ionic Attraction Theory of Ionized Solutes. Iv. The Influence of Variation of Dielectric Constant on the Limiting Law for Small Concentrations J. Am. Chem. Soc. 1925, 47, 2129-2134
    • (1925) J. Am. Chem. Soc. , vol.47 , pp. 2129-2134
    • Debye, P.1    Pauling, L.2
  • 45
    • 0019538149 scopus 로고
    • Molecular Aspects of Ligand-Binding to Serum-Albumin
    • Kragh-Hansen, U. Molecular Aspects of Ligand-Binding to Serum-Albumin Pharmacol. Rev. 1981, 33, 17-53
    • (1981) Pharmacol. Rev. , vol.33 , pp. 17-53
    • Kragh-Hansen, U.1
  • 46
    • 0023354355 scopus 로고
    • Protein Binding as a Primary Determinant of the Clinical Pharmacokinetic Properties of Nonsteroidal Antiinflammatory. Drugs
    • Lin, J. H.; Cocchetto, D. M.; Duggan, D. E. Protein Binding as a Primary Determinant of the Clinical Pharmacokinetic Properties of Nonsteroidal Antiinflammatory. Drugs Clin. Pharmacokinet. 1987, 12, 402-432
    • (1987) Clin. Pharmacokinet. , vol.12 , pp. 402-432
    • Lin, J.H.1    Cocchetto, D.M.2    Duggan, D.E.3
  • 47
    • 0033973926 scopus 로고    scopus 로고
    • Influence of Dietary Components on the Gastrointestinal Metabolism and Transport of Drugs
    • Evans, A. M. Influence of Dietary Components on the Gastrointestinal Metabolism and Transport of Drugs Ther. Drug Monit. 2000, 22, 131-136
    • (2000) Ther. Drug Monit. , vol.22 , pp. 131-136
    • Evans, A.M.1
  • 49
    • 0027491794 scopus 로고
    • Study of Interaction of Carprofen and Its Enantiomers with Human Serum-Albumin 0.1. Mechanism of Binding Studied by Dialysis and Spectroscopic Methods
    • Rahman, M. H.; Maruyama, T.; Okada, T.; Yamasaki, K.; Otagiri, M. Study of Interaction of Carprofen and Its Enantiomers with Human Serum-Albumin 0.1. Mechanism of Binding Studied by Dialysis and Spectroscopic Methods Biochem. Pharmacol. 1993, 46, 1721-1731
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 1721-1731
    • Rahman, M.H.1    Maruyama, T.2    Okada, T.3    Yamasaki, K.4    Otagiri, M.5
  • 50
    • 0039397801 scopus 로고
    • Synthetic Food Colours
    • 2 nd ed. Furia, T. E. CRC Press: Boca Raton, FL
    • Noonan, J. E.; Meggos, H. Synthetic Food Colours. In Handbook of Food Additives, 2 nd ed.; Furia, T. E., Ed.; CRC Press: Boca Raton, FL, 1980; pp 339-383.
    • (1980) Handbook of Food Additives , pp. 339-383
    • Noonan, J.E.1    Meggos, H.2
  • 51
    • 58949096544 scopus 로고    scopus 로고
    • The Use of Coumarins as Environmentally-Sensitive Fluorescent Probes of Heterogeneous Inclusion Systems
    • Wagner, B. D. The Use of Coumarins as Environmentally-Sensitive Fluorescent Probes of Heterogeneous Inclusion Systems Molecules 2009, 14, 210-237
    • (2009) Molecules , vol.14 , pp. 210-237
    • Wagner, B.D.1
  • 52
    • 0027257511 scopus 로고
    • Anticoagulant-Related Bleeding - Clinical Epidemiology, Prediction, and Prevention
    • Landefeld, C. S.; Beyth, R. J. Anticoagulant-Related Bleeding-Clinical Epidemiology, Prediction, and Prevention Am. J. Med. 1993, 95, 315-328
    • (1993) Am. J. Med. , vol.95 , pp. 315-328
    • Landefeld, C.S.1    Beyth, R.J.2
  • 53
    • 0001851995 scopus 로고
    • Some Aspects of the Structure and Conformational Properties of Serum Albumin
    • Rosenoer, V. M. Oratz, M. Rothschild, M. A. Pergamon Press: New York
    • Foster, J. F. Some Aspects of the Structure and Conformational Properties of Serum Albumin. In Albumin Structure, Function and Uses; Rosenoer, V. M.; Oratz, M.; Rothschild, M. A., Eds.; Pergamon Press: New York, 1977; pp 53-84.
