메뉴 건너뛰기




Volumn 84, Issue 3, 2008, Pages 750-757

Molecular recognition in partially folded states of a transporter protein: Temperature-dependent specificity of bovine serum albumin

Author keywords

[No Author keywords available]

Indexed keywords

BOVINE SERUM ALBUMIN; LIGAND;

EID: 42549159378     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.2007.00252.x     Document Type: Article
Times cited : (4)

References (29)
  • 1
    • 0034039993 scopus 로고    scopus 로고
    • Ligand binding proteins: Their potential for application in systems for controlled delivery and uptake of ligands
    • de Wolf, F. A. G. M. Brett (2000) Ligand binding proteins: Their potential for application in systems for controlled delivery and uptake of ligands. Pharmacol. Rev. 52, 207 236.
    • (2000) Pharmacol. Rev. , vol.52 , pp. 207-236
    • De Wolf, F.A.1    Brett, G.M.2
  • 2
    • 0034254742 scopus 로고    scopus 로고
    • Role of Arg-410 and Tyr-411 in human serum albumin for ligand binding and esterase-like activity
    • Watanabe, H., S. Tanase, K. Nakajou, T. Maruyama, U. Kragh-Hansen M. Otagiri (2000) Role of Arg-410 and Tyr-411 in human serum albumin for ligand binding and esterase-like activity. Biochem. J. 349, 813 819.
    • (2000) Biochem. J. , vol.349 , pp. 813-819
    • Watanabe, H.1    Tanase, S.2    Nakajou, K.3    Maruyama, T.4    Kragh-Hansen, U.5    Otagiri, M.6
  • 3
    • 0032872988 scopus 로고    scopus 로고
    • Characterization of solute binding at human serum albumin site II and its geometry using a biochromatographic approach
    • Peyrin, E., Y. C. Guillaume C. Guinchard (1999) Characterization of solute binding at human serum albumin site II and its geometry using a biochromatographic approach. Biophys. J. 77, 1206 1212.
    • (1999) Biophys. J. , vol.77 , pp. 1206-1212
    • Peyrin, E.1    Guillaume, Y.C.2    Guinchard, C.3
  • 4
    • 0016801988 scopus 로고
    • The characterization of two specific drug binding sites on human serum albumin
    • Sudlow, G., D. J. Birkett D. N. Wade (1975) The characterization of two specific drug binding sites on human serum albumin. Mol. Pharmacol. 11, 824 832.
    • (1975) Mol. Pharmacol. , vol.11 , pp. 824-832
    • Sudlow, G.1    Birkett, D.J.2    Wade, D.N.3
  • 5
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He, X. M. D. C. Carter (1992) Atomic structure and chemistry of human serum albumin. Nature 358, 209 215.
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 6
    • 0033062612 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin at 2.5 Å resolution
    • Sugio, S., A. Kashima, S. Mochizuki, M. Noda K. Kobayashi (1999) Crystal structure of human serum albumin at 2.5 Å resolution. Prot. Eng. 12, 439 446.
    • (1999) Prot. Eng. , vol.12 , pp. 439-446
    • Sugio, S.1    Kashima, A.2    Mochizuki, S.3    Noda, M.4    Kobayashi, K.5
  • 7
    • 33745470061 scopus 로고    scopus 로고
    • Ultrafast solvation dynamics of human serum albumin: Correlations with conformational transitions and site selected recognition
    • Qiu, W., L. Zhang, Y. Yang, O. Okobiah, L. Wang, D. Zhong A. H. Zewail (2006) Ultrafast solvation dynamics of human serum albumin: Correlations with conformational transitions and site selected recognition. J. Phys. Chem. B 110, 10540 10549.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 10540-10549
    • Qiu, W.1    Zhang, L.2    Yang, Y.3    Okobiah, O.4    Wang, L.5    Zhong, D.6    Zewail, A.H.7
  • 8
    • 0031852954 scopus 로고    scopus 로고
    • Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods
    • Flora, K., J. D. Brennan, G. A. Baker, M. A. Doody F. V. Bright (1998) Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods. Biophys. J. 75, 1084 1096.
    • (1998) Biophys. J. , vol.75 , pp. 1084-1096
    • Flora, K.1    Brennan, J.D.2    Baker, G.A.3    Doody, M.A.4    Bright, F.V.5
  • 9
    • 0242398970 scopus 로고    scopus 로고
    • The interaction of bovine serum albumin with sodium dodecyl sulfate: Binding of the surfactant and conformational change of the protein induced by the binding
    • Takeda, K. Y. Moriyama (1997) The interaction of bovine serum albumin with sodium dodecyl sulfate: Binding of the surfactant and conformational change of the protein induced by the binding. Curr. Topics Coll. Intf. Sc. 1, 109 135.
