메뉴 건너뛰기




Volumn 8, Issue 10, 2007, Pages 825-838

How telomeres are replicated

Author keywords

[No Author keywords available]

Indexed keywords

DNA; KU ANTIGEN; TELOMERASE;

EID: 34648843213     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2259     Document Type: Review
Times cited : (376)

References (169)
  • 1
    • 0000813303 scopus 로고
    • The production of homozygous deficient tissues with mutant characteristics by means of the aberrant mitotic behavior of ring-shaped chromosomes
    • McClintock, B. The production of homozygous deficient tissues with mutant characteristics by means of the aberrant mitotic behavior of ring-shaped chromosomes. Genetics 23, 315-376 (1938).
    • (1938) Genetics , vol.23 , pp. 315-376
    • McClintock, B.1
  • 2
    • 0027421043 scopus 로고
    • Loss of a yeast telomere: Arrest, recovery, and chromosome loss
    • Sandell, L. L. & Zakian, V. A. Loss of a yeast telomere: arrest, recovery, and chromosome loss. Cell 75, 729-739 (1993).
    • (1993) Cell , vol.75 , pp. 729-739
    • Sandell, L.L.1    Zakian, V.A.2
  • 3
    • 0032489012 scopus 로고    scopus 로고
    • TRF2 protects human telomeres from end-to-end fusions
    • van Steensel, B., Smogorzewska, A. & de Lange, T. TRF2 protects human telomeres from end-to-end fusions. Cell 92, 401-413 (1998).
    • (1998) Cell , vol.92 , pp. 401-413
    • van Steensel, B.1    Smogorzewska, A.2    de Lange, T.3
  • 4
    • 24944460598 scopus 로고    scopus 로고
    • Shelterin: The protein complex that shapes and safeguards human telomeres
    • de Lange, T. Shelterin: the protein complex that shapes and safeguards human telomeres. Genes Dev. 19, 2100-2110 (2005).
    • (2005) Genes Dev , vol.19 , pp. 2100-2110
    • de Lange, T.1
  • 5
    • 18744414764 scopus 로고    scopus 로고
    • The telomerase cycle: Normal and pathological aspects
    • Brunori, M., Luciano, P., Gilson, E. & Geli, V. The telomerase cycle: normal and pathological aspects. J. Mol. Med. 83, 244-257 (2005).
    • (2005) J. Mol. Med , vol.83 , pp. 244-257
    • Brunori, M.1    Luciano, P.2    Gilson, E.3    Geli, V.4
  • 6
    • 0022402513 scopus 로고
    • Identification of a specific telomere terminal transferase activity in Tetrahymena extracts
    • Greider, C. W. & Blackburn, E. H. Identification of a specific telomere terminal transferase activity in Tetrahymena extracts. Cell 43, 405-413 (1985).
    • (1985) Cell , vol.43 , pp. 405-413
    • Greider, C.W.1    Blackburn, E.H.2
  • 7
    • 0019887426 scopus 로고
    • Replication of the extrachromosomal ribosomal RNA genes of Tetrahymena thermophilia
    • Cech, T. R. & Brehm, S. L. Replication of the extrachromosomal ribosomal RNA genes of Tetrahymena thermophilia. Nucleic Acids Res. 9, 3531-3543 (1981).
    • (1981) Nucleic Acids Res , vol.9 , pp. 3531-3543
    • Cech, T.R.1    Brehm, S.L.2
  • 9
    • 0036606186 scopus 로고    scopus 로고
    • Saccharomyces Rrm3p, a 5′ to 3′ DNA helicase that promotes replication fork progression through telomeric and subtelomeric DNA
    • Ivessa, A. S., Zhou, J. Q., Schulz, V. P., Monson, E. K. & Zakian, V. A. Saccharomyces Rrm3p, a 5′ to 3′ DNA helicase that promotes replication fork progression through telomeric and subtelomeric DNA. Genes Dev. 16, 1383-1396 (2002).
    • (2002) Genes Dev , vol.16 , pp. 1383-1396
    • Ivessa, A.S.1    Zhou, J.Q.2    Schulz, V.P.3    Monson, E.K.4    Zakian, V.A.5
  • 10
    • 1942518292 scopus 로고    scopus 로고
    • Anatomy and dynamics of DNA replication fork movement in yeast telomeric regions
    • Makovets, S., Herskowitz, I. & Blackburn, E. H. Anatomy and dynamics of DNA replication fork movement in yeast telomeric regions. Mol. Cell. Biol. 24, 4019-4031 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 4019-4031
    • Makovets, S.1    Herskowitz, I.2    Blackburn, E.H.3
  • 11
    • 33645747064 scopus 로고    scopus 로고
