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Volumn , Issue , 2008, Pages 1-255

Principles and Applications of Fluorescence Spectroscopy

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EID: 84889389215     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470692059     Document Type: Book
Times cited : (137)

References (141)
  • 1
    • 0022369577 scopus 로고
    • Fluorescence studies on the interaction between two cytochromes extracted from the yeast Hansenula anomala
    • Albani, J. (1985). Fluorescence studies on the interaction between two cytochromes extracted from the yeast Hansenula anomala. Archives of Biochemistry and Biophysics, 243, 292-297.
    • (1985) Archives of Biochemistry and Biophysics , vol.243 , pp. 292-297
    • Albani, J.1
  • 2
    • 0001279898 scopus 로고    scopus 로고
    • Asymmetric sulfoxidation catalyzed by a vanadium-containing bromoperoxidase
    • Andersson, M., Willets, A. and Allenmark, S. (1997). Asymmetric sulfoxidation catalyzed by a vanadium-containing bromoperoxidase. Journal of Organic Chemistry, 62, 8455-8458.
    • (1997) Journal of Organic Chemistry , vol.62 , pp. 8455-8458
    • Andersson, M.1    Willets, A.2    Allenmark, S.3
  • 3
    • 4544339576 scopus 로고    scopus 로고
    • First principle calculations for the active centres in vanadium-containing chloroperoxidase and its functional models: geometrical and spectral properties
    • Borowski, T., Szczepanik,W., Chruszcz, M. and Broclawik, E. (2004). First principle calculations for the active centres in vanadium-containing chloroperoxidase and its functional models: geometrical and spectral properties. International Journal of Quantum Chemistry, 99, 864-875.
    • (2004) International Journal of Quantum Chemistry , vol.99 , pp. 864-875
    • Borowski, T.1    Szczepanik, W.2    Chruszcz, M.3    Broclawik, E.4
  • 4
    • 33646927894 scopus 로고    scopus 로고
    • Laboratoryevolved vanadium chloroperoxidase exhibits 100-fold higher halogenating activity at alkaline pH Catalyic effect from first and second coordination sphere mutations
    • Hasan, Z., Renirie, R., Kerkman, R., Ruijssenaars, H.J.,Hartog, A.F. andWever, R. (2006). Laboratoryevolved vanadium chloroperoxidase exhibits 100-fold higher halogenating activity at alkaline pH. Catalyic effect from first and second coordination sphere mutations. Journal of Biological Chemistry, 281, 9738-9744.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 9738-9744
    • Hasan, Z.1    Renirie, R.2    Kerkman, R.3    Ruijssenaars, H.J.4    Hartog, A.F.5    Wever, R.6
  • 5
    • 0033588375 scopus 로고    scopus 로고
    • Heterologous expression of the vanadium-containing chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and site-directed mutagenesis of the active site residues His496, Lys353, Arg360, Arg490
    • Hemrika,W., Renirie, R.,Macedo-Ribeiro, S.,Messerschmidt, A. andWever, R. (1999). Heterologous expression of the vanadium-containing chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and site-directed mutagenesis of the active site residues His496, Lys353, Arg360, Arg490. Journal of Biological Chemistry, 274, 23820-23827.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 23820-23827
    • Hemrika, W.1    Renirie, R.2    Macedo-Ribeiro, S.3    Messerschmidt, A.4    Wever, R.5
  • 6
    • 0032935211 scopus 로고    scopus 로고
    • X-ray crystal structure of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis
    • Macedo-Ribeiro, S., Hemrika,W., Renirie, R.,Wever, R. and Messerschmidt, A. (1999). X-ray crystal structure of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis. Journal of Biological Inorganic Chemistry, 4, 209-219.
    • (1999) Journal of Biological Inorganic Chemistry , vol.4 , pp. 209-219
    • Macedo-Ribeiro, S.1    Hemrika, W.2    Renirie, R.3    Wever, R.4    Messerschmidt, A.5
  • 7
    • 0030906620 scopus 로고    scopus 로고
    • Implications for the catalytic mechanism of the vanadium-containing enzyme chloroperoxidase from the fungus Curvularia inaequalis by X-ray structures of the native and peroxide form
    • Messerschmidt, A., Prade, L. and Wever, R. (1997). Implications for the catalytic mechanism of the vanadium-containing enzyme chloroperoxidase from the fungus Curvularia inaequalis by X-ray structures of the native and peroxide form. Journal of Biological Chemistry, 378, 309-315.
    • (1997) Journal of Biological Chemistry , vol.378 , pp. 309-315
    • Messerschmidt, A.1    Prade, L.2    Wever, R.3
  • 8
    • 0033118532 scopus 로고    scopus 로고
    • Phosphate and vanadate in biological systems: chemical relatives or more?
    • Plass, W. (1999). Phosphate and vanadate in biological systems: chemical relatives or more? Angewandte Chemie, 38, 909-912.
    • (1999) Angewandte Chemie , vol.38 , pp. 909-912
    • Plass, W.1
  • 10
    • 0034620587 scopus 로고    scopus 로고
    • Cofactor and substrate binding to vanadium chloroperoxidase determined by UV-VIS spectroscopy and evidence for high affinity for pervanadate
    • Renirie, R., Hemrika, W., Piersma, S. R. and Wever, R. (2000a). Cofactor and substrate binding to vanadium chloroperoxidase determined by UV-VIS spectroscopy and evidence for high affinity for pervanadate. Biochemistry, 39, 1133-1141.
    • (2000) Biochemistry , vol.39 , pp. 1133-1141
    • Renirie, R.1    Hemrika, W.2    Piersma, S.R.3    Wever, R.4
  • 11
    • 0034697301 scopus 로고    scopus 로고
    • Peroxidase and phosphatase activity of active-site mutants of vanadium chloroperoxidase fromthe fungus Curvularia inaequalis
    • Renirie, R., Hemrika, W. and Wever, R. (2000b). Peroxidase and phosphatase activity of active-site mutants of vanadium chloroperoxidase fromthe fungus Curvularia inaequalis. Journal of Biological Chemistry, 275, 11650-11657.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 11650-11657
    • Renirie, R.1    Hemrika, W.2    Wever, R.3
  • 12
    • 0033368448 scopus 로고    scopus 로고
    • Probing the scope of the sulfoxidation activity of vanadium bromoperoxidase from Ascophyllum nodosum
    • Ten Brink, H.B., Holland, H.L., Schoemaker, H.E., van Lingen, H. andWever, R. (1999). Probing the scope of the sulfoxidation activity of vanadium bromoperoxidase from Ascophyllum nodosum. Tetrahedron: Asymmetry, 10, 4563-4572.
    • (1999) Tetrahedron: Asymmetry , vol.10 , pp. 4563-4572
    • Brink, T.H.B.1    Holland, H.L.2    Schoemaker, H.E.3    Van Lingen, H.4    Wever, R.5
  • 13
    • 77956741418 scopus 로고
    • Ultraviolet absorption spectra of proteins and amino acids
    • Wetlaufer,D.B. (1962). Ultraviolet absorption spectra of proteins and amino acids. Advances in Protein Chemistry, 17, 303-390.
    • (1962) Advances in Protein Chemistry , vol.17 , pp. 303-390
    • Wetlaufer, D.B.1
  • 15
    • 0842265913 scopus 로고    scopus 로고
    • Tertiary structure of human α1-acid glycoprotein (orosomucoid). Straightforward fluorescence experiments revealing the presence of a binding pocket
    • Albani, J.R. (2004) Tertiary structure of human α1-acid glycoprotein (orosomucoid). Straightforward fluorescence experiments revealing the presence of a binding pocket. Carbohydrate Research 339, 607-612.
