메뉴 건너뛰기




Volumn , Issue , 2013, Pages 173-198

Analyses of RNA-ligand interactions by fluorescence anisotropy

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84930212106     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4614-3991-2_9     Document Type: Chapter
Times cited : (4)

References (38)
  • 2
    • 58249093392 scopus 로고    scopus 로고
    • Using fl uorophore-labeled oligonucleotides to measure af fi nities of protein-DNA interactions
    • Anderson BJ, Larkin C, Guja K, Schildbach JF (2008) Using fl uorophore-labeled oligonucleotides to measure af fi nities of protein-DNA interactions. Methods Enzymol 450:253-272
    • (2008) Methods Enzymol , vol.450 , pp. 253-272
    • Anderson, B.J.1    Larkin, C.2    Guja, K.3    Schildbach, J.F.4
  • 3
    • 17544365656 scopus 로고    scopus 로고
    • Kinetic and thermodynamic analysis of the interaction between TRAP ( trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA
    • Baumann C, Otridge J, Gollnick P (1996) Kinetic and thermodynamic analysis of the interaction between TRAP ( trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA. J Biol Chem 271:12269-12274
    • (1996) J Biol Chem , vol.271 , pp. 12269-12274
    • Baumann, C.1    Otridge, J.2    Gollnick, P.3
  • 4
    • 0019241817 scopus 로고
    • The thermodynamics of nucleotide binding to proteins
    • Beaudette NV, Langerman N (1980) The thermodynamics of nucleotide binding to proteins. CRC Crit Rev Biochem 9:145-169
    • (1980) CRC Crit Rev Biochem , vol.9 , pp. 145-169
    • Beaudette, N.V.1    Langerman, N.2
  • 5
    • 0021891880 scopus 로고
    • Time-resolved fluorescence of proteins
    • Beechem JM, Brand L (1985) Time-resolved fluorescence of proteins. Annu Rev Biochem 54:43-71
    • (1985) Annu Rev Biochem , vol.54 , pp. 43-71
    • Beechem, J.M.1    Brand, L.2
  • 6
    • 41949126822 scopus 로고    scopus 로고
    • Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3 ' to 5 ' helicase partner of the nuclear exosome
    • Bernstein J, Patterson DN, Wilson GM, Toth EA (2008) Characterization of the essential activities of Saccharomyces cerevisiae Mtr4p, a 3 ' to 5 ' helicase partner of the nuclear exosome. J Biol Chem 283:4930-4942
    • (2008) J Biol Chem , vol.283 , pp. 4930-4942
    • Bernstein, J.1    Patterson, D.N.2    Wilson, G.M.3    Toth, E.A.4
  • 7
    • 0010108989 scopus 로고    scopus 로고
    • Quantitative determination of equilibrium binding isotherms for multiple ligand-macromolecule interactions using spectroscopic methods
    • In: Gore MG (ed). Oxford University Press, Oxford, UK
    • Bujalowski W, Jezewska MJ (2000) Quantitative determination of equilibrium binding isotherms for multiple ligand-macromolecule interactions using spectroscopic methods. In: Gore MG (ed) Spectrophotometry and spectro fl uorimetry. Oxford University Press, Oxford, UK, pp 141-165
    • (2000) Spectrophotometry and spectro fluorimetry , pp. 141-165
    • Bujalowski, W.1    Jezewska, M.J.2
  • 8
    • 0029071516 scopus 로고
    • Protein-RNA recognition
    • Draper DE (1995) Protein-RNA recognition. Annu Rev Biochem 64:593-620
    • (1995) Annu Rev Biochem , vol.64 , pp. 593-620
    • Draper, D.E.1
  • 9
    • 0033927902 scopus 로고    scopus 로고
    • In vitro properties of the conserved mammalian protein hnRNPD suggest a role in telomere maintenance
    • Eversole A, Maizels N (2000) In vitro properties of the conserved mammalian protein hnRNPD suggest a role in telomere maintenance. Mol Cell Biol 20:5425-5432
    • (2000) Mol Cell Biol , vol.20 , pp. 5425-5432
    • Eversole, A.1    Maizels, N.2
  • 10
    • 0032175112 scopus 로고    scopus 로고
    • Technological advances in high-throughput screening
