메뉴 건너뛰기




Volumn 390, Issue 1, 2009, Pages 1-13

NUTS and BOLTS: Applications of fluorescence-detected sedimentation

Author keywords

Analytical ultracentrifugation; Fluorescence detected sedimentation; Green fluorescent protein

Indexed keywords

CENTRIFUGATION; FLUORESCENCE; MACROMOLECULES; NUTS (FASTENERS); SEDIMENTATION;

EID: 65649116623     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.11.033     Document Type: Article
Times cited : (76)

References (25)
  • 1
    • 35449002345 scopus 로고    scopus 로고
    • Analytical ultracentrifugation: sedimentation velocity and sedimentation equilibrium
    • Correia J.J., and Detrich H. (Eds), Elsevier, San Diego
    • Cole J.L., Lary J.W., Moody T.P., and Laue T.M. Analytical ultracentrifugation: sedimentation velocity and sedimentation equilibrium. In: Correia J.J., and Detrich H. (Eds). Methods in Cell Biology vol. 84 (2007), Elsevier, San Diego 143-179
    • (2007) Methods in Cell Biology , vol.84 , pp. 143-179
    • Cole, J.L.1    Lary, J.W.2    Moody, T.P.3    Laue, T.M.4
  • 2
    • 33748565349 scopus 로고    scopus 로고
    • Analytical ultracentrifugation for the study of protein association and assembly
    • Howlett G.J., Minton A.P., and Rivas G. Analytical ultracentrifugation for the study of protein association and assembly. Curr. Opin. Chem. Biol. 10 (2006) 430-436
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 430-436
    • Howlett, G.J.1    Minton, A.P.2    Rivas, G.3
  • 3
    • 65649153954 scopus 로고    scopus 로고
    • Applications Data Note for Spinco Division of Beckman Instruments, Palo Alto, CA
    • T.M. Laue, Optical systems of the XLA ultracentrifuge, Applications Data Note for Spinco Division of Beckman Instruments, Palo Alto, CA, 1996.
    • (1996) Optical systems of the XLA ultracentrifuge
    • Laue, T.M.1
  • 4
    • 1642325812 scopus 로고    scopus 로고
    • Fluorescence detection for the XLI ultracentrifuge
    • MacGregor I.K., Anderson A.L., and Laue T.M. Fluorescence detection for the XLI ultracentrifuge. Biophys. Chem. 108 (2004) 165-185
    • (2004) Biophys. Chem. , vol.108 , pp. 165-185
    • MacGregor, I.K.1    Anderson, A.L.2    Laue, T.M.3
  • 5
    • 33947273492 scopus 로고    scopus 로고
    • A light intensity measurement system for the analytical ultracentrifuge
    • Laue T.M., Austin J.B., and Rau D.A. A light intensity measurement system for the analytical ultracentrifuge. Prog. Colloid Polym. Sci. 131 (2006) 1-8
    • (2006) Prog. Colloid Polym. Sci. , vol.131 , pp. 1-8
    • Laue, T.M.1    Austin, J.B.2    Rau, D.A.3
  • 6
    • 0017119840 scopus 로고
    • UV laser scanning and fluorescence monitoring of analytical ultracentrifugation with an on-line computer system
    • Crepeau R.H., Conrad R.H., and Edelstein S.J. UV laser scanning and fluorescence monitoring of analytical ultracentrifugation with an on-line computer system. Biophys. Chem. 5 (1976) 27-39
    • (1976) Biophys. Chem. , vol.5 , pp. 27-39
    • Crepeau, R.H.1    Conrad, R.H.2    Edelstein, S.J.3
  • 7
    • 0025245195 scopus 로고
    • A fluorescence detection system for the analytical ultracentrifuge and its application to proteins, nucleic acids, and viruses
    • Schmidt B., Rappold W., Rosenbaum V., Fischer R., and Riesner D. A fluorescence detection system for the analytical ultracentrifuge and its application to proteins, nucleic acids, and viruses. Colloid Polym. Sci. 268 (1989) 45-54
    • (1989) Colloid Polym. Sci. , vol.268 , pp. 45-54