    • (2004) Carbohydrate Research , vol.339 , pp. 607-612
    • Albani, J.R.1
  • 16
    • 33748907733 scopus 로고    scopus 로고
    • Progesterone binding to the tryptophan residues of human α1-acid glycoprotein
    • Albani, J.R. (2006) Progesterone binding to the tryptophan residues of human α1-acid glycoprotein. Carbohydrate Research, 341, 2557-2564.
    • (2006) Carbohydrate Research , vol.341 , pp. 2557-2564
    • Albani, J.R.1
  • 17
    • 0032427349 scopus 로고    scopus 로고
    • Interaction between Calcofluor White and carbohydrates of α1-acid glycoprotein
    • 194-200
    • Albani, J.R. and Plancke, Y.D. (1998 and 1999) Interaction between Calcofluor White and carbohydrates of α1-acid glycoprotein. Carbohydrate Research 314, 169-175 and 318, 194-200.
    • (1998) Carbohydrate Research , vol.314 , pp. 169-175
    • Albani, J.R.1    Plancke, Y.D.2
  • 18
    • 0032755450 scopus 로고    scopus 로고
    • Dynamics of carbohydrate residues of α1-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra and emission anisotropy studies of CalcofluorWhite
    • Albani, J.R., Sillen, A., Coddeville, B., Plancke, Y.D. and Engelborghs, Y. (1999) Dynamics of carbohydrate residues of α1-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra and emission anisotropy studies of CalcofluorWhite. Carbohydrate Research 322, 87-94.
    • (1999) Carbohydrate Research , vol.322 , pp. 87-94
    • Albani, J.R.1    Sillen, A.2    Coddeville, B.3    Plancke, Y.D.4    Engelborghs, Y.5
  • 19
    • 0034710250 scopus 로고    scopus 로고
    • Interaction between carbohydrate residues of α1-acid glycoprotein (orosomucoid) and saturating concentrations of CalcofluorWhite
    • Albani, J.R., Sillen, A., Plancke, Y.D., Coddeville, B. and Engelborghs, Y. (2000) Interaction between carbohydrate residues of α1-acid glycoprotein (orosomucoid) and saturating concentrations of CalcofluorWhite. A fluorescence study. Carbohydrate Research 327, 333-340.
    • (2000) A fluorescence study. Carbohydrate Research , vol.327 , pp. 333-340
    • Albani, J.R.1    Sillen, A.2    Plancke, Y.D.3    Coddeville, B.4    Engelborghs, Y.5
  • 20
    • 49049145511 scopus 로고
    • Structural elucidation, using h.p.l.c.-m.s and g.l.c.-m.s., of the acidic polysaccharide secreted by Rhizobium meliloti strain 1021*1,*2
    • Åman, P.,McNeil, M., Franzén, L.-E., Darvill, A.G. and Albersheim, P. (1981) Structural elucidation, using h.p.l.c.-m.s. and g.l.c.-m.s., of the acidic polysaccharide secreted by Rhizobium meliloti strain 1021*1,*2. Carbohydrate Research 95, 263-282.
    • (1981) Carbohydrate Research , vol.95 , pp. 263-282
    • Åman, P.1    McNeil, M.2    Franzén, L.-E.3    Darvill, A.G.4    Albersheim, P.5
  • 22
    • 0029669985 scopus 로고    scopus 로고
    • Glycosylation of α1-acid glycoprotein in septic shock: changes in degree of branching and in expression of sialyl Lewis(x) groups
    • Brinkman-Van der Linden, E.C., van Ommen, E.C. and van Dijk,W. (1996) Glycosylation of α1-acid glycoprotein in septic shock: changes in degree of branching and in expression of sialyl Lewis(x) groups. Glycoconjugate Journal 13, 27-31.
    • (1996) Glycoconjugate Journal , vol.13 , pp. 27-31
    • Brinkman-Van Der Linden, E.C.1    Van Ommen, E.C.2    Van Dijk, W.3
  • 23
    • 0014410322 scopus 로고
    • Steroid-protein interactions. XVII. Influence of solvent environment on interaction between human α1-acid glycoprotein and progesterone
    • Canguly, M. and Westphal, U. (1968, Steroid-protein interactions. XVII. Influence of solvent environment on interaction between human α1-acid glycoprotein and progesterone. Journal of Biological Chemistry 243, 6130-6139.
    • (1968) Journal of Biological Chemistry , vol.243 , pp. 6130-6139
    • Canguly, M.1    Westphal, U.2
  • 24
    • 0017366051 scopus 로고
    • Interactions of α1-acid glycoprotein with the immune system. I. Purification and effects upon lymphocyte responsiveness
    • Chiu, K.M.,Mortensen, R.F.,Osmand,A.P. and Gewurz, H. (1977, Interactions of α1-acid glycoprotein with the immune system. I. Purification and effects upon lymphocyte responsiveness. Immunology 32, 997-1005.
    • (1977) Immunology , vol.32 , pp. 997-1005
    • Chiu, K.M.1    Mortensen, R.F.2    Osmand, A.P.3    Gewurz, H.4
  • 25
    • 0037014997 scopus 로고    scopus 로고
    • Interaction between carbohydrate residues of α1-acid glycoprotein (orosomucoid) and progesterone A fluorescence study
    • De Ceukeleire, M. and Albani, J.R. (2002) Interaction between carbohydrate residues of α1-acid glycoprotein (orosomucoid) and progesterone. A fluorescence study. Carbohydrate Research 337, 1405-1410.
    • (2002) Carbohydrate Research , vol.337 , pp. 1405-1410
    • Ceukeleire, D.M.1    Albani, J.R.2
  • 26
    • 0023390753 scopus 로고
    • Structure and expression of the genes coding for human α1-acid glycoprotein
    • Dente, L., Pizza, M.G., Metspalu, A. and Cortese, R. (1987) Structure and expression of the genes coding for human α1-acid glycoprotein. EMBO Journal 6, 2289-2296.
    • (1987) EMBO Journal , vol.6 , pp. 2289-2296
    • Dente, L.1    Pizza, M.G.2    Metspalu, A.3    Cortese, R.4
  • 27
    • 84889460975 scopus 로고    scopus 로고
    • Doctor Fungus website, Candida endophthalmitis., WWW document, accessed on 20 March
    • Doctor Fungus website, Candida endophthalmitis. [WWW document]. URL http://216.239.59.104/ search?q=cache:1n8Cng6jaK4J:www.doctorfungus.org/mycoses/human/candida/Endophthalmitis.htm + clinical + studies,+ Calcofluor + white&hl = fr [accessed on 20 March, 2006].
    • (2006)
  • 28
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C. and von Hippel, P.H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Analytical Biochemistry 182, 319-326. Erratum in: Analytical Biochememistry 1990, 189, 283.
    • (1989) Analytical Biochemistry , vol.182
    • Gill, S.C.1    Von Hippel, P.H.2
  • 29
    • 0033774769 scopus 로고    scopus 로고
    • Discrimination between viable and dead encephalitozoon cuniculi (microsporidian) spores by dual staining with Sytox Green and CalcofluorWhite M2R
    • Green, L.C., LeBlanc, P.J. and Didier, E.S. (2000) Discrimination between viable and dead encephalitozoon cuniculi (microsporidian) spores by dual staining with Sytox Green and CalcofluorWhite M2R. Journal of Clinical Microbiology 38, 3811-3814.
