메뉴 건너뛰기




Volumn 37, Issue 11, 2012, Pages 499-506

Counting protein molecules using quantitative fluorescence microscopy

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENT DYE;

EID: 84867912638     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2012.08.002     Document Type: Review
Times cited : (105)

References (72)
  • 1
    • 70350223561 scopus 로고    scopus 로고
    • Function and assembly of DNA looping, clustering, and microtubule attachment complexes within a eukaryotic kinetochore
    • Anderson M., et al. Function and assembly of DNA looping, clustering, and microtubule attachment complexes within a eukaryotic kinetochore. Mol. Biol. Cell 2009, 20:4131-4139.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4131-4139
    • Anderson, M.1
  • 2
    • 81355149553 scopus 로고    scopus 로고
    • CENP-A exceeds microtubule attachment sites in centromere clusters of both budding and fission yeast
    • Coffman V.C., et al. CENP-A exceeds microtubule attachment sites in centromere clusters of both budding and fission yeast. J. Cell Biol. 2011, 195:563-572.
    • (2011) J. Cell Biol. , vol.195 , pp. 563-572
    • Coffman, V.C.1
  • 3
    • 84860299710 scopus 로고    scopus 로고
    • An extended gamma-tubulin ring functions as a stable platform in microtubule nucleation
    • Erlemann S., et al. An extended gamma-tubulin ring functions as a stable platform in microtubule nucleation. J. Cell Biol. 2012, 197:59-74.
    • (2012) J. Cell Biol. , vol.197 , pp. 59-74
    • Erlemann, S.1
  • 4
    • 77955829616 scopus 로고    scopus 로고
    • A non-ring-like form of the Dam1 complex modulates microtubule dynamics in fission yeast
    • Gao Q., et al. A non-ring-like form of the Dam1 complex modulates microtubule dynamics in fission yeast. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:13330-13335.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 13330-13335
    • Gao, Q.1
  • 5
    • 56349157171 scopus 로고    scopus 로고
    • Chromosome congression by Kinesin-5 motor-mediated disassembly of longer kinetochore microtubules
    • Gardner M.K., et al. Chromosome congression by Kinesin-5 motor-mediated disassembly of longer kinetochore microtubules. Cell 2008, 135:894-906.
    • (2008) Cell , vol.135 , pp. 894-906
    • Gardner, M.K.1
  • 6
    • 44149083326 scopus 로고    scopus 로고
    • Molecular architecture of the kinetochore-microtubule attachment site is conserved between point and regional centromeres
    • Joglekar A.P., et al. Molecular architecture of the kinetochore-microtubule attachment site is conserved between point and regional centromeres. J. Cell Biol. 2008, 181:587-594.
    • (2008) J. Cell Biol. , vol.181 , pp. 587-594
    • Joglekar, A.P.1
  • 7
    • 33744804567 scopus 로고    scopus 로고
    • Molecular architecture of a kinetochore-microtubule attachment site
    • Joglekar A.P., et al. Molecular architecture of a kinetochore-microtubule attachment site. Nat. Cell Biol. 2006, 8:581-585.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 581-585
    • Joglekar, A.P.1
  • 8
    • 77953574250 scopus 로고    scopus 로고
    • Vertebrate kinetochore protein architecture: protein copy number
    • Johnston K., et al. Vertebrate kinetochore protein architecture: protein copy number. J. Cell Biol. 2010, 189:937-943.
    • (2010) J. Cell Biol. , vol.189 , pp. 937-943
    • Johnston, K.1
  • 9
    • 79955509029 scopus 로고    scopus 로고
    • Assembly and architecture of precursor nodes during fission yeast cytokinesis
    • Laporte D., et al. Assembly and architecture of precursor nodes during fission yeast cytokinesis. J. Cell Biol. 2011, 192:1005-1021.
    • (2011) J. Cell Biol. , vol.192 , pp. 1005-1021
    • Laporte, D.1
  • 10
    • 33748926752 scopus 로고    scopus 로고
    • Stoichiometry and turnover in single, functioning membrane protein complexes
    • Leake M.C., et al. Stoichiometry and turnover in single, functioning membrane protein complexes. Nature 2006, 443:355-358.
