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Volumn 55, Issue 1, 2011, Pages 114-124

Lomefloxacin promotes the interaction between human serum albumin and transferrin: A mechanistic insight into the emergence of antibiotic's side effects

Author keywords

Albumin; Lomefloxacin; Protein protein interaction; Transferrin

Indexed keywords

HYDROGEN; LOMEFLOXACIN; SERUM ALBUMIN; TRANSFERRIN;

EID: 79951768026     PISSN: 07317085     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jpba.2010.12.029     Document Type: Article
Times cited : (69)

References (30)
  • 1
    • 0036468995 scopus 로고    scopus 로고
    • Kinetic studies of protein-protein interactions
    • Schreiber G. Kinetic studies of protein-protein interactions. Curr. Opin. Struct. Biol. 2002, 12:41-47.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 41-47
    • Schreiber, G.1
  • 2
    • 34548394483 scopus 로고    scopus 로고
    • Human protein-protein interaction networks and the value for drug discovery
    • Ruffner H., Bauer A., Bouwmeester T. Human protein-protein interaction networks and the value for drug discovery. Drug Discov. Today 2007, 12:709-716.
    • (2007) Drug Discov. Today , vol.12 , pp. 709-716
    • Ruffner, H.1    Bauer, A.2    Bouwmeester, T.3
  • 5
    • 33748041958 scopus 로고    scopus 로고
    • Effects of protein aggregates: an immunologic perspective
    • Rosenberg A.S. Effects of protein aggregates: an immunologic perspective. AAPS J. 2006, 8:E501-E507.
    • (2006) AAPS J. , vol.8
    • Rosenberg, A.S.1
  • 6
    • 26844498710 scopus 로고    scopus 로고
    • Sequence determinants of protein aggregation: tools to increase protein solubility
    • Ventura S. Sequence determinants of protein aggregation: tools to increase protein solubility. Microb. Cell Factories 2005, 4:1-8.
    • (2005) Microb. Cell Factories , vol.4 , pp. 1-8
    • Ventura, S.1
  • 7
    • 0034647092 scopus 로고    scopus 로고
    • Interactions of proteins in aqueous electrolyte solutions from fluorescence anisotropy and circular-dichroism measurements
    • Anderson C.O., Niesen J.F.M., Blanch H.W., Prausnitz J.M. Interactions of proteins in aqueous electrolyte solutions from fluorescence anisotropy and circular-dichroism measurements. Biophys. Chem. 2000, 84:177-188.
    • (2000) Biophys. Chem. , vol.84 , pp. 177-188
    • Anderson, C.O.1    Niesen, J.F.M.2    Blanch, H.W.3    Prausnitz, J.M.4
  • 8
    • 61649105725 scopus 로고    scopus 로고
    • Molecular interaction between apo or holo α-lactalbumin and lysosyme: formation of heterodimers as assessed by fluorescence measurements
    • Nigen M., Tilly V.L., Croguennec T., Drouin-Kucma D., Bouhallab S. Molecular interaction between apo or holo α-lactalbumin and lysosyme: formation of heterodimers as assessed by fluorescence measurements. Biochim. Biophys. Acta 2009, 1794:709-715.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 709-715
    • Nigen, M.1    Tilly, V.L.2    Croguennec, T.3    Drouin-Kucma, D.4    Bouhallab, S.5
  • 10
    • 0017352615 scopus 로고
    • Thermodynamic studies on subunit assembly in human hemoglobin. Temperature dependence of the dimer-tetramer association constants for oxygenated and unliganded hemoglobins
    • Ip S.H.C., Ackers G. Thermodynamic studies on subunit assembly in human hemoglobin. Temperature dependence of the dimer-tetramer association constants for oxygenated and unliganded hemoglobins. J. Biol. Chem. 1977, 252:82-87.
    • (1977) J. Biol. Chem. , vol.252 , pp. 82-87
    • Ip, S.H.C.1    Ackers, G.2
  • 11
    • 0036164684 scopus 로고    scopus 로고
    • Estimation of drug-protein binding parameters on assuming the validity of thermodynamic equilibrium
    • Soltes L., Mach M. Estimation of drug-protein binding parameters on assuming the validity of thermodynamic equilibrium. J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. 2002, 768:113-119.
    • (2002) J. Chromatogr. B: Anal. Technol. Biomed. Life Sci. , vol.768 , pp. 113-119
    • Soltes, L.1    Mach, M.2
  • 13
    • 78650945088 scopus 로고    scopus 로고
    • Comparison of binding interaction of lomefloxacin to serum albumin and serum transferrin by resonance Rayleigh scattering and fluorescence quenching methods
    • Vahedian-Movahed H., Saberi M.R., Chamani J. Comparison of binding interaction of lomefloxacin to serum albumin and serum transferrin by resonance Rayleigh scattering and fluorescence quenching methods. J. Biomol. Struct. Dyn. 2011, 28:483-502.
