메뉴 건너뛰기




Volumn 10, Issue 6, 2010, Pages 731-737

Fluorescence anisotropy and resonance energy transfer: Powerful tools for measuring real time protein dynamics in a physiological environment

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED DNA POLYMERASE BETA; MYOSIN; MYOSIN V;

EID: 78149498081     PISSN: 14714892     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.coph.2010.09.013     Document Type: Review
Times cited : (32)

References (76)
  • 1
    • 58249085344 scopus 로고    scopus 로고
    • Fluorescence approaches to quantifying biomolecular interactions
    • Royer C.A., Scarlata S.F. Fluorescence approaches to quantifying biomolecular interactions. Methods Enzymol 2008, 450:79-106.
    • (2008) Methods Enzymol , vol.450 , pp. 79-106
    • Royer, C.A.1    Scarlata, S.F.2
  • 2
    • 8344221191 scopus 로고    scopus 로고
    • Designing novel spectral classes of proteins with a tryptophan-expanded genetic code
    • Budisa N., Pal P.P. Designing novel spectral classes of proteins with a tryptophan-expanded genetic code. Biol Chem 2004, 385:893-904.
    • (2004) Biol Chem , vol.385 , pp. 893-904
    • Budisa, N.1    Pal, P.P.2
  • 3
    • 55849112685 scopus 로고    scopus 로고
    • Azatryptophans endow proteins with intrinsic blue fluorescence
    • Lepthien S., Hoesl M.G., Merkel L., Budisa N. Azatryptophans endow proteins with intrinsic blue fluorescence. Proc Natl Acad Sci USA 2008, 105:16095-16100.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 16095-16100
    • Lepthien, S.1    Hoesl, M.G.2    Merkel, L.3    Budisa, N.4
  • 4
    • 77049098842 scopus 로고    scopus 로고
    • Non-natural amino acid fluorophores for one- and two-step fluorescence resonance energy transfer applications. Anal Biochem
    • Rogers JM, Lippert LG, Gai F: Non-natural amino acid fluorophores for one- and two-step fluorescence resonance energy transfer applications. Anal Biochem 2010, 399:182-189.
    • (2010) , vol.399 , pp. 182-189
    • Rogers, J.M.1    Lippert, L.G.2    Gai, F.3
  • 5
    • 65549136134 scopus 로고    scopus 로고
    • Position-specific incorporation of fluorescent non-natural amino acids into maltose-binding protein for detection of ligand binding by FRET and fluorescence quenching
    • Iijima I., Hohsaka T. Position-specific incorporation of fluorescent non-natural amino acids into maltose-binding protein for detection of ligand binding by FRET and fluorescence quenching. Chembiochem 2009, 10:999-1006.
    • (2009) Chembiochem , vol.10 , pp. 999-1006
    • Iijima, I.1    Hohsaka, T.2
  • 6
    • 76649117121 scopus 로고    scopus 로고
    • Blue fluorescent amino acids as in vivo building blocks for proteins. Chembiochem
    • Merkel L, Hoesl MG, Albrecht M, Schmidt A, Budisa N: Blue fluorescent amino acids as in vivo building blocks for proteins. Chembiochem 2010, 11:305-314.
    • (2010) , vol.11 , pp. 305-314
    • Merkel, L.1    Hoesl, M.G.2    Albrecht, M.3    Schmidt, A.4    Budisa, N.5
  • 7
    • 33750324246 scopus 로고    scopus 로고
    • FRET analysis of protein conformational change through position-specific incorporation of fluorescent amino acids
    • Kajihara D., Abe R., Iijima I., Komiyama C., Sisido M., Hohsaka T. FRET analysis of protein conformational change through position-specific incorporation of fluorescent amino acids. Nat Methods 2006, 3:923-929.