    • (2000) Journal of Clinical Microbiology , vol.38 , pp. 3811-3814
    • Green, L.C.1    LeBlanc, P.J.2    Didier, E.S.3
  • 30
    • 0020319277 scopus 로고
    • The binding of spin-labeled propranolol and spin labeled progesterone by orosomucoid
    • Kirley, T.L., Spargue, E.D. and Halsall, H.B. (1982) The binding of spin-labeled propranolol and spin labeled progesterone by orosomucoid. Biophysical Chemistry 15, 209-216.
    • (1982) Biophysical Chemistry , vol.15 , pp. 209-216
    • Kirley, T.L.1    Spargue, E.D.2    Halsall, H.B.3
  • 31
    • 0017263227 scopus 로고
    • Steroid-protein interactions XXXIV. Chemical modification of α1-acid glycoprotein for characterization of the progesterone binding site
    • Kute, T. and Westphal, U. (1976) Steroid-protein interactions. XXXIV. Chemical modification of α1-acid glycoprotein for characterization of the progesterone binding site. Biochimica et Biophysica Acta 420, 195-213.
    • (1976) Biochimica et Biophysica Acta , vol.420 , pp. 195-213
    • Kute, T.1    Westphal, U.2
  • 32
    • 0028981441 scopus 로고
    • Glycoforms of serum α1-acid glycoprotein as markers of inflammation and cancer
    • Mackiewicz, A. and Mackiewicz, K. (1995) Glycoforms of serum α1-acid glycoprotein as markers of inflammation and cancer. Glycoconjugate Journal 12, 241-247.
    • (1995) Glycoconjugate Journal , vol.12 , pp. 241-247
    • Mackiewicz, A.1    Mackiewicz, K.2
  • 33
    • 0014120299 scopus 로고
    • Specificity of binding of hexopyranosyl polysaccharides with fluorescent brightener
    • Maeda, H. and Ishida, N. (1967) Specificity of binding of hexopyranosyl polysaccharides with fluorescent brightener. Journal of Biochemistry 62, 276-278.
    • (1967) Journal of Biochemistry , vol.62 , pp. 276-278
    • Maeda, H.1    Ishida, N.2
  • 34
    • 17444437477 scopus 로고
    • The Physical Chemistry of Dye Absorption
    • Academic Press, New York.
    • Rattee, I.D. and Greur, M.M. (1974) The Physical Chemistry of Dye Absorption. Academic Press, New York.
    • (1974)
    • Rattee, I.D.1    Greur, M.M.2
  • 36
    • 0015694574 scopus 로고
    • Structure of α1-acid glycoprotein The complete amino acid sequence,multiple amino acid substitutions and homologywith theimmunoglobulins
    • Schmid, K., Kaufmann, H., Isemura, S. et al. (1973) Structure of α1-acid glycoprotein. The complete amino acid sequence,multiple amino acid substitutions and homologywith theimmunoglobulins. Biochemistry 12, 2711-2724.
    • (1973) Biochemistry , vol.12 , pp. 2711-2724
    • Schmid, K.1    Kaufmann, H.2    Isemura, S.3
  • 38
    • 0028981439 scopus 로고
    • α1-acid glycoprotein (orosomucoid): pathophysiological changes in glycosylation in relation to its function
    • Van Dijk, W., Havenaar, E.C. and Brinkman-Van der Linden, E.C. (1995) α1-acid glycoprotein (orosomucoid): pathophysiological changes in glycosylation in relation to its function. Glycoconjugate Journal 12, 227-233.
    • (1995) Glycoconjugate Journal , vol.12 , pp. 227-233
    • Dijk, V.W.1    Havenaar, E.C.2    Brinkman-Van Der Linden, E.C.3
  • 39
    • 0032574722 scopus 로고    scopus 로고
    • The Rhizobium meliloti ExoK and ExsH glycanases specifically depolymerize nascent succinoglycan chains
    • York, G.M. and Walker, G.C. (1998) The Rhizobium meliloti ExoK and ExsH glycanases specifically depolymerize nascent succinoglycan chains. Proceedings of the National Academy of Sciences USA 95, 4912-4917.
    • (1998) Proceedings of the National Academy of Sciences USA , vol.95 , pp. 4912-4917
    • York, G.M.1    Walker, G.C.2
  • 40
    • 38549112269 scopus 로고
    • Red CellMetabolism,AManual of BiochemicalMethods
    • Grune&Stratton New York.
    • Beutler, E. (1971) Red CellMetabolism,AManual of BiochemicalMethods, pp. 56-68.Grune&Stratton New York.
    • (1971) , pp. 56-68
    • Beutler, E.1
  • 41
    • 0001430940 scopus 로고
    • Adenylate kinase (myokinase): UV-method
    • In: H.U. Bergmeyer (ed.), (3rd edn), Verlag Chemie,Weinheim, Federal Republic of Germany.
    • Brolin, S.E. (1983) Adenylate kinase (myokinase): UV-method. In: H.U. Bergmeyer (ed.),Methods of Enzymatic Analysis (3rd edn), Vol. 3, pp. 540-545. Verlag Chemie,Weinheim, Federal Republic of Germany.
    • (1983) Methods of Enzymatic Analysis , vol.3 , pp. 540-545
    • Brolin, S.E.1
  • 42
    • 0001206338 scopus 로고
    • Pyruvate
    • In: H.U. Bergmeyer (ed.), 3rd edn, Verlag Chemie,Weinheim.
    • Lamprecht,W. andHeinz, F. (1984) Pyruvate. In: H.U. Bergmeyer (ed.),Methods of Enzymatic Analysis (3rd edn),Vol. 6, pp. 555-561. Verlag Chemie,Weinheim.
    • (1984) Methods of Enzymatic Analysis , vol.6 , pp. 555-561
    • Lamprecht, W.1    Heinz, F.2
  • 43
    • 0001486532 scopus 로고
    • L(+)-lactate
    • In: H.U. Bergmeyer (ed.), 3rd edn, Verlag Chemie,Weinheim.
    • Noll, F. (1984) L(+)-lactate. In: H.U. Bergmeyer (ed.),Methods of Enzymatic Analysis (3rd edn),Vol. 6, pp. 582-528. Verlag Chemie,Weinheim.
    • (1984) Methods of Enzymatic Analysis , vol.6 , pp. 582-528
    • Noll, F.1
  • 44
    • 0039523549 scopus 로고
    • Adenosinetriphosphatases
    • In: H.U. Bergmeyer (ed.), 3rd edn, Verlag Chemie,Weinham.
    • Penefsky, H.S. and Bruist, M.F. (1984) Adenosinetriphosphatases. In: H.U. Bergmeyer (ed.),Methods of Enzymatic Analysis (3rd edn),Vol. 4, pp. 324-328. Verlag Chemie,Weinham.
    • (1984) Methods of Enzymatic Analysis , vol.4 , pp. 324-328
    • Penefsky, H.S.1    Bruist, M.F.2
  • 45
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 46
    • 0027351945 scopus 로고
    • Structural models of primary cell walls in flowering plants:consistency of molecular structure with the physical properties of the walls during growth
    • Carpita, N.C. and Gibeaut, D.M. (1993). Structural models of primary cell walls in flowering plants:consistency of molecular structure with the physical properties of the walls during growth. Plant Journal, 3, 1-30.