    • (2011) J. Biomol. Struct. Dyn. , vol.28 , pp. 483-502
    • Vahedian-Movahed, H.1    Saberi, M.R.2    Chamani, J.3
  • 15
    • 13544254423 scopus 로고    scopus 로고
    • Transferrin: structure, function and potential therapeutic actions
    • Gomme P.T., McCann K.B. Transferrin: structure, function and potential therapeutic actions. Drug Discov. Today 2005, 10:267-273.
    • (2005) Drug Discov. Today , vol.10 , pp. 267-273
    • Gomme, P.T.1    McCann, K.B.2
  • 16
    • 0346995454 scopus 로고    scopus 로고
    • Bilirubin toxicity in developing nervous system
    • Shapiro S.M. Bilirubin toxicity in developing nervous system. Pediatr. Neurol. 2003, 29:410-421.
    • (2003) Pediatr. Neurol. , vol.29 , pp. 410-421
    • Shapiro, S.M.1
  • 19
    • 40849121069 scopus 로고    scopus 로고
    • Resonance energy transfer and ligand binding studies on pH-induced folded states of human serum albumin
    • Kumar Shaw A., Kumar Pal S. Resonance energy transfer and ligand binding studies on pH-induced folded states of human serum albumin. J. Photochem. Photobiol. B 2008, 90:187-197.
    • (2008) J. Photochem. Photobiol. B , vol.90 , pp. 187-197
    • Kumar Shaw, A.1    Kumar Pal, S.2
  • 20
    • 0034193510 scopus 로고    scopus 로고
    • Protein docking using spherical polar Fourier correlations
    • Ritchie D.W., Kemp G.J.L. protein docking using spherical polar Fourier correlations. Proteins 2000, 39:178-194.
    • (2000) Proteins , vol.39 , pp. 178-194
    • Ritchie, D.W.1    Kemp, G.J.L.2
  • 22
    • 0037016375 scopus 로고    scopus 로고
    • Second derivative fluorescence spectroscopy of tryptophan in proteins
    • Mazo-Villarias A. Second derivative fluorescence spectroscopy of tryptophan in proteins. J. Biochem. Biophys. Methods 2002, 50:163-178.
    • (2002) J. Biochem. Biophys. Methods , vol.50 , pp. 163-178
    • Mazo-Villarias, A.1
  • 23
    • 16244362365 scopus 로고    scopus 로고
    • Second derivative tryptophan fluorescence spectroscopy as a tool to characterize partially unfolded intermediate of proteins
    • Kumar V., Sharma V.K., Kalonia D.S. Second derivative tryptophan fluorescence spectroscopy as a tool to characterize partially unfolded intermediate of proteins. Int. J. Pharm. 2005, 294:193-199.
    • (2005) Int. J. Pharm. , vol.294 , pp. 193-199
    • Kumar, V.1    Sharma, V.K.2    Kalonia, D.S.3
  • 24
    • 0002593607 scopus 로고
    • Synchronized excitation of fluorescence emission spectra
    • Lloyd J.B.F. synchronized excitation of fluorescence emission spectra. Nature 1971, 231:64-65.
    • (1971) Nature , vol.231 , pp. 64-65
    • Lloyd, J.B.F.1
  • 25
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer L. Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 1978, 47:819-846.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 26
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: forces contributing to stability
    • Ross P.D., Subramanian S. Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 1981, 20:3096-3102.
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 27
    • 0013800421 scopus 로고
    • The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: a fluorescent probe of non-polar binding sites
    • Stryer L. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin: a fluorescent probe of non-polar binding sites. J. Mol. Biol. 1965, 13:482-495.
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 28
    • 0002051528 scopus 로고
    • Depolarized Rayleigh light scattering in absorption bands measured in lycopene solution
    • Anglister J., Steinberg I.Z. Depolarized Rayleigh light scattering in absorption bands measured in lycopene solution. Chem. Phys. Lett. 1979, 65:50-54.
    • (1979) Chem. Phys. Lett. , vol.65 , pp. 50-54
    • Anglister, J.1    Steinberg, I.Z.2
  • 30
    • 12344324721 scopus 로고    scopus 로고
    • Thermodynamics of the interaction of xanthine oxidase with superoxide dismutase studied by isothermal titration calorimetry and fluorescence spectroscopy
    • Zhuo Y.L., Liao J.M., Du F., Liang Y. Thermodynamics of the interaction of xanthine oxidase with superoxide dismutase studied by isothermal titration calorimetry and fluorescence spectroscopy. Thermochim. Acta 2005, 426:173-178.
    • (2005) Thermochim. Acta , vol.426 , pp. 173-178
    • Zhuo, Y.L.1    Liao, J.M.2    Du, F.3    Liang, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.