메뉴 건너뛰기




Volumn 1240, Issue , 2015, Pages 63-95

Native purification and labeling of RNA for single molecule fluorescence studies

Author keywords

Biotin labeling of RNA; Fluorophore labeling of RNA; Non denaturing purification; Non denaturing RNA transcription; RNA folding; Single molecule fluorescence resonance energy transfer

Indexed keywords

BIOTIN; ESTER; OLIGONUCLEOTIDE; PERIODATE; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; RNA; RNA POLYMERASE; UNTRANSLATED RNA; BACTERIOPHAGE T7 RNA POLYMERASE; BENZENESULFONIC ACID DERIVATIVE; BOVINE SERUM ALBUMIN; DNA DIRECTED RNA POLYMERASE; FLUORESCENT DYE; MACROGOL DERIVATIVE; PERIODIC ACID; POLYADENYLIC ACID; RIBOSWITCH; STREPTAVIDIN; VIRUS PROTEIN;

EID: 84919625133     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-1896-6_6     Document Type: Article
Times cited : (26)

References (86)
  • 2
    • 67650713931 scopus 로고    scopus 로고
    • The structural and functional diversity of metabolite-binding riboswitches
    • Roth A, Breaker RR (2009) The structural and functional diversity of metabolite-binding riboswitches. Annu Rev Biochem 78:305-334
    • (2009) Annu Rev Biochem , vol.78 , pp. 305-334
    • Roth, A.1    Breaker, R.R.2
  • 3
    • 58849093262 scopus 로고    scopus 로고
    • Revisiting the principles of microRNA target recognition and mode of action
    • Brodersen P, Voinnet O (2009) Revisiting the principles of microRNA target recognition and mode of action. Nat Rev Mol Cell Biol 10:141-148
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 141-148
    • Brodersen, P.1    Voinnet, O.2
  • 4
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: Design principles of a dynamic RNP machine
    • Wahl MC, Will CL, Luhrmann R (2009) The spliceosome: design principles of a dynamic RNP machine. Cell 136:701-718
    • (2009) Cell , vol.136 , pp. 701-718
    • Wahl, M.C.1    Will, C.L.2    Luhrmann, R.3
  • 5
    • 0042658199 scopus 로고    scopus 로고
    • RNA, the first macromolecular catalyst: The ribosome is a ribozyme
    • Steitz TA, Moore PB (2003) RNA, the first macromolecular catalyst: the ribosome is a ribozyme. Trends Biochem Sci 28:411-418
    • (2003) Trends Biochem Sci , vol.28 , pp. 411-418
    • Steitz, T.A.1    Moore, P.B.2
  • 6
    • 33745862398 scopus 로고    scopus 로고
    • The biogenesis and regulation of telomerase holoenzymes
    • Collins K (2006) The biogenesis and regulation of telomerase holoenzymes. Nat Rev Mol Cell Biol 7:484-494
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 484-494
    • Collins, K.1
  • 8
    • 80053041142 scopus 로고    scopus 로고
    • Riboswitches: Discovery of drugs that target bacterial gene-regulatory RNAs
    • Deigan KE, Ferre-D'Amare AR (2011) Riboswitches: discovery of drugs that target bacterial gene-regulatory RNAs. Acc Chem Res 44:1329-1338
    • (2011) Acc Chem Res , vol.44 , pp. 1329-1338
    • Deigan, K.E.1    Ferre-D'amare, A.R.2
  • 9
    • 55249114833 scopus 로고    scopus 로고
    • Structural insights into amino acid binding and gene control by a lysine riboswitch
    • Serganov A, Huang L, Patel DJ (2008) Structural insights into amino acid binding and gene control by a lysine riboswitch. Nature 455:1263-1267
    • (2008) Nature , vol.455 , pp. 1263-1267
    • Serganov, A.1    Huang, L.2    Patel, D.J.3
  • 11
    • 80455178803 scopus 로고    scopus 로고
