메뉴 건너뛰기




Volumn 15, Issue 4, 2010, Pages 196-203

Advances in imaging RNA in plants

Author keywords

[No Author keywords available]

Indexed keywords

PHOTOPROTEIN; PLANT RNA;

EID: 77950630323     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tplants.2010.01.005     Document Type: Review
Times cited : (18)

References (83)
  • 1
    • 70349254021 scopus 로고    scopus 로고
    • Exploring the function-location nexus: using multiple lines of evidence in defining the subcellular location of plant proteins
    • Millar A.H., et al. Exploring the function-location nexus: using multiple lines of evidence in defining the subcellular location of plant proteins. Plant Cell 21 (2009) 1625-1631
    • (2009) Plant Cell , vol.21 , pp. 1625-1631
    • Millar, A.H.1
  • 2
    • 68349154286 scopus 로고    scopus 로고
    • Getting the message across: cytoplasmic ribonucleoprotein complexes
    • Bailey-Serres J., et al. Getting the message across: cytoplasmic ribonucleoprotein complexes. Trends Plant Sci. 14 (2009) 443-453
    • (2009) Trends Plant Sci. , vol.14 , pp. 443-453
    • Bailey-Serres, J.1
  • 3
    • 0036809125 scopus 로고    scopus 로고
    • The nuclear connection in RNA transport and localization
    • Farina K.L., and Singer R.H. The nuclear connection in RNA transport and localization. Trends Cell Biol. 12 (2002) 466-472
    • (2002) Trends Cell Biol. , vol.12 , pp. 466-472
    • Farina, K.L.1    Singer, R.H.2
  • 4
    • 0038121152 scopus 로고    scopus 로고
    • Signal recognition particle-dependent protein targeting, universal to all kingdoms of life
    • Koch H.G., et al. Signal recognition particle-dependent protein targeting, universal to all kingdoms of life. Rev. Physiol. Biochem. Pharmacol. 146 (2003) 55-94
    • (2003) Rev. Physiol. Biochem. Pharmacol. , vol.146 , pp. 55-94
    • Koch, H.G.1
  • 5
    • 16544384639 scopus 로고    scopus 로고
    • Targeting proteins to endoplasmic reticulum-derived compartments in plants. The importance of RNA localization
    • Crofts A.J., et al. Targeting proteins to endoplasmic reticulum-derived compartments in plants. The importance of RNA localization. Plant Physiol. 136 (2004) 3414-3419
    • (2004) Plant Physiol. , vol.136 , pp. 3414-3419
    • Crofts, A.J.1
  • 6
    • 40449115740 scopus 로고    scopus 로고
    • Signal sequence- and translation-independent mRNA localization to the endoplasmic reticulum
    • Pyhtila B., et al. Signal sequence- and translation-independent mRNA localization to the endoplasmic reticulum. RNA 14 (2008) 445-453
    • (2008) RNA , vol.14 , pp. 445-453
    • Pyhtila, B.1
  • 7
    • 0036883471 scopus 로고    scopus 로고
    • mRNA localization in plants: targeting to the cell's cortical region and beyond
    • Okita T.W., and Choi S.-B. mRNA localization in plants: targeting to the cell's cortical region and beyond. Curr. Opin. Plant Biol. 5 (2003) 553-559
    • (2003) Curr. Opin. Plant Biol. , vol.5 , pp. 553-559
    • Okita, T.W.1    Choi, S.-B.2
  • 8
    • 33748204183 scopus 로고    scopus 로고
    • Messages on the move: the role of the cytoskeleton in mRNA localization and translation in plants
    • Muench D.G., and Park N.-I. Messages on the move: the role of the cytoskeleton in mRNA localization and translation in plants. Can. J. Bot. 84 (2006) 572-580
    • (2006) Can. J. Bot. , vol.84 , pp. 572-580
    • Muench, D.G.1    Park, N.-I.2
  • 9
    • 56749096054 scopus 로고    scopus 로고
    • Translational control of localized mRNAs: restricting protein synthesis in space and time
    • Besse F., and Ephrussi A. Translational control of localized mRNAs: restricting protein synthesis in space and time. Nat. Rev. Mol. Cell Biol. 9 (2008) 971-980
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 971-980
    • Besse, F.1    Ephrussi, A.2
  • 10
    • 63449085035 scopus 로고    scopus 로고