    • (2006) Nat Methods , vol.3 , pp. 923-929
    • Kajihara, D.1    Abe, R.2    Iijima, I.3    Komiyama, C.4    Sisido, M.5    Hohsaka, T.6
  • 8
    • 67650741184 scopus 로고    scopus 로고
    • Non-natural amino acids. Preface
    • Muir T.W. Non-natural amino acids. Preface. Methods Enzymol 2009, 462:xiii-xv.
    • (2009) Methods Enzymol , vol.462
    • Muir, T.W.1
  • 11
    • 0034682824 scopus 로고    scopus 로고
    • Tryptophan 512 is sensitive to conformational changes in the rigid relay loop of smooth muscle myosin during the MgATPase cycle
    • Yengo C.M., Chrin L.R., Rovner A.S., Berger C.L. Tryptophan 512 is sensitive to conformational changes in the rigid relay loop of smooth muscle myosin during the MgATPase cycle. J Biol Chem 2000, 275:25481-25487.
    • (2000) J Biol Chem , vol.275 , pp. 25481-25487
    • Yengo, C.M.1    Chrin, L.R.2    Rovner, A.S.3    Berger, C.L.4
  • 13
    • 58149396567 scopus 로고    scopus 로고
    • Early closure of a long loop in the refolding of adenylate kinase: a possible key role of non-local interactions in the initial folding steps
    • Orevi T., Ben Ishay E., Pirchi M., Jacob M.H., Amir D., Haas E. Early closure of a long loop in the refolding of adenylate kinase: a possible key role of non-local interactions in the initial folding steps. J Mol Biol 2009, 385:1230-1242.
    • (2009) J Mol Biol , vol.385 , pp. 1230-1242
    • Orevi, T.1    Ben Ishay, E.2    Pirchi, M.3    Jacob, M.H.4    Amir, D.5    Haas, E.6
  • 15
    • 0036738673 scopus 로고    scopus 로고
    • Specific labeling of polypeptides at amino-terminal cysteine residues using Cy5-benzyl thioester
    • Schuler B., Pannell L.K. Specific labeling of polypeptides at amino-terminal cysteine residues using Cy5-benzyl thioester. Bioconjug Chem 2002, 13:1039-1043.
    • (2002) Bioconjug Chem , vol.13 , pp. 1039-1043
    • Schuler, B.1    Pannell, L.K.2
  • 17
  • 18
    • 0037140742 scopus 로고    scopus 로고
    • New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications
    • Adams S.R., Campbell R.E., Gross L.A., Martin B.R., Walkup G.K., Yao Y., Llopis J., Tsien R.Y. New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications. J Am Chem Soc 2002, 124:6063-6076.
    • (2002) J Am Chem Soc , vol.124 , pp. 6063-6076
    • Adams, S.R.1    Campbell, R.E.2    Gross, L.A.3    Martin, B.R.4    Walkup, G.K.5    Yao, Y.6    Llopis, J.7    Tsien, R.Y.8
  • 19
    • 0034581376 scopus 로고    scopus 로고
    • Fluorescent labeling of recombinant proteins in living cells with FlAsH
    • Griffin B.A., Adams S.R., Jones J., Tsien R.Y. Fluorescent labeling of recombinant proteins in living cells with FlAsH. Methods Enzymol 2000, 327:565-578.
    • (2000) Methods Enzymol , vol.327 , pp. 565-578
    • Griffin, B.A.1    Adams, S.R.2    Jones, J.3    Tsien, R.Y.4
  • 20
    • 33745213371 scopus 로고    scopus 로고
    • CrAsH: a biarsenical multi-use affinity probe with low non-specific fluorescence
    • Cao H., Chen B., Squier T.C., Mayer M.U. CrAsH: a biarsenical multi-use affinity probe with low non-specific fluorescence. Chem Commun (Camb) 2006, 2601-2603.
