메뉴 건너뛰기




Volumn 330, Issue , 2013, Pages 47-66

Investigation of quadruplex structure under physiological conditions using in-cell NMR

Author keywords

G quadruplex; In vivo; In cell NMR; Molecular crowding; Xenopus laevis

Indexed keywords

GUANINE QUADRUPLEX; NUCLEIC ACID;

EID: 84875902527     PISSN: 03401022     EISSN: None     Source Type: Book Series    
DOI: 10.1007/128-2012-332     Document Type: Review
Times cited : (25)

References (59)
  • 1
  • 2
    • 33846928449 scopus 로고    scopus 로고
    • G-quadruplexes in promoters throughout the human genome
    • Huppert JL, Balasubramanian S (2007) G-quadruplexes in promoters throughout the human genome. Nucleic Acids Res 35:406
    • (2007) Nucleic Acids Res , vol.35 , pp. 406
    • Huppert, J.L.1    Balasubramanian, S.2
  • 3
    • 77955809107 scopus 로고    scopus 로고
    • Making sense of G-quadruplex and i-motif functions in oncogene promoters
    • Brooks TA, Kendrick S, Hurley L (2010) Making sense of G-quadruplex and i-motif functions in oncogene promoters. FEBS J 277:3459
    • (2010) FEBS J , vol.277 , pp. 3459
    • Brooks, T.A.1    Kendrick, S.2    Hurley, L.3
  • 4
    • 77955791569 scopus 로고    scopus 로고
    • G-quadruplex nucleic acids and human disease
    • Wu Y, Brosh RM Jr (2010) G-quadruplex nucleic acids and human disease. FEBS J 277:3470
    • (2010) FEBS J , vol.277 , pp. 3470
    • Wu, Y.1    Brosh Jr., R.M.2
  • 5
    • 65249186097 scopus 로고    scopus 로고
    • Non-B DNA conformations as determinants of mutagenesis and human disease
    • Bacolla A, Wells RD (2009) Non-B DNA conformations as determinants of mutagenesis and human disease. Mol Carcinog 48:273
    • (2009) Mol Carcinog , vol.48 , pp. 273
    • Bacolla, A.1    Wells, R.D.2
  • 6
    • 45849141605 scopus 로고    scopus 로고
    • Building objects from nucleic acids for a nanometer world
    • Heckel A, Famulok M (2008) Building objects from nucleic acids for a nanometer world. Biochimie 90:1096
    • (2008) Biochimie , vol.90 , pp. 1096
    • Heckel, A.1    Famulok, M.2
  • 7
    • 81455140677 scopus 로고    scopus 로고
    • The application of DNA and RNA G-quadruplexes to therapeutic medicines
    • Collie GW, Parkinson GN (2011) The application of DNA and RNA G-quadruplexes to therapeutic medicines. Chem Soc Rev 40:5867
    • (2011) Chem Soc Rev , vol.40 , pp. 5867
    • Collie, G.W.1    Parkinson, G.N.2
  • 9
    • 23844438712 scopus 로고    scopus 로고
    • Not so crystal clear: The structure of the human telomere G-quadruplex in solution differs from that present in a crystal
    • Li J, Correia JJ, Wang L, Trent JO, Chaires JB (2005) Not so crystal clear: the structure of the human telomere G-quadruplex in solution differs from that present in a crystal. Nucleic Acids Res 33:4649
    • (2005) Nucleic Acids Res , vol.33 , pp. 4649
    • Li, J.1    Correia, J.J.2    Wang, L.3    Trent, J.O.4    Chaires, J.B.5
  • 10
    • 76349097100 scopus 로고    scopus 로고
    • Human telomeric G-quadruplex: Structures of DNA and RNA sequences
    • Phan AT (2010) Human telomeric G-quadruplex: structures of DNA and RNA sequences. FEBS J 277:1107
    • (2010) FEBS J , vol.277 , pp. 1107
    • Phan, A.T.1
  • 11
    • 47249089630 scopus 로고    scopus 로고
    • Polymorphism of human telomeric quadruplex structures
    • Dai J, Carver M, Yang D (2008) Polymorphism of human telomeric quadruplex structures. Biochimie 90:1172
    • (2008) Biochimie , vol.90 , pp. 1172