    • RNA localization and polarity: from A(PC) to Z(BP)
    • Mili S., and Macara I.G. RNA localization and polarity: from A(PC) to Z(BP). Trends Cell Biol. 19 (2009) 156-164
    • (2009) Trends Cell Biol. , vol.19 , pp. 156-164
    • Mili, S.1    Macara, I.G.2
  • 11
    • 0034669149 scopus 로고    scopus 로고
    • Root hair formation: F-actin dependent tip growth is initiated by local assembly of profilin-supported F-actin meshworks accumulated within expansin-enriched bulges
    • Baluška F., et al. Root hair formation: F-actin dependent tip growth is initiated by local assembly of profilin-supported F-actin meshworks accumulated within expansin-enriched bulges. Dev. Biol. 227 (2000) 618-632
    • (2000) Dev. Biol. , vol.227 , pp. 618-632
    • Baluška, F.1
  • 12
    • 65249173477 scopus 로고    scopus 로고
    • Cytoskeleton-associated large RNP complexes in tobacco male gametophyte (EPPs) are associated with ribosomes and are involved in protein synthesis, processing, and localization
    • Honys D., et al. Cytoskeleton-associated large RNP complexes in tobacco male gametophyte (EPPs) are associated with ribosomes and are involved in protein synthesis, processing, and localization. J. Proteome Res. 8 (2009) 2015-2031
    • (2009) J. Proteome Res. , vol.8 , pp. 2015-2031
    • Honys, D.1
  • 13
    • 62449119033 scopus 로고    scopus 로고
    • Paternal control of embryonic patterning in Arabidopsis thaliana
    • Bayer M., et al. Paternal control of embryonic patterning in Arabidopsis thaliana. Science 323 (2009) 1485-1488
    • (2009) Science , vol.323 , pp. 1485-1488
    • Bayer, M.1
  • 14
    • 0028072134 scopus 로고
    • Interactions of eukaryotic elongation factor 2 with actin: a possible link between protein synthetic machinery and cytoskeleton
    • Bektas M., et al. Interactions of eukaryotic elongation factor 2 with actin: a possible link between protein synthetic machinery and cytoskeleton. FEBS Lett. 356 (1994) 89-93
    • (1994) FEBS Lett. , vol.356 , pp. 89-93
    • Bektas, M.1
  • 15
    • 0030868980 scopus 로고    scopus 로고
    • Efficient mammalian protein synthesis requires an intact F-actin system
    • Stapulionis R., et al. Efficient mammalian protein synthesis requires an intact F-actin system. J. Biol. Chem. 272 (1997) 24980-24986
    • (1997) J. Biol. Chem. , vol.272 , pp. 24980-24986
    • Stapulionis, R.1
  • 16
    • 0036175770 scopus 로고    scopus 로고
    • Interactions of elongation factor 1α with F-actin and β-actin mRNA: implications for anchoring mRNA in cell protrusions
    • Liu G., et al. Interactions of elongation factor 1α with F-actin and β-actin mRNA: implications for anchoring mRNA in cell protrusions. Mol. Biol. Cell 13 (2002) 579-592
    • (2002) Mol. Biol. Cell , vol.13 , pp. 579-592
    • Liu, G.1
  • 17
    • 64849083498 scopus 로고    scopus 로고
    • The 5′cap of tobacco mosaic virus (TMV) is required for virion attachment to the actin/endoplasmic reticulum network during early infection
    • Christensen N.M., et al. The 5′cap of tobacco mosaic virus (TMV) is required for virion attachment to the actin/endoplasmic reticulum network during early infection. Traffic 10 (2009) 536-551
    • (2009) Traffic , vol.10 , pp. 536-551
    • Christensen, N.M.1
  • 18
    • 70349780560 scopus 로고    scopus 로고
    • The eIF3 interactome reveals the translasome, a supercomplex linking protein synthesis and degradation machineries
    • Sha Z., et al. The eIF3 interactome reveals the translasome, a supercomplex linking protein synthesis and degradation machineries. Mol. Cell 36 (2009) 141-152
    • (2009) Mol. Cell , vol.36 , pp. 141-152
    • Sha, Z.1
  • 19
    • 72949113853 scopus 로고    scopus 로고
    • Emerging role for the cytoskeleton as an organizer and regulator of translation
    • Kim S., and Coulombe P.A. Emerging role for the cytoskeleton as an organizer and regulator of translation. Nat. Rev. Mol. Cell Biol. 11 (2010) 75-81
