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Volumn 1763, Issue 5-6, 2006, Pages 561-575

High resolution imaging of live mitochondria

Author keywords

FLIP; Fluorescence microscopy; FRAP; Fusion assay; Mitochondria; Photoactivation; Self labeling protein tag

Indexed keywords

FLUORESCENT DYE; HYBRID PROTEIN; MITOCHONDRIAL PROTEIN;

EID: 33745750949     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2006.04.004     Document Type: Review
Times cited : (117)

References (193)
  • 1
    • 0015847803 scopus 로고
    • Mitochondrion of yeast: Ultrastructural evidence for one giant, branched organelle per cell
    • Hoffmann H.P., and Avers C.J. Mitochondrion of yeast: Ultrastructural evidence for one giant, branched organelle per cell. Science 181 (1973) 749-751
    • (1973) Science , vol.181 , pp. 749-751
    • Hoffmann, H.P.1    Avers, C.J.2
  • 2
    • 0028047262 scopus 로고
    • Dynamics of mitochondria in living cells: shape changes, dislocations, fusion, and fission of mitochondria
    • Bereiter-Hahn J., and Voth M. Dynamics of mitochondria in living cells: shape changes, dislocations, fusion, and fission of mitochondria. Microsc. Res. Tech. 27 (1994) 198-219
    • (1994) Microsc. Res. Tech. , vol.27 , pp. 198-219
    • Bereiter-Hahn, J.1    Voth, M.2
  • 3
    • 0030841103 scopus 로고    scopus 로고
    • Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA
    • Nunnari J., Marshall W.F., Straight A., Murray A., Sedat J.W., and Walter P. Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA. Mol. Biol. Cell 8 (1997) 1233-1242
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1233-1242
    • Nunnari, J.1    Marshall, W.F.2    Straight, A.3    Murray, A.4    Sedat, J.W.5    Walter, P.6
  • 4
    • 33745736330 scopus 로고    scopus 로고
    • Mitochondrial membrane dynamics, cristae remodelling and apoptosis
    • Heath-Engel H.M., and Shore G.C. Mitochondrial membrane dynamics, cristae remodelling and apoptosis. Biochim. Biophys. Acta 1763 (2006) 549-560
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 549-560
    • Heath-Engel, H.M.1    Shore, G.C.2
  • 5
    • 0037418906 scopus 로고    scopus 로고
    • Light microscopy techniques for live cell imaging
    • Stephens D.J., and Allan V.J. Light microscopy techniques for live cell imaging. Science 300 (2003) 82-86
    • (2003) Science , vol.300 , pp. 82-86
    • Stephens, D.J.1    Allan, V.J.2
  • 7
    • 0343090208 scopus 로고    scopus 로고
    • Slow fluorescent indicators of membrane potential: a survey of different approaches to probe response analysis
    • Plasek J., and Sigler K. Slow fluorescent indicators of membrane potential: a survey of different approaches to probe response analysis. J. Photochem. Photobiol., B 33 (1996) 101-124
    • (1996) J. Photochem. Photobiol., B , vol.33 , pp. 101-124
    • Plasek, J.1    Sigler, K.2
  • 8
    • 0035229641 scopus 로고    scopus 로고
    • Assessment of mitochondrial membrane potential in situ using single potentiometric dyes and a novel fluorescence resonance energy transfer technique
    • Dykens J.A., and Stout A.K. Assessment of mitochondrial membrane potential in situ using single potentiometric dyes and a novel fluorescence resonance energy transfer technique. Methods Cell Biol. 65 (2001) 285-309
    • (2001) Methods Cell Biol. , vol.65 , pp. 285-309
    • Dykens, J.A.1    Stout, A.K.2
  • 9
    • 0037286364 scopus 로고    scopus 로고
    • Imaging mitochondrial function in intact cells
    • Duchen M.R., Surin A., and Jacobson J. Imaging mitochondrial function in intact cells. Methods Enzymol. 361 (2003) 353-389
    • (2003) Methods Enzymol. , vol.361 , pp. 353-389
    • Duchen, M.R.1    Surin, A.2    Jacobson, J.3
  • 10
    • 0032538051 scopus 로고    scopus 로고
    • Quantitative assay by flow cytometry of the mitochondrial membrane potential in intact cells
    • Rottenberg H., and Wu S. Quantitative assay by flow cytometry of the mitochondrial membrane potential in intact cells. Biochim. Biophys. Acta 1404 (1998) 393-404
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 393-404
    • Rottenberg, H.1    Wu, S.2
  • 11
    • 0030612749 scopus 로고    scopus 로고
    • 6(3) or rhodamine 123, is a reliable fluorescent probe to assess delta psi changes in intact cells: implications for studies on mitochondrial functionality during apoptosis
    • 6(3) or rhodamine 123, is a reliable fluorescent probe to assess delta psi changes in intact cells: implications for studies on mitochondrial functionality during apoptosis. FEBS Lett. 411 (1997) 77-82
    • (1997) FEBS Lett. , vol.411 , pp. 77-82
    • Salvioli, S.1    Ardizzoni, A.2    Franceschi, C.3    Cossarizza, A.4
  • 12
    • 0034017782 scopus 로고    scopus 로고
    • Evaluation of fluorescent dyes for the detection of mitochondrial membrane potential changes in cultured cardiomyocytes
    • Mathur A., Hong Y., Kemp B.K., Barrientos A.A., and Erusalimsky J.D. Evaluation of fluorescent dyes for the detection of mitochondrial membrane potential changes in cultured cardiomyocytes. Cardiovasc. Res. 46 (2000) 126-138
    • (2000) Cardiovasc. Res. , vol.46 , pp. 126-138
    • Mathur, A.1    Hong, Y.2    Kemp, B.K.3    Barrientos, A.A.4    Erusalimsky, J.D.5
  • 14
    • 0021260735 scopus 로고
    • Hydrophobic acridine dyes for fluorescence staining of mitochondria in living cells. 2. Comparison of staining of living and fixed HeLa-cells with NAO and DPPAO
    • Erbrich U., Septinus M., Naujok A., and Zimmermann H.W. Hydrophobic acridine dyes for fluorescence staining of mitochondria in living cells. 2. Comparison of staining of living and fixed HeLa-cells with NAO and DPPAO. Histochemistry 80 (1984) 385-398
    • (1984) Histochemistry , vol.80 , pp. 385-398
    • Erbrich, U.1    Septinus, M.2    Naujok, A.3    Zimmermann, H.W.4
  • 15
    • 0023928504 scopus 로고
    • Membrane potential can be determined in individual cells from the nernstian distribution of cationic dyes
    • Ehrenberg B., Montana V., Wei M.D., Wuskell J.P., and Loew L.M. Membrane potential can be determined in individual cells from the nernstian distribution of cationic dyes. Biophys. J. 53 (1988) 785-894
    • (1988) Biophys. J. , vol.53 , pp. 785-894
    • Ehrenberg, B.1    Montana, V.2    Wei, M.D.3    Wuskell, J.P.4    Loew, L.M.5
  • 16
    • 34548576414 scopus 로고
    • Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea
    • Shimomura O., Johnson F.H., and Saiga Y. Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. J. Cell. Comp. Physiol. 59 (1962) 223-239
    • (1962) J. Cell. Comp. Physiol. , vol.59 , pp. 223-239
    • Shimomura, O.1    Johnson, F.H.2    Saiga, Y.3
  • 19
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie M., Tu Y., Euskirchen G., Ward W.W., and Prasher D.C. 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    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 20