    • (1993) Plant Journal , vol.3 , pp. 1-30
    • Carpita, N.C.1    Gibeaut, D.M.2
  • 47
    • 0141558968 scopus 로고    scopus 로고
    • Kinetic studies on endo-beta-galactosidase by a novel colorimetric assay and synthesis of N-acetyllactosaminerepeating oligosaccharide beta-glycosides using its transglycosylation activity
    • Murata, T., Hattori, T., Amarume, S., Koichi, A. and Usui, T. (2003). Kinetic studies on endo-beta-galactosidase by a novel colorimetric assay and synthesis of N-acetyllactosaminerepeating oligosaccharide beta-glycosides using its transglycosylation activity. European Journal of Biochemistry, 270, 3709-3719.
    • (2003) European Journal of Biochemistry , vol.270 , pp. 3709-3719
    • Murata, T.1    Hattori, T.2    Amarume, S.3    Koichi, A.4    Usui, T.5
  • 49
    • 0000297592 scopus 로고
    • Molecular size and separability features of pea cell wall polysaccharides: implications for models of primary structure
    • Talbott, L.D. and Ray, P.M. (1992). Molecular size and separability features of pea cell wall polysaccharides: implications for models of primary structure. Plant Physiology, 98, 357-368. http://www.mpbio.com/product_info.php?cPath=491_1_12&products_id=150039&depth=nested& keywords=beta%20galactosidase Bailey, J.E. and Ollis, D.F. (1986). Biochemical Engineering Fundamentals (2nd edn), Chapter 3, McGraw-Hill, New York.
    • (1986) Plant Physiology , vol.98 , pp. 357-368
    • Talbott, L.D.1    Ray, P.M.2
  • 50
    • 0005238601 scopus 로고
    • A standardizedWohlgemuth procedure for alphaamylase activity
    • Sandstedt, R.M., Kneen, E. and Blish, M.J. (1939). A standardizedWohlgemuth procedure for alphaamylase activity. Cereal Chemistry 16, 712-723.
    • (1939) Cereal Chemistry , vol.16 , pp. 712-723
    • Sandstedt, R.M.1    Kneen, E.2    Blish, M.J.3
  • 52
    • 33745444045 scopus 로고    scopus 로고
    • Structure and Dynamics of Macromolecules: Absorption and Fluorescence Studies
    • Elsevier, Amsterdam.
    • Albani, J.R. (2004). Structure and Dynamics of Macromolecules: Absorption and Fluorescence Studies, Elsevier, Amsterdam.
    • (2004)
    • Albani, J.R.1
  • 53
    • 34547336610 scopus 로고    scopus 로고
    • New insights in the interpretation of tryptophan fluorescence
    • J. of fluorescence, in press.
    • Albani, J.R. (2007). New insights in the interpretation of tryptophan fluorescence. Origin of the fluorescence lifetime and characterization of a new fluorescence parameter in proteins: the emission to excitation ratio. J. of fluorescence, in press.
    • (2007)
    • Albani, J.R.1
  • 54
    • 0018407386 scopus 로고
    • Time-resolved fluorescence measurements
    • Badea,M.G. and Brand, L. (1979). Time-resolved fluorescence measurements.Methods in Enzymology, 61, 378-425.
    • (1979) Methods in Enzymology , vol.61 , pp. 378-425
    • Badea, M.G.1    Brand, L.2
  • 56
    • 0345328130 scopus 로고    scopus 로고
    • Photophysical studies on binding of curcumin to bovine serum albumin
    • Barik, A., Priyadarsini, K.I. and Mohan, H. (2003). Photophysical studies on binding of curcumin to bovine serum albumin. Photochemistry and Photobiology, 77, 597-603.
    • (2003) Photochemistry and Photobiology , vol.77 , pp. 597-603
    • Barik, A.1    Priyadarsini, K.I.2    Mohan, H.3
  • 57
    • 0001420666 scopus 로고
    • Instrument to measure fluorescence lifetimes in the millimicrosecond region
    • Bennett, R.G. (1960). Instrument to measure fluorescence lifetimes in the millimicrosecond region. Review of Scientific Instruments, 31, 1275-1279.
    • (1960) Review of Scientific Instruments , vol.31 , pp. 1275-1279
    • Bennett, R.G.1
  • 58
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • Burstein, E.A.,Vedenkina, N.S. and Ivkova,M.N. (1973). Fluorescence and the location of tryptophan residues in protein molecules. Photochemistry and Photobiology, 18, 263-279.
    • (1973) Photochemistry and Photobiology , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkova, M.N.3
  • 59
    • 0003970345 scopus 로고
    • Biophysical Chemistry
    • W.H. Freeman, New York.
    • Cantor, R.C. and Schimmel, P.R. (1980). Biophysical Chemistry,W.H. Freeman, New York.
    • (1980)
    • Cantor, R.C.1    Schimmel, P.R.2
  • 61
    • 0021473933 scopus 로고
    • Tyrosine modification of glucose dehydrogenase from Bacillus megaterium Effect of tetranitromethane on the enzyme in the tetrameric and monomeric state
    • Froschle, M., Ulmer,W. and Jany, K.D. (1984). Tyrosine modification of glucose dehydrogenase from Bacillus megaterium. Effect of tetranitromethane on the enzyme in the tetrameric and monomeric state. European Journal of Biochemistry, 142, 533-540.
    • (1984) European Journal of Biochemistry , vol.142 , pp. 533-540
    • Froschle, M.1    Ulmer, W.2    Jany, K.D.3
  • 62
    • 84889493160 scopus 로고    scopus 로고
    • Handbook,Molecular Probes. 10th edn.
    • Handbook,Molecular Probes. 10th edn. (2005). http://probes.invitrogen.com/
    • (2005)
  • 63
    • 0002994534 scopus 로고
    • Über den Mechanismus des Photolumineszenz von Farbstoffphosphoren
    • Jablonski, A. (1935). Über den Mechanismus des Photolumineszenz von Farbstoffphosphoren. Zeitschrift fur Physik, 94, 38-64.
    • (1935) Zeitschrift fur Physik , vol.94 , pp. 38-64
    • Jablonski, A.1
  • 64
    • 36449000480 scopus 로고
    • Stroboscopic optical boxcar technique for the determination of fluorescence lifetimes
    • James, D.R., Siemiarczuk, A. and Ware, W.R. (1992). Stroboscopic optical boxcar technique for the determination of fluorescence lifetimes. Review of Scientific Instruments, 63, 1710-1716.
    • (1992) Review of Scientific Instruments , vol.63 , pp. 1710-1716
    • James, D.R.1    Siemiarczuk, A.2    Ware, W.R.3
  • 65
    • 0004040064 scopus 로고    scopus 로고
    • Principles of Fluorescence Spectroscopy
    • 2nd edn), Plenum, New York.
    • Lakowicz, J.R. (1999). Principles of Fluorescence Spectroscopy (2nd edn), Plenum, New York.
    • (1999)
    • Lakowicz, J.R.1
  • 67
    • 0035969959 scopus 로고    scopus 로고
    • Probing structure and dynamics of DNA with 2-aminopurine: effects of local environment on fluorescence
    • Rachofsky, E.L., Osman, R. and Ross, J.B. (2001). Probing structure and dynamics of DNA with 2-aminopurine: effects of local environment on fluorescence. Biochemistry, 40, 946-956.