    • (2006) Nature , vol.443 , pp. 355-358
    • Leake, M.C.1
  • 11
    • 55749095038 scopus 로고    scopus 로고
    • Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging
    • Leake M.C., et al. Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by in vivo single-molecule imaging. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:15376-15381.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 15376-15381
    • Leake, M.C.1
  • 12
    • 77951197000 scopus 로고    scopus 로고
    • Overlapping and distinct functions for cofilin, coronin and Aip1 in actin dynamics in vivo
    • Lin M.-C., et al. Overlapping and distinct functions for cofilin, coronin and Aip1 in actin dynamics in vivo. J. Cell Sci. 2010, 123:1329-1342.
    • (2010) J. Cell Sci. , vol.123 , pp. 1329-1342
    • Lin, M.-C.1
  • 13
    • 59349084461 scopus 로고    scopus 로고
    • Motor- and tail-dependent targeting of dynein to microtubule plus ends and the cell cortex
    • Markus S.M., et al. Motor- and tail-dependent targeting of dynein to microtubule plus ends and the cell cortex. Curr. Biol. 2009, 19:196-205.
    • (2009) Curr. Biol. , vol.19 , pp. 196-205
    • Markus, S.M.1
  • 14
    • 40449130757 scopus 로고    scopus 로고
    • Dynactin function in mitotic spindle positioning
    • Moore J.K., et al. Dynactin function in mitotic spindle positioning. Traffic 2008, 9:510-527.
    • (2008) Traffic , vol.9 , pp. 510-527
    • Moore, J.K.1
  • 15
    • 77951537332 scopus 로고    scopus 로고
    • Stoichiometry and architecture of active DNA replication machinery in Escherichia coli
    • Reyes-Lamothe R., et al. Stoichiometry and architecture of active DNA replication machinery in Escherichia coli. Science 2010, 328:498-501.
    • (2010) Science , vol.328 , pp. 498-501
    • Reyes-Lamothe, R.1
  • 16
    • 65649107604 scopus 로고    scopus 로고
    • Condensin regulates the stiffness of vertebrate centromeres
    • Ribeiro S.A., et al. Condensin regulates the stiffness of vertebrate centromeres. Mol. Biol. Cell 2009, 20:2371-2380.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2371-2380
    • Ribeiro, S.A.1
  • 17
    • 64049090249 scopus 로고    scopus 로고
    • Bir1 is required for the tension checkpoint
    • Shimogawa M.M., et al. Bir1 is required for the tension checkpoint. Mol. Biol. Cell 2009, 20:915-923.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 915-923
    • Shimogawa, M.M.1
  • 18
    • 77955647583 scopus 로고    scopus 로고
    • Quantitative analysis of the mechanism of endocytic actin patch assembly and disassembly in fission yeast
    • Sirotkin V., et al. Quantitative analysis of the mechanism of endocytic actin patch assembly and disassembly in fission yeast. Mol. Biol. Cell 2010, 21:2894-2904.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2894-2904
    • Sirotkin, V.1
  • 19
    • 70349906784 scopus 로고    scopus 로고
    • A CAAX motif can compensate for the PH domain of Num1 for cortical dynein attachment
    • Tang X., et al. A CAAX motif can compensate for the PH domain of Num1 for cortical dynein attachment. Cell Cycle 2009, 8:3182-3190.
    • (2009) Cell Cycle , vol.8 , pp. 3182-3190
    • Tang, X.1
  • 20
    • 66149144790 scopus 로고    scopus 로고
    • Kinetochore asymmetry defines a single yeast lineage
    • Thorpe P.H., et al. Kinetochore asymmetry defines a single yeast lineage. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:6673-6678.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 6673-6678
    • Thorpe, P.H.1
  • 21
    • 82255183874 scopus 로고    scopus 로고
    • Subcellular and single-molecule imaging of plant fluorescent proteins using total internal reflection fluorescence microscopy (TIRFM)
    • Vizcay-Barrena G., et al. Subcellular and single-molecule imaging of plant fluorescent proteins using total internal reflection fluorescence microscopy (TIRFM). J. Exp. Bot. 2011, 62:5419-5428.
