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Volumn 109, Issue 50, 2012, Pages 20413-20418

Telomere- and telomerase-interacting protein that unfolds telomere G-quadruplex and promotes telomere extension in mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

DNA; GUANINE QUADRUPLEX; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN A2; TELOMERASE; TELOMERIC DNA; UNCLASSIFIED DRUG;

EID: 84870883495     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1200232109     Document Type: Article
Times cited : (52)

References (72)
  • 1
    • 0030760917 scopus 로고    scopus 로고
    • Telomere control of replicative lifespan
    • Morin GB (1997) Telomere control of replicative lifespan. Exp Gerontol 32(4-5):375-382.
    • (1997) Exp Gerontol , vol.32 , Issue.4-5 , pp. 375-382
    • Morin, G.B.1
  • 2
    • 0028564951 scopus 로고
    • Specific association of human telomerase activity with immortal cells and cancer
    • Kim NW, et al. (1994) Specific association of human telomerase activity with immortal cells and cancer. Science 266(5193):2011-2015.
    • (1994) Science , vol.266 , Issue.5193 , pp. 2011-2015
    • Kim, N.W.1
  • 3
    • 0035830494 scopus 로고    scopus 로고
    • Cdc13 delivers separate complexes to the telomere for end protection and replication
    • DOI 10.1016/S0092-8674(01)00226-4
    • Pennock E, Buckley K, Lundblad V (2001) Cdc13 delivers separate complexes to the telomere for end protection and replication. Cell 104(3):387-396. (Pubitemid 32206459)
    • (2001) Cell , vol.104 , Issue.3 , pp. 387-396
    • Pennock, E.1    Buckley, K.2    Lundblad, V.3
  • 4
    • 47549086947 scopus 로고    scopus 로고
    • How Telomerase Reaches Its End: Mechanism of Telomerase Regulation by the Telomeric Complex
    • DOI 10.1016/j.molcel.2008.06.013, PII S1097276508004310
    • Bianchi A, Shore D (2008) How telomerase reaches its end: Mechanism of telomerase regulation by the telomeric complex. Mol Cell 31(2):153-165. (Pubitemid 352005819)
    • (2008) Molecular Cell , vol.31 , Issue.2 , pp. 153-165
    • Bianchi, A.1    Shore, D.2
  • 5
    • 77952771824 scopus 로고    scopus 로고
    • Multiple mechanisms for elongation processivity within the reconstituted tetrahymena telomerase holoenzyme
    • Min B, Collins K (2010) Multiple mechanisms for elongation processivity within the reconstituted tetrahymena telomerase holoenzyme. J Biol Chem 285(22):16434-16443.
    • (2010) J Biol Chem , vol.285 , Issue.22 , pp. 16434-16443
    • Min, B.1    Collins, K.2
  • 6
    • 68549136741 scopus 로고    scopus 로고
    • G-quadruplex structures: In vivo evidence and function
    • Lipps HJ, Rhodes D (2009) G-quadruplex structures: In vivo evidence and function. Trends Cell Biol 19(8):414-422.