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 75-81
    • Kim, S.1    Coulombe, P.A.2
  • 20
    • 58149269508 scopus 로고    scopus 로고
    • Plant stress granules and mRNA processing bodies are distinct from heat stress granules
    • Weber C., et al. Plant stress granules and mRNA processing bodies are distinct from heat stress granules. Plant J. 56 (2008) 517-530
    • (2008) Plant J. , vol.56 , pp. 517-530
    • Weber, C.1
  • 21
    • 66249103703 scopus 로고    scopus 로고
    • RNA granules: post-transcriptional and epigenetic modulators of gene expression
    • Anderson P., and Kedersha N. RNA granules: post-transcriptional and epigenetic modulators of gene expression. Nat. Rev. Mol. Cell Biol. 10 (2009) 430-436
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 430-436
    • Anderson, P.1    Kedersha, N.2
  • 22
    • 4644242349 scopus 로고    scopus 로고
    • RNA silencing in plants
    • Baulcombe D.C. RNA silencing in plants. Nature 431 (2004) 356-363
    • (2004) Nature , vol.431 , pp. 356-363
    • Baulcombe, D.C.1
  • 23
    • 40649090437 scopus 로고    scopus 로고
    • MicroRNA metabolism in plants
    • Chen X. MicroRNA metabolism in plants. Curr. Top. Microbiol. Immunol. 320 (2008) 117-136
    • (2008) Curr. Top. Microbiol. Immunol. , vol.320 , pp. 117-136
    • Chen, X.1
  • 24
    • 69949117622 scopus 로고    scopus 로고
    • Multivesicular bodies associate with components of miRNA effector complexes and modulate miRNA activity
    • Gibbings D.J., et al. Multivesicular bodies associate with components of miRNA effector complexes and modulate miRNA activity. Nat. Cell Biol. 11 (2009) 1143-1149
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1143-1149
    • Gibbings, D.J.1
  • 25
    • 38849164219 scopus 로고    scopus 로고
    • RNA silencing movement in plants
    • Kalantidis K., et al. RNA silencing movement in plants. Biol. Cell 100 (2008) 13-26
    • (2008) Biol. Cell , vol.100 , pp. 13-26
    • Kalantidis, K.1
  • 26
    • 61849115258 scopus 로고    scopus 로고
    • Pattern formation via small RNA mobility
    • Chitwood D.H. Pattern formation via small RNA mobility. Genes Dev. 23 (2009) 549-554
    • (2009) Genes Dev. , vol.23 , pp. 549-554
    • Chitwood, D.H.1
  • 27
    • 41849109875 scopus 로고    scopus 로고
    • MicroRNA399 is a long-distance signal for the regulation of plant phosphate homeostasis
    • Pant B.D., et al. MicroRNA399 is a long-distance signal for the regulation of plant phosphate homeostasis. Plant J. 53 (2008) 731-738
    • (2008) Plant J. , vol.53 , pp. 731-738
    • Pant, B.D.1
  • 28
    • 70349153538 scopus 로고    scopus 로고
    • The sequences of Arabidopsis GA-INSENSITIVE RNA constitute the motifs that are necessary and sufficient for RNA long-distance trafficking
    • Huang N.-C., and Yu T.-S. The sequences of Arabidopsis GA-INSENSITIVE RNA constitute the motifs that are necessary and sufficient for RNA long-distance trafficking. Plant J. 59 (2009) 921-929
    • (2009) Plant J. , vol.59 , pp. 921-929
    • Huang, N.-C.1    Yu, T.-S.2
  • 29
    • 0034641909 scopus 로고    scopus 로고
    • Messenger RNA targeting of rice seed storage proteins to specific ER subdomains
    • Choi S.-B., et al. Messenger RNA targeting of rice seed storage proteins to specific ER subdomains. Nature 407 (2000) 765-767
    • (2000) Nature , vol.407 , pp. 765-767
    • Choi, S.-B.1
  • 30
    • 38349168419 scopus 로고    scopus 로고
    • Calreticulin mRNA and protein are localized to protein bodies in storage maize callus cells
    • Šamaj J., et al. Calreticulin mRNA and protein are localized to protein bodies in storage maize callus cells. Plant Cell Rep. 27 (2008) 231-239
    • (2008) Plant Cell Rep. , vol.27 , pp. 231-239
    • Šamaj, J.1
  • 31
    • 70349490931 scopus 로고    scopus 로고