    • Molecular sensing by the aptamer domain of the FMN riboswitch: A general model for ligand binding by conformational selection
    • Vicens Q, Mondragon E, Batey RT (2011) Molecular sensing by the aptamer domain of the FMN riboswitch: a general model for ligand binding by conformational selection. Nucleic Acids Res 39:8586-8598
    • (2011) Nucleic Acids Res , vol.39 , pp. 8586-8598
    • Vicens, Q.1    Mondragon, E.2    Batey, R.T.3
  • 13
    • 79960114180 scopus 로고    scopus 로고
    • Comparison of a preQ1 riboswitch aptamer in metabolite-bound and free states with implications for gene regulation
    • Jenkins JL, Krucinska J, McCarty RM, Bandarian V, Wedekind JE (2011) Comparison of a preQ1 riboswitch aptamer in metabolite-bound and free states with implications for gene regulation. J Biol Chem 286:24626-24637
    • (2011) J Biol Chem , vol.286 , pp. 24626-24637
    • Jenkins, J.L.1    Krucinska, J.2    McCarty, R.M.3    Bandarian, V.4    Wedekind, J.E.5
  • 14
    • 84864185753 scopus 로고    scopus 로고
    • Pseudoknot Preorganization of the PreQ(1) Class I Riboswitch
    • Santner T, Rieder U, Kreutz C, Micura R (2012) Pseudoknot Preorganization of the PreQ(1) Class I Riboswitch. J Am Chem Soc 134:11928-11931
    • (2012) J Am Chem Soc , vol.134 , pp. 11928-11931
    • Santner, T.1    Rieder, U.2    Kreutz, C.3    Micura, R.4
  • 15
    • 0023651444 scopus 로고
    • Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates
    • Milligan JF, Groebe DR, Witherell GW, Uhlenbeck OC (1987) Oligoribonucleotide synthesis using T7 RNA polymerase and synthetic DNA templates. Nucleic Acids Res 15: 8783-8798
    • (1987) Nucleic Acids Res , vol.15 , pp. 8783-8798
    • Milligan, J.F.1    Groebe, D.R.2    Witherell, G.W.3    Uhlenbeck, O.C.4
  • 16
    • 36749064979 scopus 로고    scopus 로고
    • Folding of noncoding RNAs during transcription facilitated by pausing-induced normative structures
    • Wong TN, Sosnick TR, Pan T (2007) Folding of noncoding RNAs during transcription facilitated by pausing-induced normative structures. Proc Natl Acad Sci U S A 104:17995-18000
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 17995-18000
    • Wong, T.N.1    Sosnick, T.R.2    Pan, T.3
  • 17
    • 35548989806 scopus 로고    scopus 로고
    • Kinetic redistribution of native and misfolded RNAs by a DEAD-box chaperone
    • Bhaskaran H, Russell R (2007) Kinetic redistribution of native and misfolded RNAs by a DEAD-box chaperone. Nature 449:1014-1018
    • (2007) Nature , vol.449 , pp. 1014-1018
    • Bhaskaran, H.1    Russell, R.2
  • 18
    • 38449108345 scopus 로고    scopus 로고
    • RNA misfolding and the action of chaperones
    • Russell R (2008) RNA misfolding and the action of chaperones. Front Biosci 13:1-20
    • (2008) Front Biosci , vol.13 , pp. 1-20
    • Russell, R.1
  • 19
    • 0029258928 scopus 로고
    • Keeping RNA happy
    • Uhlenbeck OC (1995) Keeping RNA happy. RNA 1:4-6
    • (1995) RNA , vol.1 , pp. 4-6
    • Uhlenbeck, O.C.1
  • 20
    • 77958599400 scopus 로고    scopus 로고
    • Nondenaturing purification of co-transcriptionally folded RNA avoids common folding heterogeneity
    • Pereira MJ, Behera V, Walter NG (2010) Nondenaturing purification of co-transcriptionally folded RNA avoids common folding heterogeneity. PLoS One 5:e12953
    • (2010) PLoS One , vol.e12953 , pp. 5
    • Pereira, M.J.1    Behera, V.2    Walter, N.G.3
  • 21
    • 79959409852 scopus 로고    scopus 로고