    • (2009) Trends Cell Biol , vol.19 , Issue.8 , pp. 414-422
    • Lipps, H.J.1    Rhodes, D.2
  • 7
    • 33644865847 scopus 로고    scopus 로고
    • Extension of G-quadruplex DNA by ciliate telomerase
    • DOI 10.1038/sj.emboj.7601006, PII 7601006
    • Oganesian L, Moon IK, Bryan TM, Jarstfer MB (2006) Extension of G-quadruplex DNA by ciliate telomerase. EMBO J 25(5):1148-1159. (Pubitemid 43372127)
    • (2006) EMBO Journal , vol.25 , Issue.5 , pp. 1148-1159
    • Oganesian, L.1    Moon, I.K.2    Bryan, T.M.3    Jarstfer, M.B.4
  • 8
    • 40249101623 scopus 로고    scopus 로고
    • G-quadruplex preferentially forms at the very 3′ end of vertebrate telomeric DNA
    • DOI 10.1093/nar/gkm1137
    • Tang J, et al. (2008) G-quadruplex preferentially forms at the very 3′ end of vertebrate telomeric DNA. Nucleic Acids Res 36(4):1200-1208. (Pubitemid 351330937)
    • (2008) Nucleic Acids Research , vol.36 , Issue.4 , pp. 1200-1208
    • Tang, J.1    Kan, Z.-Y.2    Yao, Y.3    Wang, Q.4    Hao, Y.-H.5    Tan, Z.6
  • 9
    • 0025877846 scopus 로고
    • Inhibition of telomerase by G-quartet DNA structures
    • Zahler AM, Williamson JR, Cech TR, Prescott DM (1991) Inhibition of telomerase by G-quartet DNA structures. Nature 350(6320):718-720. (Pubitemid 21912306)
    • (1991) Nature , vol.350 , Issue.6320 , pp. 718-720
    • Zahler, A.M.1    Williamson, J.R.2    Cech, T.R.3    Prescott, D.M.4
  • 10
    • 0032554620 scopus 로고    scopus 로고
    • Effect of DNA secondary structure on human telomerase activity
    • DOI 10.1021/bi972681p
    • Fletcher TM, Sun D, Salazar M, Hurley LH (1998) Effect of DNA secondary structure on human telomerase activity. Biochemistry 37(16):5536-5541. (Pubitemid 28241936)
    • (1998) Biochemistry , vol.37 , Issue.16 , pp. 5536-5541
    • Fletcher, T.M.1    Sun, D.2    Salazar, M.3    Hurley, L.H.4
  • 11
    • 80051762076 scopus 로고    scopus 로고
    • G-quadruplex formation at the 3′ end of telomere DNA inhibits its extension by telomerase, polymerase and unwinding by helicase
    • Wang Q, et al. (2011) G-quadruplex formation at the 3′ end of telomere DNA inhibits its extension by telomerase, polymerase and unwinding by helicase. Nucleic Acids Res 39(14):6229-6237.
    • (2011) Nucleic Acids Res , vol.39 , Issue.14 , pp. 6229-6237
    • Wang, Q.1
  • 12
    • 0035844082 scopus 로고    scopus 로고
    • Pot1, the putative telomere end-binding protein in fission yeast and humans
    • DOI 10.1126/science.1060036
    • Baumann P, Cech TR (2001) Pot1, the putative telomere end-binding protein in fission yeast and humans. Science 292(5519):1171-1175. (Pubitemid 32440940)
    • (2001) Science , vol.292 , Issue.5519 , pp. 1171-1175
    • Baumann, P.1    Cech, T.R.2
  • 13
    • 12844265975 scopus 로고    scopus 로고
    • Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection
    • Lei M, Podell ER, Cech TR (2004) Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection. Nat Struct Mol Biol 11(12):1223-1229.
    • (2004) Nat Struct Mol Biol , vol.11 , Issue.12 , pp. 1223-1229
    • Lei, M.1    Podell, E.R.2    Cech, T.R.3
  • 14
    • 11844280894 scopus 로고    scopus 로고
    • Human protection of telomeres 1 (POT1) is a negative regulator of telomerase activity in vitro
    • DOI 10.1128/MCB.25.2.808-818.2005
    • Kelleher C, Kurth I, Lingner J (2005) Human protection of telomeres 1 (POT1) is a negative regulator of telomerase activity in vitro. Mol Cell Biol 25(2):808-818. (Pubitemid 40096600)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.2 , pp. 808-818
    • Kelleher, C.1    Kurth, I.2    Lingner, J.3
  • 15
    • 33846691378 scopus 로고    scopus 로고
    • The POT1-TPP1 telomere complex is a telomerase processivity factor
    • DOI 10.1038/nature05454, PII NATURE05454
    • Wang F, et al. (2007) The POT1-TPP1 telomere complex is a telomerase processivity factor. Nature 445(7127):506-510. (Pubitemid 46197626)
    • (2007) Nature , vol.445 , Issue.7127 , pp. 506-510
