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Volumn 102, Issue 12, 2012, Pages 2866-2875

Conformational analysis of a genetically encoded FRET biosensor by SAXS

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENT DYE; LIPOCORTIN 4;

EID: 84862695182     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.05.009     Document Type: Article
Times cited : (19)

References (41)
  • 1
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • M. Chalfie, and Y. Tu D.C. Prasher Green fluorescent protein as a marker for gene expression Science 263 1994 802 805
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Prasher, D.C.3
  • 2
    • 0031011418 scopus 로고    scopus 로고
    • Detection in living cells of Ca2+-dependent changes in the fluorescence emission of an indicator composed of two green fluorescent protein variants linked by a calmodulin-binding sequence. A new class of fluorescent indicators
    • V.A. Romoser, P.M. Hinkle, and A. Persechini Detection in living cells of Ca2+-dependent changes in the fluorescence emission of an indicator composed of two green fluorescent protein variants linked by a calmodulin-binding sequence. A new class of fluorescent indicators J. Biol. Chem. 272 1997 13270 13274
    • (1997) J. Biol. Chem. , vol.272 , pp. 13270-13274
    • Romoser, V.A.1    Hinkle, P.M.2    Persechini, A.3
  • 3
    • 0030610646 scopus 로고    scopus 로고
    • 2+ based on green fluorescent proteins and calmodulin
    • 2+ based on green fluorescent proteins and calmodulin Nature 388 1997 882 887
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1    Llopis, J.2    Tsien, R.Y.3
  • 4
    • 0037780971 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
    • J.D. Violin, and J. Zhang A.C. Newton A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C J. Cell Biol. 161 2003 899 909
    • (2003) J. Cell Biol. , vol.161 , pp. 899-909
    • Violin, J.D.1    Zhang, J.2    Newton, A.C.3
  • 5
    • 4444377903 scopus 로고    scopus 로고
    • Novel single chain cAMP sensors for receptor-induced signal propagation
    • V.O. Nikolaev, and M. Bünemann M.J. Lohse Novel single chain cAMP sensors for receptor-induced signal propagation J. Biol. Chem. 279 2004 37215 37218
    • (2004) J. Biol. Chem. , vol.279 , pp. 37215-37218
    • Nikolaev, V.O.1    Bünemann, M.2    Lohse, M.J.3
  • 6
    • 17844388845 scopus 로고    scopus 로고
    • Visualizing the mechanical activation of Src
    • Y. Wang, and E.L. Botvinick S. Chien Visualizing the mechanical activation of Src Nature 434 2005 1040 1045
    • (2005) Nature , vol.434 , pp. 1040-1045
    • Wang, Y.1    Botvinick, E.L.2    Chien, S.3
  • 7
    • 45749115811 scopus 로고    scopus 로고
    • Midzone activation of aurora B in anaphase produces an intracellular phosphorylation gradient
    • B.G. Fuller, and M.A. Lampson D.L. Brautigan Midzone activation of aurora B in anaphase produces an intracellular phosphorylation gradient Nature 453 2008 1132 1136
    • (2008) Nature , vol.453 , pp. 1132-1136
    • Fuller, B.G.1    Lampson, M.A.2    Brautigan, D.L.3
  • 8
    • 77954486800 scopus 로고    scopus 로고
    • Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics
    • C. Grashoff, and B.D. Hoffman M.A. Schwartz Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics Nature 466 2010 263 266
    • (2010) Nature , vol.466 , pp. 263-266
    • Grashoff, C.1    Hoffman, B.D.2    Schwartz, M.A.3
  • 9
    • 71049131212 scopus 로고    scopus 로고
    • Recent progress in strategies for the creation of protein-based fluorescent biosensors
    • H. Wang, E. Nakata, and I. Hamachi Recent progress in strategies for the creation of protein-based fluorescent biosensors ChemBioChem 10 2009 2560 2577
    • (2009) ChemBioChem , vol.10 , pp. 2560-2577
    • Wang, H.1    Nakata, E.2    Hamachi, I.3
  • 10
    • 77951211821 scopus 로고    scopus 로고
    • Fluorescent biosensors of intracellular targets from genetically encoded reporters to modular polypeptide probes
    • M.C. Morris Fluorescent biosensors of intracellular targets from genetically encoded reporters to modular polypeptide probes Cell Biochem. Biophys. 56 2010 19 37
    • (2010) Cell Biochem. Biophys. , vol.56 , pp. 19-37
    • Morris, M.C.1
  • 11
    • 4644368371 scopus 로고    scopus 로고
    • Genetically encoded FRET probe for PKC activity based on pleckstrin
    • A. Schleifenbaum, and G. Stier C. Schultz Genetically encoded FRET probe for PKC activity based on pleckstrin J. Am. Chem. Soc. 126 2004 11786 11787
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 11786-11787
    • Schleifenbaum, A.1    Stier, G.2    Schultz, C.3
  • 12
    • 79955894911 scopus 로고    scopus 로고