    • The shape-shifting quasispecies of RNA: One sequence, many functional folds
    • Marek MS, Johnson-Buck A, Walter NG (2011) The shape-shifting quasispecies of RNA: one sequence, many functional folds. Phys Chem Chem Phys 13:11524-11537
    • (2011) Phys Chem Chem Phys , vol.13 , pp. 11524-11537
    • Marek, M.S.1    Johnson-Buck, A.2    Walter, N.G.3
  • 22
    • 44449134820 scopus 로고    scopus 로고
    • A practical guide to single-molecule FRET
    • Roy R, Hohng S, Ha T (2008) A practical guide to single-molecule FRET. Nat Methods 5:507-516
    • (2008) Nat Methods , vol.5 , pp. 507-516
    • Roy, R.1    Hohng, S.2    Ha, T.3
  • 23
    • 44449097780 scopus 로고    scopus 로고
    • Do-it-yourself guide: How to use the modern single-molecule toolkit
    • Walter NG, Huang CY, Manzo AJ, Sobhy MA (2008) Do-it-yourself guide: how to use the modern single-molecule toolkit. Nat Methods 5:475-489
    • (2008) Nat Methods , vol.5 , pp. 475-489
    • Walter, N.G.1    Huang, C.Y.2    Manzo, A.J.3    Sobhy, M.A.4
  • 24
    • 84865832249 scopus 로고    scopus 로고
    • Analysis of RNA folding and ribonucleoprotein assembly by single-molecule fluorescence spectroscopy
    • Pljevaljcic G, Robertson-Anderson R, van der Schans E, Millar D (2012) Analysis of RNA folding and ribonucleoprotein assembly by single-molecule fluorescence spectroscopy. Methods Mol Biol 875:271-295
    • (2012) Methods Mol Biol , vol.875 , pp. 271-295
    • Pljevaljcic, G.1    Robertson-Anderson, R.2    Van Der Schans, E.3    Millar, D.4
  • 25
    • 58149083620 scopus 로고    scopus 로고
    • A rugged free energy landscape separates multiple functional RNA folds throughout denaturation
    • Ditzler MA, Rueda D, Mo J, Hakansson K, Walter NG (2008) A rugged free energy landscape separates multiple functional RNA folds throughout denaturation. Nucleic Acids Res 36:7088-7099
    • (2008) Nucleic Acids Res , vol.36 , pp. 7088-7099
    • Ditzler, M.A.1    Rueda, D.2    Mo, J.3    Hakansson, K.4    Walter, N.G.5
  • 28
    • 34547892257 scopus 로고    scopus 로고
    • Dissecting the multistep reaction pathway of an RNA enzyme by single-molecule kinetic "fingerprinting"
    • Liu S, Bokinsky G, Walter NG, Zhuang X (2007) Dissecting the multistep reaction pathway of an RNA enzyme by single-molecule kinetic "fingerprinting". Proc Natl Acad Sci U S A 104:12634-12639
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 12634-12639
    • Liu, S.1    Bokinsky, G.2    Walter, N.G.3    Zhuang, X.4
  • 29
  • 30
    • 0037165996 scopus 로고    scopus 로고
    • Correlating structural dynamics and function in single ribozyme molecules
    • Zhuang X, Kim H, Pereira MJ, Babcock HP, Walter NG, Chu S (2002) Correlating structural dynamics and function in single ribozyme molecules. Science 296:1473-1476
    • (2002) Science , vol.296 , pp. 1473-1476
    • Zhuang, X.1    Kim, H.2    Pereira, M.J.3    Babcock, H.P.4    Walter, N.G.5    Chu, S.6
  • 32
    • 58149085388 scopus 로고    scopus 로고
    • Leakage and slow allostery limit performance of single drug-sensing aptazyme molecules based on the hammerhead ribozyme
    • de Silva C, Walter NG (2009) Leakage and slow allostery limit performance of single drug-sensing aptazyme molecules based on the hammerhead ribozyme. RNA 15:76-84
    • (2009) RNA , vol.15 , pp. 76-84
    • De Silva, C.1    Walter, N.G.2
  • 33
    • 78649677325 scopus 로고    scopus 로고