    • (1997) Curr. Topics Coll. Intf. Sc. , vol.1 , pp. 109-135
    • Takeda, K.1    Moriyama, Y.2
  • 10
    • 0024801380 scopus 로고
    • Conformational change of bovine serum albumin by heat treatment
    • Takeda, K., A. Wada, K. Yamamoto, Y. Moriyama K. Aoki (1989) Conformational change of bovine serum albumin by heat treatment. J. Prot. Chem. 8, 653 659.
    • (1989) J. Prot. Chem. , vol.8 , pp. 653-659
    • Takeda, K.1    Wada, A.2    Yamamoto, K.3    Moriyama, Y.4    Aoki, K.5
  • 11
    • 0031896612 scopus 로고    scopus 로고
    • Species differences of serum albumins: II. Chemical and thermal stability
    • Kosa, T., T. Maruyama M. Otagiri (1998) Species differences of serum albumins: II. Chemical and thermal stability. Pharma. Res. 15, 449 454.
    • (1998) Pharma. Res. , vol.15 , pp. 449-454
    • Kosa, T.1    Maruyama, T.2    Otagiri, M.3
  • 12
    • 4344603721 scopus 로고    scopus 로고
    • Vibrational circular dichroism spectra of protein films: Thermal denaturation of bovine serum albumin
    • Shanmugam, G. P. L. Polavarapu (2004) Vibrational circular dichroism spectra of protein films: Thermal denaturation of bovine serum albumin. Biophys. Chem. 111, 73 77.
    • (2004) Biophys. Chem. , vol.111 , pp. 73-77
    • Shanmugam, G.1    Polavarapu, P.L.2
  • 13
    • 0030465765 scopus 로고    scopus 로고
    • Differential scanning calorimetric studies on bovine serum albumin IV. Effect of anionic surfactants with various lengths of hydrocarbon chain
    • Yamasaki, M., T. Yamashita, H. Yano, K. Tatsumi K. Aoki (1996) Differential scanning calorimetric studies on bovine serum albumin IV. Effect of anionic surfactants with various lengths of hydrocarbon chain. Int. J. Biol. Macromol. 19, 241 246.
    • (1996) Int. J. Biol. Macromol. , vol.19 , pp. 241-246
    • Yamasaki, M.1    Yamashita, T.2    Yano, H.3    Tatsumi, K.4    Aoki, K.5
  • 14
    • 0025046965 scopus 로고
    • Differential scanning calorimetric studies on bovine serum albumin: I. Effects of pH and ionic strength
    • Yamasaki, M., H. Yano K. Aoki (1990) Differential scanning calorimetric studies on bovine serum albumin: I. Effects of pH and ionic strength. Int. J. Biol. Macromol. 12, 263 268.
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 263-268
    • Yamasaki, M.1    Yano, H.2    Aoki, K.3
  • 15
    • 0030979596 scopus 로고    scopus 로고
    • DSC studies on bovine serum albumin denaturation effects of ionic strength and SDS concentration
    • Giancola, C., C. de Sena, D. Fessas, G. Graziano G. Barone (1997) DSC studies on bovine serum albumin denaturation effects of ionic strength and SDS concentration. Int. J. Biol. Macromol. 20, 193 204.
    • (1997) Int. J. Biol. Macromol. , vol.20 , pp. 193-204
    • Giancola, C.1    De Sena, C.2    Fessas, D.3    Graziano, G.4    Barone, G.5
  • 16
    • 33646774999 scopus 로고    scopus 로고
    • Adsorption-induced conformational changes of proteins onto ceramic particles: Differential scanning calorimetry and FTIR analysis
    • Brandes, N., P. B. Welzel, C. Werner L. W. Kroh (2006) Adsorption-induced conformational changes of proteins onto ceramic particles: Differential scanning calorimetry and FTIR analysis. J. Coll. Int. Sci. 299, 56 69.
    • (2006) J. Coll. Int. Sci. , vol.299 , pp. 56-69
    • Brandes, N.1    Welzel, P.B.2    Werner, C.3    Kroh, L.W.4
  • 17
    • 4544230814 scopus 로고    scopus 로고
    • Ultrafast hydration dynamics in protein unfolding: Human serum albumin
    • Kamal, J. K. A., L. Zhao A. H. Zewail (2004) Ultrafast hydration dynamics in protein unfolding: Human serum albumin. Proc. Natl Acad. Sci. USA 101, 13411 13416.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 13411-13416
    • Kamal, J.K.A.1    Zhao, L.2    Zewail, A.H.3
  • 18
    • 0025294091 scopus 로고
    • Fluorescence lifetime and rotational correlation time of bovine serum albumin-sodium dodecyl sulphate complex labeled with 1-dimethylaminonaphthalene- 5-sulphonyl chloride: Effect of disulphide bridges in the protein on the fluorescence parameters
    • Takeda, K. K. Yamamoto (1989) Fluorescence lifetime and rotational correlation time of bovine serum albumin-sodium dodecyl sulphate complex labeled with 1-dimethylaminonaphthalene-5-sulphonyl chloride: Effect of disulphide bridges in the protein on the fluorescence parameters. J. Prot. Chem. 9, 17 22.