    • (2011) J. Exp. Bot. , vol.62 , pp. 5419-5428
    • Vizcay-Barrena, G.1
  • 22
    • 38149062718 scopus 로고    scopus 로고
    • Pericentric chromatin is organized into an intramolecular loop in mitosis
    • Yeh E., et al. Pericentric chromatin is organized into an intramolecular loop in mitosis. Curr. Biol. 2008, 18:81-90.
    • (2008) Curr. Biol. , vol.18 , pp. 81-90
    • Yeh, E.1
  • 23
    • 78149309083 scopus 로고    scopus 로고
    • Detrimental incorporation of excess Cenp-A/Cid and Cenp-C into Drosophila centromeres is prevented by limiting amounts of the bridging factor Cal1
    • Schittenhelm R.B., et al. Detrimental incorporation of excess Cenp-A/Cid and Cenp-C into Drosophila centromeres is prevented by limiting amounts of the bridging factor Cal1. J. Cell Sci. 2010, 123:3768-3779.
    • (2010) J. Cell Sci. , vol.123 , pp. 3768-3779
    • Schittenhelm, R.B.1
  • 24
    • 0142215475 scopus 로고    scopus 로고
    • Global analysis of protein expression in yeast
    • Ghaemmaghami S., et al. Global analysis of protein expression in yeast. Nature 2003, 425:737-741.
    • (2003) Nature , vol.425 , pp. 737-741
    • Ghaemmaghami, S.1
  • 25
    • 0037388094 scopus 로고    scopus 로고
    • Genome-wide analysis of mRNA translation profiles in Saccharomyces cerevisiae
    • Arava Y., et al. Genome-wide analysis of mRNA translation profiles in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:3889-3894.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3889-3894
    • Arava, Y.1
  • 26
    • 0142184341 scopus 로고    scopus 로고
    • Global analysis of protein localization in budding yeast
    • Huh W.-K., et al. Global analysis of protein localization in budding yeast. Nature 2003, 425:686-691.
    • (2003) Nature , vol.425 , pp. 686-691
    • Huh, W.-K.1
  • 27
    • 37249003338 scopus 로고    scopus 로고
    • Counting kinetochore protein numbers in budding yeast using genetically encoded fluorescent proteins
    • Joglekar A.P., et al. Counting kinetochore protein numbers in budding yeast using genetically encoded fluorescent proteins. Methods Cell Biol. 2008, 85:127-151.
    • (2008) Methods Cell Biol. , vol.85 , pp. 127-151
    • Joglekar, A.P.1
  • 28
    • 34247843089 scopus 로고    scopus 로고
    • Subunit counting in membrane-bound proteins
    • Ulbrich M.H., Isacoff E.Y. Subunit counting in membrane-bound proteins. Nat. Methods 2007, 4:319-321.
    • (2007) Nat. Methods , vol.4 , pp. 319-321
    • Ulbrich, M.H.1    Isacoff, E.Y.2
  • 29
    • 57949097314 scopus 로고    scopus 로고
    • Chapter 9: counting proteins in living cells by quantitative fluorescence microscopy with internal standards
    • Wu J.-Q., et al. Chapter 9: counting proteins in living cells by quantitative fluorescence microscopy with internal standards. Methods Cell Biol. 2008, 89:253-273.
    • (2008) Methods Cell Biol. , vol.89 , pp. 253-273
    • Wu, J.-Q.1
  • 30
    • 34547510914 scopus 로고    scopus 로고
    • Membrane protein stoichiometry determined from the step-wise photobleaching of dye-labelled subunits
    • Das S.K., et al. Membrane protein stoichiometry determined from the step-wise photobleaching of dye-labelled subunits. Chembiochem 2007, 8:994-999.