    • Long-range tertiary interactions in single hammerhead ribozymes bias motional sampling toward catalytically active conformations
    • McDowell SE, Jun JM, Walter NG (2010) Long-range tertiary interactions in single hammerhead ribozymes bias motional sampling toward catalytically active conformations. RNA 16:2414-2426
    • (2010) RNA , vol.16 , pp. 2414-2426
    • McDowell, S.E.1    Jun, J.M.2    Walter, N.G.3
  • 36
    • 84862109207 scopus 로고    scopus 로고
    • Allosteric tertiary interactions preorganize the c-di-GMP riboswitch and accelerate ligand binding
    • Wood S, Ferre-D'Amare AR Rueda D (2012) Allosteric tertiary interactions preorganize the c-di-GMP riboswitch and accelerate ligand binding. ACS Chem Biol 7:920-927
    • (2012) ACS Chem Biol , vol.7 , pp. 920-927
    • Wood, S.1    Ferre-D'amare, A.R.2    Rueda, D.3
  • 38
    • 84862907770 scopus 로고    scopus 로고
    • Functional importance of telomerase pseu-doknot revealed by single-molecule analysis
    • Mihalusova M, Wu JY, Zhuang X (2011) Functional importance of telomerase pseu-doknot revealed by single-molecule analysis. Proc Natl Acad Sci U S A 108:20339-20344
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 20339-20344
    • Mihalusova, M.1    Wu, J.Y.2    Zhuang, X.3
  • 39
    • 84861860470 scopus 로고    scopus 로고
    • Single-molecule FRET reveals the folding dynamics of the human telomerase RNA pseudoknot domain
    • Hengesbach M, Kim NK, Feigon J, Stone MD (2012) Single-molecule FRET reveals the folding dynamics of the human telomerase RNA pseudoknot domain. Angew Chem Int Ed Engl 51:5876-5879
    • (2012) Angew Chem Int Ed Engl , vol.51 , pp. 5876-5879
    • Hengesbach, M.1    Kim, N.K.2    Feigon, J.3    Stone, M.D.4
  • 40
    • 2442638925 scopus 로고    scopus 로고
    • A general method for rapid and nondenaturing purification of RNAs
    • Kieft JS, Batey RT (2004) A general method for rapid and nondenaturing purification of RNAs. RNA 10:988-995
    • (2004) RNA , vol.10 , pp. 988-995
    • Kieft, J.S.1    Batey, R.T.2
  • 41
    • 34447527363 scopus 로고    scopus 로고
    • Improved native affinity purification of RNA
    • Batey RT, Kieft JS (2007) Improved native affinity purification of RNA. RNA 13:1384-1389
    • (2007) RNA , vol.13 , pp. 1384-1389
    • Batey, R.T.1    Kieft, J.S.2
  • 42
    • 69449104554 scopus 로고    scopus 로고
    • Preparation of group I introns for biochemical studies and crystallization assays by native affinity purification
    • Vicens Q, Gooding AR, Duarte LF, Batey RT (2009) Preparation of group I introns for biochemical studies and crystallization assays by native affinity purification. PLoS One 4:e6740
    • (2009) PLoS One , vol.4 , pp. e6740
    • Vicens, Q.1    Gooding, A.R.2    Duarte, L.F.3    Batey, R.T.4
  • 44
    • 18144435106 scopus 로고    scopus 로고
    • Rapid preparation of RNA samples for NMR spectroscopy and X-ray crystallography
    • Cheong HK, Hwang E, Lee C, Choi BS, Cheong C (2004) Rapid preparation of RNA samples for NMR spectroscopy and X-ray crystallography. Nucleic Acids Res 32:e84
    • (2004) Nucleic Acids Res , vol.32 , pp. e84
    • Cheong, H.K.1    Hwang, E.2    Lee, C.3    Choi, B.S.4    Cheong, C.5
  • 45
    • 80455155999 scopus 로고    scopus 로고
    • RNAs synthesized using photocleavable biotinylated nucleotides have dramatically improved catalytic efficiency