    • Wang, F.1    Podell, E.R.2    Zaug, A.J.3    Yang, Y.4    Baciu, P.5    Cech, T.R.6    Lei, M.7
  • 16
    • 20144382152 scopus 로고    scopus 로고
    • Switching human telomerase on and off with hPOT1 protein in vitro
    • DOI 10.1074/jbc.M502212200
    • Lei M, Zaug AJ, Podell ER, Cech TR (2005) Switching human telomerase on and off with hPOT1 protein in vitro. J Biol Chem 280(21):20449-20456. (Pubitemid 40776744)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.21 , pp. 20449-20456
    • Lei, M.1    Zaug, A.J.2    Podell, E.R.3    Cech, T.R.4
  • 18
    • 21444433242 scopus 로고    scopus 로고
    • Structure of hnRNP D complexed with single-stranded telomere DNA and unfolding of the quadruplex by heterogeneous nuclear ribonucleoprotein D
    • DOI 10.1074/jbc.M411822200
    • Enokizono Y, et al. (2005) Structure of hnRNP D complexed with single-stranded telomere DNA and unfolding of the quadruplex by heterogeneous nuclear ribonucleoprotein D. J Biol Chem 280(19):18862-18870. (Pubitemid 41379588)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.19 , pp. 18862-18870
    • Enokizono, Y.1    Konishi, Y.2    Nagata, K.3    Ouhashi, K.4    Uesugi, S.5    Ishikawa, F.6    Katahira, M.7
  • 19
    • 0037148269 scopus 로고    scopus 로고
    • A model for heterogeneous nuclear ribonucleoproteins in telomere and telomerase regulation
    • DOI 10.1038/sj/onc/1205086
    • Ford LP, Wright WE, Shay JW (2002) A model for heterogeneous nuclear ribonucleoproteins in telomere and telomerase regulation. Oncogene 21(4):580-583. (Pubitemid 34146257)
    • (2002) Oncogene , vol.21 , Issue.4 REV. ISS. 1 , pp. 580-583
    • Ford, L.P.1    Wright, W.E.2    Shay, J.W.3
  • 20
    • 0034462197 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoproteins C1 and C2 associate with the RNA component of human telomerase
    • DOI 10.1128/MCB.20.23.9084-9091.2000
    • Ford LP, Suh JM, Wright WE, Shay JW (2000) Heterogeneous nuclear ribonucleoproteins C1 and C2 associate with the RNA component of human telomerase. Mol Cell Biol 20(23):9084-9091. (Pubitemid 32245937)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.23 , pp. 9084-9091
    • Ford, L.P.1    Suh, J.M.2    Wright, W.E.3    Shay, J.W.4
  • 21
    • 0035368412 scopus 로고    scopus 로고
    • hnRNP A1 may interact simultaneously with telomeric DNA and the human telomerase RNA in vitro
    • Fiset S, Chabot B (2001) hnRNP A1 may interact simultaneously with telomeric DNA and the human telomerase RNA in vitro. Nucleic Acids Res 29(11):2268-2275.
    • (2001) Nucleic Acids Res , vol.29 , Issue.11 , pp. 2268-2275
    • Fiset, S.1    Chabot, B.2
  • 22
    • 0029838246 scopus 로고    scopus 로고
    • hnRNP proteins and B23 are the major proteins of the internal nuclear matrix of HeLa S3 cells
    • DOI 10.1002/(SICI)1097-4644(199608)62:2<275::AID-JCB15>3.0.CO;2-K
    • Mattern KA, Humbel BM, Muijsers AO, de Jong L, van Driel R (1996) hnRNP proteins and B23 are the major proteins of the internal nuclear matrix of HeLa S3 cells. J Cell Biochem 62(2):275-289. (Pubitemid 26287211)
    • (1996) Journal of Cellular Biochemistry , vol.62 , Issue.2 , pp. 275-289
    • Mattern, K.A.1    Humbel, B.M.2    Muijsers, A.O.3    De Jong, L.4    Van Driel, R.5
  • 23
    • 0344074646 scopus 로고    scopus 로고
    • Regulated tissue-specific expression of antagonistic pre-mRNA splicing factors
    • Hanamura A, Cáceres JF, Mayeda A, Franza BR, Jr., Krainer AR (1998) Regulated tissue-specific expression of antagonistic pre-mRNA splicing factors. RNA 4(4):430-444. (Pubitemid 28160784)
    • (1998) RNA , vol.4 , Issue.4 , pp. 430-444
    • Hanamura, A.1    Caceres, J.F.2    Mayeda, A.3    Franza Jr., B.R.4    Krainer, A.R.5
  • 24
    • 0026607355 scopus 로고
    • A protein which specifically binds to single stranded TTAGGGn repeats
    • McKay SJ, Cooke H (1992) A protein which specifically binds to single stranded TTAGGGn repeats. Nucleic Acids Res 20(6):1387-1391.
