메뉴 건너뛰기




Volumn 5, Issue 9, 2010, Pages

Sets of RNA repeated tags and Hybridization-sensitive fluorescent probes for distinct images of RNA in a living cell

Author keywords

[No Author keywords available]

Indexed keywords

3' UNTRANSLATED REGION; ARTICLE; CONTROLLED STUDY; DIMERIZATION; EXCITON CONTROLLED HYBRIDIZATION SENSITIVE OLIGONUCLEOTIDE PROBE; GENE EXPRESSION; HUMAN; HUMAN CELL; IMAGING; PHOTOCHEMISTRY; PLASMID; PROTEIN BINDING; RNA HYBRIDIZATION; RNA PROBE; RNA SYNTHESIS; SENSITIVITY ANALYSIS; SEQUENCE TAGGED SITE; TEMPERATURE; CELL; CELL NUCLEUS; CHEMISTRY; CYTOLOGY; EVALUATION; GENETIC PROCEDURES; GENETICS; HELA CELL; METHODOLOGY; NUCLEIC ACID HYBRIDIZATION; STAINING;

EID: 77958552723     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0013003     Document Type: Article
Times cited : (36)

References (41)
  • 1
    • 69049101215 scopus 로고    scopus 로고
    • Lighting up mRNA localization in Drosophila oogenesis
    • Becalska AN, Gavis ER (2009) Lighting up mRNA localization in Drosophila oogenesis. Development 136: 2493-2503.
    • (2009) Development , vol.136 , pp. 2493-2503
    • Becalska, A.N.1    Gavis, E.R.2
  • 2
    • 0035871382 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of brain-derived neurotrophic factor mRNA induction in the vestibulo-olivary network during vestibular compensation
    • Li YX, Hashimoto T, Tokuyama W, Miyashita Y, Okuno H (2001) Spatiotemporal dynamics of brain-derived neurotrophic factor mRNA induction in the vestibulo-olivary network during vestibular compensation. J Neurosci 21: 2738-2748.
    • (2001) J Neurosci , vol.21 , pp. 2738-2748
    • Li, Y.X.1    Hashimoto, T.2    Tokuyama, W.3    Miyashita, Y.4    Okuno, H.5
  • 3
    • 70349895664 scopus 로고    scopus 로고
    • The transcriptional regulation and cell-specific expression of the MAPK-activated protein kinase MK5
    • Gerits N, Shiryaev A, Kostenko S, Klenow H, Shiryaeva O, et al. (2009) The transcriptional regulation and cell-specific expression of the MAPK-activated protein kinase MK5. Cell Mol Biol Lett 14: 548-574.
    • (2009) Cell Mol Biol Lett , vol.14 , pp. 548-574
    • Gerits, N.1    Shiryaev, A.2    Kostenko, S.3    Klenow, H.4    Shiryaeva, O.5
  • 4
    • 0035891415 scopus 로고    scopus 로고
    • Real-time monitoring of intracellular mRNA hybridization inside single living cells
    • Perlette J, Tan W (2001) Real-time monitoring of intracellular mRNA hybridization inside single living cells. Anal Chem 73: 5544-5550.
    • (2001) Anal Chem , vol.73 , pp. 5544-5550
    • Perlette, J.1    Tan, W.2
  • 5
    • 67651151407 scopus 로고    scopus 로고
    • Fluorescent probes for live-cell RNA detection
    • Bao G, Rhee WJ, Tsourkas A (2009) Fluorescent probes for live-cell RNA detection. Ann Rev Biomed Eng 11: 25-47.
    • (2009) Ann Rev Biomed Eng , vol.11 , pp. 25-47
    • Bao, G.1    Rhee, W.J.2    Tsourkas, A.3
  • 6
    • 65449131152 scopus 로고    scopus 로고
    • Imaging intracellular RNA distribution and dynamics in living cells
    • Tyagi S (2009) Imaging intracellular RNA distribution and dynamics in living cells. Nat Methods 6: 331-338.