    • (2001) Biochemistry , vol.40 , pp. 946-956
    • Rachofsky, E.L.1    Osman, R.2    Ross, J.B.3
  • 68
    • 0000329591 scopus 로고
    • Tetranitromethane A reagent for the nitration of tyrosine and tyrosyl residues of proteins
    • Riordan, J.F.,Wacker,W.E.C. and Vallee, B.L. (1966). Tetranitromethane. A reagent for the nitration of tyrosine and tyrosyl residues of proteins. Journal of The American Chemical Society, 88, 4104-4105.
    • (1966) Journal of The American Chemical Society , vol.88 , pp. 4104-4105
    • Riordan, J.F.1    Wacker, W.E.C.2    Vallee, B.L.3
  • 70
    • 0013514978 scopus 로고
    • Fluorescence lifetimes: theory, instrumentation and application of nanosecond fluorometry
    • Ph.D. thesis, University of Illinois at Urbana Champaign. Published by University Microfilms International.
    • Spencer, R.D. (1970). Fluorescence lifetimes: theory, instrumentation and application of nanosecond fluorometry. Ph.D. thesis, University of Illinois at Urbana Champaign. Published by University Microfilms International.
    • (1970)
    • Spencer, R.D.1
  • 71
    • 0003475878 scopus 로고    scopus 로고
    • Molecular Fluorescence: Principles and Applications
    • Wiley-VCH,Weinheim.
    • Valeur, B. (2002). Molecular Fluorescence: Principles and Applications,Wiley-VCH,Weinheim.
    • (2002)
    • Valeur, B.1
  • 73
    • 34547336610 scopus 로고    scopus 로고
    • New insights in the interpretation of tryptophan fluorescence. Origin of the fluorescence lifetime and characterization of a new fluorescence parameter in proteins: the emission to excitation ratio
    • J. of fluorescence, in press.
    • Albani, J.R. (2007). New insights in the interpretation of tryptophan fluorescence. Origin of the fluorescence lifetime and characterization of a new fluorescence parameter in proteins: the emission to excitation ratio. J. of fluorescence, in press.
    • (2007)
    • Albani, J.R.1
  • 74
    • 0029850169 scopus 로고    scopus 로고
    • Log-normal description of fluorescence spectra of organic fluorophores
    • Burstein, E.A. and Emelyanenko, V.L. (1996). Log-normal description of fluorescence spectra of organic fluorophores. Photochemistry and Photobiology, 64, 316-320.
    • (1996) Photochemistry and Photobiology , vol.64 , pp. 316-320
    • Burstein, E.A.1    Emelyanenko, V.L.2
  • 75
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • Burstein, E.A.,Vedenkina, N.S. and Ivkova, M.N. (1973). Fluorescence and the location of tryptophan residues in protein molecules. Photochemistry and Photobiology, 18, 263-279.
    • (1973) Photochemistry and Photobiology , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkova, M.N.3
  • 76
    • 0014402266 scopus 로고
    • Fluorescence and protein structure: XV Tryptophan fluorescence in a helical muscle protein
    • Cogwill, R.W. (1968). Fluorescence and protein structure: XV. Tryptophan fluorescence in a helical muscle protein. Biochimica et Biophysica Acta, 168, 432-438.
    • (1968) Biochimica et Biophysica Acta , vol.168 , pp. 432-438
    • Cogwill, R.W.1
  • 77
    • 0036586018 scopus 로고    scopus 로고
    • Examination of the molecular structure of food products using front-face fluorescence spectroscopy
    • Dufour, E. (2002). Examination of the molecular structure of food products using front-face fluorescence spectroscopy. American Laboratory, 34, 51-55.
    • (2002) American Laboratory , vol.34 , pp. 51-55
    • Dufour, E.1
  • 78
    • 84889459438 scopus 로고
    • The variation of the extinction coefficient of vitamin A with solvent
    • Gillam, A.E. and El Ridi, M.S. (1938). The variation of the extinction coefficient of vitamin A with solvent. The Biochemical Journal, 32, 820-825.
    • (1938) The Biochemical Journal , vol.32 , pp. 820-825
    • Gillam, A.E.1    Ridi, E.M.S.2
  • 79
    • 0017104628 scopus 로고
    • Fluroescence of proteins in 6-M guanidine hydrochloride A method for the quantitative determination of tryptophan
    • Pajot, P. (1976). Fluroescence of proteins in 6-M guanidine hydrochloride. A method for the quantitative determination of tryptophan. European Journal of Biochemistry, 63, 263-269.
    • (1976) European Journal of Biochemistry , vol.63 , pp. 263-269
    • Pajot, P.1
  • 80
    • 0014027356 scopus 로고
    • Proteins in 6 M Guanidine Hydrochloride Demonstration of random behaviour
    • Tanford, C., Kawahara, K. and Lapanje, S. (1966). Proteins in 6 M Guanidine Hydrochloride. Demonstration of random behaviour. Journal of Biological Chemistry, 241, 1921-1923.
    • (1966) Journal of Biological Chemistry , vol.241 , pp. 1921-1923
    • Tanford, C.1    Kawahara, K.2    Lapanje, S.3
  • 81
    • 0000697562 scopus 로고
    • Proteins as random coils I. Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride
    • Tanford, C., Kawahara, K. and Lapanje, S. (1967). Proteins as random coils. I. Intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride. Journal of the American Chemical Society, 89, 729-736.
    • (1967) Journal of the American Chemical Society , vol.89 , pp. 729-736
    • Tanford, C.1    Kawahara, K.2    Lapanje, S.3
  • 82
    • 0001516275 scopus 로고
    • The ultraviolet fluorescence of proteins in neutral solution
    • Teale, F.W.J. (1960). The ultraviolet fluorescence of proteins in neutral solution. The Biochemical Journal, 76, 381-388.
    • (1960) The Biochemical Journal , vol.76 , pp. 381-388
    • Teale, F.W.J.1
  • 83
    • 0023128930 scopus 로고
    • Fluctuation domains in myoglobin Fluorescence quenching studies
    • Albani, J. and Alpert, B. (1987). Fluctuation domains in myoglobin. Fluorescence quenching studies. European Journal of Biochemistry, 162, 175-178.
    • (1987) European Journal of Biochemistry , vol.162 , pp. 175-178
    • Albani, J.1    Alpert, B.2
  • 84
    • 0029328569 scopus 로고
    • Interaction between human α1-acid glycoprotein (orosomucoid) and 2-p-toluidinylnaphthalene-6-sulfonate
    • Albani, J., Vos, R., Willaert, K. and Engelborghs, Y. (1995). Interaction between human α1-acid glycoprotein (orosomucoid) and 2-p-toluidinylnaphthalene-6-sulfonate. Photochemistry and Photobiology, 62, 30-34.
    • (1995) Photochemistry and Photobiology , vol.62 , pp. 30-34
    • Albani, J.1    Vos, R.2    Willaert, K.3    Engelborghs, Y.4
  • 85
    • 0000476880 scopus 로고    scopus 로고
    • Dynamics of Lens culinaris agglutinin studied by red-edge excitation spectra and anisotropy measurements of 2-p-toluidinylnaphthalene-6-sulfonate (TNS) and of tryptophan residues
    • Albani, J.R. (1996). Dynamics of Lens culinaris agglutinin studied by red-edge excitation spectra and anisotropy measurements of 2-p-toluidinylnaphthalene-6-sulfonate (TNS) and of tryptophan residues. Journal of Fluorescence, 6, 199-208.