    • (2006) Chem Commun (Camb) , pp. 2601-2603
    • Cao, H.1    Chen, B.2    Squier, T.C.3    Mayer, M.U.4
  • 21
    • 34548457794 scopus 로고    scopus 로고
    • A red cy3-based biarsenical fluorescent probe targeted to a complementary binding peptide
    • Cao H., Xiong Y., Wang T., Chen B., Squier T.C., Mayer M.U. A red cy3-based biarsenical fluorescent probe targeted to a complementary binding peptide. J Am Chem Soc 2007, 129:8672-8673.
    • (2007) J Am Chem Soc , vol.129 , pp. 8672-8673
    • Cao, H.1    Xiong, Y.2    Wang, T.3    Chen, B.4    Squier, T.C.5    Mayer, M.U.6
  • 22
    • 34547218393 scopus 로고    scopus 로고
    • Identification of an orthogonal peptide binding motif for biarsenical multiuse affinity probes
    • Chen B., Cao H., Yan P., Mayer M.U., Squier T.C. Identification of an orthogonal peptide binding motif for biarsenical multiuse affinity probes. Bioconjug Chem 2007, 18:1259-1265.
    • (2007) Bioconjug Chem , vol.18 , pp. 1259-1265
    • Chen, B.1    Cao, H.2    Yan, P.3    Mayer, M.U.4    Squier, T.C.5
  • 23
    • 77953865084 scopus 로고    scopus 로고
    • Springer, New York, NY, J.R. Lakowicz (Ed.)
    • Principles of Fluorescence Spectroscopy 2006, Springer, New York, NY. edn 3. J.R. Lakowicz (Ed.).
    • (2006) Principles of Fluorescence Spectroscopy
  • 24
    • 0036176741 scopus 로고    scopus 로고
    • FRET tells us about proximities, distances, orientations and dynamic properties
    • Clegg R.M. FRET tells us about proximities, distances, orientations and dynamic properties. J Biotechnol 2002, 82:177-179.
    • (2002) J Biotechnol , vol.82 , pp. 177-179
    • Clegg, R.M.1
  • 25
    • 0034807927 scopus 로고    scopus 로고
    • Single-molecule fluorescence resonance energy transfer
    • Ha T. Single-molecule fluorescence resonance energy transfer. Methods 2001, 25:78-86.
    • (2001) Methods , vol.25 , pp. 78-86
    • Ha, T.1
  • 26
    • 0001605715 scopus 로고
    • Intramolecular energy transfer and molecular conformation
    • Dale R.E., Eisinger J. Intramolecular energy transfer and molecular conformation. Proc Natl Acad Sci USA 1976, 73:271-273.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 271-273
    • Dale, R.E.1    Eisinger, J.2
  • 27
    • 0018464261 scopus 로고
    • The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer
    • Dale R.E., Eisinger J., Blumberg W.E. The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer. Biophys J 1979, 26:161-193.
    • (1979) Biophys J , vol.26 , pp. 161-193
    • Dale, R.E.1    Eisinger, J.2    Blumberg, W.E.3
  • 28
    • 18744389451 scopus 로고    scopus 로고
    • The study of protein folding and dynamics by determination of intramolecular distance distributions and their fluctuations using ensemble and single-molecule FRET measurements
    • Haas E. The study of protein folding and dynamics by determination of intramolecular distance distributions and their fluctuations using ensemble and single-molecule FRET measurements. Chemphyschem 2005, 6:858-870.
    • (2005) Chemphyschem , vol.6 , pp. 858-870
    • Haas, E.1
  • 29
    • 57649123142 scopus 로고    scopus 로고
    • Structural studies of interactions between cardiac troponin I and actin in regulated thin filament using Forster resonance energy transfer
    • Xing J., Chinnaraj M., Zhang Z., Cheung H.C., Dong W.J. Structural studies of interactions between cardiac troponin I and actin in regulated thin filament using Forster resonance energy transfer. Biochemistry 2008, 47:13383-13393.