    • Dai, J.1    Carver, M.2    Yang, D.3
  • 12
    • 80052222296 scopus 로고    scopus 로고
    • The parallel G-quadruplex structure of vertebrate telomeric repeat sequences is not the preferred folding topology under physiological conditions
    • Hansel R, Lohr F, Foldynova-Trantirkova S, Bamberg E, Trantirek L, Dotsch V (2011) The parallel G-quadruplex structure of vertebrate telomeric repeat sequences is not the preferred folding topology under physiological conditions. Nucleic Acids Res 39:5768
    • (2011) Nucleic Acids Res , vol.39 , pp. 5768
    • Hansel, R.1    Lohr, F.2    Foldynova-Trantirkova, S.3    Bamberg, E.4    Trantirek, L.5    Dotsch, V.6
  • 13
    • 79959509289 scopus 로고    scopus 로고
    • Structure of human telomeric DNA in crowded solution
    • Heddi B, Phan AT (2011) Structure of human telomeric DNA in crowded solution. J Am Chem Soc 133:9824
    • (2011) J Am Chem Soc , vol.133 , pp. 9824
    • Heddi, B.1    Phan, A.T.2
  • 15
    • 39049183349 scopus 로고    scopus 로고
    • Structure and stability of DNA quadruplexes under molecular crowding conditions
    • Karimata H, Miyoshi D, Sugimoto N (2005) Structure and stability of DNA quadruplexes under molecular crowding conditions. Nucleic Acids Symp Ser (Oxf) 239
    • (2005) Nucleic Acids Symp ser (Oxf) , vol.239
    • Karimata, H.1    Miyoshi, D.2    Sugimoto, N.3
  • 16
    • 67749124298 scopus 로고    scopus 로고
    • Structure of the human telomere in K+ solution: A stable basket-type G-quadruplex with only two G-tetrad layers
    • Lim KW, Amrane S, Bouaziz S, Xu W, Mu Y, Patel DJ, Luu KN, Phan AT (2009) Structure of the human telomere in K+ solution: a stable basket-type G-quadruplex with only two G-tetrad layers. J Am Chem Soc 131:4301
    • (2009) J Am Chem Soc , vol.131 , pp. 4301
    • Lim, K.W.1    Amrane, S.2    Bouaziz, S.3    Xu, W.4    Mu, Y.5    Patel, D.J.6    Luu, K.N.7    Phan, A.T.8
  • 17
    • 78650109518 scopus 로고    scopus 로고
    • Hydration is a major determinant of the G-quadruplex stability and conformation of the human telomere 3' sequence of d[AG(3)[TTAG(3)]( 3)]
    • Miller MC, Buscaglia R, Chaires JB, Lane AN, Trent JO (2010) Hydration is a major determinant of the G-quadruplex stability and conformation of the human telomere 3' sequence of d[AG(3)[TTAG(3)](3)]. J Am Chem Soc 132:17105-17107
    • (2010) J Am Chem Soc , vol.132 , pp. 17105-17107
    • Miller, M.C.1    Buscaglia, R.2    Chaires, J.B.3    Lane, A.N.4    Trent, J.O.5
  • 19
    • 0037142071 scopus 로고    scopus 로고
    • Crystal structure of parallel quadruplexes from human telomeric DNA
    • Parkinson GN, Lee MP, Neidle S (2002) Crystal structure of parallel quadruplexes from human telomeric DNA. Nature 417:876
    • (2002) Nature , vol.417 , pp. 876
    • Parkinson, G.N.1    Lee, M.P.2    Neidle, S.3
  • 21
    • 34548762534 scopus 로고    scopus 로고
    • Human telomeric DNA forms parallel-stranded intramolecular G-quadruplex in K+ solution under molecular crowding condition
    • Xue Y, Kan ZY, Wang Q, Yao Y, Liu J, Hao YH, Tan Z (2007) Human telomeric DNA forms parallel-stranded intramolecular G-quadruplex in K+ solution under molecular crowding condition. J Am Chem Soc 129:11185
    • (2007) J Am Chem Soc , vol.129 , pp. 11185
    • Xue, Y.1    Kan, Z.Y.2    Wang, Q.3    Yao, Y.4    Liu, J.5    Hao, Y.H.6    Tan, Z.7
  • 22
    • 0037189914 scopus 로고    scopus 로고
    • Characterization and thermodynamic properties of quadruplex/duplex competition