    • Luo Y, Eldho NV, Sintim HO, Dayie TK (2011) RNAs synthesized using photocleavable biotinylated nucleotides have dramatically improved catalytic efficiency. Nucleic Acids Res 39:8559-8571
    • (2011) Nucleic Acids Res , vol.39 , pp. 8559-8571
    • Luo, Y.1    Eldho, N.V.2    Sintim, H.O.3    Dayie, T.K.4
  • 46
    • 33846446409 scopus 로고    scopus 로고
    • Rapid purification of RNAs using fast performance liquid chromatography (FPLC)
    • Kim I, McKenna SA, Viani Puglisi E, Puglisi JD (2007) Rapid purification of RNAs using fast performance liquid chromatography (FPLC). RNA 13:289-294
    • (2007) RNA , vol.13 , pp. 289-294
    • Kim, I.1    McKenna, S.A.2    Viani Puglisi, E.3    Puglisi, J.D.4
  • 47
    • 77149143215 scopus 로고    scopus 로고
    • Rapid, nondenaturing RNA purification using weak anion-exchange fast performance liquid chromatography
    • Easton LE, Shibata Y, Lukavsky PJ (2010) Rapid, nondenaturing RNA purification using weak anion-exchange fast performance liquid chromatography. RNA 16:647-653
    • (2010) RNA , vol.16 , pp. 647-653
    • Easton, L.E.1    Shibata, Y.2    Lukavsky, P.J.3
  • 48
    • 79958753068 scopus 로고    scopus 로고
    • RNA labeling, conjugation and ligation
    • Paredes E, Evans M, Das SR (2011) RNA labeling, conjugation and ligation. Methods 54:251-259
    • (2011) Methods , vol.54 , pp. 251-259
    • Paredes, E.1    Evans, M.2    Das, S.R.3
  • 49
    • 0032824909 scopus 로고    scopus 로고
    • Site-specific labeling of RNA with fluorophores and other structural probes
    • Qin PZ, Pyle AM (1999) Site-specific labeling of RNA with fluorophores and other structural probes. Methods 18:60-70
    • (1999) Methods , vol.18 , pp. 60-70
    • Qin, P.Z.1    Pyle, A.M.2
  • 50
    • 0034808071 scopus 로고    scopus 로고
    • Structural dynamics of catalytic RNA highlighted by fluorescence resonance energy transfer
    • Walter NG (2001) Structural dynamics of catalytic RNA highlighted by fluorescence resonance energy transfer. Methods 25:19-30
    • (2001) Methods , vol.25 , pp. 19-30
    • Walter, N.G.1
  • 51
    • 44249099969 scopus 로고    scopus 로고
    • Probing RNA structural dynamics and function by fluorescence resonance energy transfer (FRET)
    • Chapter 11:Unit 11
    • Walter NG (2003) Probing RNA structural dynamics and function by fluorescence resonance energy transfer (FRET). Curr Protoc Nucleic Acid Chem Chapter 11:Unit 11 10
    • (2003) Curr Protoc Nucleic Acid Chem , pp. 10
    • Walter, N.G.1
  • 52
    • 26644468824 scopus 로고    scopus 로고
    • Novel cyanine-AMP conjugates for efficient 5' RNA fluorescent labeling by one-step transcription and replacement of [gamma-32P]ATP in RNA structural investigation
    • Li N, Yu C, Huang F (2005) Novel cyanine-AMP conjugates for efficient 5' RNA fluorescent labeling by one-step transcription and replacement of [gamma-32P]ATP in RNA structural investigation. Nucleic Acids Res 33:e37
    • (2005) Nucleic Acids Res , vol.33 , pp. e37
    • Li, N.1    Yu, C.2    Huang, F.3
  • 53
    • 33846551354 scopus 로고    scopus 로고
    • Counting of six pRNAs of phi29 DNA-packaging motor with customized single-molecule dual-view system
    • Shu D, Zhang H, Jin J, Guo P (2007) Counting of six pRNAs of phi29 DNA-packaging motor with customized single-molecule dual-view system. EMBO J 26:527-537
    • (2007) EMBO J , vol.26 , pp. 527-537
    • Shu, D.1    Zhang, H.2    Jin, J.3    Guo, P.4