    • (2008) Biochemistry , vol.47 , pp. 13383-13393
    • Xing, J.1    Chinnaraj, M.2    Zhang, Z.3    Cheung, H.C.4    Dong, W.J.5
  • 30
    • 33747623305 scopus 로고    scopus 로고
    • End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation
    • Moglich A., Joder K., Kiefhaber T. End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation. Proc Natl Acad Sci USA 2006, 103:12394-12399.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 12394-12399
    • Moglich, A.1    Joder, K.2    Kiefhaber, T.3
  • 31
    • 65249086776 scopus 로고    scopus 로고
    • Time-resolved fluorescence resonance energy transfer study shows a compact denatured state of the B domain of protein A
    • Huang F., Lerner E., Sato S., Amir D., Haas E., Fersht A.R. Time-resolved fluorescence resonance energy transfer study shows a compact denatured state of the B domain of protein A. Biochemistry 2009, 48:3468-3476.
    • (2009) Biochemistry , vol.48 , pp. 3468-3476
    • Huang, F.1    Lerner, E.2    Sato, S.3    Amir, D.4    Haas, E.5    Fersht, A.R.6
  • 32
    • 0038279986 scopus 로고    scopus 로고
    • Alpha-synuclein: its biological function and role in neurodegenerative diseases
    • Kaplan B., Ratner V., Haas E. Alpha-synuclein: its biological function and role in neurodegenerative diseases. J Mol Neurosci 2003, 20:83-92.
    • (2003) J Mol Neurosci , vol.20 , pp. 83-92
    • Kaplan, B.1    Ratner, V.2    Haas, E.3
  • 33
    • 0028243146 scopus 로고
    • Characterization of the three tyrosine residues of delta 5-3-ketosteroid isomerase by time-resolved fluorescence and circular dichroism
    • Wu P., Li Y.K., Talalay P., Brand L. Characterization of the three tyrosine residues of delta 5-3-ketosteroid isomerase by time-resolved fluorescence and circular dichroism. Biochemistry 1994, 33:7415-7422.
    • (1994) Biochemistry , vol.33 , pp. 7415-7422
    • Wu, P.1    Li, Y.K.2    Talalay, P.3    Brand, L.4
  • 34
    • 0027728948 scopus 로고
    • Compact thermally-denatured state of a staphylococcal nuclease mutant from resonance energy transfer measurements
    • Wu P.G., James E., Brand L. Compact thermally-denatured state of a staphylococcal nuclease mutant from resonance energy transfer measurements. Biophys Chem 1993, 48:123-133.
    • (1993) Biophys Chem , vol.48 , pp. 123-133
    • Wu, P.G.1    James, E.2    Brand, L.3
  • 37
    • 0034705335 scopus 로고    scopus 로고
    • Determination of intramolecular distance distribution during protein folding on the millisecond timescale
    • Ratner V., Sinev M., Haas E. Determination of intramolecular distance distribution during protein folding on the millisecond timescale. J Mol Biol 2000, 299:1363-1371.
    • (2000) J Mol Biol , vol.299 , pp. 1363-1371
    • Ratner, V.1    Sinev, M.2    Haas, E.3
  • 38
    • 0036071848 scopus 로고    scopus 로고
    • The natively helical chain segment 169-188 of Escherichia coli adenylate kinase is formed in the latest phase of the refolding transition
    • Ratner V., Kahana E., Haas E. The natively helical chain segment 169-188 of Escherichia coli adenylate kinase is formed in the latest phase of the refolding transition. J Mol Biol 2002, 320:1135-1145.
    • (2002) J Mol Biol , vol.320 , pp. 1135-1145
    • Ratner, V.1    Kahana, E.2    Haas, E.3
  • 39
    • 77249095424 scopus 로고    scopus 로고
    • Fluorescence anisotropy: from single molecules to live cells. Analyst
    • Gradinaru CC, Marushchak DO, Samim M, Krull UJ: Fluorescence anisotropy: from single molecules to live cells. Analyst 2010, 135:452-459.