    • (2007) Chembiochem , vol.8 , pp. 994-999
    • Das, S.K.1
  • 31
    • 33846551354 scopus 로고    scopus 로고
    • Counting of six pRNAs of phi29 DNA-packaging motor with customized single-molecule dual-view system
    • Shu D., et al. Counting of six pRNAs of phi29 DNA-packaging motor with customized single-molecule dual-view system. EMBO J. 2007, 26:527-537.
    • (2007) EMBO J. , vol.26 , pp. 527-537
    • Shu, D.1
  • 32
    • 70449709536 scopus 로고    scopus 로고
    • Intraflagellar transport particle size scales inversely with flagellar length: revisiting the balance-point length control model
    • Engel B.D., et al. Intraflagellar transport particle size scales inversely with flagellar length: revisiting the balance-point length control model. J. Cell Biol. 2009, 187:81-89.
    • (2009) J. Cell Biol. , vol.187 , pp. 81-89
    • Engel, B.D.1
  • 33
    • 77955102352 scopus 로고    scopus 로고
    • Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells
    • Taniguchi Y., et al. Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells. Science 2010, 329:533-538.
    • (2010) Science , vol.329 , pp. 533-538
    • Taniguchi, Y.1
  • 34
    • 84859409970 scopus 로고    scopus 로고
    • Characterization of Mid1 domains for targeting and scaffolding in fission yeast cytokinesis
    • Lee I.-J., Wu J.-Q. Characterization of Mid1 domains for targeting and scaffolding in fission yeast cytokinesis. J. Cell Sci. 2012, 125:2973-2985.
    • (2012) J. Cell Sci. , vol.125 , pp. 2973-2985
    • Lee, I.-J.1    Wu, J.-Q.2
  • 35
    • 67649612733 scopus 로고    scopus 로고
    • Accuracy and precision in quantitative fluorescence microscopy
    • Waters J.C. Accuracy and precision in quantitative fluorescence microscopy. J. Cell Biol. 2009, 185:1135-1148.
    • (2009) J. Cell Biol. , vol.185 , pp. 1135-1148
    • Waters, J.C.1
  • 36
    • 81355161263 scopus 로고    scopus 로고
    • Point centromeres contain more than a single centromere-specific Cse4 (CENP-A) nucleosome
    • Lawrimore J., et al. Point centromeres contain more than a single centromere-specific Cse4 (CENP-A) nucleosome. J. Cell Biol. 2011, 195:573-582.
    • (2011) J. Cell Biol. , vol.195 , pp. 573-582
    • Lawrimore, J.1
  • 37
    • 0034691034 scopus 로고    scopus 로고
    • Real-time light-driven dynamics of the fluorescence emission in single green fluorescent protein molecules
    • Garcia-Parajo M.F., et al. Real-time light-driven dynamics of the fluorescence emission in single green fluorescent protein molecules. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:7237-7242.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 7237-7242
    • Garcia-Parajo, M.F.1
  • 38
    • 81355149569 scopus 로고    scopus 로고
    • Setting a new standard for kinetochores
    • Short B. Setting a new standard for kinetochores. J. Cell Biol. 2011, 195:539.
    • (2011) J. Cell Biol. , vol.195 , pp. 539
    • Short, B.1
  • 39
    • 0035800739 scopus 로고    scopus 로고
    • Individual rotavirus-like particles containing 120 molecules of fluorescent protein are visible in living cells
    • Charpilienne A., et al. Individual rotavirus-like particles containing 120 molecules of fluorescent protein are visible in living cells. J. Biol. Chem. 2001, 276:29361-29367.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29361-29367
    • Charpilienne, A.1
  • 40
    • 26844562643 scopus 로고    scopus 로고
    • Counting cytokinesis proteins globally and locally in fission yeast
    • Wu J.-Q., Pollard T.D. Counting cytokinesis proteins globally and locally in fission yeast. Science 2005, 310:310-314.
    • (2005) Science , vol.310 , pp. 310-314
    • Wu, J.-Q.1    Pollard, T.D.2
  • 41
    • 0032517767 scopus 로고    scopus 로고
    • Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells
    • Hirschberg K., et al. Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells. J. Cell Biol. 1998, 143:1485-1503.