    • 0028777967 scopus 로고
    • Aequorea green fluorescent protein. Expression of the gene and fluorescence characteristics of the recombinant protein
    • Inouye S., and Tsuji F.I. Aequorea green fluorescent protein. Expression of the gene and fluorescence characteristics of the recombinant protein. FEBS Lett. 341 (1994) 277-280
    • (1994) FEBS Lett. , vol.341 , pp. 277-280
    • Inouye, S.1    Tsuji, F.I.2
  • 21
    • 0029311281 scopus 로고
    • Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells
    • Rizzuto R., Brini M., Pizzo P., Murgia M., and Pozzan T. Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells. Curr. Biol. 5 (1995) 635-642
    • (1995) Curr. Biol. , vol.5 , pp. 635-642
    • Rizzuto, R.1    Brini, M.2    Pizzo, P.3    Murgia, M.4    Pozzan, T.5
  • 22
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner N.C., Campbell R.E., Steinbach P.A., Giepmans B.N., Palmer A.E., and Tsien R.Y. Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat. Biotechnol. 22 (2004) 1567-1572
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5    Tsien, R.Y.6
  • 23
    • 27944475132 scopus 로고    scopus 로고
    • Fluorescent proteins as a toolkit for in vivo imaging
    • Chudakov D.M., Lukyanov S., and Lukyanov K.A. Fluorescent proteins as a toolkit for in vivo imaging. Trends Biotechnol. 23 (2005) 605-613
    • (2005) Trends Biotechnol. , vol.23 , pp. 605-613
    • Chudakov, D.M.1    Lukyanov, S.2    Lukyanov, K.A.3
  • 24
    • 3042591096 scopus 로고    scopus 로고
    • Cross-linking ATP synthase complexes in vivo eliminates mitochondrial cristae
    • Gavin P.D., Prescott M., Luff S.E., and Devenish R.J. Cross-linking ATP synthase complexes in vivo eliminates mitochondrial cristae. J. Cell Sci. 117 (2004) 2333-2343
    • (2004) J. Cell Sci. , vol.117 , pp. 2333-2343
    • Gavin, P.D.1    Prescott, M.2    Luff, S.E.3    Devenish, R.J.4
  • 26
  • 29
    • 0031885535 scopus 로고    scopus 로고
    • Green fluorescent protein as a noninvasive intracellular pH indicator
    • Kneen M., Farinas J., Li Y., and Verkman A.S. Green fluorescent protein as a noninvasive intracellular pH indicator. Biophys. J. 74 (1998) 1591-1599
    • (1998) Biophys. J. , vol.74 , pp. 1591-1599
    • Kneen, M.1    Farinas, J.2    Li, Y.3    Verkman, A.S.4
  • 30
    • 0032499784 scopus 로고    scopus 로고
    • Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins
    • Llopis J., McCaffery J.M., Miyawaki A., Farquhar M.G., and Tsien R.Y. Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 6803-6808
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6803-6808
    • Llopis, J.1    McCaffery, J.M.2    Miyawaki, A.3    Farquhar, M.G.4    Tsien, R.Y.5
  • 31
    • 1642483415 scopus 로고    scopus 로고
    • Mitochondrial pH monitored by a new engineered green fluorescent protein mutant
    • Abad M.F., Di Benedetto G., Magalhaes P.J., Filippin L., and Pozzan T. Mitochondrial pH monitored by a new engineered green fluorescent protein mutant. J. Biol. Chem. 279 (2004) 11521-11529
    • (2004) J. Biol. Chem. , vol.279 , pp. 11521-11529
    • Abad, M.F.1    Di Benedetto, G.2    Magalhaes, P.J.3    Filippin, L.4    Pozzan, T.5
  • 32
    • 10644280072 scopus 로고    scopus 로고
    • pH difference across the outer mitochondrial membrane measured with a green fluorescent protein mutant
    • Porcelli A.M., Ghelli A., Zanna C., Pinton P., Rizzuto R., and Rugolo M. pH difference across the outer mitochondrial membrane measured with a green fluorescent protein mutant. Biochem. Biophys. Res. Commun. 326 (2005) 799-804
    • (2005) Biochem. Biophys. Res. Commun. , vol.326 , pp. 799-804
    • Porcelli, A.M.1    Ghelli, A.2    Zanna, C.3    Pinton, P.4    Rizzuto, R.5    Rugolo, M.6
  • 33
  • 38
    • 4744340701 scopus 로고    scopus 로고
    • Mitochondriomics or what makes us breathe
    • Reichert A.S., and Neupert W. Mitochondriomics or what makes us breathe. Trends Genet. 20 (2004) 555-562
    • (2004) Trends Genet. , vol.20 , pp. 555-562
    • Reichert, A.S.1    Neupert, W.2
  • 40
    • 0141683553 scopus 로고    scopus 로고
    • A fusion of disciplines: chemical approaches to exploit fusion proteins for functional genomics
    • Johnsson N., and Johnsson K. A fusion of disciplines: chemical approaches to exploit fusion proteins for functional genomics. ChemBioChem 4 (2003) 803-810
    • (2003) ChemBioChem , vol.4 , pp. 803-810
    • Johnsson, N.1    Johnsson, K.2
  • 41
    • 13844276672 scopus 로고    scopus 로고
    • Site-specific labeling of proteins with small molecules in live cells
    • Chen I., and Ting A.Y. Site-specific labeling of proteins with small molecules in live cells. Curr. Opin. Biotechnol. 16 (2005) 35-40
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 35-40
    • Chen, I.1    Ting, A.Y.2
  • 42
    • 23444448243 scopus 로고    scopus 로고
    • Adding value to fusion proteins through covalent labelling
    • Gronemeyer T., Godin G., and Johnsson K. Adding value to fusion proteins through covalent labelling. Curr. Opin. Biotechnol. 16 (2005) 453-458
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 453-458
    • Gronemeyer, T.1    Godin, G.2    Johnsson, K.3
  • 43
    • 13444261101 scopus 로고    scopus 로고
    • Selective chemical labeling of proteins in living cells
    • Miller L.W., and Cornish V.W. Selective chemical labeling of proteins in living cells. Curr. Opin. Chem. Biol. 9 (2005) 56-61
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 56-61
    • Miller, L.W.1    Cornish, V.W.2
  • 45
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin B.A., Adams S.R., and Tsien R.Y. Specific covalent labeling of recombinant protein molecules inside live cells. Science 281 (1998) 269-672
    • (1998) Science , vol.281 , pp. 269-672
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 48
    • 9444247617 scopus 로고    scopus 로고
    • Short tetracysteine tags to beta-tubulin demonstrate the significance of small labels for live cell imaging
    • Andresen M., Schmitz-Salue R., and Jakobs S. Short tetracysteine tags to beta-tubulin demonstrate the significance of small labels for live cell imaging. Mol. Biol. Cell 15 (2004) 5616-5622
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5616-5622
    • Andresen, M.1    Schmitz-Salue, R.2    Jakobs, S.3
  • 50
    • 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., and 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. 124 (2002) 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
  • 51
    • 0034802605 scopus 로고    scopus 로고
    • 2 binds not only to CCXXCC motifs but also non-specifically to endogenous cysteine-rich proteins
    • 2 binds not only to CCXXCC motifs but also non-specifically to endogenous cysteine-rich proteins. Pflugers Arch. 442 (2001) 859-866