    • (2010) , vol.135 , pp. 452-459
    • Gradinaru, C.C.1    Marushchak, D.O.2    Samim, M.3    Krull, U.J.4
  • 40
    • 77956213053 scopus 로고    scopus 로고
    • Dynamic fluorescence depolarization: a powerful tool to explore protein folding on the ribosome
    • Weinreis S.A., Ellis J.P., Cavagnero S. Dynamic fluorescence depolarization: a powerful tool to explore protein folding on the ribosome. Methods 2010, 52:57-73.
    • (2010) Methods , vol.52 , pp. 57-73
    • Weinreis, S.A.1    Ellis, J.P.2    Cavagnero, S.3
  • 41
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • Roy R., Hohng S., Ha T. A practical guide to single-molecule FRET. Nat Methods 2008, 5:507-516.
    • (2008) Nat Methods , vol.5 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 42
    • 78049249328 scopus 로고    scopus 로고
    • Surfing on a new wave of single-molecule fluorescence methods. Phys Biol
    • Hohlbein J, Gryte K, Heilemann M, Kapanidis AN: Surfing on a new wave of single-molecule fluorescence methods. Phys Biol 2010, 7:031001.
    • (2010) , vol.7 , pp. 031001
    • Hohlbein, J.1    Gryte, K.2    Heilemann, M.3    Kapanidis, A.N.4
  • 44
    • 39149087014 scopus 로고    scopus 로고
    • Protein folding studied by single-molecule FRET
    • Schuler B., Eaton W.A. Protein folding studied by single-molecule FRET. Curr Opin Struct Biol 2008, 18:16-26.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 16-26
    • Schuler, B.1    Eaton, W.A.2
  • 46
    • 77957089197 scopus 로고    scopus 로고
    • Droplet confinement and fluorescence measurement of single molecules. Methods Enzymol
    • Goldner LS, Jofre AM, Tang J: Droplet confinement and fluorescence measurement of single molecules. Methods Enzymol 2010, 472:61-88.
    • (2010) , vol.472 , pp. 61-88
    • Goldner, L.S.1    Jofre, A.M.2    Tang, J.3
  • 48
    • 22244467998 scopus 로고    scopus 로고
    • Single-molecule enzymology of chymotrypsin using water-in-oil emulsion
    • Lee A.I., Brody J.P. Single-molecule enzymology of chymotrypsin using water-in-oil emulsion. Biophys J 2005, 88:4303-4311.
    • (2005) Biophys J , vol.88 , pp. 4303-4311
    • Lee, A.I.1    Brody, J.P.2
  • 49
    • 23744433971 scopus 로고    scopus 로고
    • Surfaces and orientations: much to FRET about?
    • Rasnik I., McKinney S.A., Ha T. Surfaces and orientations: much to FRET about?. Acc Chem Res 2005, 38:542-548.
    • (2005) Acc Chem Res , vol.38 , pp. 542-548
    • Rasnik, I.1    McKinney, S.A.2    Ha, T.3
  • 50
    • 33846839535 scopus 로고    scopus 로고
    • Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations
    • Merchant K.A., Best R.B., Louis J.M., Gopich I.V., Eaton W.A. Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations. Proc Natl Acad Sci USA 2007, 104:1528-1533.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1528-1533
    • Merchant, K.A.1    Best, R.B.2    Louis, J.M.3    Gopich, I.V.4    Eaton, W.A.5
  • 51
    • 8544278025 scopus 로고    scopus 로고
    • DNA polymerase fidelity: kinetics, structure, and checkpoints
    • Joyce C.M., Benkovic S.J. DNA polymerase fidelity: kinetics, structure, and checkpoints. Biochemistry 2004, 43:14317-14324.