    • Fernandes PB (1998) Technological advances in high-throughput screening. Curr Opin Chem Biol 2:597-603
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 597-603
    • Fernandes, P.B.1
  • 11
    • 34547103988 scopus 로고    scopus 로고
    • Speci fi c protein domains mediate cooperative assembly of HuR oligomers on AU-rich mRNA-destabilizing sequences
    • Fialcowitz-White EJ, Brewer BY, Ballin JD, Willis CD, Toth EA, Wilson GM (2007) Speci fi c protein domains mediate cooperative assembly of HuR oligomers on AU-rich mRNA-destabilizing sequences. J Biol Chem 282:20948-20959
    • (2007) J Biol Chem , vol.282 , pp. 20948-20959
    • Fialcowitz-White, E.J.1    Brewer, B.Y.2    Ballin, J.D.3    Willis, C.D.4    Toth, E.A.5    Wilson, G.M.6
  • 12
    • 77249095424 scopus 로고    scopus 로고
    • Fluorescence anisotropy: from single molecules to live cells
    • Gradinaru CC, Marushchak DO, Samim M, Krull UJ (2010) Fluorescence anisotropy: from single molecules to live cells. Analyst 135:452-459
    • (2010) Analyst , vol.135 , pp. 452-459
    • Gradinaru, C.C.1    Marushchak, D.O.2    Samim, M.3    Krull, U.J.4
  • 14
    • 0024378717 scopus 로고
    • Role of the hydrophobic effect in stability of site-specific protein-DNA complexes
    • Ha JH, Spolar RS, Record MT Jr (1989) Role of the hydrophobic effect in stability of site-specific protein-DNA complexes. J Mol Biol 209:801-816
    • (1989) J Mol Biol , vol.209 , pp. 801-816
    • Ha, J.H.1    Spolar, R.S.2    Record, M.T.3
  • 15
    • 0042468972 scopus 로고    scopus 로고
    • Fluorescence polarization competition assay: the range of resolvable inhibitor potency is limited by the af fi nity of the fl uorescent ligand
    • Huang X (2003) Fluorescence polarization competition assay: the range of resolvable inhibitor potency is limited by the af fi nity of the fl uorescent ligand. J Biomol Screen 8:34-38
    • (2003) J Biomol Screen , vol.8 , pp. 34-38
    • Huang, X.1
  • 16
    • 77952538407 scopus 로고    scopus 로고
    • Fluorescence polarization/anisotropy in diagnostics and imaging
    • Jameson DM, Ross JA (2010) Fluorescence polarization/anisotropy in diagnostics and imaging. Chem Rev 110:2685-2708
    • (2010) Chem Rev , vol.110 , pp. 2685-2708
    • Jameson, D.M.1    Ross, J.A.2
  • 17
    • 0028934572 scopus 로고
    • Fluorescence anisotropy applied to biomolecular interactions
    • Jameson DM, Sawyer WH (1995) Fluorescence anisotropy applied to biomolecular interactions. Methods Enzymol 246:283-300
    • (1995) Methods Enzymol , vol.246 , pp. 283-300
    • Jameson, D.M.1    Sawyer, W.H.2
  • 19
    • 34249875986 scopus 로고    scopus 로고
    • Competitive binding of AUF1 and TIAR to MYC mRNA controls its translation
    • Liao B, Hu Y, Brewer G (2007) Competitive binding of AUF1 and TIAR to MYC mRNA controls its translation. Nat Struct Mol Biol 14:511-518
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 511-518
    • Liao, B.1    Hu, Y.2    Brewer, G.3
  • 20
    • 0026351773 scopus 로고
    • Thermodynamic methods for model-independent determination of equilibrium binding isotherms for protein-DNA interactions: spectroscopic approaches to monitor binding
    • Lohman TM, Bujalowski W (1991) Thermodynamic methods for model-independent determination of equilibrium binding isotherms for protein-DNA interactions: spectroscopic approaches to monitor binding. Methods Enzymol 208:258-290
    • (1991) Methods Enzymol , vol.208 , pp. 258-290
    • Lohman, T.M.1    Bujalowski, W.2
  • 21
    • 33751257755 scopus 로고    scopus 로고
    • Endotoxic shock in AUF1 knockout mice mediated by failure to degrade proin fl ammatory cytokine mRNAs