    • (1977) Albumin Structure, Function and Uses , pp. 53-84
    • Foster, J.F.1
  • 54
    • 33845957358 scopus 로고    scopus 로고
    • Determination of 13 Synthetic Food Colorants in Water-Soluble Foods by Reversed-Phase High-Performance Liquid Chromatography Coupled with Diode-Array Detector
    • Minioti, K. S.; Sakellariou, C. F.; Thomaidis, N. S. Determination of 13 Synthetic Food Colorants in Water-Soluble Foods by Reversed-Phase High-Performance Liquid Chromatography Coupled with Diode-Array Detector Anal. Chim. Acta 2007, 583, 103-110
    • (2007) Anal. Chim. Acta , vol.583 , pp. 103-110
    • Minioti, K.S.1    Sakellariou, C.F.2    Thomaidis, N.S.3
  • 55
    • 0021953019 scopus 로고
    • Interaction of Warfarin with Human-Serum Albumin - A Stoichiometric Description
    • Larsen, F. G.; Larsen, C. G.; Jakobsen, P.; Brodersen, R. Interaction of Warfarin with Human-Serum Albumin-a Stoichiometric Description Mol. Pharmacol. 1985, 27, 263-270
    • (1985) Mol. Pharmacol. , vol.27 , pp. 263-270
    • Larsen, F.G.1    Larsen, C.G.2    Jakobsen, P.3    Brodersen, R.4
  • 57
    • 0033116302 scopus 로고    scopus 로고
    • More about the Inner Filter Effect: Corrections of Stern-Volmer Fluorescence Quenching Constants Are Necessary at Very Low Optical Absorption of the Quencher
    • Borissevitch, I. E. More About the Inner Filter Effect: Corrections of Stern-Volmer Fluorescence Quenching Constants Are Necessary at Very Low Optical Absorption of the Quencher J. Lumin. 1999, 81, 219-224
    • (1999) J. Lumin. , vol.81 , pp. 219-224
    • Borissevitch, I.E.1
  • 58
    • 0032495131 scopus 로고    scopus 로고
    • Investigation of the Interaction between Acridine Orange and Bovine Serum Albumin
    • Feng, X. Z.; Lin, Z.; Yang, L. J.; Wang, C.; Bai, C. L. Investigation of the Interaction between Acridine Orange and Bovine Serum Albumin Talanta 1998, 47, 1223-1229
    • (1998) Talanta , vol.47 , pp. 1223-1229
    • Feng, X.Z.1    Lin, Z.2    Yang, L.J.3    Wang, C.4    Bai, C.L.5
  • 59
    • 0020081536 scopus 로고
    • Fluorimetric Analysis of the Binding of Warfarin to Human-Serum Albumin- Equilibrium and Kinetic-Study
    • Maes, V.; Engelborghs, Y.; Hoebeke, J.; Maras, Y.; Vercruysse, A. Fluorimetric Analysis of the Binding of Warfarin to Human-Serum Albumin- Equilibrium and Kinetic-Study Mol. Pharmacol. 1982, 21, 100-107
    • (1982) Mol. Pharmacol. , vol.21 , pp. 100-107
    • Maes, V.1    Engelborghs, Y.2    Hoebeke, J.3    Maras, Y.4    Vercruysse, A.5
  • 60
    • 73349120806 scopus 로고    scopus 로고
    • Stewart Computational Chemistry: Colorado Springs, CO
    • Stewart, J. J. P. Mopac2009; Stewart Computational Chemistry: Colorado Springs, CO, 2008.