    • (2001) Pflugers Arch. , vol.442 , pp. 859-866
    • Stroffekova, K.1    Proenza, C.2    Beam, K.G.3
  • 52
    • 27144448780 scopus 로고    scopus 로고
    • Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity
    • Martin B.R., Giepmans B.N., Adams S.R., and Tsien R.Y. Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity. Nat. Biotechnol. 23 (2005) 1308-1314
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1308-1314
    • Martin, B.R.1    Giepmans, B.N.2    Adams, S.R.3    Tsien, R.Y.4
  • 53
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • Keppler A., Gendreizig S., Gronemeyer T., Pick H., Vogel H., and Johnsson K. A general method for the covalent labeling of fusion proteins with small molecules in vivo. Nat. Biotechnol. 21 (2003) 86-89
    • (2003) Nat. Biotechnol. , vol.21 , pp. 86-89
    • Keppler, A.1    Gendreizig, S.2    Gronemeyer, T.3    Pick, H.4    Vogel, H.5    Johnsson, K.6
  • 54
    • 0037399074 scopus 로고    scopus 로고
    • Directed evolution of o6-alkylguanine-DNA alkyltransferase for efficient labeling of fusion proteins with small molecules in vivo
    • Juillerat A., Gronemeyer T., Keppler A., Gendreizig S., Pick H., Vogel H., and Johnsson K. Directed evolution of o6-alkylguanine-DNA alkyltransferase for efficient labeling of fusion proteins with small molecules in vivo. Chem. Biol. 10 (2003) 313-317
    • (2003) Chem. Biol. , vol.10 , pp. 313-317
    • Juillerat, A.1    Gronemeyer, T.2    Keppler, A.3    Gendreizig, S.4    Pick, H.5    Vogel, H.6    Johnsson, K.7
  • 56
    • 33644808569 scopus 로고    scopus 로고
    • Snap-tag mediated live cell labeling as an alternative to GFP in anaerobic organisms
    • Regoes A., and Hehl A.B. Snap-tag mediated live cell labeling as an alternative to GFP in anaerobic organisms. BioTechniques 39 (2005) 809-810
    • (2005) BioTechniques , vol.39 , pp. 809-810
    • Regoes, A.1    Hehl, A.B.2
  • 57
    • 0030087711 scopus 로고    scopus 로고
    • Double labelling of subcellular structures with organelle-targeted GFP mutants in vivo
    • Rizzuto R., Brini M., De Giorgi F., Rossi R., Heim R., Tsien R.Y., and Pozzan T. Double labelling of subcellular structures with organelle-targeted GFP mutants in vivo. Curr. Biol. 6 (1996) 183-188
    • (1996) Curr. Biol. , vol.6 , pp. 183-188
    • Rizzuto, R.1    Brini, M.2    De Giorgi, F.3    Rossi, R.4    Heim, R.5    Tsien, R.Y.6    Pozzan, T.7
  • 58
    • 0037007227 scopus 로고    scopus 로고
    • Mitochondria are morphologically and functionally heterogeneous within cells
    • Collins T.J., Berridge M.J., Lipp P., and Bootman M.D. Mitochondria are morphologically and functionally heterogeneous within cells. EMBO J. 21 (2002) 1616-1627
    • (2002) EMBO J. , vol.21 , pp. 1616-1627
    • Collins, T.J.1    Berridge, M.J.2    Lipp, P.3    Bootman, M.D.4
  • 59
    • 0043166392 scopus 로고    scopus 로고
    • Dynamics of mitochondrial morphology in healthy cells and during apoptosis
    • Karbowski M., and Youle R.J. Dynamics of mitochondrial morphology in healthy cells and during apoptosis. Cell Death Differ. 10 (2003) 870-880
    • (2003) Cell Death Differ. , vol.10 , pp. 870-880
    • Karbowski, M.1    Youle, R.J.2
  • 60
    • 0034029619 scopus 로고    scopus 로고
    • Mitochondria-targeted GFP highlights the heterogeneity of mitochondrial shape, size and movement within living plant cells
    • Logan D.C., and Leaver C.J. Mitochondria-targeted GFP highlights the heterogeneity of mitochondrial shape, size and movement within living plant cells. J. Exp. Bot. 51 (2000) 865-871
    • (2000) J. Exp. Bot. , vol.51 , pp. 865-871
    • Logan, D.C.1    Leaver, C.J.2
  • 61
    • 0036009370 scopus 로고    scopus 로고
    • Plant mitochondria move on F-actin, but their positioning in the cortical cytoplasm depends on both F-actin and microtubules
    • VanGestel K., Kohler R.H., and Verbelen J.P. Plant mitochondria move on F-actin, but their positioning in the cortical cytoplasm depends on both F-actin and microtubules. J. Exp. Bot. 53 (2002) 659-667
    • (2002) J. Exp. Bot. , vol.53 , pp. 659-667
    • VanGestel, K.1    Kohler, R.H.2    Verbelen, J.P.3
  • 62
    • 0037768628 scopus 로고    scopus 로고
    • Spatial and temporal dynamics of budding yeast mitochondria lacking the division component Fis1p
    • Jakobs S., Martini N., Schauss A.C., Egner A., Westermann B., and Hell S.W. Spatial and temporal dynamics of budding yeast mitochondria lacking the division component Fis1p. J. Cell Sci. 116 (2003) 2005-2014
    • (2003) J. Cell Sci. , vol.116 , pp. 2005-2014
    • Jakobs, S.1    Martini, N.2    Schauss, A.C.3    Egner, A.4    Westermann, B.5    Hell, S.W.6
  • 63
    • 9244263050 scopus 로고    scopus 로고
    • Live cell imaging of mitochondrial movement along actin cables in budding yeast
    • Fehrenbacher K.L., Yang H.C., Gay A.C., Huckaba T.M., and Pon L.A. Live cell imaging of mitochondrial movement along actin cables in budding yeast. Curr. Biol. 14 (2004) 1996-2004
    • (2004) Curr. Biol. , vol.14 , pp. 1996-2004
    • Fehrenbacher, K.L.1    Yang, H.C.2    Gay, A.C.3    Huckaba, T.M.4    Pon, L.A.5
  • 64
    • 4644229005 scopus 로고    scopus 로고
    • Importance of mitochondrial dynamics during meiosis and sporulation
    • Gorsich S.W., and Shaw J.M. Importance of mitochondrial dynamics during meiosis and sporulation. Mol. Biol. Cell 15 (2004) 4369-4381
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4369-4381
    • Gorsich, S.W.1    Shaw, J.M.2
  • 66
    • 16844377411 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in the control of apoptosis
    • Perfettini J.L., Roumier T., and Kroemer G. Mitochondrial fusion and fission in the control of apoptosis. Trends Cell Biol. 15 (2005) 179-183
    • (2005) Trends Cell Biol. , vol.15 , pp. 179-183
    • Perfettini, J.L.1    Roumier, T.2    Kroemer, G.3
  • 67
    • 0029750188 scopus 로고    scopus 로고
    • Four-dimensional imaging: computer visualization of 3D movements in living specimens
    • Thomas C., DeVries P., Hardin J., and White J. Four-dimensional imaging: computer visualization of 3D movements in living specimens. Science 273 (1996) 603-607
    • (1996) Science , vol.273 , pp. 603-607
    • Thomas, C.1    DeVries, P.2    Hardin, J.3    White, J.4
  • 68
    • 0034574342 scopus 로고    scopus 로고
    • Raising the speed limits for 4D fluorescence microscopy
    • Hammond A.T., and Glick B.S. Raising the speed limits for 4D fluorescence microscopy. Traffic 1 (2000) 935-940
    • (2000) Traffic , vol.1 , pp. 935-940
    • Hammond, A.T.1    Glick, B.S.2
  • 69
    • 0042839654 scopus 로고    scopus 로고
    • 4D imaging to assay complex dynamics in live specimens
    • Gerlich D., and Ellenberg J. 4D imaging to assay complex dynamics in live specimens. Nat. Cell Biol. (2003) S14-S19
    • (2003) Nat. Cell Biol.