    • (1996) Journal of Fluorescence , vol.6 , pp. 199-208
    • Albani, J.R.1
  • 86
    • 39049180959 scopus 로고    scopus 로고
    • Effect of the secondary structure of carbohydrate residues of α1-acid glycoprotein (orosomucoid) on the local dynamics of Trp residues
    • Albani, J.R. (2004). Effect of the secondary structure of carbohydrate residues of α1-acid glycoprotein (orosomucoid) on the local dynamics of Trp residues. Chemistry and Biodiversity, 1, 152-160.
    • (2004) Chemistry and Biodiversity , vol.1 , pp. 152-160
    • Albani, J.R.1
  • 88
    • 0032532547 scopus 로고    scopus 로고
    • Resolution of the heterogeneous fluorescence in multi-tryptophan proteins: ascorbate oxidase
    • Di Venere, A., Mei, G., Gilardi, G. et al. (1998). Resolution of the heterogeneous fluorescence in multi-tryptophan proteins: ascorbate oxidase. European Journal of Biochemistry, 257, 337-343.
    • (1998) European Journal of Biochemistry , vol.257 , pp. 337-343
    • Venere, D.A.1    Mei, G.2    Gilardi, G.3
  • 89
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies
    • Eftink, M.R. and Ghiron, C.A. (1976). Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies. Biochemistry, 15, 672-680
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 90
    • 0033841882 scopus 로고    scopus 로고
    • Development in aquatic humic chemistry
    • Frimmel, H.F. (2000). Development in aquatic humic chemistry. Agronomie, 20,451-463.
    • (2000) Agronomie , vol.20 , pp. 451-463
    • Frimmel, H.F.1
  • 91
    • 84889350187 scopus 로고    scopus 로고
    • Biodisponibilité des hydrocarbures polycycliques dans les écosystèmes aquatiques:influence de la matière organique naturelle et anthropique
    • Thèse de doctorat à l'Ecole Nationale du Génie Rural, des Eaux et Forêts Centre de Paris.
    • Gourlay, C. (2004). Biodisponibilité des hydrocarbures polycycliques dans les écosystèmes aquatiques:influence de la matière organique naturelle et anthropique. Thèse de doctorat à l'Ecole Nationale du Génie Rural, des Eaux et Forêts Centre de Paris.
    • (2004)
    • Gourlay, C.1
  • 92
    • 0022584692 scopus 로고
    • Quenching by acrylamide and temperature of a fluorescent probe attached to the active site of ribonuclease
    • Jullien, M.,Garel, J-R.,Merola,F. and Brochon J.-C. (1986). Quenching by acrylamide and temperature of a fluorescent probe attached to the active site of ribonuclease. European Biophysical Journal, 13, 131-137.
    • (1986) European Biophysical Journal , vol.13 , pp. 131-137
    • Jullien, M.1    Garel, J.-R.2    Merola, F.3    Brochon, J.-C.4
  • 93
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
    • Lehrer, S.S. (1971). Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry, 10, 3254-3263
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 94
    • 0033216705 scopus 로고    scopus 로고
    • Relationships between structure and binding affinity of humic substances for polycyclic aromatic hydrocarbons: relevance of molecular descriptors
    • Perminova, I., Grechishcheva, N. and Petrosyan, V. (1999). Relationships between structure and binding affinity of humic substances for polycyclic aromatic hydrocarbons: relevance of molecular descriptors. Environmental Science and Technology, 33, 3781-3787.
    • (1999) Environmental Science and Technology , vol.33 , pp. 3781-3787
    • Perminova, I.1    Grechishcheva, N.2    Petrosyan, V.3
  • 95
    • 0023646685 scopus 로고
    • Ligand binding and protein dynamics:a fluorescence depolarization study of aspartate transcarbamylase from Escherichia coli
    • Royer, C.A., Tauc, P., Hervé, G. and Brochon, J.-C. (1987). Ligand binding and protein dynamics:a fluorescence depolarization study of aspartate transcarbamylase from Escherichia coli. Biochemistry, 26, 6472-6478.
    • (1987) Biochemistry , vol.26 , pp. 6472-6478
    • Royer, C.A.1    Tauc, P.2    Hervé, G.3    Brochon, J.-C.4
  • 96
    • 0242417052 scopus 로고    scopus 로고
    • Spectroscopic studies of the interaction of bichromophoric cyanine dyes with DNA Effect of ionic strength
    • Schaberle, F.A., Kuz'min, V.A. and Borissevitch, I.E. (2003). Spectroscopic studies of the interaction of bichromophoric cyanine dyes with DNA. Effect of ionic strength. Biochimica Biophysica Acta, 1621, 183-191.
    • (2003) Biochimica Biophysica Acta , vol.1621 , pp. 183-191
    • Schaberle, F.A.1    Kuz'min, V.A.2    Borissevitch, I.E.3
  • 97
    • 0013514978 scopus 로고
    • Fluorescence lifetimes: theory, instrumentation and application of nanosecond fluorometry
    • Ph.D. thesis, University of Illinois at Urbana Champaign. Published by University Microfilms International, Ann Arbor, MI.
    • Spencer, R.D. (1970). Fluorescence lifetimes: theory, instrumentation and application of nanosecond fluorometry. Ph.D. thesis, University of Illinois at Urbana Champaign. Published by University Microfilms International, Ann Arbor, MI.
    • (1970)
    • Spencer, R.D.1
  • 98
    • 0002388667 scopus 로고
    • Uber die Abklingungszeit der Fluoreszenz
    • Stern, O. and Volmer, M. (1919). Uber die Abklingungszeit der Fluoreszenz. Physikalische Zeitschrift, 20, 183-188.
    • (1919) Physikalische Zeitschrift , vol.20 , pp. 183-188
    • Stern, O.1    Volmer, M.2
  • 99
    • 0001823360 scopus 로고
    • Polarizations and assignments of transitions: The method of photoselection
    • Albrecht, A.C. (1961). Polarizations and assignments of transitions: The method of photoselection. Journal of Molecular Spectroscopy, 6, 84.
    • (1961) Journal of Molecular Spectroscopy , vol.6 , pp. 84
    • Albrecht, A.C.1
  • 100
    • 0014963392 scopus 로고
    • Conformational studies on modified proteins and peptides Artificialmyoglobins prepared with modified and metalloporphyrins
    • Andres, S.F. and Atassi, M.Z. (1970). Conformational studies on modified proteins and peptides. Artificialmyoglobins prepared with modified and metalloporphyrins. Biochemistry, 9, 2268-2275.
    • (1970) Biochemistry , vol.9 , pp. 2268-2275
    • Andres, S.F.1    Atassi, M.Z.2
  • 101
    • 33645658254 scopus 로고
    • Polarized light in spectroscopy and photochemistry
    • A.A. Lamola (ed.), Dekker, New York.
    • Dörr, F. (1971). Polarized light in spectroscopy and photochemistry, in: A.A. Lamola (ed.), Creation and Detection of the Excited States, pp. 53-122, Dekker, New York.
    • (1971) Creation and Detection of the Excited States , pp. 53-122
    • Dörr, F.1
  • 102
    • 84889403710 scopus 로고
    • Etude par fluorescence de molécule HbdesFe thesis
    • University of Paris
    • Sebban P. (1979). Etude par fluorescence de molécule HbdesFe thesis, University of Paris 7.