    • (2009) Nat Methods , vol.6 , pp. 331-338
    • Tyagi, S.1
  • 7
    • 50249187299 scopus 로고    scopus 로고
    • Hybridization-sensitive on-off DNA probe: Application of the exciton coupling effect to effective fluorescence quenching
    • Ikeda S, Okamoto A (2008) Hybridization-sensitive on-off DNA probe: Application of the exciton coupling effect to effective fluorescence quenching. Chem Asian J 3: 958-968.
    • (2008) Chem Asian J , vol.3 , pp. 958-968
    • Ikeda, S.1    Okamoto, A.2
  • 8
    • 70350504861 scopus 로고    scopus 로고
    • Reevaluation of absolute luminescence quantum yields of standard solutions using a spectrometer with an integrating sphere and a back-thinned CCD detector
    • Suzuki K, Kobayashi A, Kaneko S, Takehira K, Yoshihara T, et al. (2009) Reevaluation of absolute luminescence quantum yields of standard solutions using a spectrometer with an integrating sphere and a back-thinned CCD detector. Phys Chem Chem Phys 11: 9850-9860.
    • (2009) Phys Chem Chem Phys , vol.11 , pp. 9850-9860
    • Suzuki, K.1    Kobayashi, A.2    Kaneko, S.3    Takehira, K.4    Yoshihara, T.5
  • 9
    • 56049095074 scopus 로고    scopus 로고
    • Exploration of human ORFeome: High-throughput preparation of ORF clones and efficient characterization of their protein products
    • Nagase T, Yamakawa H, Tadokoro S, Nakajima D, Inoue S, et al. (2008) Exploration of human ORFeome: High-throughput preparation of ORF clones and efficient characterization of their protein products. DNA Res 15: 137-149.
    • (2008) DNA Res , vol.15 , pp. 137-149
    • Nagase, T.1    Yamakawa, H.2    Tadokoro, S.3    Nakajima, D.4    Inoue, S.5
  • 10
    • 4344698577 scopus 로고    scopus 로고
    • The use of recombinant methods and molecular engineering in protein crystallization
    • Derewenda ZS (2004) The use of recombinant methods and molecular engineering in protein crystallization. Methods 34: 354-363.
    • (2004) Methods , vol.34 , pp. 354-363
    • Derewenda, Z.S.1
  • 11
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighboring histidine-residues
    • Hochuli E, Dobeli H, Schacher A (1987) New metal chelate adsorbent selective for proteins and peptides containing neighboring histidine-residues. J Chromatogr 411: 177-184.
    • (1987) J Chromatogr , vol.411 , pp. 177-184
    • Hochuli, E.1    Dobeli, H.2    Schacher, A.3
  • 12
    • 0035814333 scopus 로고    scopus 로고
    • Site-specific incorporation of fluorescent probes into protein: Hexahistidine-tag-mediated fluorescent labeling with (Ni2+: Nitrilotriacetic acid)n-fluorochrome conjugates
    • Kapanidis AN, Ebright YW, Ebright RH (2001) Site-specific incorporation of fluorescent probes into protein: Hexahistidine-tag-mediated fluorescent labeling with (Ni2+: Nitrilotriacetic acid)n-fluorochrome conjugates. J Am Chem Soc 123: 12123-12125.
    • (2001) J Am Chem Soc , vol.123 , pp. 12123-12125
    • Kapanidis, A.N.1    Ebright, Y.W.2    Ebright, R.H.3
  • 13
    • 77049121012 scopus 로고    scopus 로고
    • Hexahistidine-tag-specific optical probes for analyses of proteins and their interactions
    • Zhao C, Hellman LM, Zhan X, Bowman WS, Whiteheart SW, et al. (2010) Hexahistidine-tag-specific optical probes for analyses of proteins and their interactions. Anal Biochem 399: 237-245.
    • (2010) Anal Biochem , vol.399 , pp. 237-245
    • Zhao, C.1    Hellman, L.M.2    Zhan, X.3    Bowman, W.S.4    Whiteheart, S.W.5
  • 15
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin BA, Adams SR, Tsien RY (1998) Specific covalent labeling of recombinant protein molecules inside live cells. Science 281: 269-272.