    • Miller, K. M., Rog, O. & Cooper, J. P. Semi-conservative DNA replication through telomeres requires Taz1. Nature 440, 824-828 (2006). Before this study it was assumed that telomere-binding proteins impede replication fork progression. Conversely, this study shows that Taz1 is crucial for efficient replication fork progression through the telomere.
    • Miller, K. M., Rog, O. & Cooper, J. P. Semi-conservative DNA replication through telomeres requires Taz1. Nature 440, 824-828 (2006). Before this study it was assumed that telomere-binding proteins impede replication fork progression. Conversely, this study shows that Taz1 is crucial for efficient replication fork progression through the telomere.
  • 12
    • 0024348466 scopus 로고
    • DNA primase and the replication of the telomeres in Oxytricha nova
    • Zahler, A. M. & Prescott, D. M. DNA primase and the replication of the telomeres in Oxytricha nova. Nucleic Acids Res. 17, 6299-6317 (1989).
    • (1989) Nucleic Acids Res , vol.17 , pp. 6299-6317
    • Zahler, A.M.1    Prescott, D.M.2
  • 13
    • 0036312043 scopus 로고    scopus 로고
    • Ray, S., Karamysheva, Z., Wang, L., Shippen, D. E. & Price, C. M. Interactions between telomerase and primase physically link the telomere and chromosome replication machinery. Mol. Cell. Biol. 22, 5859-5868 (2002). A physical association of telomerase and primase is shown in Euplotes crassus, supporting the proposed coordinated regulation of telomeric G- and C-strand synthesis.
    • Ray, S., Karamysheva, Z., Wang, L., Shippen, D. E. & Price, C. M. Interactions between telomerase and primase physically link the telomere and chromosome replication machinery. Mol. Cell. Biol. 22, 5859-5868 (2002). A physical association of telomerase and primase is shown in Euplotes crassus, supporting the proposed coordinated regulation of telomeric G- and C-strand synthesis.
  • 14
    • 0344490247 scopus 로고    scopus 로고
    • Replication proteins influence the maintenance of telomere length and telomerase protein stability
    • Dahlen, M., Sunnerhagen, P. & Wang, T. S. Replication proteins influence the maintenance of telomere length and telomerase protein stability. Mol. Cell. Biol. 23, 3031-3042 (2003).
    • (2003) Mol. Cell. Biol , vol.23 , pp. 3031-3042
    • Dahlen, M.1    Sunnerhagen, P.2    Wang, T.S.3
  • 15
    • 0033556028 scopus 로고    scopus 로고
    • Telomeric chromatin modulates replication timing near chromosome ends
    • Stevenson, J. B. & Gottschling, D. E. Telomeric chromatin modulates replication timing near chromosome ends. Genes Dev. 13, 146-151 (1999).
    • (1999) Genes Dev , vol.13 , pp. 146-151
    • Stevenson, J.B.1    Gottschling, D.E.2
  • 16
    • 0035197623 scopus 로고    scopus 로고
    • Completion of replication map of Saccharomyces cerevisiae chromosome III
    • Poloumienko, A., Dershowitz, A., De, J. & Newlon, C. S. Completion of replication map of Saccharomyces cerevisiae chromosome III. Mol. Biol. Cell 12, 3317-3327 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3317-3327
    • Poloumienko, A.1    Dershowitz, A.2    De, J.3    Newlon, C.S.4
  • 17
    • 0036211190 scopus 로고    scopus 로고
    • Telomeric proteins regulate episomal maintenance of Epstein-Barr virus origin of plasmid replication
    • Deng, Z. et al. Telomeric proteins regulate episomal maintenance of Epstein-Barr virus origin of plasmid replication. Mol. Cell 9, 493-503 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 493-503
    • Deng, Z.1
  • 18
    • 33846969882 scopus 로고    scopus 로고
    • A topological mechanism for TRF2-enhanced strand invasion
    • Amiard, S. et al. A topological mechanism for TRF2-enhanced strand invasion. Nature Struct. Mol. Biol. 14, 147-154 (2007).
    • (2007) Nature Struct. Mol. Biol , vol.14 , pp. 147-154
    • Amiard, S.1
  • 19
    • 33750801681 scopus 로고    scopus 로고