    • (2004) Biochemistry , vol.43 , pp. 14317-14324
    • Joyce, C.M.1    Benkovic, S.J.2
  • 52
    • 44949114390 scopus 로고    scopus 로고
    • Fingers-closing and other rapid conformational changes in DNA polymerase I (Klenow fragment) and their role in nucleotide selectivity
    • Joyce C.M., Potapova O., Delucia A.M., Huang X., Basu V.P., Grindley N.D. Fingers-closing and other rapid conformational changes in DNA polymerase I (Klenow fragment) and their role in nucleotide selectivity. Biochemistry 2008, 47:6103-6116.
    • (2008) Biochemistry , vol.47 , pp. 6103-6116
    • Joyce, C.M.1    Potapova, O.2    Delucia, A.M.3    Huang, X.4    Basu, V.P.5    Grindley, N.D.6
  • 53
    • 23044492225 scopus 로고    scopus 로고
    • Motions of the fingers subdomain of klentaq1 are fast and not rate limiting: implications for the molecular basis of fidelity in DNA polymerases
    • Rothwell P.J., Mitaksov V., Waksman G. Motions of the fingers subdomain of klentaq1 are fast and not rate limiting: implications for the molecular basis of fidelity in DNA polymerases. Mol Cell 2005, 19:345-355.
    • (2005) Mol Cell , vol.19 , pp. 345-355
    • Rothwell, P.J.1    Mitaksov, V.2    Waksman, G.3
  • 54
    • 77955283864 scopus 로고    scopus 로고
    • Structure and dynamics of the kinesin-microtubule interaction revealed by fluorescence polarization microscopy. Methods Cell Biol
    • Sosa H, Asenjo AB, Peterman EJ: Structure and dynamics of the kinesin-microtubule interaction revealed by fluorescence polarization microscopy. Methods Cell Biol 2010, 95:505-519.
    • (2010) , vol.95 , pp. 505-519
    • Sosa, H.1    Asenjo, A.B.2    Peterman, E.J.3
  • 55
    • 0034995132 scopus 로고    scopus 로고
    • ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy
    • Sosa H., Peterman E.J., Moerner W.E., Goldstein L.S. ADP-induced rocking of the kinesin motor domain revealed by single-molecule fluorescence polarization microscopy. Nat Struct Biol 2001, 8:540-544.
    • (2001) Nat Struct Biol , vol.8 , pp. 540-544
    • Sosa, H.1    Peterman, E.J.2    Moerner, W.E.3    Goldstein, L.S.4
  • 56
    • 23244457898 scopus 로고    scopus 로고
    • Rotational motions of macro-molecules by single-molecule fluorescence microscopy
    • Rosenberg S.A., Quinlan M.E., Forkey J.N., Goldman Y.E. Rotational motions of macro-molecules by single-molecule fluorescence microscopy. Acc Chem Res 2005, 38:583-593.
    • (2005) Acc Chem Res , vol.38 , pp. 583-593
    • Rosenberg, S.A.1    Quinlan, M.E.2    Forkey, J.N.3    Goldman, Y.E.4
  • 58
    • 77950520992 scopus 로고    scopus 로고
    • Single-molecule stepping and structural dynamics of myosin X. Nat Struct Mol Biol
    • Sun Y, Sato O, Ruhnow F, Arsenault ME, Ikebe M, Goldman YE: Single-molecule stepping and structural dynamics of myosin X. Nat Struct Mol Biol 2010, 17:485-491.
    • (2010) , vol.17 , pp. 485-491
    • Sun, Y.1    Sato, O.2    Ruhnow, F.3    Arsenault, M.E.4    Ikebe, M.5    Goldman, Y.E.6
  • 59
    • 23244466867 scopus 로고    scopus 로고
    • Measurement of single macromolecule orientation by total internal reflection fluorescence polarization microscopy
    • Forkey J.N., Quinlan M.E., Goldman Y.E. Measurement of single macromolecule orientation by total internal reflection fluorescence polarization microscopy. Biophys J 2005, 89:1261-1271.