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 16
    • 0037134035 scopus 로고    scopus 로고
    • Multicolor and electron microscopic imaging of connexin trafficking
    • Gaietta G, Deerinck TJ, Adams SR, Bouwer J, Tour O, et al. (2002) Multicolor and electron microscopic imaging of connexin trafficking. Science 296: 503-507.
    • (2002) Science , vol.296 , pp. 503-507
    • Gaietta, G.1    Deerinck, T.J.2    Adams, S.R.3    Bouwer, J.4    Tour, O.5
  • 17
    • 33747613117 scopus 로고    scopus 로고
    • Oligo-Asp Tag/Zn(II) complex probe as a new pair for labeling and fluorescence imaging of proteins
    • Ojida A, Honda K, Shinmi D, Kiyonaka S, Mori Y, et al. (2006) Oligo-Asp Tag/Zn(II) complex probe as a new pair for labeling and fluorescence imaging of proteins. J Am Chem Soc 128: 10452-10459.
    • (2006) J Am Chem Soc , vol.128 , pp. 10452-10459
    • Ojida, A.1    Honda, K.2    Shinmi, D.3    Kiyonaka, S.4    Mori, Y.5
  • 18
    • 34548127647 scopus 로고    scopus 로고
    • Pyrene excimer-based dualemission detection of a oligoaspartate tag-fused protein by using a Zn-11- DpaTyr probe
    • Honda K, Fujishima S, Ojida A, Hamachi I (2007) Pyrene excimer-based dualemission detection of a oligoaspartate tag-fused protein by using a Zn-11- DpaTyr probe. Chembiochem 8: 1370-1372.
    • (2007) Chembiochem , vol.8 , pp. 1370-1372
    • Honda, K.1    Fujishima, S.2    Ojida, A.3    Hamachi, I.4
  • 19
    • 33749069983 scopus 로고    scopus 로고
    • Ratiometric fluorescence detection of a tag fused protein using the dual-emission artificial molecular probe
    • Honda K, Nakata E, Ojida A, Hamachi I (2006) Ratiometric fluorescence detection of a tag fused protein using the dual-emission artificial molecular probe. Chem Commun. pp 4024-4026.
    • (2006) Chem Commun , pp. 4024-4026
    • Honda, K.1    Nakata, E.2    Ojida, A.3    Hamachi, I.4
  • 20
    • 63049130350 scopus 로고    scopus 로고
    • Singlemolecule imaging of β-actin mRNAs in the cytoplasm of a living cell
    • Yamagishi M, Ishihama Y, Shirasaki Y, Kurama H, Funatsu T (2009) Singlemolecule imaging of β-actin mRNAs in the cytoplasm of a living cell. Exp Cell Res 315: 1142-1147.
    • (2009) Exp Cell Res , vol.315 , pp. 1142-1147
    • Yamagishi, M.1    Ishihama, Y.2    Shirasaki, Y.3    Kurama, H.4    Funatsu, T.5
  • 21
    • 0347156907 scopus 로고    scopus 로고
    • Single mRNA molecules demonstrate probabilistic movement in living mammalian cells
    • Fusco D, Accornero N, Lavoie B, Shenoy SM, Blanchard JM, et al. (2003) Single mRNA molecules demonstrate probabilistic movement in living mammalian cells. Curr. Biol 13: 161-167.
    • (2003) Curr. Biol , vol.13 , pp. 161-167
    • Fusco, D.1    Accornero, N.2    Lavoie, B.3    Shenoy, S.M.4    Blanchard, J.M.5
  • 22
    • 33846958757 scopus 로고    scopus 로고
    • Dynamics of bidirectional transport of Arc mRNA in neuronal dendrites
    • Dynes JL, Steward O (2007) Dynamics of bidirectional transport of Arc mRNA in neuronal dendrites. J Comp Neurol 500: 433-447.