    • Identification of cis-localization elements of the maize 10-kDa δ-zein and their use in targeting RNAs to specific cortical endoplasmic reticulum subdomains
    • Washida H., et al. Identification of cis-localization elements of the maize 10-kDa δ-zein and their use in targeting RNAs to specific cortical endoplasmic reticulum subdomains. Plant J. 60 (2009) 146-155
    • (2009) Plant J. , vol.60 , pp. 146-155
    • Washida, H.1
  • 32
    • 70349899132 scopus 로고    scopus 로고
    • Identification of cis-localization elements that target glutelin RNAs to a specific subdomain of the cortical endoplasmic reticulum in rice endosperm cells
    • Washida H., et al. Identification of cis-localization elements that target glutelin RNAs to a specific subdomain of the cortical endoplasmic reticulum in rice endosperm cells. Plant Cell Physiol. 50 (2009) 1710-1714
    • (2009) Plant Cell Physiol. , vol.50 , pp. 1710-1714
    • Washida, H.1
  • 33
    • 65449131152 scopus 로고    scopus 로고
    • Imaging intracellular RNA distribution and dynamics in living cells
    • Tyagi S. Imaging intracellular RNA distribution and dynamics in living cells. Nat. Methods 6 (2009) 331-338
    • (2009) Nat. Methods , vol.6 , pp. 331-338
    • Tyagi, S.1
  • 34
    • 0032185810 scopus 로고    scopus 로고
    • Localization of ASH1 mRNA particles in living yeast
    • Bertrand E., et al. Localization of ASH1 mRNA particles in living yeast. Mol. Cell 2 (1998) 437-445
    • (1998) Mol. Cell , vol.2 , pp. 437-445
    • Bertrand, E.1
  • 35
    • 0027960331 scopus 로고
    • Crystal structure of an RNA bacteriophage coat protein-operator complex
    • Valegård K., et al. Crystal structure of an RNA bacteriophage coat protein-operator complex. Nature 371 (1994) 623-626
    • (1994) Nature , vol.371 , pp. 623-626
    • Valegård, K.1
  • 36
    • 0030454007 scopus 로고    scopus 로고
    • Mutagenesis of a stacking contact in the MS2 coat protein-RNA complex
    • LeCuyer K.A., et al. Mutagenesis of a stacking contact in the MS2 coat protein-RNA complex. EMBO J. 15 (1996) 6847-6853
    • (1996) EMBO J. , vol.15 , pp. 6847-6853
    • LeCuyer, K.A.1
  • 37
    • 1842712418 scopus 로고    scopus 로고
    • Enod40, a short open reading frame-containing mRNA, induces cytoplasmic localization of a nuclear RNA binding protein in Medicago truncatula
    • Campalans A., et al. Enod40, a short open reading frame-containing mRNA, induces cytoplasmic localization of a nuclear RNA binding protein in Medicago truncatula. Plant Cell 16 (2004) 1047-1059
    • (2004) Plant Cell , vol.16 , pp. 1047-1059
    • Campalans, A.1
  • 38
    • 34548805997 scopus 로고    scopus 로고
    • Location of a possible miRNA processing site in SmD3/SmB nuclear bodies in Arabidopsis
    • Fujioka Y., et al. Location of a possible miRNA processing site in SmD3/SmB nuclear bodies in Arabidopsis. Plant Cell Physiol. 48 (2007) 1243-1253
    • (2007) Plant Cell Physiol. , vol.48 , pp. 1243-1253
    • Fujioka, Y.1
  • 39
    • 34247368510 scopus 로고    scopus 로고
    • Identification of nuclear dicing bodies containing proteins for microRNA biogenesis in living Arabidopsis plants
    • Fang Y., and Spector D.L. Identification of nuclear dicing bodies containing proteins for microRNA biogenesis in living Arabidopsis plants. Curr. Biol. 17 (2007) 818-823
    • (2007) Curr. Biol. , vol.17 , pp. 818-823
    • Fang, Y.1    Spector, D.L.2
  • 40
    • 3843126332 scopus 로고    scopus 로고
    • RNA dynamics in live Escherichia coli cells
    • Golding I., and Cox E.C. RNA dynamics in live Escherichia coli cells. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 11310-11315
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 11310-11315
    • Golding, I.1    Cox, E.C.2
  • 41
    • 0141681117 scopus 로고    scopus 로고