    • Li W, Wu P, Ohmichi T, Sugimoto N (2002) Characterization and thermodynamic properties of quadruplex/duplex competition. FEBS Lett 526:77
    • (2002) FEBS Lett , vol.526 , pp. 77
    • Li, W.1    Wu, P.2    Ohmichi, T.3    Sugimoto, N.4
  • 23
    • 0345868518 scopus 로고    scopus 로고
    • Duplex dissociation of telomere DNAs induced by molecular crowding
    • Miyoshi D, Matsumura S, Nakano S, Sugimoto N (2004) Duplex dissociation of telomere DNAs induced by molecular crowding. J Am Chem Soc 126:165
    • (2004) J Am Chem Soc , vol.126 , pp. 165
    • Miyoshi, D.1    Matsumura, S.2    Nakano, S.3    Sugimoto, N.4
  • 24
    • 33746600695 scopus 로고    scopus 로고
    • Structure of the human telomere in K+ solution: An intramolecular (3+1) G-quadruplex scaffold
    • Luu KN, Phan AT, Kuryavyi V, Lacroix L, Patel DJ (2006) Structure of the human telomere in K+ solution: an intramolecular (3+1) G-quadruplex scaffold. J Am Chem Soc 128:9963
    • (2006) J Am Chem Soc , vol.128 , pp. 9963
    • Luu, K.N.1    Phan, A.T.2    Kuryavyi, V.3    Lacroix, L.4    Patel, D.J.5
  • 25
    • 34548550548 scopus 로고    scopus 로고
    • Structure of the Hybrid-2 type intramolecular human telomeric G-quadruplex in K+ solution: Insights into structure polymorphism of the human telomeric sequence
    • Dai J, Carver M, Punchihewa C, Jones RA, Yang D (2007) Structure of the Hybrid-2 type intramolecular human telomeric G-quadruplex in K+ solution: insights into structure polymorphism of the human telomeric sequence. Nucleic Acids Res 35:4927
    • (2007) Nucleic Acids Res , vol.35 , pp. 4927
    • Dai, J.1    Carver, M.2    Punchihewa, C.3    Jones, R.A.4    Yang, D.5
  • 26
    • 0027918585 scopus 로고
    • Solution structure of the human telomeric repeat d[AG3(T2AG3)3]
    • Wang Y, Patel DJ (1993) Solution structure of the human telomeric repeat d[AG3(T2AG3)3] G-tetraplex. Structure 1:263
    • (1993) G-tetraplex. Structure , vol.1 , pp. 263
    • Wang, Y.1    Patel, D.J.2
  • 27
    • 0035807847 scopus 로고    scopus 로고
    • In-cell NMR spectroscopy
    • Serber Z, Dotsch V (2001) In-cell NMR spectroscopy. Biochemistry 40:14317
    • (2001) Biochemistry , vol.40 , pp. 14317
    • Serber, Z.1    Dotsch, V.2
  • 29
    • 0035913735 scopus 로고    scopus 로고
    • Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy
    • Serber Z, Ledwidge R, Miller SM, Dotsch V (2001) Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy. J Am Chem Soc 123:8895
    • (2001) J Am Chem Soc , vol.123 , pp. 8895
    • Serber, Z.1    Ledwidge, R.2    Miller, S.M.3    Dotsch, V.4
  • 30
    • 33747059858 scopus 로고    scopus 로고
    • Quantitative NMR analysis of the protein G B1 domain in Xenopus laevis egg extracts and intact oocytes
    • Selenko P, Serber Z, Gadea B, Ruderman J, Wagner G (2006) Quantitative NMR analysis of the protein G B1 domain in Xenopus laevis egg extracts and intact oocytes. Proc Natl Acad Sci USA 103:11904
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11904
    • Selenko, P.1    Serber, Z.2    Gadea, B.3    Ruderman, J.4    Wagner, G.5
  • 35
    • 0027503286 scopus 로고
    • Characterization of the nuclear binding sites of oligodeoxyribonucleotides and their analogs
    • Clarenc JP, Lebleu B, Leonetti JP (1993) Characterization of the nuclear binding sites of oligodeoxyribonucleotides and their analogs. J Biol Chem 268:5600
    • (1993) J Biol Chem , vol.268 , pp. 5600