    • Gerlich, D.1    Ellenberg, J.2
  • 70
    • 0035033890 scopus 로고    scopus 로고
    • Autofluorescent proteins in single-molecule research: applications to live cell imaging microscopy
    • Harms G.S., Cognet L., Lommerse P.H., Blab G.A., and Schmidt T. Autofluorescent proteins in single-molecule research: applications to live cell imaging microscopy. Biophys. J. 80 (2001) 2396-2408
    • (2001) Biophys. J. , vol.80 , pp. 2396-2408
    • Harms, G.S.1    Cognet, L.2    Lommerse, P.H.3    Blab, G.A.4    Schmidt, T.5
  • 72
    • 0033672549 scopus 로고    scopus 로고
    • Mitochondria-targeted green fluorescent proteins: convenient tools for the study of organelle biogenesis in Saccharomyces cerevisiae
    • Westermann B., and Neupert W. Mitochondria-targeted green fluorescent proteins: convenient tools for the study of organelle biogenesis in Saccharomyces cerevisiae. Yeast 16 (2000) 1421-1427
    • (2000) Yeast , vol.16 , pp. 1421-1427
    • Westermann, B.1    Neupert, W.2
  • 73
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p
    • Mozdy A.D., McCaffery J.M., and Shaw J.M. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J. Cell Biol. 151 (2000) 367-379
    • (2000) J. Cell Biol. , vol.151 , pp. 367-379
    • Mozdy, A.D.1    McCaffery, J.M.2    Shaw, J.M.3
  • 74
    • 0035911963 scopus 로고    scopus 로고
    • Ugo1 encodes an outer membrane protein required for mitochondrial fusion
    • Sesaki H., and Jensen R.E. Ugo1 encodes an outer membrane protein required for mitochondrial fusion. J. Cell Biol. 152 (2001) 1123-1134
    • (2001) J. Cell Biol. , vol.152 , pp. 1123-1134
    • Sesaki, H.1    Jensen, R.E.2
  • 77
    • 0037415638 scopus 로고    scopus 로고
    • The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion
    • Wong E.D., Wagner J.A., Scott S.V., Okreglak V., Holewinske T.J., Cassidy-Stone A., and Nunnari J. The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion. J. Cell Biol. 160 (2003) 303-311
    • (2003) J. Cell Biol. , vol.160 , pp. 303-311
    • Wong, E.D.1    Wagner, J.A.2    Scott, S.V.3    Okreglak, V.4    Holewinske, T.J.5    Cassidy-Stone, A.6    Nunnari, J.7
  • 78
    • 3142546895 scopus 로고    scopus 로고
    • Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion
    • Sesaki H., and Jensen R.E. Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion. J. Biol. Chem. 279 (2004) 28298-28303
    • (2004) J. Biol. Chem. , vol.279 , pp. 28298-28303
    • Sesaki, H.1    Jensen, R.E.2
  • 79
    • 12144280303 scopus 로고    scopus 로고
    • Mdm31 and Mdm32 are inner membrane proteins required for maintenance of mitochondrial shape and stability of mitochondrial DNA nucleoids in yeast
    • Dimmer K.S., Jakobs S., Vogel F., Altmann K., and Westermann B. Mdm31 and Mdm32 are inner membrane proteins required for maintenance of mitochondrial shape and stability of mitochondrial DNA nucleoids in yeast. J. Cell Biol. 168 (2005) 103-115
    • (2005) J. Cell Biol. , vol.168 , pp. 103-115
    • Dimmer, K.S.1    Jakobs, S.2    Vogel, F.3    Altmann, K.4    Westermann, B.5
  • 80
    • 33644843425 scopus 로고    scopus 로고
    • Mitochondria as a connected population: ensuring continuity of the mitochondrial genome during plant cell dedifferentiation through massive mitochondrial fusion
    • Sheahan M.B., McCurdy D.W., and Rose R.J. Mitochondria as a connected population: ensuring continuity of the mitochondrial genome during plant cell dedifferentiation through massive mitochondrial fusion. Plant J. 44 (2005) 744-755
    • (2005) Plant J. , vol.44 , pp. 744-755
    • Sheahan, M.B.1    McCurdy, D.W.2    Rose, R.J.3
  • 81
    • 0036906665 scopus 로고    scopus 로고
    • Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins
    • Legros F., Lombes A., Frachon P., and Rojo M. Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins. Mol. Biol. Cell 13 (2002) 4343-4354
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4343-4354
    • Legros, F.1    Lombes, A.2    Frachon, P.3    Rojo, M.4
  • 82
    • 0037459089 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology by membrane potential, and Drp1-dependent division and Fzo1-dependent fusion reaction in mammalian cells
    • Ishihara N., Jofuku A., Eura Y., and Mihara K. Regulation of mitochondrial morphology by membrane potential, and Drp1-dependent division and Fzo1-dependent fusion reaction in mammalian cells. Biochem. Biophys. Res. Commun. 301 (2003) 891-898
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 891-898
    • Ishihara, N.1    Jofuku, A.2    Eura, Y.3    Mihara, K.4
  • 83
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • Chen H., Detmer S.A., Ewald A.J., Griffin E.E., Fraser S.E., and Chan D.C. Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J. Cell Biol. 160 (2003) 189-200
    • (2003) J. Cell Biol. , vol.160 , pp. 189-200
    • Chen, H.1    Detmer, S.A.2    Ewald, A.J.3    Griffin, E.E.4    Fraser, S.E.5    Chan, D.C.6
  • 84
    • 0037434879 scopus 로고    scopus 로고
    • Fusion of mitochondria in mammalian cells is dependent on the mitochondrial inner membrane potential and independent of microtubules or actin
    • Mattenberger Y., James D.I., and Martinou J.C. Fusion of mitochondria in mammalian cells is dependent on the mitochondrial inner membrane potential and independent of microtubules or actin. FEBS Lett. 538 (2003) 53-59
    • (2003) FEBS Lett. , vol.538 , pp. 53-59
    • Mattenberger, Y.1    James, D.I.2    Martinou, J.C.3
  • 86
    • 0034647238 scopus 로고    scopus 로고
    • Antiparallel leucine zipper-directed protein reassembly: application to the green fluorescent protein
    • Ghosh I., Hamilton A.D., and Regan L. Antiparallel leucine zipper-directed protein reassembly: application to the green fluorescent protein. J. Am. Chem. Soc. 122 (2000) 5658-5659
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 5658-5659
    • Ghosh, I.1    Hamilton, A.D.2    Regan, L.3
  • 87
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu C.D., Chinenov Y., and Kerppola T.K. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9 (2002) 789-798
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 88
    • 11844252081 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism
    • Magliery T.J., Wilson C.G., Pan W., Mishler D., Ghosh I., Hamilton A.D., and Regan L. Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism. J. Am. Chem. Soc. 127 (2005) 146-157
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 146-157
    • Magliery, T.J.1    Wilson, C.G.2    Pan, W.3    Mishler, D.4    Ghosh, I.5    Hamilton, A.D.6    Regan, L.7
  • 89
    • 24144454858 scopus 로고    scopus 로고
    • Detecting protein-protein interactions with GFP-fragment reassembly
    • Wilson C.G., Magliery T.J., and Regan L. Detecting protein-protein interactions with GFP-fragment reassembly. Nat. Methods 1 (2004) 255-562
    • (2004) Nat. Methods , vol.1 , pp. 255-562
    • Wilson, C.G.1    Magliery, T.J.2    Regan, L.3
  • 90
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • Hu C.D., and Kerppola T.K. Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nat. Biotechnol. 21 (2003) 539-545
    • (2003) Nat. Biotechnol. , vol.21 , pp. 539-545
    • Hu, C.D.1    Kerppola, T.K.2
  • 91
    • 18144394763 scopus 로고    scopus 로고
    • Capturing protein interactions in the secretory pathway of living cells