    • (1992) Nucleic Acids Res , vol.20 , Issue.6 , pp. 1387-1391
    • McKay, S.J.1    Cooke, H.2
  • 25
    • 34147095342 scopus 로고    scopus 로고
    • Protein composition of catalytically active human telomerase from immortal cells
    • DOI 10.1126/science.1138596
    • Cohen SB, et al. (2007) Protein composition of catalytically active human telomerase from immortal cells. Science 315(5820):1850-1853. (Pubitemid 46580145)
    • (2007) Science , vol.315 , Issue.5820 , pp. 1850-1853
    • Cohen, S.B.1    Graham, M.E.2    Lovrecz, G.O.3    Bache, N.4    Robinson, P.J.5    Reddel, R.R.6
  • 26
    • 0026541384 scopus 로고
    • Human telomeres are attached to the nuclear matrix
    • de Lange T (1992) Human telomeres are attached to the nuclear matrix. EMBO J 11(2):717-724.
    • (1992) EMBO J , vol.11 , Issue.2 , pp. 717-724
    • De Lange, T.1
  • 28
    • 0018858066 scopus 로고
    • A fixed site of DNA replication in eucaryotic cells
    • Pardoll DM, Vogelstein B, Coffey DS (1980) A fi xed site of DNA replication in eucaryotic cells. Cell 19(2):527-536. (Pubitemid 10152900)
    • (1980) Cell , vol.19 , Issue.2 , pp. 527-536
    • Pardoll, D.M.1    Vogelstein, B.2    Coffey, D.S.3
  • 29
    • 68049088928 scopus 로고    scopus 로고
    • Telomere extension occurs at most chromosome ends and is uncoupled from fill-in in human cancer cells
    • Zhao Y, et al. (2009) Telomere extension occurs at most chromosome ends and is uncoupled from fill-in in human cancer cells. Cell 138(3):463-475.
    • (2009) Cell , vol.138 , Issue.3 , pp. 463-475
    • Zhao, Y.1
  • 30
    • 0033538846 scopus 로고    scopus 로고
    • Association of chromosome territories with the nuclear matrix. Disruption of human chromosome territories correlates with the release of a subset of nuclear matrix proteins
    • Ma H, Siegel AJ, Berezney R (1999) Association of chromosome territories with the nuclear matrix. Disruption of human chromosome territories correlates with the release of a subset of nuclear matrix proteins. J Cell Biol 146(3):531-542.
    • (1999) J Cell Biol , vol.146 , Issue.3 , pp. 531-542
    • Ma, H.1    Siegel, A.J.2    Berezney, R.3
  • 31
    • 54249169010 scopus 로고    scopus 로고
    • Identification of low-abundance alternatively spliced mRNA variants by exon exclusive reverse transcriptase polymerase chain reaction
    • Wang F, Zhao Y, Hao YH, Tan Z (2008) Identification of low-abundance alternatively spliced mRNA variants by exon exclusive reverse transcriptase polymerase chain reaction. Anal Biochem 383(2):307-310.