    • Clarenc, J.P.1    Lebleu, B.2    Leonetti, J.P.3
  • 36
    • 0027181381 scopus 로고
    • Intracellular disposition and metabolism of fluorescently-labeled unmodified and modified oligonucleotides microinjected into mammalian cells
    • Fisher TL, Terhorst T, Cao X, Wagner RW (1993) Intracellular disposition and metabolism of fluorescently-labeled unmodified and modified oligonucleotides microinjected into mammalian cells. Nucleic Acids Res 21:3857
    • (1993) Nucleic Acids Res , vol.21 , pp. 3857
    • Fisher, T.L.1    Terhorst, T.2    Cao, X.3    Wagner, R.W.4
  • 39
    • 0025009248 scopus 로고
    • Transformation of the amphibian oocyte into the egg: Structural and biochemical events
    • Bement WM, Capco DG (1990) Transformation of the amphibian oocyte into the egg: structural and biochemical events. J Electron Microsc Tech 16:202
    • (1990) J Electron Microsc Tech , vol.16 , pp. 202
    • Bement, W.M.1    Capco, D.G.2
  • 40
    • 0025869747 scopus 로고
    • Cycling of intracellular free calcium and intracellular pH in Xenopus embryos: A possible role in the control of the cell cycle
    • Grandin N, Charbonneau M (1991) Cycling of intracellular free calcium and intracellular pH in Xenopus embryos: a possible role in the control of the cell cycle. J Cell Sci 99(Pt 1):5
    • (1991) J Cell Sci , vol.99 , Issue.PART 1 , pp. 5
    • Grandin, N.1    Charbonneau, M.2
  • 41
    • 0026099287 scopus 로고
    • Intracellular free calcium oscillates during cell division of Xenopus embryos
    • Grandin N, Charbonneau M (1991) Intracellular free calcium oscillates during cell division of Xenopus embryos. J Cell Biol 112:711
    • (1991) J Cell Biol , vol.112 , pp. 711
    • Grandin, N.1    Charbonneau, M.2
  • 42
    • 0025976144 scopus 로고
    • Changes in intracellular free calcium activity in Xenopus eggs following imposed intracellular pH changes using weak acids and weak bases
    • Grandin N, Charbonneau M (1991) Changes in intracellular free calcium activity in Xenopus eggs following imposed intracellular pH changes using weak acids and weak bases. Biochim Biophys Acta 1091:242
    • (1991) Biochim Biophys Acta , vol.1091 , pp. 242
    • Grandin, N.1    Charbonneau, M.2
  • 44
    • 35348858197 scopus 로고    scopus 로고
    • The degree of macromolecular crowding in the cytoplasm and nucleoplasm of mammalian cells is conserved
    • Guigas G, Kalla C, Weiss M (2007) The degree of macromolecular crowding in the cytoplasm and nucleoplasm of mammalian cells is conserved. FEBS Lett 581:5094
    • (2007) FEBS Lett , vol.581 , pp. 5094
    • Guigas, G.1    Kalla, C.2    Weiss, M.3
  • 45
    • 34447263750 scopus 로고    scopus 로고
    • Probing the nanoscale viscoelasticity of intracellular fluids in living cells
    • Guigas G, Kalla C, WeissM(2007) Probing the nanoscale viscoelasticity of intracellular fluids in living cells. Biophys J 93:316
    • (2007) Biophys J , vol.93 , pp. 316
    • Guigas, G.1    Weissm, K.C.2
  • 46
    • 77249127365 scopus 로고    scopus 로고
    • Single ovalbumin molecules exploring nucleoplasm and nucleoli of living cell nuclei
    • Speil J, Kubitscheck U (2010) Single ovalbumin molecules exploring nucleoplasm and nucleoli of living cell nuclei. Biochim Biophys Acta 1803:396
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 396
    • Speil, J.1    Kubitscheck, U.2
  • 47
    • 0030614424 scopus 로고    scopus 로고