    • Nyfeler B., Michnick S.W., and Hauri H.P. Capturing protein interactions in the secretory pathway of living cells. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 6350-6355
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 6350-6355
    • Nyfeler, B.1    Michnick, S.W.2    Hauri, H.P.3
  • 92
    • 33644861986 scopus 로고    scopus 로고
    • Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions
    • Shyu Y.J., Liu H., Deng X., and Hu C.D. Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions. BioTechniques 40 (2006) 61-66
    • (2006) BioTechniques , vol.40 , pp. 61-66
    • Shyu, Y.J.1    Liu, H.2    Deng, X.3    Hu, C.D.4
  • 93
    • 13244296604 scopus 로고    scopus 로고
    • Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein
    • Cabantous S., Terwilliger T.C., and Waldo G.S. Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Nat. Biotechnol. 23 (2005) 102-107
    • (2005) Nat. Biotechnol. , vol.23 , pp. 102-107
    • Cabantous, S.1    Terwilliger, T.C.2    Waldo, G.S.3
  • 94
    • 0016272796 scopus 로고
    • A microfluorimetric study of translational diffusion in erythrocyte membranes
    • Peters R., Peters J., Tews K.H., and Bahr W. A microfluorimetric study of translational diffusion in erythrocyte membranes. Biochim. Biophys. Acta 367 (1974) 282-294
    • (1974) Biochim. Biophys. Acta , vol.367 , pp. 282-294
    • Peters, R.1    Peters, J.2    Tews, K.H.3    Bahr, W.4
  • 95
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • Axelrod D., Koppel D.E., Schlessinger J., Elson E., and Webb W.W. Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys. J. 16 (1976) 1055-1069
    • (1976) Biophys. J. , vol.16 , pp. 1055-1069
    • Axelrod, D.1    Koppel, D.E.2    Schlessinger, J.3    Elson, E.4    Webb, W.W.5
  • 96
    • 0017236539 scopus 로고
    • Measurement of membrane protein lateral diffusion in single cells
    • Edidin M., Zagyansky Y., and Lardner T.J. Measurement of membrane protein lateral diffusion in single cells. Science 191 (1976) 466-468
    • (1976) Science , vol.191 , pp. 466-468
    • Edidin, M.1    Zagyansky, Y.2    Lardner, T.J.3
  • 97
    • 0017253004 scopus 로고
    • Measurement of the translational mobility of concanavalin A in glycerol-saline solutions and on the cell surface by fluorescence recovery after photobleaching
    • Jacobson K., Wu E.S., and Poste G. Measurement of the translational mobility of concanavalin A in glycerol-saline solutions and on the cell surface by fluorescence recovery after photobleaching. Biochim. Biophys. Acta 433 (1976) 215-222
    • (1976) Biochim. Biophys. Acta , vol.433 , pp. 215-222
    • Jacobson, K.1    Wu, E.S.2    Poste, G.3
  • 99
    • 0034976147 scopus 로고    scopus 로고
    • From fixed to FRAP: measuring protein mobility and activity in living cells
    • Reits E.A.J., and Neefjes J.J. From fixed to FRAP: measuring protein mobility and activity in living cells. Nat. Cell Biol. 3 (2001) E145-E147
    • (2001) Nat. Cell Biol. , vol.3
    • Reits, E.A.J.1    Neefjes, J.J.2
  • 101
    • 13844298835 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling revealed by FRAP and FLIP technologies
    • Köster M., Frahm T., and Hauser H. Nucleocytoplasmic shuttling revealed by FRAP and FLIP technologies. Curr. Opin. Biotechnol. 16 (2005) 28-34
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 28-34
    • Köster, M.1    Frahm, T.2    Hauser, H.3
  • 102
    • 13244291467 scopus 로고    scopus 로고
    • FRAP analysis of binding: proper and fitting
    • Sprague B.L., and McNally J.G. FRAP analysis of binding: proper and fitting. Trends Cell Biol. 15 (2005) 84-91
    • (2005) Trends Cell Biol. , vol.15 , pp. 84-91
    • Sprague, B.L.1    McNally, J.G.2
  • 105
    • 0035146891 scopus 로고    scopus 로고
    • Mitochondrial filaments and clusters as intracellular power-transmitting cables
    • Skulachev V.P. Mitochondrial filaments and clusters as intracellular power-transmitting cables. Trends Biochem. Sci. 26 (2001) 23-29
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 23-29
    • Skulachev, V.P.1
  • 107
    • 0038609470 scopus 로고    scopus 로고
    • Mitochondria are morphologically heterogeneous within cells
    • Collins T.J., and Bootman M.D. Mitochondria are morphologically heterogeneous within cells. J. Exp. Biol. 206 (2003) 1993-2000
    • (2003) J. Exp. Biol. , vol.206 , pp. 1993-2000
    • Collins, T.J.1    Bootman, M.D.2
  • 108
    • 0035901525 scopus 로고    scopus 로고
    • Perinuclear, perigranular and sub-plasmalemmal mitochondria have distinct functions in the regulation of cellular calcium transport
    • Park M.K., Ashby M.C., Erdemli G., Petersen O.H., and Tepikin A.V. Perinuclear, perigranular and sub-plasmalemmal mitochondria have distinct functions in the regulation of cellular calcium transport. EMBO J. 20 (2001) 1374-1863
    • (2001) EMBO J. , vol.20 , pp. 1374-1863
    • Park, M.K.1    Ashby, M.C.2    Erdemli, G.3    Petersen, O.H.4    Tepikin, A.V.5
  • 109
  • 110
    • 0031968609 scopus 로고    scopus 로고
    • Monte carlo analysis of obstructed diffusion in three dimensions-Application to molecular diffusion in organelles
    • Olveczky B.P., and Verkman A.S. Monte carlo analysis of obstructed diffusion in three dimensions-Application to molecular diffusion in organelles. Biophys. J. 74 (1998) 2722-2730
    • (1998) Biophys. J. , vol.74 , pp. 2722-2730
    • Olveczky, B.P.1    Verkman, A.S.2
  • 111
    • 0014347959 scopus 로고
    • Chemical and physical fixation of isolated mitochondria in low-energy and high-energy states
    • Hackenbrock C.R. Chemical and physical fixation of isolated mitochondria in low-energy and high-energy states. Proc. Natl. Acad. Sci. U. S. A. 61 (1968) 598-605
    • (1968) Proc. Natl. Acad. Sci. U. S. A. , vol.61 , pp. 598-605
    • Hackenbrock, C.R.1
  • 112
    • 0018854310 scopus 로고
    • The infrastructure of the mitochondrial matrix
    • Srere P.A. The infrastructure of the mitochondrial matrix. Trends Biochem. Sci. 5 (1980) 120-121
    • (1980) Trends Biochem. Sci. , vol.5 , pp. 120-121
    • Srere, P.A.1
  • 113
    • 0037174943 scopus 로고    scopus 로고
    • Diffusion of tricarboxylic acid cycle enzymes in the mitochondrial matrix in vivo. Evidence for restricted mobility of a multienzyme complex
    • Haggie P.M., and Verkman A.S. Diffusion of tricarboxylic acid cycle enzymes in the mitochondrial matrix in vivo. Evidence for restricted mobility of a multienzyme complex. J. Biol. Chem. 277 (2002) 40782-40788
    • (2002) J. Biol. Chem. , vol.277 , pp. 40782-40788
    • Haggie, P.M.1    Verkman, A.S.2
  • 116
    • 0031241658 scopus 로고    scopus 로고
    • Photoactivation of green fluorescent protein
    • Sawin K.E., and Nurse P. Photoactivation of green fluorescent protein. Curr. Biol. 7 (1997) R606-R607
    • (1997) Curr. Biol. , vol.7
    • Sawin, K.E.1    Nurse, P.2
  • 117
    • 0142246587 scopus 로고    scopus 로고
    • Photoconversion of matrix targeted GFP enables analysis of continuity and intermixing of the mitochondrial lumen
    • Jakobs S., Schauss A.C., and Hell S.W. Photoconversion of matrix targeted GFP enables analysis of continuity and intermixing of the mitochondrial lumen. FEBS Lett. 554 (2003) 194-200
    • (2003) FEBS Lett. , vol.554 , pp. 194-200
    • Jakobs, S.1    Schauss, A.C.2    Hell, S.W.3
  • 119
    • 1242307475 scopus 로고    scopus 로고
    • Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the bax activation phase of apoptosis
    • Karbowski M., Arnoult D., Chen H., Chan D.C., Smith C.L., and Youle R.J. Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the bax activation phase of apoptosis. J. Cell Biol. 164 (2004) 493-499
    • (2004) J. Cell Biol. , vol.164 , pp. 493-499
    • Karbowski, M.1    Arnoult, D.2    Chen, H.3    Chan, D.C.4    Smith, C.L.5    Youle, R.J.6
  • 120
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • Patterson G.H., and Lippincott-Schwartz J. A photoactivatable GFP for selective photolabeling of proteins and cells. Science 297 (2002) 1873-1877
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 121
    • 0036789916 scopus 로고    scopus 로고
    • An optical marker based on the UV-induced green-to-red photoconversion of a fluorescent protein
    • Ando R., Hama H., Yamamoto-Hino M., Mizuno H., and Miyawaki A. An optical marker based on the UV-induced green-to-red photoconversion of a fluorescent protein. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 12651-12656
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12651-12656
    • Ando, R.1    Hama, H.2    Yamamoto-Hino, M.3    Mizuno, H.4    Miyawaki, A.5
  • 122
    • 35949038838 scopus 로고
    • Thermodynamic fluctuations in a reacting system: measurement by fluorescence correlation spectroscopy
    • Magde D., Elson E., and Webb W.W. Thermodynamic fluctuations in a reacting system: measurement by fluorescence correlation spectroscopy. Phys. Rev. Lett. 29 (1972) 705-708
    • (1972) Phys. Rev. Lett. , vol.29 , pp. 705-708
    • Magde, D.1    Elson, E.2    Webb, W.W.3
  • 123
    • 0028229903 scopus 로고
    • Sorting single molecules: application to diagnostics and evolutionary biotechnology
    • Eigen M., and Rigler R. Sorting single molecules: application to diagnostics and evolutionary biotechnology. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 5740-5747
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 5740-5747
    • Eigen, M.1    Rigler, R.2
  • 125
    • 0035775836 scopus 로고    scopus 로고
    • Fluorescence correlation microscopy (FCM): Fluorescence correlation spectroscopy (FCS) in cell biology, in: Springer series in chemical physics
    • Springer-Verlag, Berlin
    • Brock R., and Jovin T.M. Fluorescence correlation microscopy (FCM): Fluorescence correlation spectroscopy (FCS) in cell biology, in: Springer series in chemical physics. Fluorescence Correlation Spectroscopy: Theory and Applications vol. 65 (2001), Springer-Verlag, Berlin 132-161
    • (2001) Fluorescence Correlation Spectroscopy: Theory and Applications , vol.65 , pp. 132-161
    • Brock, R.1    Jovin, T.M.2
  • 126
    • 0037154114 scopus 로고    scopus 로고
    • Biological and chemical applications of fluorescence correlation spectroscopy: A review
    • Hess S.T., Huang S., Heikal A.A., and Webb W.W. Biological and chemical applications of fluorescence correlation spectroscopy: A review. Biochemistry 41 (2002) 697-705
    • (2002) Biochemistry , vol.41 , pp. 697-705
    • Hess, S.T.1    Huang, S.2    Heikal, A.A.3    Webb, W.W.4
  • 128
    • 23944488300 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy with autofluorescent proteins
    • Kohl T., and Schwille P. Fluorescence correlation spectroscopy with autofluorescent proteins. Adv. Biochem. Eng. Biotechnol. 95 (2005) 107-142
    • (2005) Adv. Biochem. Eng. Biotechnol. , vol.95 , pp. 107-142
    • Kohl, T.1    Schwille, P.2
  • 129
    • 0030895059 scopus 로고    scopus 로고
    • Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution
    • Schwille P., Meyer-Almes F.J., and Rigler R. Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution. Biophys. J. 72 (1997) 1878-1886
    • (1997) Biophys. J. , vol.72 , pp. 1878-1886
    • Schwille, P.1    Meyer-Almes, F.J.2    Rigler, R.3
  • 130
    • 0034641711 scopus 로고    scopus 로고
    • Simultaneous two-photon excitation of distinct labels for dual-color fluorescence crosscorrelation analysis
    • Heinze K.G., Koltermann A., and Schwille P. Simultaneous two-photon excitation of distinct labels for dual-color fluorescence crosscorrelation analysis. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 10377-10382
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 10377-10382
    • Heinze, K.G.1    Koltermann, A.2    Schwille, P.3
  • 132
    • 27744432013 scopus 로고    scopus 로고
    • Temporally resolved interactions between antigen-stimulated IgE receptors and Lyn kinase on living cells
    • Larson D.R., Gosse J.A., Holowka D.A., Baird B.A., and Webb W.W. Temporally resolved interactions between antigen-stimulated IgE receptors and Lyn kinase on living cells. J. Cell Biol. 171 (2005) 527-536
    • (2005) J. Cell Biol. , vol.171 , pp. 527-536
    • Larson, D.R.1    Gosse, J.A.2    Holowka, D.A.3    Baird, B.A.4    Webb, W.W.5
  • 133
    • 84981779372 scopus 로고
    • Intermolecular energy migration and fluorescence
    • Förster T. Intermolecular energy migration and fluorescence. Ann. Phys. (Leipzig) 2 (1948) 55-75
    • (1948) Ann. Phys. (Leipzig) , vol.2 , pp. 55-75
    • Förster, T.1
  • 136
    • 0028295796 scopus 로고
    • Resonance energy transfer: methods and applications
    • Wu P., and Brand L. Resonance energy transfer: methods and applications. Anal. Biochem. 218 (1994) 1-13
    • (1994) Anal. Biochem. , vol.218 , pp. 1-13
    • Wu, P.1    Brand, L.2
  • 137
    • 0034846540 scopus 로고    scopus 로고
    • Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy
    • Kenworthy A.K. Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy. Methods 24 (2001) 289-296
    • (2001) Methods , vol.24 , pp. 289-296
    • Kenworthy, A.K.1
  • 138
    • 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. The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo. Curr. Opin. Struct. Biol. 11 (2001) 573-578
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 573-578
    • Truong, K.1    Ikura, M.2
  • 140
    • 0035957110 scopus 로고    scopus 로고
    • Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer
    • Mizuno H., Sawano A., Eli P., Hama H., and Miyawaki A. Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer. Biochemistry 40 (2001) 2502-2510
    • (2001) Biochemistry , vol.40 , pp. 2502-2510
    • Mizuno, H.1    Sawano, A.2    Eli, P.3    Hama, H.4    Miyawaki, A.5
  • 141
    • 3142736368 scopus 로고    scopus 로고
    • Cyan-emitting and orange-emitting fluorescent proteins as a donor/acceptor pair for fluorescence resonance energy transfer
    • Karasawa S., Araki T., Nagai T., Mizuno H., and Miyawaki A. Cyan-emitting and orange-emitting fluorescent proteins as a donor/acceptor pair for fluorescence resonance energy transfer. Biochem. J. 381 (2004) 307-312
    • (2004) Biochem. J. , vol.381 , pp. 307-312
    • Karasawa, S.1    Araki, T.2    Nagai, T.3    Mizuno, H.4    Miyawaki, A.5
  • 142
  • 143
    • 21444436724 scopus 로고    scopus 로고
    • Evolutionary optimization of fluorescent proteins for intracellular FRET
    • Nguyen A.W., and Daugherty P.S. Evolutionary optimization of fluorescent proteins for intracellular FRET. Nat. Biotechnol. 23 (2005) 355-360
    • (2005) Nat. Biotechnol. , vol.23 , pp. 355-360
    • Nguyen, A.W.1    Daugherty, P.S.2
  • 145
    • 20044386366 scopus 로고    scopus 로고
    • 0-ATP synthase complex interactions in vivo can occur in the absence of the dimer specific subunit e