    • Lu JY, Sadri N, Schneider RJ (2006) Endotoxic shock in AUF1 knockout mice mediated by failure to degrade proin fl ammatory cytokine mRNAs. Genes Dev 20:3174-3184
    • (2006) Genes Dev , vol.20 , pp. 3174-3184
    • Lu, J.Y.1    Sadri, N.2    Schneider, R.J.3
  • 22
    • 0037675905 scopus 로고    scopus 로고
    • Communication between eukaryotic translation initiation factors 1 and 1A on the yeast small ribosomal subunit
    • Maag D, Lorsch JR (2003) Communication between eukaryotic translation initiation factors 1 and 1A on the yeast small ribosomal subunit. J Mol Biol 330:917-924
    • (2003) J Mol Biol , vol.330 , pp. 917-924
    • Maag, D.1    Lorsch, J.R.2
  • 23
    • 33644674229 scopus 로고    scopus 로고
    • Analysis of RNA-protein interactions by a microplate-based fluorescence anisotropy assay
    • Mao C, Flavin KG, Wang S, Dodson R, Ross J, Shapiro DJ (2006) Analysis of RNA-protein interactions by a microplate-based fluorescence anisotropy assay. Anal Biochem 350:222-232
    • (2006) Anal Biochem , vol.350 , pp. 222-232
    • Mao, C.1    Flavin, K.G.2    Wang, S.3    Dodson, R.4    Ross, J.5    Shapiro, D.J.6
  • 24
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5 ' cap-binding protein (eIF4E) bound to 7-methyl-GDP
    • Marcotrigiano J, Gingras AC, Sonenberg N, Burley SK (1997) Cocrystal structure of the messenger RNA 5 ' cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell 89:951-961
    • (1997) Cell , vol.89 , pp. 951-961
    • Marcotrigiano, J.1    Gingras, A.C.2    Sonenberg, N.3    Burley, S.K.4
  • 26
    • 77956940474 scopus 로고    scopus 로고
    • The 5 ' -7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and to block an alternative pathway
    • Mitchell SF, Walker SE, Algire MA, Park EH, Hinnebusch AG, Lorsch JR (2010) The 5 ' -7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and to block an alternative pathway. Mol Cell 39:950-962
    • (2010) Mol Cell , vol.39 , pp. 950-962
    • Mitchell, S.F.1    Walker, S.E.2    Algire, M.A.3    Park, E.H.4    Hinnebusch, A.G.5    Lorsch, J.R.6
  • 27
    • 0033773937 scopus 로고    scopus 로고
    • Fluorescence polarization and anisotropy in high throughput screening: perspectives and primer
    • Owicki JC (2000) Fluorescence polarization and anisotropy in high throughput screening: perspectives and primer. J Biomol Screen 5:297-306
    • (2000) J Biomol Screen , vol.5 , pp. 297-306
    • Owicki, J.C.1
  • 28
    • 79953035983 scopus 로고    scopus 로고
    • Features of double-stranded RNA-binding domains of RNA helicase A are necessary for selective recognitions and translation of complex mRNAs
    • Ranji A, Shkriabai N, Kvaratskhelia M, Musier-Forsyth K, Boris-Lawrie K (2011) Features of double-stranded RNA-binding domains of RNA helicase A are necessary for selective recognitions and translation of complex mRNAs. J Biol Chem 286:5328-5337
    • (2011) J Biol Chem , vol.286 , pp. 5328-5337
    • Ranji, A.1    Shkriabai, N.2    Kvaratskhelia, M.3    Musier-Forsyth, K.4    Boris-Lawrie, K.5
  • 29
    • 0035311445 scopus 로고    scopus 로고
    • A kinetic study of analyte-receptor binding and dissociation, and dissociation alone, for biosensor applications: a fractal analysis
    • Sadana A (2001) A kinetic study of analyte-receptor binding and dissociation, and dissociation alone, for biosensor applications: a fractal analysis. Anal Biochem 291:34-47
    • (2001) Anal Biochem , vol.291 , pp. 34-47
    • Sadana, A.1
  • 30
    • 79251545169 scopus 로고    scopus 로고
    • RNA-binding protein AUF1 regulates lipopolysaccharide-induced IL-10 expression by activating I k B kinase complex in monocytes