    • (1989) J. Prot. Chem. , vol.9 , pp. 17-22
    • Takeda, K.1    Yamamoto, K.2
  • 19
    • 0037230054 scopus 로고    scopus 로고
    • Protective effect of small amounts of sodium dodecyl sulphate on the helical structure of bovine serum albumin in thermal denaturation
    • Moriyama, Y., Y. Kawasaka K. Takeda (2003) Protective effect of small amounts of sodium dodecyl sulphate on the helical structure of bovine serum albumin in thermal denaturation. J. Coll. Int. Sci. 257, 41 46.
    • (2003) J. Coll. Int. Sci. , vol.257 , pp. 41-46
    • Moriyama, Y.1    Kawasaka, Y.2    Takeda, K.3
  • 20
    • 34248155667 scopus 로고    scopus 로고
    • Systematic investigation of the thermodynamics of HSA adsorption to N-iso-propylacrylamide/N-tert-butylacrylamide copolymer nanoparticles. Effects of particle size and hydrophobicity
    • Lindman, S., I. Lynch, E. Thulin, H. Nilsson, K. A. Dawson S. Linse (2007) Systematic investigation of the thermodynamics of HSA adsorption to N-iso-propylacrylamide/N-tert-butylacrylamide copolymer nanoparticles. Effects of particle size and hydrophobicity. Nano. Lett. 7, 914 920.
    • (2007) Nano. Lett. , vol.7 , pp. 914-920
    • Lindman, S.1    Lynch, I.2    Thulin, E.3    Nilsson, H.4    Dawson, K.A.5    Linse, S.6
  • 21
    • 2342424274 scopus 로고    scopus 로고
    • Synthesis and characterization of active ester-functionalized polypyrrole-silica nanoparticles: Application to the covalent attachment of proteins
    • Azioune, A., A. B. Slimane, L. A. Hamou, A. Pleuvy, M. M. Chehimi, C. Perruchot S. P. Armes (2004) Synthesis and characterization of active ester-functionalized polypyrrole-silica nanoparticles: Application to the covalent attachment of proteins. Langmuir 20, 3350 3356.
    • (2004) Langmuir , vol.20 , pp. 3350-3356
    • Azioune, A.1    Slimane, A.B.2    Hamou, L.A.3    Pleuvy, A.4    Chehimi, M.M.5    Perruchot, C.6    Armes, S.P.7
  • 24
    • 0037920996 scopus 로고    scopus 로고
    • Thermodynamics of protein folding and stability
    • Cooper, A. (1999) Thermodynamics of protein folding and stability. Protein: A Comprehensive Treatise 2, 217 270.
    • (1999) Protein: A Comprehensive Treatise , vol.2 , pp. 217-270
    • Cooper, A.1
  • 25
    • 33947481462 scopus 로고
    • The thermodynamics of protein denaturation. I. the denaturation of chymotrypsinogen
    • Brandts, J. F. (1964) The thermodynamics of protein denaturation. I. The denaturation of chymotrypsinogen. J. Am. Chem. Soc. 86, 4291 4301.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 4291-4301
    • Brandts, J.F.1
  • 26
    • 25844447139 scopus 로고    scopus 로고
    • Detergent binding as a sensor of hydrophobicity and polar interactions in the binding cavities of proteins
    • Peyre, V., V. Lair, V. Andre, G. le Maire, U. Kragh-Hansen, M. le Maire J. V. Moller (2005) Detergent binding as a sensor of hydrophobicity and polar interactions in the binding cavities of proteins. Langmuir 21, 8865 8875.
    • (2005) Langmuir , vol.21 , pp. 8865-8875
    • Peyre, V.1    Lair, V.2    Andre, V.3    Le Maire, G.4    Kragh-Hansen, U.5    Le Maire, M.6    Moller, J.V.7
  • 28
    • 33845375827 scopus 로고
    • Small-angle neutron scattering from hexadecyltrimethylammonium bromide micelles in aqueous solutions
    • Berr, S. S., E. Caponetti, J. S. Johnson, J. R. R. M. Jones L. J. Magid (1986) Small-angle neutron scattering from hexadecyltrimethylammonium bromide micelles in aqueous solutions. J. Phys. Chem. 90, 5766 5770.
    • (1986) J. Phys. Chem. , vol.90 , pp. 5766-5770
    • Berr, S.S.1    Caponetti, E.2    Johnson, J.S.3    Jones, J.R.R.M.4    Magid, L.J.5
  • 29
    • 0021099449 scopus 로고
    • Resonance energy transfer between cysteine-34, tryptophan-214 and tyrosine 411 of human serum albumin
    • Hagag, N., E. R. Birnbaum D. W. Darnall (1983) Resonance energy transfer between cysteine-34, tryptophan-214 and tyrosine 411 of human serum albumin. Biochemistry 22, 2420 2427.
    • (1983) Biochemistry , vol.22 , pp. 2420-2427
    • Hagag, N.1    Birnbaum, E.R.2    Darnall, D.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.