    • (2008) Anal Biochem , vol.383 , Issue.2 , pp. 307-310
    • Wang, F.1    Zhao, Y.2    Hao, Y.H.3    Tan, Z.4
  • 32
    • 0027481140 scopus 로고
    • Mammalian heterogeneous ribonucleoprotein A1 and its constituent domains. Nucleic acid interaction, structural stability and self-association
    • DOI 10.1006/jmbi.1993.1093
    • Casas-Finet JR, et al. (1993) Mammalian heterogeneous ribonucleoprotein A1 and its constituent domains. Nucleic acid interaction, structural stability and self-association. J Mol Biol 229(4):873-889. (Pubitemid 23091809)
    • (1993) Journal of Molecular Biology , vol.229 , Issue.4 , pp. 873-889
    • Casas-Finet, J.R.1    Smith Jr., J.D.2    Kumar, A.3    Kim, J.G.4    Wilson, S.H.5    Karpel, R.L.6
  • 34
    • 1842529179 scopus 로고    scopus 로고
    • DNA binding features of human POT1: A nonamer 5′-TAGGGTTAG-3′ minimal binding site, sequence specificity, and internal binding to multimeric sites
    • DOI 10.1074/jbc.M312309200
    • Loayza D, Parsons H, Donigian J, Hoke K, de Lange T (2004) DNA binding features of human POT1: A nonamer 5′-TAGGGTTAG-3′ minimal binding site, sequence specificity, and internal binding to multimeric sites. J Biol Chem 279(13):13241-13248. (Pubitemid 38445903)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 13241-13248
    • Loayza, D.1    Parsons, H.2    Donigian, J.3    Hoke, K.4    De Lange, T.5
  • 35
    • 34250633242 scopus 로고    scopus 로고
    • An exonuclease I hydrolysis assay for evaluating G-quadruplex stabilization by small molecules
    • Yao Y, Wang Q, Hao YH, Tan Z (2007) An exonuclease I hydrolysis assay for evaluating G-quadruplex stabilization by small molecules. Nucleic Acids Res 35(9):e68.
    • (2007) Nucleic Acids Res , vol.35 , Issue.9
    • Yao, Y.1    Wang, Q.2    Hao, Y.H.3    Tan, Z.4
  • 36
    • 33745365364 scopus 로고    scopus 로고
    • Molecular crowding induces telomere G-quadruplex formation under salt-deficient conditions and enhances its competition with duplex formation
    • Kan ZY, et al. (2006) Molecular crowding induces telomere G-quadruplex formation under salt-deficient conditions and enhances its competition with duplex formation. Angew Chem Int Ed Engl 45(10):1629-1632.
    • (2006) Angew Chem Int Ed Engl , vol.45 , Issue.10 , pp. 1629-1632
    • Kan, Z.Y.1
  • 37
    • 15944368044 scopus 로고    scopus 로고
    • Telomere-end processing: The terminal nucleotidesof human chromosomes
    • DOI 10.1016/j.molcel.2005.02.035
    • Sfeir AJ, Chai W, Shay JW, Wright WE (2005) Telomere-end processing the terminal nucleotides of human chromosomes. Mol Cell 18(1):131-138. (Pubitemid 40444654)
    • (2005) Molecular Cell , vol.18 , Issue.1 , pp. 131-138
    • Sfeir, A.J.1    Chai, W.2    Shay, J.W.3    Wright, W.E.4
  • 38
    • 0034598919 scopus 로고    scopus 로고
    • Secondary structure of vertebrate telomerase RNA
    • Chen JL, Blasco MA, Greider CW (2000) Secondary structure of vertebrate telomerase RNA. Cell 100(5):503-514.
    • (2000) Cell , vol.100 , Issue.5 , pp. 503-514
    • Chen, J.L.1    Blasco, M.A.2    Greider, C.W.3
  • 39
    • 0030743347 scopus 로고    scopus 로고
    • Advances in quantification and characterization of telomerase activity by the telomeric repeat amplification protocol (TRAP)
    • DOI 10.1093/nar/25.13.2595
    • Kim NW, Wu F (1997) Advances in quantification and characterization of telomerase activity by the telomeric repeat amplification protocol (TRAP). Nucleic Acids Res 25(13):2595-2597. (Pubitemid 27298154)
    • (1997) Nucleic Acids Research , vol.25 , Issue.13 , pp. 2595-2597
    • Kim, N.W.1    Wu, F.2
  • 40
    • 0037096736 scopus 로고    scopus 로고
    • Detection of telomerase inhibitors based on G-quadruplex ligands by a modified telomeric repeat amplification protocol assay
    • Gomez D, Mergny JL, Riou JF (2002) Detection of telomerase inhibitors based on g-quadruplex ligands by a modified telomeric repeat amplification protocol assay. Cancer Res 62(12):3365-3368. (Pubitemid 34651379)
    • (2002) Cancer Research , vol.62 , Issue.12 , pp. 3365-3368
    • Gomez, D.1    Mergny, J.-L.2    Riou, J.-F.3
  • 41
    • 0037439107 scopus 로고    scopus 로고
    • Determinants in mammalian telomerase RNA that mediate enzyme processivity and cross-species incompatibility
    • Chen JL, Greider CW (2003) Determinants in mammalian telomerase RNA that mediate enzyme processivity and cross-species incompatibility. EMBO J 22(2):304-314.