  • 54
    • 78650694123 scopus 로고    scopus 로고
    • Click chemistry for rapid labeling and ligation of RNA
    • Paredes E, Das SR (2011) Click chemistry for rapid labeling and ligation of RNA. Chembiochem 12:125-131
    • (2011) Chembiochem , vol.12 , pp. 125-131
    • Paredes, E.1    Das, S.R.2
  • 55
    • 0021111245 scopus 로고
    • Biotin and fluorescent labeling of RNA using T4 RNA ligase
    • Richardson RW, Gumport RI (1983) Biotin and fluorescent labeling of RNA using T4 RNA ligase. Nucleic Acids Res 11:6167-6184
    • (1983) Nucleic Acids Res , vol.11 , pp. 6167-6184
    • Richardson, R.W.1    Gumport, R.I.2
  • 56
    • 84861566819 scopus 로고    scopus 로고
    • Site-specific terminal and internal labeling of RNA by poly(A) polymerase tailing and copper-catalyzed or copper-free strain-promoted click chemistry
    • Winz ML, Samanta A, Benzinger D, Jaschke A (2012) Site-specific terminal and internal labeling of RNA by poly(A) polymerase tailing and copper-catalyzed or copper-free strain-promoted click chemistry. Nucleic Acids Res 40:e78
    • (2012) Nucleic Acids Res , vol.40 , pp. e78
    • Winz, M.L.1    Samanta, A.2    Benzinger, D.3    Jaschke, A.4
  • 57
    • 84864410802 scopus 로고    scopus 로고
    • Optimization of acetonitrile co-solvent and copper stoichiometry for pseudo-ligandless click chemistry with nucleic acids
    • Paredes E, Das SR (2012) Optimization of acetonitrile co-solvent and copper stoichiometry for pseudo-ligandless click chemistry with nucleic acids. Bioorg Med Chem Lett 22:5313-5316
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 5313-5316
    • Paredes, E.1    Das, S.R.2
  • 58
    • 55749099506 scopus 로고    scopus 로고
    • Irreversible chemical steps control intersubunit dynamics during translation
    • Marshall RA, Dorywalska M, Puglisi JD (2008) Irreversible chemical steps control intersubunit dynamics during translation. Proc Natl Acad Sci U S A 105:15364-15369
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 15364-15369
    • Marshall, R.A.1    Dorywalska, M.2    Puglisi, J.D.3
  • 59
    • 12844274892 scopus 로고    scopus 로고
    • Efficient fluorescence labeling of a large RNA through oligonucleotide hybridization
    • Smith GJ, Sosnick TR, Scherer NF, Pan T (2005) Efficient fluorescence labeling of a large RNA through oligonucleotide hybridization. RNA 11:234-239
    • (2005) RNA , vol.11 , pp. 234-239
    • Smith, G.J.1    Sosnick, T.R.2    Scherer, N.F.3    Pan, T.4
  • 60
    • 78650006466 scopus 로고    scopus 로고
    • Methods of site-specific labeling of RNA with fluorescent dyes
    • Solomatin S, Herschlag D (2009) Methods of site-specific labeling of RNA with fluorescent dyes. Methods Enzymol 469:47-68
    • (2009) Methods Enzymol , vol.469 , pp. 47-68
    • Solomatin, S.1    Herschlag, D.2
  • 61
    • 79957610306 scopus 로고    scopus 로고
    • Removal of covalent heterogeneity reveals simple folding behavior for P4-P6 RNA
    • Greenfeld M, Solomatin SV, Herschlag D (2011) Removal of covalent heterogeneity reveals simple folding behavior for P4-P6 RNA. J Biol Chem 286:19872-19879
    • (2011) J Biol Chem , vol.286 , pp. 19872-19879
    • Greenfeld, M.1    Solomatin, S.V.2    Herschlag, D.3
  • 63
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker M (2003) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res 31:3406-3415