    • Genetically encodable fluorescent biosensors for tracking signaling dynamics in living cells
    • R.J. Newman, M.D. Fosbrink, and J. Zhang Genetically encodable fluorescent biosensors for tracking signaling dynamics in living cells Chem. Rev. 111 2011 3614 3666
    • (2011) Chem. Rev. , vol.111 , pp. 3614-3666
    • Newman, R.J.1    Fosbrink, M.D.2    Zhang, J.3
  • 13
    • 79960490475 scopus 로고    scopus 로고
    • Rapid development of genetically encoded FRET reporters
    • A. Piljić, and I. de Diego C. Schultz Rapid development of genetically encoded FRET reporters ACS Chem. Biol. 6 2011 685 691
    • (2011) ACS Chem. Biol. , vol.6 , pp. 685-691
    • Piljić, A.1    De Diego, I.2    Schultz, C.3
  • 14
    • 33745627481 scopus 로고    scopus 로고
    • Annexin A4 self-association modulates general membrane protein mobility in living cells
    • A. Piljic, and C. Schultz Annexin A4 self-association modulates general membrane protein mobility in living cells Mol. Biol. Cell 17 2006 3318 3328
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3318-3328
    • Piljic, A.1    Schultz, C.2
  • 15
    • 42449154333 scopus 로고    scopus 로고
    • Simultaneous recording of multiple cellular events by FRET
    • A. Piljic, and C. Schultz Simultaneous recording of multiple cellular events by FRET ACS Chem. Biol. 3 2008 156 160
    • (2008) ACS Chem. Biol. , vol.3 , pp. 156-160
    • Piljic, A.1    Schultz, C.2
  • 16
    • 0035799337 scopus 로고    scopus 로고
    • Phosphorylation mutants elucidate the mechanism of annexin IV-mediated membrane aggregation
    • M.A. Kaetzel, and Y.D. Mo B.A. Seaton Phosphorylation mutants elucidate the mechanism of annexin IV-mediated membrane aggregation Biochemistry 40 2001 4192 4199
    • (2001) Biochemistry , vol.40 , pp. 4192-4199
    • Kaetzel, M.A.1    Mo, Y.D.2    Seaton, B.A.3
  • 17
    • 84981779372 scopus 로고
    • Zwischenmolekulare Energiewanderung und Fluoreszenz
    • T. Förster Zwischenmolekulare Energiewanderung und Fluoreszenz Annal. Phys. 437 1948 55 75
    • (1948) Annal. Phys. , vol.437 , pp. 55-75
    • Förster, T.1
  • 18
    • 34247891681 scopus 로고    scopus 로고
    • A computational tool for designing FRET protein biosensors by rigid-body sampling of their conformational space
    • E. Pham, and J. Chiang K. Truong A computational tool for designing FRET protein biosensors by rigid-body sampling of their conformational space Structure 15 2007 515 523
    • (2007) Structure , vol.15 , pp. 515-523
    • Pham, E.1    Chiang, J.2    Truong, K.3
  • 22
    • 77956190770 scopus 로고    scopus 로고
    • Structural characterization of proteins and complexes using small-angle X-ray solution scattering
    • H.D.T. Mertens, and D.I. Svergun Structural characterization of proteins and complexes using small-angle X-ray solution scattering J. Struct. Biol. 172 2010 128 141
    • (2010) J. Struct. Biol. , vol.172 , pp. 128-141
    • Mertens, H.D.T.1    Svergun, D.I.2
  • 23
    • 0034633010 scopus 로고    scopus 로고
    • Förster distances between green fluorescent protein pairs
    • G.H. Patterson, D.W. Piston, and B.G. Barisas Förster distances between green fluorescent protein pairs Anal. Biochem. 284 2000 438 440
    • (2000) Anal. Biochem. , vol.284 , pp. 438-440
    • Patterson, G.H.1    Piston, D.W.2    Barisas, B.G.3
  • 24
    • 34248347847 scopus 로고    scopus 로고
    • Upgrade of the small-angle X-ray scattering beamline X33 at the European Molecular Biology Laboratory, Hamburg
    • M.W. Roessle, and R. Klaering D.I. Svergun Upgrade of the small-angle X-ray scattering beamline X33 at the European Molecular Biology Laboratory, Hamburg J. Appl. Crystallogr. 40 2007 s190 s194
    • (2007) J. Appl. Crystallogr. , vol.40
    • Roessle, M.W.1    Klaering, R.2    Svergun, D.I.3
  • 25
    • 51949084084 scopus 로고    scopus 로고
    • Automated sample-changing robot for solution scattering experiments at the EMBL Hamburg SAXS station X33
    • A.R. Round, and D. Franke M. Roessle Automated sample-changing robot for solution scattering experiments at the EMBL Hamburg SAXS station X33 J. Appl. Crystallogr. 41 2008 913 917
    • (2008) J. Appl. Crystallogr. , vol.41 , pp. 913-917
    • Round, A.R.1    Franke, D.2    Roessle, M.3
  • 27
    • 0001498978 scopus 로고
    • La diffraction des rayons X aux trés petits angles: Application à l'étude de phénomènes ultramicroscopiques
    • A. Guinier La diffraction des rayons X aux trés petits angles: application à l'étude de phénomènes ultramicroscopiques Phys. (Paris) 12 1939 161 237
    • (1939) Phys. (Paris) , vol.12 , pp. 161-237
    • Guinier, A.1
  • 28
    • 0026244044 scopus 로고
    • GNOM - A program package for small-angle scattering data processing