    • (1998) J. Cell Biol. , vol.143 , pp. 1485-1503
    • Hirschberg, K.1
  • 42
    • 84859599040 scopus 로고    scopus 로고
    • 'Point' centromeres of Saccharomyces harbor single centromere-specific nucleosomes
    • Henikoff S., Henikoff J.G. 'Point' centromeres of Saccharomyces harbor single centromere-specific nucleosomes. Genetics 2012, 190:1575-1577.
    • (2012) Genetics , vol.190 , pp. 1575-1577
    • Henikoff, S.1    Henikoff, J.G.2
  • 43
    • 2642546649 scopus 로고    scopus 로고
    • Spindle checkpoint protein dynamics at kinetochores in living cells
    • Howell B.J., et al. Spindle checkpoint protein dynamics at kinetochores in living cells. Curr. Biol. 2004, 14:953-964.
    • (2004) Curr. Biol. , vol.14 , pp. 953-964
    • Howell, B.J.1
  • 44
    • 0037026486 scopus 로고    scopus 로고
    • Actin dynamics in the contractile ring during cytokinesis in fission yeast
    • Pelham R.J., Chang F. Actin dynamics in the contractile ring during cytokinesis in fission yeast. Nature 2002, 419:82-86.
    • (2002) Nature , vol.419 , pp. 82-86
    • Pelham, R.J.1    Chang, F.2
  • 45
    • 30944467113 scopus 로고    scopus 로고
    • A guide to choosing fluorescent proteins
    • Shaner N.C., et al. A guide to choosing fluorescent proteins. Nat. Methods 2005, 2:905-909.
    • (2005) Nat. Methods , vol.2 , pp. 905-909
    • Shaner, N.C.1
  • 46
    • 77955640606 scopus 로고    scopus 로고
    • Fluorescent proteins and their applications in imaging living cells and tissues
    • Chudakov D.M., et al. Fluorescent proteins and their applications in imaging living cells and tissues. Physiol. Rev. 2010, 90:1103-1163.
    • (2010) Physiol. Rev. , vol.90 , pp. 1103-1163
    • Chudakov, D.M.1
  • 47
    • 79957590332 scopus 로고    scopus 로고
    • Probing cellular protein complexes using single-molecule pull-down
    • Jain A., et al. Probing cellular protein complexes using single-molecule pull-down. Nature 2011, 473:484-488.
    • (2011) Nature , vol.473 , pp. 484-488
    • Jain, A.1
  • 48
    • 84855842282 scopus 로고    scopus 로고
    • Formins filter modified actin subunits during processive elongation
    • Chen Q., et al. Formins filter modified actin subunits during processive elongation. J. Struct. Biol. 2012, 177:32-39.
    • (2012) J. Struct. Biol. , vol.177 , pp. 32-39
    • Chen, Q.1
  • 49
    • 77955867185 scopus 로고    scopus 로고
    • Genome editing with engineered zinc finger nucleases
    • Urnov F.D., et al. Genome editing with engineered zinc finger nucleases. Nat. Rev. Genet. 2010, 11:636-646.
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 636-646
    • Urnov, F.D.1
  • 50
    • 84860747716 scopus 로고    scopus 로고
    • FLASH assembly of TALENs for high-throughput genome editing
    • Reyon D., et al. FLASH assembly of TALENs for high-throughput genome editing. Nat. Biotech. 2012, 30:460-465.
    • (2012) Nat. Biotech. , vol.30 , pp. 460-465
    • Reyon, D.1
  • 51
    • 0035970084 scopus 로고    scopus 로고
    • Single-molecule measurements calibrate green fluorescent protein surface densities on transparent beads for use with 'knock-in' animals and other expression systems
    • Chiu C.-S., et al. Single-molecule measurements calibrate green fluorescent protein surface densities on transparent beads for use with 'knock-in' animals and other expression systems. J. Neurosci. Methods 2001, 105:55-63.