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 64
    • 50649121477 scopus 로고    scopus 로고
    • Advances in single-molecule fluorescence methods for molecular biology
    • Joo C, Balci H, Ishitsuka Y, Buranachai C, Ha T (2008) Advances in single-molecule fluorescence methods for molecular biology. Annu Rev Biochem 77:51-76
    • (2008) Annu Rev Biochem , vol.77 , pp. 51-76
    • Joo, C.1    Balci, H.2    Ishitsuka, Y.3    Buranachai, C.4    Ha, T.5
  • 65
    • 0037284103 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy in cell biology
    • Axelrod D (2003) Total internal reflection fluorescence microscopy in cell biology. Methods Enzymol 361:1-33
    • (2003) Methods Enzymol , vol.361 , pp. 1-33
    • Axelrod, D.1
  • 66
    • 34347237194 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: Novel variations of an established technique
    • Haustein E, Schwille P (2007) Fluorescence correlation spectroscopy: novel variations of an established technique. Annu Rev Biophys Biomol Struct 36:151-169
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 151-169
    • Haustein, E.1    Schwille, P.2
  • 67
    • 13444292841 scopus 로고    scopus 로고
    • Single molecule high-resolution colocalization of Cy3 and Cy5 attached to macromolecules measures intramolecular distances through time
    • Churchman LS, Okten Z, Rock RS, Dawson JF, Spudich JA (2005) Single molecule high-resolution colocalization of Cy3 and Cy5 attached to macromolecules measures intramolecular distances through time. Proc Natl Acad Sci U S A 102:1419-1423
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 1419-1423
    • Churchman, L.S.1    Okten, Z.2    Rock, R.S.3    Dawson, J.F.4    Spudich, J.A.5
  • 68
    • 34248504534 scopus 로고    scopus 로고
    • Widefield subdiffraction imaging by accumulated binding of diffusing probes
    • Sharonov A, Hochstrasser RM (2006) Widefield subdiffraction imaging by accumulated binding of diffusing probes. Proc Natl Acad Sci U S A 103:18911-18916
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 18911-18916
    • Sharonov, A.1    Hochstrasser, R.M.2
  • 72
    • 4243504131 scopus 로고
    • Acceleration and Trapping of Particles by Radiation Pressure
    • Ashkin A (1970) Acceleration and Trapping of Particles by Radiation Pressure. Phys Rev Lett 24:156-159
    • (1970) Phys Rev Lett , vol.24 , pp. 156-159
    • Ashkin, A.1
  • 74
    • 39149087014 scopus 로고    scopus 로고
    • Protein folding studied by single-molecule FRET
    • Schuler B, Eaton WA (2008) Protein folding studied by single-molecule FRET. Curr Opin Struct Biol 18:16-26
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 16-26
    • Schuler, B.1    Eaton, W.A.2
  • 75
    • 23744470902 scopus 로고    scopus 로고
    • Single-molecule RNA folding
    • Bokinsky G, Zhuang X (2005) Single-molecule RNA folding. Acc Chem Res 38:566-573
    • (2005) Acc Chem Res , vol.38 , pp. 566-573
    • Bokinsky, G.1    Zhuang, X.2
  • 77
    • 41449108157 scopus 로고    scopus 로고
    • An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments
    • Aitken CE, Marshall RA, Puglisi JD (2008) An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments. Biophys J 94:1826-1835
    • (2008) Biophys J , vol.94 , pp. 1826-1835
    • Aitken, C.E.1    Marshall, R.A.2    Puglisi, J.D.3
  • 78
    • 33750295496 scopus 로고    scopus 로고
    • Nonblinking and long-lasting single-molecule fluorescence imaging