    • (2005) Biophys J , vol.89 , pp. 1261-1271
    • Forkey, J.N.1    Quinlan, M.E.2    Goldman, Y.E.3
  • 60
    • 0037468838 scopus 로고    scopus 로고
    • Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization
    • Forkey J.N., Quinlan M.E., Shaw M.A., Corrie J.E., Goldman Y.E. Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization. Nature 2003, 422:399-404.
    • (2003) Nature , vol.422 , pp. 399-404
    • Forkey, J.N.1    Quinlan, M.E.2    Shaw, M.A.3    Corrie, J.E.4    Goldman, Y.E.5
  • 62
    • 77954277170 scopus 로고    scopus 로고
    • Advances in cellular, subcellular, and nanoscale imaging in vitro and in vivo. Cytometry A
    • Wessels JT, Yamauchi K, Hoffman RM, Wouters FS: Advances in cellular, subcellular, and nanoscale imaging in vitro and in vivo. Cytometry A 2010, 77:667-676.
    • (2010) , vol.77 , pp. 667-676
    • Wessels, J.T.1    Yamauchi, K.2    Hoffman, R.M.3    Wouters, F.S.4
  • 63
    • 60549108756 scopus 로고    scopus 로고
    • Intracellular regions of potassium channels: Kv2.1 and heag
    • Wray D. Intracellular regions of potassium channels: Kv2.1 and heag. Eur Biophys J 2009, 38:285-292.
    • (2009) Eur Biophys J , vol.38 , pp. 285-292
    • Wray, D.1
  • 64
    • 4143091363 scopus 로고    scopus 로고
    • Voltage-gated rearrangements associated with differential beta-subunit modulation of the L-type Ca(2+) channel inactivation
    • Kobrinsky E., Kepplinger K.J., Yu A., Harry J.B., Kahr H., Romanin C., Abernethy D.R., Soldatov N.M. Voltage-gated rearrangements associated with differential beta-subunit modulation of the L-type Ca(2+) channel inactivation. Biophys J 2004, 87:844-857.
    • (2004) Biophys J , vol.87 , pp. 844-857
    • Kobrinsky, E.1    Kepplinger, K.J.2    Yu, A.3    Harry, J.B.4    Kahr, H.5    Romanin, C.6    Abernethy, D.R.7    Soldatov, N.M.8
  • 65
    • 77955947356 scopus 로고    scopus 로고
    • Live cell imaging of mechanotransduction. J R Soc Interface
    • Liu B, Kim TJ, Wang Y: Live cell imaging of mechanotransduction. J R Soc Interface 2010, 7 (Suppl 3):S365-375.
    • (2010) , vol.7 , Issue.SUPPL 3
    • Liu, B.1    Kim, T.J.2    Wang, Y.3
  • 66
    • 69349095079 scopus 로고    scopus 로고
    • Structural changes in the cytoplasmic domain of the mechanosensitive channel MscS during opening
    • Machiyama H., Tatsumi H., Sokabe M. Structural changes in the cytoplasmic domain of the mechanosensitive channel MscS during opening. Biophys J 2009, 97:1048-1057.
    • (2009) Biophys J , vol.97 , pp. 1048-1057
    • Machiyama, H.1    Tatsumi, H.2    Sokabe, M.3
  • 67
    • 77952386724 scopus 로고    scopus 로고
    • Dynamic, inter-subunit interactions between the N-terminal and central mutation regions of cardiac ryanodine receptor. J Cell Sci
    • Liu Z, Wang R, Tian X, Zhong X, Gangopadhyay J, Cole R, Ikemoto N, Chen SR, Wagenknecht T: Dynamic, inter-subunit interactions between the N-terminal and central mutation regions of cardiac ryanodine receptor. J Cell Sci 2010, 123:1775-1784.