    • (2003) EMBO J , vol.22 , Issue.2 , pp. 304-314
    • Chen, J.L.1    Greider, C.W.2
  • 43
    • 0035864173 scopus 로고    scopus 로고
    • Telomeric repeat amplification, without shortening or lengthening of the telomerase products: A method to analyze the processivity of telomerase enzyme
    • Szatmari I, Aradi J (2001) Telomeric repeat amplification, without shortening or lengthening of the telomerase products: A method to analyze the processivity of telomerase enzyme. Nucleic Acids Res 29(2):E3.
    • (2001) Nucleic Acids Res , vol.29 , Issue.2
    • Szatmari, I.1    Aradi, J.2
  • 44
    • 75649089282 scopus 로고    scopus 로고
    • Molecular crowding creates an essential environment for the formation of stable G-quadruplexes in long double-stranded DNA
    • Zheng KW, Chen Z, Hao YH, Tan Z (2010) Molecular crowding creates an essential environment for the formation of stable G-quadruplexes in long double-stranded DNA. Nucleic Acids Res 38(1):327-338.
    • (2010) Nucleic Acids Res , vol.38 , Issue.1 , pp. 327-338
    • Zheng, K.W.1    Chen, Z.2    Hao, Y.H.3    Tan, Z.4
  • 46
    • 34547117416 scopus 로고    scopus 로고
    • G-quadruplex formation in human telomeric (TTAGGG)4 sequence with complementary strand in close vicinity under molecularly crowded condition
    • Kan ZY, et al. (2007) G-quadruplex formation in human telomeric (TTAGGG)4 sequence with complementary strand in close vicinity under molecularly crowded condition. Nucleic Acids Res 35(11):3646-3653.
    • (2007) Nucleic Acids Res , vol.35 , Issue.11 , pp. 3646-3653
    • Kan, Z.Y.1
  • 47
    • 34748876539 scopus 로고    scopus 로고
    • Human Telomerase RNA Accumulation in Cajal Bodies Facilitates Telomerase Recruitment to Telomeres and Telomere Elongation
    • DOI 10.1016/j.molcel.2007.07.020, PII S1097276507004935
    • Cristofari G, et al. (2007) Human telomerase RNA accumulation in Cajal bodies facilitates telomerase recruitment to telomeres and telomere elongation. Mol Cell 27 (6):882-889. (Pubitemid 47488182)
    • (2007) Molecular Cell , vol.27 , Issue.6 , pp. 882-889
    • Cristofari, G.1    Adolf, E.2    Reichenbach, P.3    Sikora, K.4    Terns, R.M.5    Terns, M.P.6    Lingner, J.7
  • 48
    • 17944388104 scopus 로고    scopus 로고
    • Human telomerase RNA and box H/ACA scaRNAs share a common Cajal body-specific localization signal
    • DOI 10.1083/jcb.200310138
    • Jády BE, Bertrand E, Kiss T (2004) Human telomerase RNA and box H/ACA scaRNAs share a common Cajal body-specific localization signal. J Cell Biol 164(5):647-652. (Pubitemid 38282948)
    • (2004) Journal of Cell Biology , vol.164 , Issue.5 , pp. 647-652
    • Jady, B.E.1    Bertrand, E.2    Kiss, T.3
  • 50
    • 47249114945 scopus 로고    scopus 로고
    • +-induced folding of models of human telomeric DNA into G-quadruplex structures
    • DOI 10.1093/nar/gkn379
    • Gray RD, Chaires JB (2008) Kinetics and mechanism of K+- and Na+-induced folding of models of human telomeric DNA into G-quadruplex structures. Nucleic Acids Res 36(12):4191-4203. (Pubitemid 351984834)
    • (2008) Nucleic Acids Research , vol.36 , Issue.12 , pp. 4191-4203
    • Gray, R.D.1    Chaires, J.B.2
  • 53
    • 27144451010 scopus 로고    scopus 로고
    • Telomere end-binding proteins control the formation of G-quadruplex DNA structures in vivo
    • DOI 10.1038/nsmb982, PII N982
    • Paeschke K, Simonsson T, Postberg J, Rhodes D, Lipps HJ (2005) Telomere end-binding proteins control the formation of G-quadruplex DNA structures in vivo. Nat Struct Mol Biol 12(10):847-854. (Pubitemid 41486707)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.10 , pp. 847-854
    • Paeschke, K.1    Simonsson, T.2    Postberg, J.3    Rhodes, D.4    Lipps, H.J.5
  • 54
    • 3543039438 scopus 로고    scopus 로고
    • Detection of quadruplex DNA structures in human telomeres by a fluorescent carbazole derivative
    • Chang CC, et al. (2004) Detection of quadruplex DNA structures in human telomeres by a fluorescent carbazole derivative. Anal Chem 76(15):4490-4494.