    • (2008) Mopac2009
    • Stewart, J.J.P.1
  • 61
    • 11644261806 scopus 로고    scopus 로고
    • Automated Docking Using a Lamarckian Genetic Algorithm and an Empirical Binding Free Energy Function
    • Morris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated Docking Using a Lamarckian Genetic Algorithm and an Empirical Binding Free Energy Function J. Comput. Chem. 1998, 19, 1639-1662
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 63
    • 83455195623 scopus 로고    scopus 로고
    • Comprehensive. Study of Tartrazine/Cationic Surfactant Interaction
    • Shahir, A. A.; Javadian, S.; Razavizadeh, B. B. M.; Gharibi, H. Comprehensive. Study of Tartrazine/Cationic Surfactant Interaction J. Phys. Chem. B 2011, 115, 14435-14444
    • (2011) J. Phys. Chem. B , vol.115 , pp. 14435-14444
    • Shahir, A.A.1    Javadian, S.2    Razavizadeh, B.B.M.3    Gharibi, H.4
  • 64
    • 2442711715 scopus 로고    scopus 로고
    • Interactions between Some Anionic Dyes and Cationic Surfactants with Different Alkyl Chain Length Studied by the Method of Continuous Variations
    • Forte-Tavcer, P. Interactions between Some Anionic Dyes and Cationic Surfactants with Different Alkyl Chain Length Studied by the Method of Continuous Variations Dyes Pigm. 2004, 63, 181-189
    • (2004) Dyes Pigm. , vol.63 , pp. 181-189
    • Forte-Tavcer, P.1
  • 65
    • 0035933789 scopus 로고    scopus 로고
    • Crystal Structure Analysis of Warfarin Binding to Human Serum Albumin - Anatomy of Drug Site i
    • Petitpas, I.; Bhattacharya, A. A.; Twine, S.; East, M.; Curry, S. Crystal Structure Analysis of Warfarin Binding to Human Serum Albumin-Anatomy of Drug Site I J. Biol. Chem. 2001, 276, 22804-22809
    • (2001) J. Biol. Chem. , vol.276 , pp. 22804-22809
    • Petitpas, I.1    Bhattacharya, A.A.2    Twine, S.3    East, M.4    Curry, S.5
  • 67
    • 76449090649 scopus 로고    scopus 로고
    • Study of the Denaturation of Human Serum Albumin by Sodium Dodecyl Sulfate Using the Intrinsic Fluorescence of Albumin
    • Vlasova, I. M.; Saletsky, A. M. Study of the Denaturation of Human Serum Albumin by Sodium Dodecyl Sulfate Using the Intrinsic Fluorescence of Albumin J. Appl. Spectrosc. 2009, 76, 536-541
    • (2009) J. Appl. Spectrosc. , vol.76 , pp. 536-541
    • Vlasova, I.M.1    Saletsky, A.M.2
  • 68
    • 13444250971 scopus 로고    scopus 로고
    • Apparent Debye-Huckel Electrostatic Effects in the Folding of a Simple, Single Domain Protein
    • Rios, M. A. D.; Plaxco, K. W. Apparent Debye-Huckel Electrostatic Effects in the Folding of a Simple, Single Domain Protein Biochemistry 2005, 44, 1243-1250
    • (2005) Biochemistry , vol.44 , pp. 1243-1250
    • Rios, M.A.D.1    Plaxco, K.W.2
  • 71
    • 0028227096 scopus 로고
    • Structure of Serum-Albumin
    • Carter, D. C.; Ho, J. X. Structure of Serum-Albumin Adv. Protein Chem. 1994, 45, 153-203
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 73
    • 33747131772 scopus 로고    scopus 로고
    • Toward the Accurate First-Principles Prediction of Ionization Equilibria in Proteins
    • Khandogin, J.; Brooks, C. L. Toward the Accurate First-Principles Prediction of Ionization Equilibria in Proteins Biochemistry 2006, 45, 9363-9373
    • (2006) Biochemistry , vol.45 , pp. 9363-9373
    • Khandogin, J.1    Brooks, C.L.2


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