    • (2010) , vol.123 , pp. 1775-1784
    • Liu, Z.1    Wang, R.2    Tian, X.3    Zhong, X.4    Gangopadhyay, J.5    Cole, R.6    Ikemoto, N.7    Chen, S.R.8    Wagenknecht, T.9
  • 68
    • 34548417621 scopus 로고    scopus 로고
    • Fluorescent protein FRET: the good, the bad and the ugly
    • Piston D.W., Kremers G.J. Fluorescent protein FRET: the good, the bad and the ugly. Trends Biochem Sci 2007, 32:407-414.
    • (2007) Trends Biochem Sci , vol.32 , pp. 407-414
    • Piston, D.W.1    Kremers, G.J.2
  • 69
    • 70349200987 scopus 로고    scopus 로고
    • Investigating biological processes at the single molecule level using luminescent quantum dots
    • Pons T., Mattoussi H. Investigating biological processes at the single molecule level using luminescent quantum dots. Ann Biomed Eng 2009, 37:1934-1959.
    • (2009) Ann Biomed Eng , vol.37 , pp. 1934-1959
    • Pons, T.1    Mattoussi, H.2
  • 70
    • 68949125193 scopus 로고    scopus 로고
    • Random walk of processive, quantum dot-labeled myosin Va molecules within the actin cortex of COS-7 cells
    • Nelson S.R., Ali M.Y., Trybus K.M., Warshaw D.M. Random walk of processive, quantum dot-labeled myosin Va molecules within the actin cortex of COS-7 cells. Biophys J 2009, 97:509-518.
    • (2009) Biophys J , vol.97 , pp. 509-518
    • Nelson, S.R.1    Ali, M.Y.2    Trybus, K.M.3    Warshaw, D.M.4
  • 71
    • 0347004717 scopus 로고    scopus 로고
    • Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling
    • Ignatova Z., Gierasch L.M. Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. Proc Natl Acad Sci USA 2004, 101:523-528.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 523-528
    • Ignatova, Z.1    Gierasch, L.M.2
  • 72
    • 0035794242 scopus 로고    scopus 로고
    • In vitro and in vivo ligand binding to the 5HT(3) serotonin receptor characterised by time-resolved fluorescence spectroscopy
    • Vallotton P., Hovius R., Pick H., Vogel H. In vitro and in vivo ligand binding to the 5HT(3) serotonin receptor characterised by time-resolved fluorescence spectroscopy. Chembiochem 2001, 2:205-211.
    • (2001) Chembiochem , vol.2 , pp. 205-211
    • Vallotton, P.1    Hovius, R.2    Pick, H.3    Vogel, H.4
  • 73
    • 34548764387 scopus 로고    scopus 로고
    • Measuring rotational diffusion of MHC class I on live cells by polarized FPR
    • Fooksman D.R., Edidin M., Barisas B.G. Measuring rotational diffusion of MHC class I on live cells by polarized FPR. Biophys Chem 2007, 130:10-16.
    • (2007) Biophys Chem , vol.130 , pp. 10-16
    • Fooksman, D.R.1    Edidin, M.2    Barisas, B.G.3
  • 75
    • 54749125459 scopus 로고    scopus 로고
    • A cellular conformation-based screen for androgen receptor inhibitors
    • Jones J.O., Diamond M.I. A cellular conformation-based screen for androgen receptor inhibitors. ACS Chem Biol 2008, 3:412-418.
    • (2008) ACS Chem Biol , vol.3 , pp. 412-418
    • Jones, J.O.1    Diamond, M.I.2
  • 76
    • 65249166947 scopus 로고    scopus 로고
    • AR inhibitors identified by high-throughput microscopy detection of conformational change and subcellular localization
    • Jones J.O., An W.F., Diamond M.I. AR inhibitors identified by high-throughput microscopy detection of conformational change and subcellular localization. ACS Chem Biol 2009, 4:199-208.
    • (2009) ACS Chem Biol , vol.4 , pp. 199-208
    • Jones, J.O.1    An, W.F.2    Diamond, M.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.