    • (2007) J Comp Neurol , vol.500 , pp. 433-447
    • Dynes, J.L.1    Steward, O.2
  • 23
    • 3843126332 scopus 로고    scopus 로고
    • RNA dynamics in live Escherichia coli cells
    • Golding I, Cox EC (2004) RNA dynamics in live Escherichia coli cells. Proc Natl Acad Sci U S A 101: 11310-11315.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 11310-11315
    • Golding, I.1    Cox, E.C.2
  • 24
    • 0344430112 scopus 로고    scopus 로고
    • Aptamers switch on fluorescence of triphenylmethane dyes
    • Babendure JR, Adams SR, Tsien RY (2003) Aptamers switch on fluorescence of triphenylmethane dyes. J Am Chem Soc 125: 14716-14717.
    • (2003) J Am Chem Soc , vol.125 , pp. 14716-14717
    • Babendure, J.R.1    Adams, S.R.2    Tsien, R.Y.3
  • 25
    • 34247523672 scopus 로고    scopus 로고
    • Fluorescent sensors for specific RNA: A general paradigm using chemistry and combinatorial biology
    • Sparano BA, Koide K (2007) Fluorescent sensors for specific RNA: A general paradigm using chemistry and combinatorial biology. J Am Chem Soc 129: 4785-4794.
    • (2007) J Am Chem Soc , vol.129 , pp. 4785-4794
    • Sparano, B.A.1    Koide, K.2
  • 26
    • 35348969892 scopus 로고    scopus 로고
    • Light-up Hoechst-DNA aptamer pair: Generation of an aptamer-selective fluorophore from a conventional DNAstaining dye
    • Sando S, Narita A, Aoyama Y (2007) Light-up Hoechst-DNA aptamer pair: Generation of an aptamer-selective fluorophore from a conventional DNAstaining dye. Chembiochem 8: 1795-1803.
    • (2007) Chembiochem , vol.8 , pp. 1795-1803
    • Sando, S.1    Narita, A.2    Aoyama, Y.3
  • 28
    • 50249150245 scopus 로고    scopus 로고
    • Transcription monitoring using fused RNA with a dye-binding light-up aptamer as a tag: A blue fluorescent RNA
    • Sando S, Narita A, Hayami M, Aoyama Y (2008) Transcription monitoring using fused RNA with a dye-binding light-up aptamer as a tag: a blue fluorescent RNA. Chem Commun. pp 3858-3860.
    • (2008) Chem Commun , pp. 3858-3860
    • Sando, S.1    Narita, A.2    Hayami, M.3    Aoyama, Y.4
  • 31
    • 50249090083 scopus 로고    scopus 로고
    • Sequence dependence of fluorescence emission and quenching of doubly thiazole orange labeled DNA: Effective design of a hybridization-sensitive probe
    • Ikeda S, Kubota T, Kino K, Okamoto A (2008) Sequence dependence of fluorescence emission and quenching of doubly thiazole orange labeled DNA: Effective design of a hybridization-sensitive probe. Bioconjugate Chem 19: 1719-1725.
    • (2008) Bioconjugate Chem , vol.19 , pp. 1719-1725
    • Ikeda, S.1    Kubota, T.2    Kino, K.3    Okamoto, A.4
  • 32
    • 58349122886 scopus 로고    scopus 로고
    • Doubly thiazole orange-labeled DNA for live cell RNA imaging
    • Kubota T, Ikeda S, Okamoto A (2009) Doubly thiazole orange-labeled DNA for live cell RNA imaging. Bull Chem Soc Jpn 82: 110-117.
    • (2009) Bull Chem Soc Jpn , vol.82 , pp. 110-117
    • Kubota, T.1    Ikeda, S.2    Okamoto, A.3
  • 33
    • 67649211935 scopus 로고    scopus 로고
    • Hybridizationsensitive fluorescent probe for long-term monitoring of intracellular RNA
    • Kubota T, Ikeda S, Yanagisawa H, Yuki M, Okamoto A (2009) Hybridizationsensitive fluorescent probe for long-term monitoring of intracellular RNA. Bioconjugate Chem 20: 1256-1261.