    • (2004) Anal Chem , vol.76 , Issue.15 , pp. 4490-4494
    • Chang, C.C.1
  • 56
    • 77955653444 scopus 로고    scopus 로고
    • Interaction of hnRNP A1 with telomere DNA G-quadruplex structures studied at the single molecule level
    • Krüger AC, et al. (2010) Interaction of hnRNP A1 with telomere DNA G-quadruplex structures studied at the single molecule level. Eur Biophys J 39(9):1343-1350.
    • (2010) Eur Biophys J , vol.39 , Issue.9 , pp. 1343-1350
    • Krüger, A.C.1
  • 57
    • 34147207828 scopus 로고    scopus 로고
    • Tetraplex structure of fission yeast telomeric DNA and unfolding of the tetraplex on the interaction with telomeric DNA binding protein Pot1
    • DOI 10.1093/jb/mvm011
    • Torigoe H, Furukawa A (2007) Tetraplex structure of fission yeast telomeric DNA and unfolding of the tetraplex on the interaction with telomeric DNA binding protein Pot1. J Biochem 141(1):57-68. (Pubitemid 46580155)
    • (2007) Journal of Biochemistry , vol.141 , Issue.1 , pp. 57-68
    • Torigoe, H.1    Furukawa, A.2
  • 58
    • 0034640507 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein A1 and UP1 protect mammalian telomeric repeats and modulate telomere replication in vitro
    • DOI 10.1074/jbc.275.19.14509
    • Dallaire F, Dupuis S, Fiset S, Chabot B (2000) Heterogeneous nuclear ribonucleoprotein A1 and UP1 protect mammalian telomeric repeats and modulate telomere replication in vitro. J Biol Chem 275(19):14509-14516. (Pubitemid 30339738)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.19 , pp. 14509-14516
    • Dallaire, F.1    Dupuis, S.2    Fiset, S.3    Chabot, B.4
  • 59
    • 38349076683 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein A3 binds single-stranded telomeric DNA and inhibits telomerase extension in vitro
    • Huang PR, Tsai ST, Hsieh KH, Wang TC (2008) Heterogeneous nuclear ribonucleoprotein A3 binds single-stranded telomeric DNA and inhibits telomerase extension in vitro. Biochim Biophys Acta 1783(2):193-202.