    • 0-ATP synthase complex interactions in vivo can occur in the absence of the dimer specific subunit e. J. Bioenerg. Biomembr. 37 (2005) 55-66
    • (2005) J. Bioenerg. Biomembr. , vol.37 , pp. 55-66
    • Gavin, P.D.1    Prescott, M.2    Devenish, R.J.3
  • 146
    • 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. Bcl-2 and Bax interactions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer. Nat. Biotechnol. 16 (1998) 547-552
    • (1998) Nat. Biotechnol. , 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
  • 147
    • 0037069360 scopus 로고    scopus 로고
    • Confirmation by FRET in individual living cells of the absence of significant amyloid beta-mediated caspase 8 activation
    • Onuki R., Nagasaki A., Kawasaki H., Baba T., Uyeda T.Q., and Taira K. Confirmation by FRET in individual living cells of the absence of significant amyloid beta-mediated caspase 8 activation. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 14716-14721
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 14716-14721
    • Onuki, R.1    Nagasaki, A.2    Kawasaki, H.3    Baba, T.4    Uyeda, T.Q.5    Taira, K.6
  • 148
    • 0037343944 scopus 로고    scopus 로고
    • Visualization of the spatial and temporal dynamics of intracellular signaling
    • Miyawaki A. Visualization of the spatial and temporal dynamics of intracellular signaling. Dev. Cell 4 (2003) 295-305
    • (2003) Dev. Cell , vol.4 , pp. 295-305
    • Miyawaki, A.1
  • 149
    • 24644488301 scopus 로고    scopus 로고
    • 2+-sensitive fluorescent proteins
    • 2+-sensitive fluorescent proteins. Cell Calcium 38 (2005) 213-322
    • (2005) Cell Calcium , vol.38 , pp. 213-322
    • Demaurex, N.1
  • 151
    • 0031011418 scopus 로고    scopus 로고
    • 2+-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
    • 2+-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
  • 154
    • 1842790629 scopus 로고    scopus 로고
    • Genetically encoded indicators of cellular calcium dynamics based on troponin C and green fluorescent protein
    • Heim N., and Griesbeck O. Genetically encoded indicators of cellular calcium dynamics based on troponin C and green fluorescent protein. J. Biol. Chem. 279 (2004) 14280-14286
    • (2004) J. Biol. Chem. , vol.279 , pp. 14280-14286
    • Heim, N.1    Griesbeck, O.2
  • 157
    • 0035800813 scopus 로고    scopus 로고
    • (2+) to the endoplasmic reticulum and prevent the depletion of neighboring endoplasmic reticulum regions
    • (2+) to the endoplasmic reticulum and prevent the depletion of neighboring endoplasmic reticulum regions. J. Biol. Chem. 276 (2001) 29430-29439
    • (2001) J. Biol. Chem. , vol.276 , pp. 29430-29439
    • Arnaudeau, S.1    Kelley, W.L.2    Walsh Jr., J.V.3    Demaurex, N.4
  • 158
    • 0037195869 scopus 로고    scopus 로고
    • Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria
    • Arnaudeau S., Frieden M., Nakamura K., Castelbou C., Michalak M., and Demaurex N. Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria. J. Biol. Chem. 277 (2002) 46696-46705
    • (2002) J. Biol. Chem. , vol.277 , pp. 46696-46705
    • Arnaudeau, S.1    Frieden, M.2    Nakamura, K.3    Castelbou, C.4    Michalak, M.5    Demaurex, N.6
  • 161
    • 0037133634 scopus 로고    scopus 로고
    • Fast 100-nm resolution three-dimensional microscope reveals structural plasticity of mitochondria in live yeast
    • Egner A., Jakobs S., and Hell S.W. Fast 100-nm resolution three-dimensional microscope reveals structural plasticity of mitochondria in live yeast. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 3370-3375
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 3370-3375
    • Egner, A.1    Jakobs, S.2    Hell, S.W.3
  • 162
    • 60049098657 scopus 로고
    • Beiträge zur Theorie des Mikroskops und der mikroskopischen Wahrnehmung
    • Abbe E. Beiträge zur Theorie des Mikroskops und der mikroskopischen Wahrnehmung. Arch. Mikrosk. Anat. 9 (1873) 413-420
    • (1873) Arch. Mikrosk. Anat. , vol.9 , pp. 413-420
    • Abbe, E.1
  • 164
    • 0242322565 scopus 로고    scopus 로고
    • Toward fluorescence nanoscopy
    • Hell S.W. Toward fluorescence nanoscopy. Nat. Biotechnol. 21 (2003) 1347-1355
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1347-1355
    • Hell, S.W.1
  • 165
    • 5444270623 scopus 로고    scopus 로고
    • Concepts for nanoscale resolution in fluorescence microscopy
    • Hell S.W., Dyba M., and Jakobs S. Concepts for nanoscale resolution in fluorescence microscopy. Curr. Opin. Neurobiol. 14 (2004) 599-609
    • (2004) Curr. Opin. Neurobiol. , vol.14 , pp. 599-609
    • Hell, S.W.1    Dyba, M.2    Jakobs, S.3
  • 166
    • 13844275955 scopus 로고    scopus 로고
    • From micro to nano: recent advances in high-resolution microscopy
    • Garini Y., Vermolen B.J., and Young I.T. From micro to nano: recent advances in high-resolution microscopy. Curr. Opin. Biotechnol. 16 (2005) 3-12
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 3-12
    • Garini, Y.1    Vermolen, B.J.2    Young, I.T.3
  • 168
    • 84975659980 scopus 로고
    • Properties of a 4Pi-confocal fluorescence microscope
    • Hell S., and Stelzer E.H.K. Properties of a 4Pi-confocal fluorescence microscope. J. Opt. Soc. Am. A 9 (1992) 2159-2166
    • (1992) J. Opt. Soc. Am. A , vol.9 , pp. 2159-2166
    • Hell, S.1    Stelzer, E.H.K.2
  • 169
    • 0026931496 scopus 로고
    • Fundamental improvement of resolution with a 4Pi-confocal fluorescence microscope using two-photon excitation
    • Hell S.W., and Stelzer E.H.K. Fundamental improvement of resolution with a 4Pi-confocal fluorescence microscope using two-photon excitation. Opt. Commun. 93 (1992) 277-282
    • (1992) Opt. Commun. , vol.93 , pp. 277-282
    • Hell, S.W.1    Stelzer, E.H.K.2
  • 170
    • 0029213489 scopus 로고
    • Sevenfold improvement of axial resolution in 3D widefield microscopy using two objective lenses
    • Gustafsson M.G.L., Agard D.A., and Sedat J.W. Sevenfold improvement of axial resolution in 3D widefield microscopy using two objective lenses. Proc. Soc. Photo-Opt. Instrum. Eng. 2412 (1995) 147-156
    • (1995) Proc. Soc. Photo-Opt. Instrum. Eng. , vol.2412 , pp. 147-156
    • Gustafsson, M.G.L.1    Agard, D.A.2    Sedat, J.W.3
  • 171
    • 0029791160 scopus 로고    scopus 로고
    • 4Pi-confocal images with axial superresolution
    • Schrader M., and Hell S.W. 4Pi-confocal images with axial superresolution. J. Microsc. 183 (1996) 189-193
    • (1996) J. Microsc. , vol.183 , pp. 189-193
    • Schrader, M.1    Hell, S.W.2
  • 172
    • 0030747348 scopus 로고    scopus 로고
    • Far-field fluorescence microscopy with three-dimensional resolution in the 100 nm range
    • Hell S.W., Schrader M., and van der Voort H.T.M. Far-field fluorescence microscopy with three-dimensional resolution in the 100 nm range. J. Microsc. 185 (1997) 1-5
    • (1997) J. Microsc. , vol.185 , pp. 1-5
    • Hell, S.W.1    Schrader, M.2    van der Voort, H.T.M.3
  • 173
    • 0032864460 scopus 로고    scopus 로고
    • I5M: 3D widefield light microscopy with better than 100 nm axial resolution
    • Gustafsson M.G.L., Agard D.A., and Sedat J.W. I5M: 3D widefield light microscopy with better than 100 nm axial resolution. J. Microsc. 195 (1999) 10-16
    • (1999) J. Microsc. , vol.195 , pp. 10-16
    • Gustafsson, M.G.L.1    Agard, D.A.2    Sedat, J.W.3