    • A novel procedure for the localization of viral RNAs in protoplasts and whole plants
    • Zhang F., and Simon A.E. A novel procedure for the localization of viral RNAs in protoplasts and whole plants. Plant J. 35 (2003) 665-673
    • (2003) Plant J. , vol.35 , pp. 665-673
    • Zhang, F.1    Simon, A.E.2
  • 42
    • 0142124105 scopus 로고    scopus 로고
    • The transport of prolamine RNAs to prolamine protein bodies in living rice endosperm cells
    • Hamada S., et al. The transport of prolamine RNAs to prolamine protein bodies in living rice endosperm cells. Plant Cell 15 (2003) 2253-2264
    • (2003) Plant Cell , vol.15 , pp. 2253-2264
    • Hamada, S.1
  • 43
    • 56149089390 scopus 로고    scopus 로고
    • Transport of TMV movement protein particles associated with the targeting of RNA to plasmodesmata
    • Sambade A., et al. Transport of TMV movement protein particles associated with the targeting of RNA to plasmodesmata. Traffic 9 (2008) 2073-2088
    • (2008) Traffic , vol.9 , pp. 2073-2088
    • Sambade, A.1
  • 44
    • 0037560769 scopus 로고    scopus 로고
    • RNA-binding protein-mediated translational repression of transgene expression in plants
    • Cerny R.E., et al. RNA-binding protein-mediated translational repression of transgene expression in plants. Plant Mol. Biol. 52 (2003) 357-369
    • (2003) Plant Mol. Biol. , vol.52 , pp. 357-369
    • Cerny, R.E.1
  • 45
    • 47849121275 scopus 로고    scopus 로고
    • Simultaneous transport of different localized mRNA species revealed by live-cell imaging
    • Lange S., et al. Simultaneous transport of different localized mRNA species revealed by live-cell imaging. Traffic 9 (2008) 1256-1267
    • (2008) Traffic , vol.9 , pp. 1256-1267
    • Lange, S.1
  • 46
    • 34547637607 scopus 로고    scopus 로고
    • λN-GFP: an RNA reporter system for live-cell imaging
    • Daigle N., and Ellenberg J. λN-GFP: an RNA reporter system for live-cell imaging. Nat. Methods 4 (2007) 633-636
    • (2007) Nat. Methods , vol.4 , pp. 633-636
    • Daigle, N.1    Ellenberg, J.2
  • 47
    • 0022368688 scopus 로고
    • Conservation of genome form but not sequence in the transcription antitermination determinants of bacteriophages λ, φ21 and P22
    • Franklin N.C. Conservation of genome form but not sequence in the transcription antitermination determinants of bacteriophages λ, φ21 and P22. J. Mol. Biol. 181 (1985) 75-84
    • (1985) J. Mol. Biol. , vol.181 , pp. 75-84
    • Franklin, N.C.1
  • 48
    • 0037130670 scopus 로고    scopus 로고
    • Designed arginine-rich RNA-binding peptides with picomolar affinity
    • Austin R.J., et al. Designed arginine-rich RNA-binding peptides with picomolar affinity. J. Am. Chem. Soc. 124 (2002) 10966-10967
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10966-10967
    • Austin, R.J.1
  • 49
    • 2942733310 scopus 로고    scopus 로고
    • Dynamics of single mRNPs in nuclei of living cells
    • Shav-Tal Y., et al. Dynamics of single mRNPs in nuclei of living cells. Science 304 (2004) 1797-1800
    • (2004) Science , vol.304 , pp. 1797-1800
    • Shav-Tal, Y.1
  • 50
    • 27644596367 scopus 로고    scopus 로고
    • Photoactivatable fluorescent proteins
    • Lukyanov K.A., et al. Photoactivatable fluorescent proteins. Nat. Rev. Mol. Cell Biol. 6 (2005) 885-891
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 885-891
    • Lukyanov, K.A.1
  • 51
    • 70350302609 scopus 로고    scopus 로고
    • Photoactivatable fluorescent proteins for diffraction-limited and super-resolution imaging
    • Lippincott-Schwartz J., and Patterson G.H. Photoactivatable fluorescent proteins for diffraction-limited and super-resolution imaging. Trends Cell Biol. 19 (2009) 555-565
    • (2009) Trends Cell Biol. , vol.19 , pp. 555-565
    • Lippincott-Schwartz, J.1    Patterson, G.H.2
  • 52
    • 77950628949 scopus 로고    scopus 로고