    • Schmidt, B.1    Rappold, W.2    Rosenbaum, V.3    Fischer, R.4    Riesner, D.5
  • 8
    • 45549085650 scopus 로고    scopus 로고
    • The modulation of transthyretin tetramer stability by cysteine 10 adducts and the drug diflunisal: direct analysis by fluorescence-detected analytical ultracentrifugation
    • Kingsbury J.S., Laue T.M., Klimtchuk E.S., Theberge R., Costello C.E., and Connors L.H. The modulation of transthyretin tetramer stability by cysteine 10 adducts and the drug diflunisal: direct analysis by fluorescence-detected analytical ultracentrifugation. J. Biol. Chem. 283 (2008) 11887-11896
    • (2008) J. Biol. Chem. , vol.283 , pp. 11887-11896
    • Kingsbury, J.S.1    Laue, T.M.2    Klimtchuk, E.S.3    Theberge, R.4    Costello, C.E.5    Connors, L.H.6
  • 9
    • 0017802689 scopus 로고
    • A sedimentation equilibrium method for determining molecular weights of proteins with a tabletop high speed air turbine centrifuge
    • Bothwell M.A., Howlett G.J., and Schachman H.K. A sedimentation equilibrium method for determining molecular weights of proteins with a tabletop high speed air turbine centrifuge. J. Biol. Chem. 253 (1978) 2073-2077
    • (1978) J. Biol. Chem. , vol.253 , pp. 2073-2077
    • Bothwell, M.A.1    Howlett, G.J.2    Schachman, H.K.3
  • 10
    • 0027410312 scopus 로고
    • Rapid and accurate microfractionation of the contents of small centrifuge tubes: application in the measurement of molecular weight of proteins via sedimentation equilibrium
    • Darawshe S., Rivas G., and Minton A.P. Rapid and accurate microfractionation of the contents of small centrifuge tubes: application in the measurement of molecular weight of proteins via sedimentation equilibrium. Anal. Biochem. 209 (1993) 130-135
    • (1993) Anal. Biochem. , vol.209 , pp. 130-135
    • Darawshe, S.1    Rivas, G.2    Minton, A.P.3
  • 11
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78 (2000) 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 12
    • 1642368109 scopus 로고    scopus 로고
    • Analysis of heterologous interacting systems by sedimentation velocity: curve fitting algorithms for estimation of sedimentation coefficients, equilibrium, and kinetic constants
    • Stafford W.F., and Sherwood P.J. Analysis of heterologous interacting systems by sedimentation velocity: curve fitting algorithms for estimation of sedimentation coefficients, equilibrium, and kinetic constants. Biophys. Chem. 108 (2004) 231-243
    • (2004) Biophys. Chem. , vol.108 , pp. 231-243
    • Stafford, W.F.1    Sherwood, P.J.2
  • 13
    • 33745216899 scopus 로고    scopus 로고
    • Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques
    • Philo J.S. Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques. Anal. Biochem. 354 (2006) 238-246
    • (2006) Anal. Biochem. , vol.354 , pp. 238-246
    • Philo, J.S.1
  • 16
    • 58049206260 scopus 로고    scopus 로고
    • Fluorescence detection of a lipid induced tetrameric intermediate in amyloid fibril formation by apolipoprotein C-II
    • Ryan T.M., Howlett G.J., and Bailey M.F. Fluorescence detection of a lipid induced tetrameric intermediate in amyloid fibril formation by apolipoprotein C-II. J. Biol. Chem. 283 (2008) 35118-35128
    • (2008) J. Biol. Chem. , vol.283 , pp. 35118-35128
    • Ryan, T.M.1    Howlett, G.J.2    Bailey, M.F.3
  • 18
    • 37049217315 scopus 로고
    • An experimental test of the framework theory of antigen-antibody precipitation