    • (2008) Biochim Biophys Acta , vol.1783 , Issue.2 , pp. 193-202
    • Huang, P.R.1    Tsai, S.T.2    Hsieh, K.H.3    Wang, T.C.4
  • 61
    • 36749010238 scopus 로고    scopus 로고
    • Purification of Human Telomerase Complexes Identifies Factors Involved in Telomerase Biogenesis and Telomere Length Regulation
    • DOI 10.1016/j.molcel.2007.09.023, PII S1097276507006351
    • Fu D, Collins K (2007) Purification of human telomerase complexes identifies factors involved in telomerase biogenesis and telomere length regulation. Mol Cell 28(5):773-785. (Pubitemid 350217053)
    • (2007) Molecular Cell , vol.28 , Issue.5 , pp. 773-785
    • Fu, D.1    Collins, K.2
  • 63
    • 12344299676 scopus 로고    scopus 로고
    • Nuclear actin is partially associated with Cajal bodies in human cells in culture and relocates to the nuclear periphery after infection of cells by adenovirus 5
    • DOI 10.1016/j.yexcr.2004.06.034, PII S0014482704005117
    • Gedge LJ, Morrison EE, Blair GE, Walker JH (2005) Nuclear actin is partially associated with Cajal bodies in human cells in culture and relocates to the nuclear periphery after infection of cells by adenovirus 5. Exp Cell Res 303(2):229-239. (Pubitemid 40126258)
    • (2005) Experimental Cell Research , vol.303 , Issue.2 , pp. 229-239
    • Gedge, L.J.E.1    Morrison, E.E.2    Blair, G.E.3    Walker, J.H.4
  • 64
    • 0028936693 scopus 로고
    • p80-coilin: A component of coiled bodies and interchromatin granule-associated zones
    • Puvion-Dutilleul F, Besse S, Chan EK, Tan EM, Puvion E (1995) p80-coilin: A component of coiled bodies and interchromatin granule-associated zones. J Cell Sci 108(Pt 3):1143-1153.
    • (1995) J Cell Sci , vol.108 , Issue.PART 3 , pp. 1143-1153
    • Puvion-Dutilleul, F.1    Besse, S.2    Chan, E.K.3    Tan, E.M.4    Puvion, E.5
  • 65
    • 0028061367 scopus 로고
    • Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins
    • Mayeda A, Munroe SH, Cáceres JF, Krainer AR (1994) Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins. EMBO J 13(22):5483-5495. (Pubitemid 24351827)
    • (1994) EMBO Journal , vol.13 , Issue.22 , pp. 5483-5495
    • Mayeda, A.1    Munroe, S.H.2    Caceres, J.F.3    Krainer, A.R.4
  • 67
    • 34548317418 scopus 로고    scopus 로고
    • Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1
    • DOI 10.1038/nature06065, PII NATURE06065
    • Denchi EL, de Lange T (2007) Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1. Nature 448(7157):1068-1071. (Pubitemid 47345583)
    • (2007) Nature , vol.448 , Issue.7157 , pp. 1068-1071
    • Denchi, E.L.1    De Lange, T.2
  • 68
    • 37849030208 scopus 로고    scopus 로고
    • Pot1 and cell cycle progression cooperate in telomere length regulation
    • Churikov D, Price CM (2008) Pot1 and cell cycle progression cooperate in telomere length regulation. Nat Struct Mol Biol 15(1):79-84.
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.1 , pp. 79-84
    • Churikov, D.1    Price, C.M.2
  • 69
    • 33846692105 scopus 로고    scopus 로고
    • TPP1 is a homologue of ciliate TEBP-beta and interacts with POT1 to recruit telomerase
    • DOI 10.1038/nature05469, PII NATURE05469
    • Xin H, et al. (2007) TPP1 is a homologue of ciliate TEBP-beta and interacts with POT1 to recruit telomerase. Nature 445(7127):559-562. (Pubitemid 46197638)
    • (2007) Nature , vol.445 , Issue.7127 , pp. 559-562
    • Xin, H.1    Liu, D.2    Wan, M.3    Safari, A.4    Kim, H.5    Sun, W.6    O'Connor, M.S.7    Songyang, Z.8
  • 70
    • 77949382591 scopus 로고    scopus 로고
    • Functional interaction between telomere protein TPP1 and telomerase
    • Zaug AJ, Podell ER, Nandakumar J, Cech TR (2010) Functional interaction between telomere protein TPP1 and telomerase. Genes Dev 24(6):613-622.
    • (2010) Genes Dev , vol.24 , Issue.6 , pp. 613-622
    • Zaug, A.J.1    Podell, E.R.2    Nandakumar, J.3    Cech, T.R.4
  • 71
    • 84864607108 scopus 로고    scopus 로고
    • TPP1 OB-fold domain controls telomere maintenance by recruiting telomerase to chromosome ends
    • Zhong FL, et al. (2012) TPP1 OB-fold domain controls telomere maintenance by recruiting telomerase to chromosome ends. Cell 150(3):481-494.
    • (2012) Cell , vol.150 , Issue.3 , pp. 481-494
    • Zhong, F.L.1


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