    • Measurement of protein motion by photobleaching
    • Stephens D. (Ed), Scion
    • Presley J.F. Measurement of protein motion by photobleaching. In: Stephens D. (Ed). Methods Express: Cell Imaging (2006), Scion 119-142
    • (2006) Methods Express: Cell Imaging , pp. 119-142
    • Presley, J.F.1
  • 53
    • 34250210525 scopus 로고    scopus 로고
    • Imaging dynamics of endogenous mitochondrial RNA in single living cells
    • Ozawa T., et al. Imaging dynamics of endogenous mitochondrial RNA in single living cells. Nat. Methods 4 (2007) 413-419
    • (2007) Nat. Methods , vol.4 , pp. 413-419
    • Ozawa, T.1
  • 54
    • 33748784359 scopus 로고    scopus 로고
    • Engineering RNA sequence specificity of pumilio repeats
    • Cheong C.-G., and Tanaka Hall T.M. Engineering RNA sequence specificity of pumilio repeats. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 13635-13639
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 13635-13639
    • Cheong, C.-G.1    Tanaka Hall, T.M.2
  • 55
    • 0037162703 scopus 로고    scopus 로고
    • Modular recognition of RNA by a human pumilio-homology domain
    • Wang X., et al. Modular recognition of RNA by a human pumilio-homology domain. Cell 110 (2002) 501-512
    • (2002) Cell , vol.110 , pp. 501-512
    • Wang, X.1
  • 56
    • 59149083312 scopus 로고    scopus 로고
    • Live-cell imaging of viral RNA genomes using a Pumilio-based reporter
    • Tilsner J., et al. Live-cell imaging of viral RNA genomes using a Pumilio-based reporter. Plant J. 57 (2009) 758-770
    • (2009) Plant J. , vol.57 , pp. 758-770
    • Tilsner, J.1
  • 57
    • 73849139654 scopus 로고    scopus 로고
    • Sequential recruitment of the endoplasmic reticulum and chloroplasts for plant potyvirus replication
    • Wei T., et al. Sequential recruitment of the endoplasmic reticulum and chloroplasts for plant potyvirus replication. J. Virol. 84 (2010) 799-809
    • (2010) J. Virol. , vol.84 , pp. 799-809
    • Wei, T.1
  • 58
    • 70349241918 scopus 로고    scopus 로고
    • Molecular characterization of Arabidopsis thaliana PUF proteins - binding specificity and target candidates
    • Francischini C.W., and Quaggio R.B. Molecular characterization of Arabidopsis thaliana PUF proteins - binding specificity and target candidates. FEBS J. 276 (2009) 5456-5470
    • (2009) FEBS J. , vol.276 , pp. 5456-5470
    • Francischini, C.W.1    Quaggio, R.B.2
  • 59
    • 60349124749 scopus 로고    scopus 로고
    • Understanding and engineering RNA sequence specificity of PUF proteins
    • Lu G., et al. Understanding and engineering RNA sequence specificity of PUF proteins. Curr. Opin. Struct. Biol. 19 (2009) 110-115
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 110-115
    • Lu, G.1
  • 60
    • 58149095365 scopus 로고    scopus 로고
    • Visualizing RNA-protein interactions inside cells by fluorescence resonance energy transfer
    • Lorenz M. Visualizing RNA-protein interactions inside cells by fluorescence resonance energy transfer. RNA 15 (2009) 97-103
    • (2009) RNA , vol.15 , pp. 97-103
    • Lorenz, M.1
  • 61
    • 34247523672 scopus 로고    scopus 로고
    • Fluorescent sensors for specific RNA: a general paradigm using chemistry and combinatorial biology
    • Sparano B.A., and Koide K. Fluorescent sensors for specific RNA: a general paradigm using chemistry and combinatorial biology. J. Am. Chem. Soc. 129 (2007) 4785-4794
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 4785-4794
    • Sparano, B.A.1    Koide, K.2
  • 62
    • 4344574101 scopus 로고    scopus 로고
    • Uncapped mRNA introduced into tobacco protoplasts can be imported into the nucleus and is trapped by leptomycin B
    • Stuger R., and Forreiter C. Uncapped mRNA introduced into tobacco protoplasts can be imported into the nucleus and is trapped by leptomycin B. Plant Cell Rep. 23 (2004) 99-103