    • Rasnik I, McKinney SA, Ha T (2006) Nonblinking and long-lasting single-molecule fluorescence imaging. Nat Methods 3:891-893
    • (2006) Nat Methods , vol.3 , pp. 891-893
    • Rasnik, I.1    McKinney, S.A.2    Ha, T.3
  • 79
    • 77957065513 scopus 로고    scopus 로고
    • Analysis of complex single-molecule FRET time trajectories
    • Blanco M, Walter NG (2010) Analysis of complex single-molecule FRET time trajectories. Methods Enzymol 472:153-178
    • (2010) Methods Enzymol , vol.472 , pp. 153-178
    • Blanco, M.1    Walter, N.G.2
  • 80
    • 33746747438 scopus 로고    scopus 로고
    • Analysis of single-molecule FRET trajectories using hidden Markov modeling
    • McKinney SA, Joo C, Ha T (2006) Analysis of single-molecule FRET trajectories using hidden Markov modeling. Biophys J 91: 1941-1951
    • (2006) Biophys J , vol.91 , pp. 1941-1951
    • McKinney, S.A.1    Joo, C.2    Ha, T.3
  • 81
    • 73449090455 scopus 로고    scopus 로고
    • Learning rates and states from biophysical time series: A Bayesian approach to model selection and single-molecule FRET data
    • Bronson JE, Fei J, Hofman JM, Gonzalez RL Jr, Wiggins CH (2009) Learning rates and states from biophysical time series: a Bayesian approach to model selection and single-molecule FRET data. Biophys J 97:3196-3205
    • (2009) Biophys J , vol.97 , pp. 3196-3205
    • Bronson, J.E.1    Fei, J.2    Hofman, J.M.3    Gonzalez, R.L.4    Wiggins, C.H.5
  • 82
    • 4444324112 scopus 로고    scopus 로고
    • Model-based fitting of single-channel dwell-time distributions
    • Qin F, Li L (2004) Model-based fitting of single-channel dwell-time distributions. Biophys J 87:1657-1671
    • (2004) Biophys J , vol.87 , pp. 1657-1671
    • Qin, F.1    Li, L.2
  • 83
    • 66449089224 scopus 로고    scopus 로고
    • The structural basis for recognition of the PreQ0 metabolite by an unusually small riboswitch aptamer domain
    • Spitale RC, Torelli AT, Krucinska J, Bandarian V, Wedekind JE (2009) The structural basis for recognition of the PreQ0 metabolite by an unusually small riboswitch aptamer domain. J Biol Chem 284:11012-11016
    • (2009) J Biol Chem , vol.284 , pp. 11012-11016
    • Spitale, R.C.1    Torelli, A.T.2    Krucinska, J.3    Bandarian, V.4    Wedekind, J.E.5
  • 84
    • 84890410887 scopus 로고    scopus 로고
    • Single transcriptional and translational riboswitches adopt similar pre-folded ensembles that follow distinct folding pathways into the same ligand-bound structure
    • Suddala KC, Rinaldi AJ, Feng J, Mustoe AM, Eichhorn CD, Al-Hashimi HM, Brooks CL, Walter NG (2013) Single transcriptional and translational riboswitches adopt similar pre-folded ensembles that follow distinct folding pathways into the same ligand-bound structure. Nucleic Acids Res 41:10462-10475
    • (2013) Nucleic Acids Res , vol.41 , pp. 10462-10475
    • Suddala, K.C.1    Rinaldi, A.J.2    Feng, J.3    Mustoe, A.M.4    Eichhorn, C.D.5    Al-Hashimi, H.M.6    Brooks, C.L.7    Walter, N.G.8
  • 86
    • 0031915525 scopus 로고    scopus 로고
    • Tailing and 3'-end labeling of RNA with yeast poly(A) polymerase and various nucleotides
    • Martin G, Keller W (1998) Tailing and 3'-end labeling of RNA with yeast poly(A) polymerase and various nucleotides. RNA 4:226-230
    • (1998) RNA , vol.4 , pp. 226-230
    • Martin, G.1    Keller, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.