    • (1979) , pp. 7
    • Sebban, P.1
  • 103
    • 0014202988 scopus 로고
    • Fluorescence depolarization of rabbit gamma globulin conjugates
    • Wahl, P. and Weber, G. (1967). Fluorescence depolarization of rabbit gamma globulin conjugates. Journal of Molecular Biology, 30, 371-382.
    • (1967) Journal of Molecular Biology , vol.30 , pp. 371-382
    • Wahl, P.1    Weber, G.2
  • 104
    • 76949127690 scopus 로고
    • Polarization of the fluorescence of macromolecules I. Theory and experimental method
    • Weber, G. (1952). Polarization of the fluorescence of macromolecules. I. Theory and experimental method. Biochemical Journal, 51, 145-155.
    • (1952) Biochemical Journal , vol.51 , pp. 145-155
    • Weber, G.1
  • 105
    • 0030452419 scopus 로고    scopus 로고
    • Fluorescence emission of ethidium bromide intercalated in defined DNA duplexes: Evaluation of hydrodynamics components
    • Duhamel, J., Kanyo, J., Dinter-Gottlieb, G. and Lu, P. (1996). Fluorescence emission of ethidium bromide intercalated in defined DNA duplexes: Evaluation of hydrodynamics components. Biochemistry, 35, 16687-16697.
    • (1996) Biochemistry , vol.35 , pp. 16687-16697
    • Duhamel, J.1    Kanyo, J.2    Dinter-Gottlieb, G.3    Lu, P.4
  • 108
    • 36949082598 scopus 로고
    • Heterogeneity in deoxyribonucleic acids I. Dependence on composition of the configurational stability of deoxyribonucleic acids
    • Marmur, J. and Doty, P. (1959). Heterogeneity in deoxyribonucleic acids. I. Dependence on composition of the configurational stability of deoxyribonucleic acids. Nature, 183, 1427-1429.
    • (1959) Nature , vol.183 , pp. 1427-1429
    • Marmur, J.1    Doty, P.2
  • 109
    • 0021760463 scopus 로고
    • Binding of ethidium and bis(methidium)spermine to Z DNA by intercalation
    • Shafer, R.H., Brown, S.C., Delbarre, A. and Wade, D. (1984). Binding of ethidium and bis(methidium)spermine to Z DNA by intercalation. Nucleic Acids Research, 12, 4679-4690.
    • (1984) Nucleic Acids Research , vol.12 , pp. 4679-4690
    • Shafer, R.H.1    Brown, S.C.2    Delbarre, A.3    Wade, D.4
  • 110
    • 33748785487 scopus 로고    scopus 로고
    • Extraction and purification of DNA
    • In: QuerciM, Jermini M,andVan den Eede,G. (eds), European commission, Joint research centre, special publication 1.03.114, edition.
    • Somma M. (2004). Extraction and purification of DNA. In: QuerciM, Jermini M,andVan den Eede,G. (eds), The Analysis of Food Samples for the Presence of Genetically, Modified Organisms. European commission, Joint research centre, special publication 1.03.114, edition.
    • (2004) The Analysis of Food Samples for the Presence of Genetically, Modified Organisms
    • Somma, M.1
  • 111
    • 0035984292 scopus 로고    scopus 로고
    • Fluorometric determination of DNA using a new ruthenium complex Ru(bpy)2PIP(V) as a nucleic acid probe
    • Song, G., Li, L., Liu, L., Fang, G., Lu, S., He, Z. and Zeng, Y. (2002). Fluorometric determination of DNA using a new ruthenium complex Ru(bpy)2PIP(V) as a nucleic acid probe. Analytical Sciences, 18, 757-759.
    • (2002) Analytical Sciences , vol.18 , pp. 757-759
    • Song, G.1    Li, L.2    Liu, L.3    Fang, G.4    Lu, S.5    He, Z.6    Zeng, Y.7
  • 113
    • 0014734013 scopus 로고
    • Decay of fluorescence emission anisotropy of the ethidium bromide-DNA complex evidence for an internal motion in DNA
    • Wahl, Ph., Paoletti, J. and Le Pecq, J.-B. (1970). Decay of fluorescence emission anisotropy of the ethidium bromide-DNA complex evidence for an internal motion in DNA. Proceedings of the National Academy of Sciences, USA, 65, 417-421.
    • (1970) Proceedings of the National Academy of Sciences, USA , vol.65 , pp. 417-421
    • Wahl, P.1    Paoletti, J.2    Pecq, L.J.-B.3
  • 114
    • 0013508985 scopus 로고    scopus 로고
    • Role of the carbohydrate moiety and of the alpha l-fucose in the stabilization and the dynamics of the Lens culinaris agglutinin-glycoprotein complex A fluorescence study
    • Albani, J.R., Debray, H.,Vincent, M. and Gallay, J. (1997). Role of the carbohydrate moiety and of the alpha l-fucose in the stabilization and the dynamics of the Lens culinaris agglutinin-glycoprotein complex. A fluorescence study. Journal of Fluorescence, 7, 293-298.
    • (1997) Journal of Fluorescence , vol.7 , pp. 293-298
    • Albani, J.R.1    Debray, H.2    Vincent, M.3    Gallay, J.4
  • 116
    • 0019877155 scopus 로고
    • The carbohydrate-binding specificity of pea and lentil lectins Fucose is an important determinant
    • Kornfeld, K.,Reitman, M.-L. and Kornfeld, R. (1981). The carbohydrate-binding specificity of pea and lentil lectins. Fucose is an important determinant. Journal of Biological Chemistry, 256, 6633-6640.
    • (1981) Journal of Biological Chemistry , vol.256 , pp. 6633-6640
    • Kornfeld, K.1    Reitman, M.-L.2    Kornfeld, R.3
  • 117
    • 0004310465 scopus 로고
    • Handbook of Physical Calculations
    • McGraw-Hill, New York.
    • Tuma, J.J. (1983). Handbook of Physical Calculations,McGraw-Hill, New York.
    • (1983)
    • Tuma, J.J.1
  • 119
    • 0037077208 scopus 로고    scopus 로고
    • Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer
    • Ayoub, M.A., Couturier, C., Lucas-Meunier, E., Angers, S., Fossier, P., Bouvier, M. and Jockers, R. (2002). Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer. Journal of Biological Chemistry, 277, 21522-21528.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 21522-21528
    • Ayoub, M.A.1    Couturier, C.2    Lucas-Meunier, E.3    Angers, S.4    Fossier, P.5    Bouvier, M.6    Jockers, R.7
  • 121
    • 0034212061 scopus 로고    scopus 로고
    • The enhanced green fluorescent protein as a tool for the analysis of protein dynamics and localization: Local fluorescence study at the single-molecule level
    • Cinelli, R.A.G., Ferrari, A., Pellegrini, V., Tyagi, M., Giacca, M. and Beltram, F. (2004). The enhanced green fluorescent protein as a tool for the analysis of protein dynamics and localization: Local fluorescence study at the single-molecule level. Photochemistry and Photobiology, 71, 771-776.
    • (2004) Photochemistry and Photobiology , vol.71 , pp. 771-776
    • Cinelli, R.A.G.1    Ferrari, A.2    Pellegrini, V.3    Tyagi, M.4    Giacca, M.5    Beltram, F.6
  • 122
    • 84981779372 scopus 로고
    • Intermolecular energy migration and fluorescence
    • Forster, T. (1948). Intermolecular energy migration and fluorescence. Annual of Physics (Leipzig), 2, 55-75.