    • (2004) Plant Cell Rep. , vol.23 , pp. 99-103
    • Stuger, R.1    Forreiter, C.2
  • 63
    • 0035917422 scopus 로고    scopus 로고
    • Drosophila wingless and pair-rule transcripts localize apically by dynein-mediated transport of RNA particles
    • Wilkie G., and Davis I. Drosophila wingless and pair-rule transcripts localize apically by dynein-mediated transport of RNA particles. Cell 105 (2001) 209-219
    • (2001) Cell , vol.105 , pp. 209-219
    • Wilkie, G.1    Davis, I.2
  • 64
    • 0029123280 scopus 로고
    • Protein translation components are colocalized in granules in oligodendrocytes
    • Barbarese E., et al. Protein translation components are colocalized in granules in oligodendrocytes. J. Cell Sci. 108 (1995) 2781-2790
    • (1995) J. Cell Sci. , vol.108 , pp. 2781-2790
    • Barbarese, E.1
  • 65
    • 0031849940 scopus 로고    scopus 로고
    • Molecular dissection of the mechanism by which potexvirus triple gene block proteins mediate cell-to-cell transport of infectious RNA
    • Lough T.J., et al. Molecular dissection of the mechanism by which potexvirus triple gene block proteins mediate cell-to-cell transport of infectious RNA. Mol. Plant Microbe Interact. 11 (1998) 801-814
    • (1998) Mol. Plant Microbe Interact. , vol.11 , pp. 801-814
    • Lough, T.J.1
  • 66
    • 0036734759 scopus 로고    scopus 로고
    • All small nuclear RNAs (snRNAs) of the [U4/U6.U5] tri-snRNP localize to nucleoli; identification of the nucleolar localization element of U6 snRNA
    • Gerbi S.A., and Lange T.S. All small nuclear RNAs (snRNAs) of the [U4/U6.U5] tri-snRNP localize to nucleoli; identification of the nucleolar localization element of U6 snRNA. Mol. Biol. Cell 13 (2002) 3123-3137
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3123-3137
    • Gerbi, S.A.1    Lange, T.S.2
  • 67
    • 0029670262 scopus 로고    scopus 로고
    • Molecular beacons: probes that fluoresce upon hybridization
    • Tyagi S., and Kramer F.R. Molecular beacons: probes that fluoresce upon hybridization. Nat. Biotechnol. 14 (1996) 303-308
    • (1996) Nat. Biotechnol. , vol.14 , pp. 303-308
    • Tyagi, S.1    Kramer, F.R.2
  • 68
    • 48949116125 scopus 로고    scopus 로고
    • Molecular beacons: an optimal multifunctional biological probe
    • Li Y., et al. Molecular beacons: an optimal multifunctional biological probe. Biochem. Biophys. Res. Comm. 373 (2008) 457-461
    • (2008) Biochem. Biophys. Res. Comm. , vol.373 , pp. 457-461
    • Li, Y.1
  • 69
    • 33645158637 scopus 로고    scopus 로고
    • Nanostructured probes for RNA detection in living cells
    • Santangelo P.J., et al. Nanostructured probes for RNA detection in living cells. Ann. Biomed. Eng. 34 (2006) 39-50
    • (2006) Ann. Biomed. Eng. , vol.34 , pp. 39-50
    • Santangelo, P.J.1
  • 70
    • 0032510736 scopus 로고    scopus 로고
    • PD-loop: a complex of duplex DNA with an oligonucleotide
    • Bukanov N.O., et al. PD-loop: a complex of duplex DNA with an oligonucleotide. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 5516-5520
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5516-5520
    • Bukanov, N.O.1
  • 71
    • 3843132105 scopus 로고    scopus 로고
    • Dual FRET molecular beacons for mRNA detection in living cells
    • Santangelo P.J., et al. Dual FRET molecular beacons for mRNA detection in living cells. Nucleic. Acids Res. 32 (2004) e57
    • (2004) Nucleic. Acids Res. , vol.32
    • Santangelo, P.J.1
  • 72
    • 0033764715 scopus 로고    scopus 로고
    • Wavelength-shifting molecular beacons
    • Tyagi S., et al. Wavelength-shifting molecular beacons. Nat. Biotechnol. 18 (2000) 1191-1196
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1191-1196
    • Tyagi, S.1
  • 73
    • 0344824383 scopus 로고    scopus 로고
    • Visualizing the distribution and transport of mRNAs in living cells