  • 174
    • 10044248656 scopus 로고    scopus 로고
    • Cooperative 4Pi excitation and detection yields sevenfold sharper optical sections in live-cell microscopy
    • Gugel H., Bewersdorf J., Jakobs S., Engelhardt J., Storz R., and Hell S.W. Cooperative 4Pi excitation and detection yields sevenfold sharper optical sections in live-cell microscopy. Biophys. J. 87 (2004) 4146-4152
    • (2004) Biophys. J. , vol.87 , pp. 4146-4152
    • Gugel, H.1    Bewersdorf, J.2    Jakobs, S.3    Engelhardt, J.4    Storz, R.5    Hell, S.W.6
  • 176
    • 16844363110 scopus 로고    scopus 로고
    • Fluorescence microscopy with super-resolved optical sections
    • Egner A., and Hell S.W. Fluorescence microscopy with super-resolved optical sections. Trends Cell Biol. 15 (2005) 207-215
    • (2005) Trends Cell Biol. , vol.15 , pp. 207-215
    • Egner, A.1    Hell, S.W.2
  • 177
    • 0035044184 scopus 로고    scopus 로고
    • 4Pi-confocal microscopy of live cells
    • Bahlmann K., Jakobs S., and Hell S.W. 4Pi-confocal microscopy of live cells. Ultramicroscopy 87 (2001) 155-164
    • (2001) Ultramicroscopy , vol.87 , pp. 155-164
    • Bahlmann, K.1    Jakobs, S.2    Hell, S.W.3
  • 178
    • 0036186582 scopus 로고    scopus 로고
    • Dual-color 4Pi-confocal microscopy with 3D-resolution in the 100 nm range
    • Kano H., Jakobs S., Nagorni M., and Hell S.W. Dual-color 4Pi-confocal microscopy with 3D-resolution in the 100 nm range. Ultramicroscopy 90 (2002) 207-213
    • (2002) Ultramicroscopy , vol.90 , pp. 207-213
    • Kano, H.1    Jakobs, S.2    Nagorni, M.3    Hell, S.W.4
  • 179
    • 0028460042 scopus 로고
    • Breaking the diffraction resolution limit by stimulated emission: stimulated emission depletion microscopy
    • Hell S.W., and Wichmann J. Breaking the diffraction resolution limit by stimulated emission: stimulated emission depletion microscopy. Opt. Lett. 19 (1994) 780-782
    • (1994) Opt. Lett. , vol.19 , pp. 780-782
    • Hell, S.W.1    Wichmann, J.2
  • 180
    • 0029309943 scopus 로고
    • Ground-state depletion fluorescence microscopy, a concept for breaking the diffraction resolution limit
    • Hell S.W., and Kroug M. Ground-state depletion fluorescence microscopy, a concept for breaking the diffraction resolution limit. Appl. Phys., B 60 (1995) 495-497
    • (1995) Appl. Phys., B , vol.60 , pp. 495-497
    • Hell, S.W.1    Kroug, M.2
  • 181
    • 0000295573 scopus 로고    scopus 로고
    • Increasing the resolution of far-field fluorescence light microscopy by point-spread-function engineering
    • Lakowicz J.R. (Ed), Plenum Press, New York
    • Hell S.W. Increasing the resolution of far-field fluorescence light microscopy by point-spread-function engineering. In: Lakowicz J.R. (Ed). Topics in Fluorescence Spectroscopy (1997), Plenum Press, New York 361-422
    • (1997) Topics in Fluorescence Spectroscopy , pp. 361-422
    • Hell, S.W.1
  • 182
    • 0142086768 scopus 로고    scopus 로고
    • Imaging and writing at the nanoscale with focused visible light through saturable optical transitions
    • Hell S.W., Jakobs S., and Kastrup L. Imaging and writing at the nanoscale with focused visible light through saturable optical transitions. Appl. Phys., A 77 (2003) 859-860
    • (2003) Appl. Phys., A , vol.77 , pp. 859-860
    • Hell, S.W.1    Jakobs, S.2    Kastrup, L.3
  • 183
    • 0034682512 scopus 로고    scopus 로고
    • Fluorescence microscopy with diffraction resolution barrier broken by stimulated emission
    • Klar T.A., Jakobs S., Dyba M., Egner A., and Hell S.W. Fluorescence microscopy with diffraction resolution barrier broken by stimulated emission. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 8206-8210
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8206-8210
    • Klar, T.A.1    Jakobs, S.2    Dyba, M.3    Egner, A.4    Hell, S.W.5
  • 184
    • 0242290929 scopus 로고    scopus 로고
    • Immunofluorescence stimulated emission depletion microscopy
    • Dyba M., Jakobs S., and Hell S.W. Immunofluorescence stimulated emission depletion microscopy. Nat. Biotechnol. 21 (2003) 1303-1304
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1303-1304
    • Dyba, M.1    Jakobs, S.2    Hell, S.W.3
  • 185
    • 33645839858 scopus 로고    scopus 로고
    • STED-microscopy reveals that synaptotagmin remains clustered after synaptic vesicle exocytosis
    • Willig K.I., Rizzoli S.O., Westphal V., Jahn R., and Hell S.W. STED-microscopy reveals that synaptotagmin remains clustered after synaptic vesicle exocytosis. Nature 440 (2006) 935-939
    • (2006) Nature , vol.440 , pp. 935-939
    • Willig, K.I.1    Rizzoli, S.O.2    Westphal, V.3    Jahn, R.4    Hell, S.W.5
  • 186
    • 0036674522 scopus 로고    scopus 로고
    • Saturated patterned excitation microscopy-A concept for optical resolution improvement
    • Heintzmann R., Jovin T.M., and Cremer C. Saturated patterned excitation microscopy-A concept for optical resolution improvement. J. Opt. Soc. Am. A 19 (2002) 1599-1609
    • (2002) J. Opt. Soc. Am. A , vol.19 , pp. 1599-1609
    • Heintzmann, R.1    Jovin, T.M.2    Cremer, C.3
  • 187
    • 24944539530 scopus 로고    scopus 로고
    • Nonlinear structured-illumination microscopy: wide-field fluorescence imaging with theoretically unlimited resolution
    • Gustafsson M.G. Nonlinear structured-illumination microscopy: wide-field fluorescence imaging with theoretically unlimited resolution. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 13081-13086
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 13081-13086
    • Gustafsson, M.G.1
  • 188
    • 29144447893 scopus 로고    scopus 로고
    • Breaking the diffraction barrier in fluorescence microscopy at low light intensities by using reversibly photoswitchable proteins
    • Hofmann M., Eggeling C., Jakobs S., and Hell S.W. Breaking the diffraction barrier in fluorescence microscopy at low light intensities by using reversibly photoswitchable proteins. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17565-17569
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 17565-17569
    • Hofmann, M.1    Eggeling, C.2    Jakobs, S.3    Hell, S.W.4
  • 190
    • 8844260411 scopus 로고    scopus 로고
    • Regulated fast nucleocytoplasmic shuttling observed by reversible protein highlighting
    • Ando R., Mizuno H., and Miyawaki A. Regulated fast nucleocytoplasmic shuttling observed by reversible protein highlighting. Science 306 (2004) 1370-1373
    • (2004) Science , vol.306 , pp. 1370-1373
    • Ando, R.1    Mizuno, H.2    Miyawaki, A.3
  • 192
    • 34547999288 scopus 로고    scopus 로고
    • Focal spots of size λ/23 open up far-field florescence microscopy at 33 nm axial resolution
    • Dyba M., and Hell S.W. Focal spots of size λ/23 open up far-field florescence microscopy at 33 nm axial resolution. Phys. Rev. Lett. 88 (2002) 163901
    • (2002) Phys. Rev. Lett. , vol.88 , pp. 163901
    • Dyba, M.1    Hell, S.W.2
  • 193
    • 0142247452 scopus 로고    scopus 로고
    • Lateral resolution of 28 nm (λ/25) in far-field fluorescence microscopy
    • Westphal V., Kastrup L., and Hell S.W. Lateral resolution of 28 nm (λ/25) in far-field fluorescence microscopy. Appl. Phys., B 77 (2003) 377-380
    • (2003) Appl. Phys., B , vol.77 , pp. 377-380
    • Westphal, V.1    Kastrup, L.2    Hell, S.W.3


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