    • 19F NMR measurements of the rotational mobility of proteins in vivo
    • Williams SP, Haggie PM, Brindle KM (1997) 19F NMR measurements of the rotational mobility of proteins in vivo. Biophys J 72:490
    • (1997) Biophys J , vol.72 , pp. 490
    • Williams, S.P.1    Haggie, P.M.2    Brindle, K.M.3
  • 48
    • 65849230728 scopus 로고    scopus 로고
    • Natural isoflavones regulate the quadruplex-duplex competition in human telomeric DNA
    • Zhang JL, Fu Y, Zheng L, Li W, Li H, Sun Q, Xiao Y, Geng F (2009) Natural isoflavones regulate the quadruplex-duplex competition in human telomeric DNA. Nucleic Acids Res 37:2471
    • (2009) Nucleic Acids Res , vol.37 , pp. 2471
    • Zhang, J.L.1    Fu, Y.2    Zheng, L.3    Li, W.4    Li, H.5    Sun, Q.6    Xiao, Y.7    Geng, F.8
  • 49
    • 45849086552 scopus 로고    scopus 로고
    • Molecular crowding effects on structure and stability of DNA
    • Miyoshi D, Sugimoto N (2008) Molecular crowding effects on structure and stability of DNA. Biochimie 90:1040
    • (2008) Biochimie , vol.90 , pp. 1040
    • Miyoshi, D.1    Sugimoto, N.2
  • 50
    • 77951298407 scopus 로고    scopus 로고
    • Models of macromolecular crowding effects and the need for quantitative comparisons with experiment
    • Elcock AH (2010) Models of macromolecular crowding effects and the need for quantitative comparisons with experiment. Curr Opin Struct Biol 20:196
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 196
    • Elcock, A.H.1
  • 51
    • 84866878929 scopus 로고    scopus 로고
    • DNA Folding in 'crowded' conditions
    • Borman S (2011) DNA Folding in 'crowded' conditions. Chem Eng News 89:6
    • (2011) Chem Eng News , vol.89 , pp. 6
    • Borman, S.1
  • 54
    • 0038725129 scopus 로고    scopus 로고
    • Overall structure and sugar dynamics of a DNA dodecamer from homo- and heteronuclear dipolar couplings and 31P chemical shift anisotropy
    • Wu Z, Delaglio F, Tjandra N, Zhurkin VB, Bax A (2003) Overall structure and sugar dynamics of a DNA dodecamer from homo- and heteronuclear dipolar couplings and 31P chemical shift anisotropy. J Biomol NMR 26:297
    • (2003) J Biomol NMR , vol.26 , pp. 297
    • Wu, Z.1    Delaglio, F.2    Tjandra, N.3    Zhurkin, V.B.4    Bax, A.5
  • 55
    • 68249145921 scopus 로고    scopus 로고
    • Observation of NMR signals from proteins introduced into living mammalian cells by reversible membrane permeabilization using a pore-forming toxin, streptolysin O
    • Ogino S, Kubo S, Umemoto R, Huang S, Nishida N, Shimada I (2009) Observation of NMR signals from proteins introduced into living mammalian cells by reversible membrane permeabilization using a pore-forming toxin, streptolysin O. J Am Chem Soc 131:10834
    • (2009) J Am Chem Soc , vol.131 , pp. 10834
    • Ogino, S.1    Kubo, S.2    Umemoto, R.3    Huang, S.4    Nishida, N.5    Shimada, I.6
  • 58
    • 80052174618 scopus 로고    scopus 로고
    • Longrange distance determination in a DNA model system inside Xenopus laevis oocytes by in-cell spin-label EPR
    • Azarkh M, Okle O, Singh V, Seemann IT, Hartig JS, Dietrich DR, Drescher M (2011) Longrange distance determination in a DNA model system inside Xenopus laevis oocytes by in-cell spin-label EPR. Chembiochem 12:1992
    • (2011) Chembiochem , vol.12 , pp. 1992
    • Azarkh, M.1    Okle, O.2    Singh, V.3    Seemann, I.T.4    Hartig, J.S.5    Dietrich, D.R.6    Drescher, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.