    • Sarkar S, Han J, Sinsimer KS, Liao B, Foster RL, Brewer G, Pestka S (2011) RNA-binding protein AUF1 regulates lipopolysaccharide-induced IL-10 expression by activating I k B kinase complex in monocytes. Mol Cell Biol 31:602-615
    • (2011) Mol Cell Biol , vol.31 , pp. 602-615
    • Sarkar, S.1    Han, J.2    Sinsimer, K.S.3    Liao, B.4    Foster, R.L.5    Brewer, G.6    Pestka, S.7
  • 31
    • 0032033151 scopus 로고    scopus 로고
    • Structure and genomic organization of the human AUF1 gene: alternative pre-mRNA splicing generates four protein isoforms
    • Wagner BJ, DeMaria CT, Sun Y, Wilson GM, Brewer G (1998) Structure and genomic organization of the human AUF1 gene: alternative pre-mRNA splicing generates four protein isoforms. Genomics 48:195-202
    • (1998) Genomics , vol.48 , pp. 195-202
    • Wagner, B.J.1    DeMaria, C.T.2    Sun, Y.3    Wilson, G.M.4    Brewer, G.5
  • 32
    • 57449093796 scopus 로고    scopus 로고
    • RNA folding and RNA-protein binding analyzed by fluorescence anisotropy and resonance energy transfer
    • In: Geddes CD, Lakowicz JR (eds). Springer, New York
    • Wilson GM (2005) RNA folding and RNA-protein binding analyzed by fluorescence anisotropy and resonance energy transfer. In: Geddes CD, Lakowicz JR (eds) Reviews in fluorescence, vol 2. Springer, New York, pp 223-243
    • (2005) Reviews in fluorescence , vol.2 , pp. 223-243
    • Wilson, G.M.1
  • 33
    • 0035976908 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of Hsp70 association with A + U-rich mRNA-destabilizing sequences
    • Wilson GM, Sutphen K, Bolikal S, Chuang K, Brewer G (2001) Thermodynamics and kinetics of Hsp70 association with A + U-rich mRNA-destabilizing sequences. J Biol Chem 276: 44450-44456
    • (2001) J Biol Chem , vol.276 , pp. 44450-44456
    • Wilson, G.M.1    Sutphen, K.2    Bolikal, S.3    Chuang, K.4    Brewer, G.5
  • 35
    • 0142138241 scopus 로고    scopus 로고
    • Analysis of protein interactions using fluorescence technologies
    • Yan Y, Marriott G (2003) Analysis of protein interactions using fluorescence technologies. Curr Opin Chem Biol 7:635-640
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 635-640
    • Yan, Y.1    Marriott, G.2
  • 36
    • 78149407588 scopus 로고    scopus 로고
    • Poly(A) tail affects equilibrium and thermodynamic behavior of tobacco etch virus mRNA with translation initiation factors elF4F, elF4B and PABP
    • Yumak H, Khan MA, Goss DJ (2010) Poly(A) tail affects equilibrium and thermodynamic behavior of tobacco etch virus mRNA with translation initiation factors elF4F, elF4B and PABP. Biochim Biophys Acta 1799:653-658
    • (2010) Biochim Biophys Acta , vol.1799 , pp. 653-658
    • Yumak, H.1    Khan, M.A.2    Goss, D.J.3
  • 37
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang JH, Chung T, Oldenburg K (1999) A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J Biomol Screen 4:67-73
    • (1999) J Biomol Screen , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.2    Oldenburg, K.3
  • 38
    • 78649865439 scopus 로고    scopus 로고
    • Alternatively expressed domains of AU-rich element RNA-binding protein 1 (AUF1) regulate RNA-binding af fi nity, RNA-induced protein oligomerization, and the local conformation of bound RNA ligands
    • Zucconi BE, Ballin JD, Brewer BY, Ross CR, Huang J, Toth EA, Wilson GM (2010) Alternatively expressed domains of AU-rich element RNA-binding protein 1 (AUF1) regulate RNA-binding af fi nity, RNA-induced protein oligomerization, and the local conformation of bound RNA ligands. J Biol Chem 285:39127-39139
    • (2010) J Biol Chem , vol.285 , pp. 39127-39139
    • Zucconi, B.E.1    Ballin, J.D.2    Brewer, B.Y.3    Ross, C.R.4    Huang, J.5    Toth, E.A.6    Wilson, G.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.