    • A.V. Semenyuk, and D.I. Svergun GNOM - a program package for small-angle scattering data processing J. Appl. Crystallogr. 24 1991 537 540
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 29
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab initio shape determination in small-angle scattering
    • D. Franke, and D.I. Svergun DAMMIF, a program for rapid ab initio shape determination in small-angle scattering J. Appl. Crystallogr. 42 2009 342 346
    • (2009) J. Appl. Crystallogr. , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 30
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • D.I. Svergun, C. Barberato, and M.H.J. Koch CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Crystallogr. 28 1995 768 773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 31
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-angle X-ray scattering
    • P. Bernadó, and E. Mylonas D.I. Svergun Structural characterization of flexible proteins using small-angle X-ray scattering J. Am. Chem. Soc. 129 2007 5656 5664
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5656-5664
    • Bernadó, P.1    Mylonas, E.2    Svergun, D.I.3
  • 32
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • M.B. Kozin, and D.I. Svergun Automated matching of high- and low-resolution structural models J. Appl. Crystallogr. 34 2001 33 41
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 33
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • V.V. Volkov, and D.I. Svergun Uniqueness of ab initio shape determination in small-angle scattering J. Appl. Crystallogr. 36 2003 860 864
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 34
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • M.V. Petoukhov, and D.I. Svergun Global rigid body modeling of macromolecular complexes against small-angle scattering data Biophys. J. 89 2005 1237 1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 35
    • 77952094752 scopus 로고    scopus 로고
    • Effect of interdomain dynamics on the structure determination of modular proteins by small-angle scattering
    • P. Bernadó Effect of interdomain dynamics on the structure determination of modular proteins by small-angle scattering Eur. Biophys. J. 39 2010 769 780
    • (2010) Eur. Biophys. J. , vol.39 , pp. 769-780
    • Bernadó, P.1
  • 36
    • 72449188596 scopus 로고    scopus 로고
    • NADPH oxidase activator p67(phox) behaves in solution as a multidomain protein with semi-flexible linkers
    • D. Durand, and C. Vivès F. Fieschi NADPH oxidase activator p67(phox) behaves in solution as a multidomain protein with semi-flexible linkers J. Struct. Biol. 169 2010 45 53
    • (2010) J. Struct. Biol. , vol.169 , pp. 45-53
    • Durand, D.1    Vivès, C.2    Fieschi, F.3
  • 37
    • 0345169163 scopus 로고    scopus 로고
    • Small-angle scattering: A view on the properties, structures and structural changes of biological macromolecules in solution
    • M.H.J. Koch, P. Vachette, and D.I. Svergun Small-angle scattering: a view on the properties, structures and structural changes of biological macromolecules in solution Q. Rev. Biophys. 36 2003 147 227
    • (2003) Q. Rev. Biophys. , vol.36 , pp. 147-227
    • Koch, M.H.J.1    Vachette, P.2    Svergun, D.I.3
  • 38
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • B.A. Griffin, S.R. Adams, and R.Y. Tsien Specific covalent labeling of recombinant protein molecules inside live cells Science 281 1998 269 272
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 39
    • 79959458043 scopus 로고    scopus 로고
    • Development of probes for cellular functions using fluorescent proteins and fluorescence resonance energy transfer
    • A. Miyawaki Development of probes for cellular functions using fluorescent proteins and fluorescence resonance energy transfer Annu. Rev. Biochem. 80 2011 357 373
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 357-373
    • Miyawaki, A.1
  • 40
    • 84862703323 scopus 로고    scopus 로고
    • Small molecule-based FRET probes
    • T. Gadella, Elsevier Amsterdam
    • A. Cobos Correa, and C. Schultz Small molecule-based FRET probes T. Gadella, FLIM and FRET 2008 Elsevier Amsterdam 225 288
    • (2008) FLIM and FRET , pp. 225-288
    • Cobos Correa, A.1    Schultz, C.2
  • 41
    • 53249113119 scopus 로고    scopus 로고
    • Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering
    • M. Cammarata, and M. Levantino H. Ihee Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering Nat. Methods 5 2008 881 886
    • (2008) Nat. Methods , vol.5 , pp. 881-886
    • Cammarata, M.1    Levantino, M.2    Ihee, H.3


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