    • (2009) Bioconjugate Chem , vol.20 , pp. 1256-1261
    • Kubota, T.1    Ikeda, S.2    Yanagisawa, H.3    Yuki, M.4    Okamoto, A.5
  • 34
    • 75149196251 scopus 로고    scopus 로고
    • Hybridization-sensitive fluorescent DNA probe with self-avoidance ability
    • Ikeda S, Kubota T, Yuki M, Yanagisawa H, Tsuruma S, et al. (2010) Hybridization-sensitive fluorescent DNA probe with self-avoidance ability. Org Biomol Chem 8: 546-551.
    • (2010) Org Biomol Chem , vol.8 , pp. 546-551
    • Ikeda, S.1    Kubota, T.2    Yuki, M.3    Yanagisawa, H.4    Tsuruma, S.5
  • 35
    • 70349932066 scopus 로고    scopus 로고
    • Exciton-controlled hybridization-sensitive fluorescent probes: Multicolor detection of nucleic acids
    • Ikeda S, Kubota T, Yuki M, Okamoto A (2009) Exciton-controlled hybridization-sensitive fluorescent probes: Multicolor detection of nucleic acids. Angew Chem, Int Ed 48: 6480-6484.
    • (2009) Angew Chem, Int Ed , vol.48 , pp. 6480-6484
    • Ikeda, S.1    Kubota, T.2    Yuki, M.3    Okamoto, A.4
  • 36
    • 0023141793 scopus 로고
    • Demonstration of RNA polymerase multiplicity in Trypanosoma brucei. Characterization and purification of α-amanitin-resistant and -sensitive enzymes
    • Earnshaw DL, Beebee TJC, Gutteridge WE (1987) Demonstration of RNA polymerase multiplicity in Trypanosoma brucei. Characterization and purification of α-amanitin-resistant and -sensitive enzymes. Biochem J 241: 649-655.
    • (1987) Biochem J , vol.241 , pp. 649-655
    • Earnshaw, D.L.1    Beebee, T.J.C.2    Gutteridge, W.E.3
  • 37
    • 0021768580 scopus 로고
    • α-Amanitin-insensitive transcription of variant surface glycoprotein genes provides further evidence for discontinuous transcription in trypanosomes
    • Kooter JM, Borst P (1984) α-Amanitin-insensitive transcription of variant surface glycoprotein genes provides further evidence for discontinuous transcription in trypanosomes. Nucleic Acids Res 12: 9457-9472.
    • (1984) Nucleic Acids Res , vol.12 , pp. 9457-9472
    • Kooter, J.M.1    Borst, P.2
  • 39
    • 27644541914 scopus 로고    scopus 로고
    • P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles in an RNA-dependent manner
    • Fox AH, Bond CS, Lamond AI (2005) P54nrb forms a heterodimer with PSP1 that localizes to paraspeckles in an RNA-dependent manner. Mol Biol Cell 16: 5304-5315.
    • (2005) Mol Biol Cell , vol.16 , pp. 5304-5315
    • Fox, A.H.1    Bond, C.S.2    Lamond, A.I.3
  • 40
    • 68949212914 scopus 로고    scopus 로고
    • Altered nuclear retention of mRNAs containing inverted repeats in Human Embryonic stem cells: Functional role of a nuclear noncoding RNA
    • Chen LL, Carmichael GG (2009) Altered nuclear retention of mRNAs containing inverted repeats in Human Embryonic stem cells: Functional role of a nuclear noncoding RNA. Mol Cell 35: 467-478.
    • (2009) Mol Cell , vol.35 , pp. 467-478
    • Chen, L.L.1    Carmichael, G.G.2
  • 41
    • 0034604296 scopus 로고    scopus 로고
    • 2.8A° Crystal structure of the malachite green aptamer
    • Baugh C, Grate D, Wilson C (2000) 2.8A° Crystal structure of the malachite green aptamer. J Mol Biol 301: 117-128.
    • (2000) J Mol Biol , vol.301 , pp. 117-128
    • Baugh, C.1    Grate, D.2    Wilson, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.