    • (2001) J. Neurosci. Methods , vol.105 , pp. 55-63
    • Chiu, C.-S.1
  • 52
    • 0036968859 scopus 로고    scopus 로고
    • Quantitation of GFP-fusion proteins in single living cells
    • Dundr M., et al. Quantitation of GFP-fusion proteins in single living cells. J. Struct. Biol. 2002, 140:92-99.
    • (2002) J. Struct. Biol. , vol.140 , pp. 92-99
    • Dundr, M.1
  • 53
    • 0034581177 scopus 로고    scopus 로고
    • Kinetic analysis of intracellular trafficking in single living cells with vesicular stomatitis virus protein G-green fluorescent protein hybrids
    • Hirschberg K., et al. Kinetic analysis of intracellular trafficking in single living cells with vesicular stomatitis virus protein G-green fluorescent protein hybrids. Methods Enzymol. 2000, 327:69-89.
    • (2000) Methods Enzymol. , vol.327 , pp. 69-89
    • Hirschberg, K.1
  • 54
    • 0035942284 scopus 로고    scopus 로고
    • Activation-dependent changes in receptor distribution and dendritic morphology in hippocampal neurons expressing P2X2-green fluorescent protein receptors
    • Khakh B.S., et al. Activation-dependent changes in receptor distribution and dendritic morphology in hippocampal neurons expressing P2X2-green fluorescent protein receptors. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:5288-5293.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 5288-5293
    • Khakh, B.S.1
  • 55
    • 0032581057 scopus 로고    scopus 로고
    • Quantitative imaging of TATA-binding protein in living yeast cells
    • Patterson G.H., et al. Quantitative imaging of TATA-binding protein in living yeast cells. Yeast 1998, 14:813-825.
    • (1998) Yeast , vol.14 , pp. 813-825
    • Patterson, G.H.1
  • 56
    • 0032615791 scopus 로고    scopus 로고
    • Quantitative imaging of the green fluorescent protein (GFP)
    • Piston D.W., et al. Quantitative imaging of the green fluorescent protein (GFP). Methods Cell Biol. 1999, 58:31-48.
    • (1999) Methods Cell Biol. , vol.58 , pp. 31-48
    • Piston, D.W.1
  • 57
    • 0038576209 scopus 로고    scopus 로고
    • Kinetic analysis of receptor-activated phosphoinositide turnover
    • Xu C., et al. Kinetic analysis of receptor-activated phosphoinositide turnover. J. Cell Biol. 2003, 161:779-791.
    • (2003) J. Cell Biol. , vol.161 , pp. 779-791
    • Xu, C.1
  • 58
    • 0030054589 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging: an emerging technique in fluorescence microscopy
    • Morgan C.G., Mitchell A.C. Fluorescence lifetime imaging: an emerging technique in fluorescence microscopy. Chromosome Res. 1996, 4:261-263.
    • (1996) Chromosome Res. , vol.4 , pp. 261-263
    • Morgan, C.G.1    Mitchell, A.C.2
  • 59
    • 84864262744 scopus 로고    scopus 로고
    • Cell-cycle-coupled structural oscillation of centromeric nucleosomes in yeast
    • Shivaraju M., et al. Cell-cycle-coupled structural oscillation of centromeric nucleosomes in yeast. Cell 2012, 150:304-316.
    • (2012) Cell , vol.150 , pp. 304-316
    • Shivaraju, M.1
  • 60
    • 35748946937 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy in living cells
    • Kim S.A., et al. Fluorescence correlation spectroscopy in living cells. Nat. Methods 2007, 4:963-973.
    • (2007) Nat. Methods , vol.4 , pp. 963-973
    • Kim, S.A.1
  • 61
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture
    • Xu Y., et al. Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture. Cell 2004, 116:711-723.