    • Pauling L., Pressman D., and Campbell D.H. An experimental test of the framework theory of antigen-antibody precipitation. Science 98 (1943) 263-264
    • (1943) Science , vol.98 , pp. 263-264
    • Pauling, L.1    Pressman, D.2    Campbell, D.H.3
  • 19
    • 0142153329 scopus 로고    scopus 로고
    • Tracer sedimentation equilibrium: a powerful tool for the quantitative characterization of macromolecular self- and hetero-association in solution
    • Rivas G., and Minton A.P. Tracer sedimentation equilibrium: a powerful tool for the quantitative characterization of macromolecular self- and hetero-association in solution. Biochem. Soc. Trans. 31 (2003) 1015-1019
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 1015-1019
    • Rivas, G.1    Minton, A.P.2
  • 20
    • 85025410333 scopus 로고
    • A quantitative theory of the precipitin reaction: II. A study of an azoprotein-antibody system
    • Heidelberger M., and Kendall F.E. A quantitative theory of the precipitin reaction: II. A study of an azoprotein-antibody system. J. Exp. Med. 62 (1935) 467-483
    • (1935) J. Exp. Med. , vol.62 , pp. 467-483
    • Heidelberger, M.1    Kendall, F.E.2
  • 21
    • 0017611984 scopus 로고
    • The concentration dependence of transport processes: a general description applicable to the sedimentation, translational diffusion, and viscosity coefficients of macromolecular solutes
    • Rowe A.J. The concentration dependence of transport processes: a general description applicable to the sedimentation, translational diffusion, and viscosity coefficients of macromolecular solutes. Biopolymers 16 (1977) 2595-2611
    • (1977) Biopolymers , vol.16 , pp. 2595-2611
    • Rowe, A.J.1
  • 22
    • 0003868932 scopus 로고
    • Blood and other body fluids
    • 61-199, Federation of American Societies for Experimental Biology, Washington, DC
    • P.L. Altman, Blood and other body fluids, ASD Technical Report 61-199, Federation of American Societies for Experimental Biology, Washington, DC, 1961.
    • (1961) ASD Technical Report
    • Altman, P.L.1
  • 23
    • 0001357930 scopus 로고
    • A boundary anomaly found in the ultracentrifugal sedimentation of mixtures
    • Johnston J.P., and Ogston A.G. A boundary anomaly found in the ultracentrifugal sedimentation of mixtures. Trans. Faraday Soc. 42 (1946) 789-799
    • (1946) Trans. Faraday Soc. , vol.42 , pp. 789-799
    • Johnston, J.P.1    Ogston, A.G.2
  • 24
    • 0017193544 scopus 로고
    • Numerical study of the Johnston-Ogston effect in two-component systems
    • Correia J.J., Johnson M.L., Weiss G.H., and Yphantis D.A. Numerical study of the Johnston-Ogston effect in two-component systems. Biophys. Chem. 5 (1976) 255-264
    • (1976) Biophys. Chem. , vol.5 , pp. 255-264
    • Correia, J.J.1    Johnson, M.L.2    Weiss, G.H.3    Yphantis, D.A.4
  • 25
    • 0034581366 scopus 로고    scopus 로고
    • Analysis of reversibly interacting macromolecular systems by time derivative sedimentation velocity
    • Johnson M.L., and Ackers G.K. (Eds), Academic Press, San Diego
    • Stafford W.F. Analysis of reversibly interacting macromolecular systems by time derivative sedimentation velocity. In: Johnson M.L., and Ackers G.K. (Eds). Methods in Enzymology, vol. 233, Part C: Energetics of Biological Macromolecules (2000), Academic Press, San Diego 302-325
    • (2000) Methods in Enzymology, vol. 233, Part C: Energetics of Biological Macromolecules , pp. 302-325
    • Stafford, W.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.