    • (1948) Annual of Physics (Leipzig) , vol.2 , pp. 55-75
    • Forster, T.1
  • 123
    • 0025895757 scopus 로고
    • Reactions and significance of cytochrome P-450 enzymes
    • Guengerich, F.P. (1991). Reactions and significance of cytochrome P-450 enzymes. Journal of Biological Chemistry, 266, 10019-10022.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 10019-10022
    • Guengerich, F.P.1
  • 124
    • 0032958863 scopus 로고    scopus 로고
    • Green fluorescent protein forms for energy transfer
    • Heim, R. (1999). Green fluorescent protein forms for energy transfer. Methods in Enzymology, 302, 408-423.
    • (1999) Methods in Enzymology , vol.302 , pp. 408-423
    • Heim, R.1
  • 126
    • 0031047006 scopus 로고    scopus 로고
    • Steady-state and picosecond-time-resolved fluorescence studies on the recombinant heme domain of Bacillus megaterium cytochrome P-450
    • Khan, K.K., Mazumdar, S., Modi, S., Sutcliffe, M., Roberts, G.C.K. and Mitra, S. (1997). Steady-state and picosecond-time-resolved fluorescence studies on the recombinant heme domain of Bacillus megaterium cytochrome P-450. European Journal of Biochemistry, 244, 361-370.
    • (1997) European Journal of Biochemistry , vol.244 , pp. 361-370
    • Khan, K.K.1    Mazumdar, S.2    Modi, S.3    Sutcliffe, M.4    Roberts, G.C.K.5    Mitra, S.6
  • 127
    • 0031865351 scopus 로고    scopus 로고
    • Bcl-2 and Bax interactions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer
    • Mahajan, N.P., Linder, K., Berry, G., Gordon, G.W., Heim, R. and Herman, B. (1998). Bcl-2 and Bax interactions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer. Nature Biotechnology, 16, 547-552.
    • (1998) Nature Biotechnology , vol.16 , pp. 547-552
    • Mahajan, N.P.1    Linder, K.2    Berry, G.3    Gordon, G.W.4    Heim, R.5    Herman, B.6
  • 128
    • 0028891348 scopus 로고
    • Fluorescence energy transfer in one dimension:Frequency-domain fluorescence study of DNA-fluorophore complex
    • Maliwal, B.P., Kusba, J. and Lakowicz, J. R. (1995). Fluorescence energy transfer in one dimension:Frequency-domain fluorescence study of DNA-fluorophore complex. Biopolymers, 35, 245-255.
    • (1995) Biopolymers , vol.35 , pp. 245-255
    • Maliwal, B.P.1    Kusba, J.2    Lakowicz, J.R.3
  • 129
    • 0036183614 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of protein-protein interactions in single living cells by multifocal multiphoton microscopy
    • Majoul, I., Straub, M., Duden, R., Hell, S.W., Soling, H.D. (2002). Fluorescence resonance energy transfer analysis of protein-protein interactions in single living cells by multifocal multiphoton microscopy. Journal of Biotechnology, 82, 267-277.
    • (2002) Journal of Biotechnology , vol.82 , pp. 267-277
    • Majoul, I.1    Straub, M.2    Duden, R.3    Hell, S.W.4    Soling, H.D.5
  • 130
    • 0022878676 scopus 로고
    • Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium
    • Narhi, L.O. and Fulco, A.J. (1986). Characterization of a catalytically self-sufficient 119,000-dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium. Journal of Biological Chemistry, 261, 7160-7169.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 7160-7169
    • Narhi, L.O.1    Fulco, A.J.2
  • 131
    • 0025784027 scopus 로고
    • Cytochrome P-450 Multiplicity of isoforms, substrates, and catalytic and regulatory mechanisms
    • Porter, T.D. and Coon, M.J. (1991). Cytochrome P-450. Multiplicity of isoforms, substrates, and catalytic and regulatory mechanisms. Journal of Biological Chemistry, 266, 13469-13472.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 13469-13472
    • Porter, T.D.1    Coon, M.J.2
  • 132
    • 0033045712 scopus 로고    scopus 로고
    • Imaging fluorescence resonance energy transfer between two green fluorescent proteins in living yeast
    • Sagot, I., Bonneu, M., Balguerie, A. and Aigle, M. (1999). Imaging fluorescence resonance energy transfer between two green fluorescent proteins in living yeast. FEBS Letters, 447, 53-57.
    • (1999) FEBS Letters , vol.447 , pp. 53-57
    • Sagot, I.1    Bonneu, M.2    Balguerie, A.3    Aigle, M.4
  • 133
    • 0021237046 scopus 로고
    • Specialized functional domains in hemoglobin: dimensions in solution of the apohemoglobin dimer labeled with fluorescein iodoacetamide
    • Sassaroli, M., Bucci, E., Liesegang, J., Fronticelli, C. and Steiner, R.F. (1984). Specialized functional domains in hemoglobin: dimensions in solution of the apohemoglobin dimer labeled with fluorescein iodoacetamide. Biochemistry, 23, 2487-2491.
    • (1984) Biochemistry , vol.23 , pp. 2487-2491
    • Sassaroli, M.1    Bucci, E.2    Liesegang, J.3    Fronticelli, C.4    Steiner, R.F.5
  • 134
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck, D.K., Hoekstra, D. and Pagano, R.E. (1981). Use of resonance energy transfer to monitor membrane fusion. Biochemistry, 20, 4093-4099.
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 135
    • 0035442412 scopus 로고    scopus 로고
    • The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo
    • Truong, K. and Ikura, M. (2001). The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo. Current Opinion in Structural Biology, 11, 573-578.
    • (2001) Current Opinion in Structural Biology , vol.11 , pp. 573-578
    • Truong, K.1    Ikura, M.2
  • 136
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins
    • Xu, Y., Piston, D.W. and Johnson, C.H. (1999). A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins. Proceedings of the National Academy of Sciences, USA, 96, 151-156.
    • (1999) Proceedings of the National Academy of Sciences, USA , vol.96 , pp. 151-156
    • Xu, Y.1    Piston, D.W.2    Johnson, C.H.3
  • 137
    • 8544283254 scopus 로고    scopus 로고
    • The comet assay for DNA damage and repair Principles, applications and limitations
    • Collins, A.R. (2004). The comet assay for DNA damage and repair. Principles, applications and limitations. Molecular Biotechnology, 26, 249-261.
    • (2004) Molecular Biotechnology , vol.26 , pp. 249-261
    • Collins, A.R.1
  • 139
  • 140
    • 84889397973 scopus 로고    scopus 로고
    • Interest of the Comet Assay for the study of environmental genotoxicity
    • Thesis, University of Metz.
    • Lemière, S. (2004). Interest of the Comet Assay for the study of environmental genotoxicity. Thesis, University of Metz.
    • (2004)
    • Lemière, S.1
  • 141
    • 0034757699 scopus 로고    scopus 로고
    • Transmitted light fluorescence microscopy revisited
    • Tran, P.T. and Chang, F. (2001). Transmitted light fluorescence microscopy revisited. The Biological Bulletin, 201, 235-236. www.cometassayindia.org www.cometassayindia.org/protocols.htm
    • (2001) The Biological Bulletin , vol.201 , pp. 235-236
    • Tran, P.T.1    Chang, F.2


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