    • Bratu D.P., et al. Visualizing the distribution and transport of mRNAs in living cells. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 13308-13313
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13308-13313
    • Bratu, D.P.1
  • 74
    • 10044298658 scopus 로고    scopus 로고
    • Imaging native β-actin mRNA in motile fibroblasts
    • Tyagi S., and Alsmadi O. Imaging native β-actin mRNA in motile fibroblasts. Biophys. J. 87 (2004) 4153-4162
    • (2004) Biophys. J. , vol.87 , pp. 4153-4162
    • Tyagi, S.1    Alsmadi, O.2
  • 75
    • 32944464429 scopus 로고    scopus 로고
    • Direct visualization of mRNA colocalization with mitochondria in living cells using molecular beacons
    • Santangelo P.J., et al. Direct visualization of mRNA colocalization with mitochondria in living cells using molecular beacons. J. Biomed. Opt. 10 (2005) 44025
    • (2005) J. Biomed. Opt. , vol.10 , pp. 44025
    • Santangelo, P.J.1
  • 76
    • 28044451048 scopus 로고    scopus 로고
    • Mechanism of mRNA transport in the nucleus
    • Vargas D.Y., et al. Mechanism of mRNA transport in the nucleus. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17008-17013
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 17008-17013
    • Vargas, D.Y.1
  • 77
    • 50849120356 scopus 로고    scopus 로고
    • Imaging and characterizing influenza A virus mRNA transport in living cells
    • Wang W., et al. Imaging and characterizing influenza A virus mRNA transport in living cells. Nucleic. Acids Res. 36 (2008) 4913-4928
    • (2008) Nucleic. Acids Res. , vol.36 , pp. 4913-4928
    • Wang, W.1
  • 78
    • 67349101852 scopus 로고    scopus 로고
    • Single molecule-sensitive probes for imaging RNA in live cells
    • Santagelo P.J., et al. Single molecule-sensitive probes for imaging RNA in live cells. Nat. Methods 6 (2009) 347-349
    • (2009) Nat. Methods , vol.6 , pp. 347-349
    • Santagelo, P.J.1
  • 79
    • 33748456465 scopus 로고    scopus 로고
    • The visible touch: in planta visualization of protein-protein interactions by fluorophore-based methods
    • Bhat R.A., et al. The visible touch: in planta visualization of protein-protein interactions by fluorophore-based methods. Plant Methods 2 (2006) 12
    • (2006) Plant Methods , vol.2 , pp. 12
    • Bhat, R.A.1
  • 80
    • 49749107169 scopus 로고    scopus 로고
    • Fluorescence-based methods in the study of protein-protein interactions in living cells
    • Ciruela F. Fluorescence-based methods in the study of protein-protein interactions in living cells. Curr. Opin. Biotechnol. 19 (2008) 338-343
    • (2008) Curr. Opin. Biotechnol. , vol.19 , pp. 338-343
    • Ciruela, F.1
  • 81
    • 59349120472 scopus 로고    scopus 로고
    • Imaging protein-protein interactions in plant cells by bimolecular fluorescence complementation assay
    • Weinthal D., and Tzfira T. Imaging protein-protein interactions in plant cells by bimolecular fluorescence complementation assay. Trends Plant Sci. 14 (2009) 59-63
    • (2009) Trends Plant Sci. , vol.14 , pp. 59-63
    • Weinthal, D.1    Tzfira, T.2
  • 82
    • 33745208135 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging
    • Stephens D. (Ed), Scion
    • Suhling K. Fluorescence lifetime imaging. In: Stephens D. (Ed). Methods Express: Cell Imaging. (2006), Scion 219-245
    • (2006) Methods Express: Cell Imaging. , pp. 219-245
    • Suhling, K.1
  • 83
    • 53249155165 scopus 로고    scopus 로고
    • Detecting protein-protein interactions in vivo with FRET using multiphoton fluorescence lifetime imaging microscopy (FLIM)
    • 12.10.1-12.10.19
    • Llères D. Detecting protein-protein interactions in vivo with FRET using multiphoton fluorescence lifetime imaging microscopy (FLIM). Curr. Protoc. Cytom. 42 (2007) 12.10.1-12.10.19
    • (2007) Curr. Protoc. Cytom. , vol.42
    • Llères, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.