    • (2004) Cell , vol.116 , pp. 711-723
    • Xu, Y.1
  • 62
    • 73849086549 scopus 로고    scopus 로고
    • Roles of formin nodes and myosin motor activity in Mid1p-dependent contractile-ring assembly during fission yeast cytokinesis
    • Coffman V.C., et al. Roles of formin nodes and myosin motor activity in Mid1p-dependent contractile-ring assembly during fission yeast cytokinesis. Mol. Biol. Cell 2009, 20:5195-5210.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 5195-5210
    • Coffman, V.C.1
  • 63
    • 26244443799 scopus 로고    scopus 로고
    • Measuring the stoichiometry and physical interactions between components elucidates the architecture of the vertebrate kinetochore
    • Emanuele M.J., et al. Measuring the stoichiometry and physical interactions between components elucidates the architecture of the vertebrate kinetochore. Mol. Biol. Cell 2005, 16:4882-4892.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4882-4892
    • Emanuele, M.J.1
  • 64
    • 67650762824 scopus 로고    scopus 로고
    • Super-resolution fluorescence microscopy
    • Huang B., et al. Super-resolution fluorescence microscopy. Annu. Rev. Biochem. 2009, 78:993-1016.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 993-1016
    • Huang, B.1
  • 65
    • 66349113402 scopus 로고    scopus 로고
    • New fluorescence microscopy methods for microbiology: sharper, faster, and quantitative
    • Gitai Z. New fluorescence microscopy methods for microbiology: sharper, faster, and quantitative. Curr. Opin. Microbiol. 2009, 12:341-346.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 341-346
    • Gitai, Z.1
  • 66
    • 84859880900 scopus 로고    scopus 로고
    • Quantitative analysis of photoactivated localization microscopy (PALM) datasets using pair-correlation analysis
    • Sengupta P., Lippincott-Schwartz J. Quantitative analysis of photoactivated localization microscopy (PALM) datasets using pair-correlation analysis. Bioessays 2012, 34:396-405.
    • (2012) Bioessays , vol.34 , pp. 396-405
    • Sengupta, P.1    Lippincott-Schwartz, J.2
  • 67
    • 79960806755 scopus 로고    scopus 로고
    • Quantitative photo activated localization microscopy: unraveling the effects of photoblinking
    • Annibale P., et al. Quantitative photo activated localization microscopy: unraveling the effects of photoblinking. PLoS ONE 2011, 6:e22678.
    • (2011) PLoS ONE , vol.6
    • Annibale, P.1
  • 68
    • 84864232821 scopus 로고    scopus 로고
    • Cnp1 deposition occurs during G2 in fission yeast
    • Cnp1 deposition occurs during G2 in fission yeast. Open Biol. 2012, 2:120078.
    • (2012) Open Biol. , vol.2 , pp. 120078
    • Lando, D.1
  • 69
    • 84855495496 scopus 로고    scopus 로고
    • Bleaching/blinking assisted localization microscopy for superresolution imaging using standard fluorescent molecules
    • Burnette D.T., et al. Bleaching/blinking assisted localization microscopy for superresolution imaging using standard fluorescent molecules. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:21081-21086.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 21081-21086
    • Burnette, D.T.1
  • 70
    • 84859832789 scopus 로고    scopus 로고
    • Functioning nanomachines seen in real-time in living bacteria using single-molecule and super-resolution fluorescence imaging
    • Chiu S.-W., Leake M.C. Functioning nanomachines seen in real-time in living bacteria using single-molecule and super-resolution fluorescence imaging. Int. J. Mol. Sci. 2011, 12:2518-2542.
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 2518-2542
    • Chiu, S.-W.1    Leake, M.C.2
  • 71
    • 79952504644 scopus 로고    scopus 로고
    • Ordered and dynamic assembly of single spliceosomes
    • Hoskins A.A., et al. Ordered and dynamic assembly of single spliceosomes. Science 2011, 331:1289-1295.
    • (2011) Science , vol.331 , pp. 1289-1295
    • Hoskins, A.A.1
  • 72
    • 33746652982 scopus 로고    scopus 로고
    • Assembly of the cytokinetic contractile ring from a broad band of nodes in fission yeast
    • Wu J.-Q., et al. Assembly of the cytokinetic contractile ring from a broad band of nodes in fission yeast. J. Cell Biol. 2006, 174:391-402.
    • (2006) J. Cell Biol. , vol.174 , pp. 391-402
    • Wu, J.-Q.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.