    • Verdun, R. E. & Karlseder, J. The DNA damage machinery and homologous recombination pathway act consecutively to protect human telomeres. Cell 127, 709-720 (2006). Shows that telomere ends need to be recognized as damaged DNA in order for end replication to be completed and for a telomere-specific structure to be formed at chromosome ends after replication.
    • Verdun, R. E. & Karlseder, J. The DNA damage machinery and homologous recombination pathway act consecutively to protect human telomeres. Cell 127, 709-720 (2006). Shows that telomere ends need to be recognized as damaged DNA in order for end replication to be completed and for a telomere-specific structure to be formed at chromosome ends after replication.
  • 20
    • 0035812808 scopus 로고    scopus 로고
    • Replication dynamics of the yeast genome
    • Raghuraman, M. K. et al. Replication dynamics of the yeast genome. Science 294, 115-121 (2001).
    • (2001) Science , vol.294 , pp. 115-121
    • Raghuraman, M.K.1
  • 21
    • 0025201982 scopus 로고
    • Position effect at S. cerevisiae telomeres: Reversible repression of Pol II transcription
    • Gottschling, D. E., Aparicio, O. M., Billington, B. L. & Zakian, V. A. Position effect at S. cerevisiae telomeres: reversible repression of Pol II transcription. Cell 63, 751-762 (1990).
    • (1990) Cell , vol.63 , pp. 751-762
    • Gottschling, D.E.1    Aparicio, O.M.2    Billington, B.L.3    Zakian, V.A.4
  • 22
    • 0026571672 scopus 로고
    • A position effect on the time of replication origin activation in yeast
    • Ferguson, B. M. & Fangman, W. L. A position effect on the time of replication origin activation in yeast. Cell 68, 333-339 (1992).
    • (1992) Cell , vol.68 , pp. 333-339
    • Ferguson, B.M.1    Fangman, W.L.2
  • 23
    • 0037019025 scopus 로고    scopus 로고
    • Control of replication timing by a transcriptional silencer
    • Zappulla, D. C., Sternglanz, R. & Leatherwood, J. Control of replication timing by a transcriptional silencer. Curr. Biol. 12, 869-875 (2002).
    • (2002) Curr. Biol , vol.12 , pp. 869-875
    • Zappulla, D.C.1    Sternglanz, R.2    Leatherwood, J.3
  • 24
    • 0033522444 scopus 로고    scopus 로고
    • Limitations of silencing at native yeast telomeres
    • Pryde, F. E. & Louis, E. J. Limitations of silencing at native yeast telomeres. EMBO J. 18, 2538-2550 (1999).
    • (1999) EMBO J , vol.18 , pp. 2538-2550
    • Pryde, F.E.1    Louis, E.J.2
  • 25
    • 0033604609 scopus 로고    scopus 로고
    • Chromosomal landscape of nucleosome-dependent gene expression and silencing in yeast
    • Wyrick, J. J. et al. Chromosomal landscape of nucleosome-dependent gene expression and silencing in yeast. Nature 402, 418-421 (1999).
    • (1999) Nature , vol.402 , pp. 418-421
    • Wyrick, J.J.1
  • 26
    • 0036791764 scopus 로고    scopus 로고
    • Ku complex controls the replication time of DNA in telomere regions
    • Cosgrove, A. J., Nieduszynski, C. A. & Donaldson, A. D. Ku complex controls the replication time of DNA in telomere regions. Genes Dev. 16, 2485-2490 (2002).
    • (2002) Genes Dev , vol.16 , pp. 2485-2490
    • Cosgrove, A.J.1    Nieduszynski, C.A.2    Donaldson, A.D.3
  • 27
    • 33645739139 scopus 로고    scopus 로고
    • The Ctf18 RFC-like complex positions yeast telomeres but does not specify their replication time
    • Hiraga, S., Robertson, E. D. & Donaldson, A. D. The Ctf18 RFC-like complex positions yeast telomeres but does not specify their replication time. EMBO J. 25, 1505-1514 (2006).
    • (2006) EMBO J , vol.25 , pp. 1505-1514
    • Hiraga, S.1    Robertson, E.D.2    Donaldson, A.D.3
  • 28
    • 0031005357 scopus 로고    scopus 로고
    • Cell cycle-dependent establishment of a late replication program
    • Raghuraman, M. K., Brewer, B. J. & Fangman, W. L. Cell cycle-dependent establishment of a late replication program. Science 276, 806-809 (1997).
    • (1997) Science , vol.276 , pp. 806-809
    • Raghuraman, M.K.1    Brewer, B.J.2    Fangman, W.L.3
  • 29
    • 0034953576 scopus 로고    scopus 로고
    • DNA replication forks pause at silent origins near the HML locus in budding yeast
    • Wang, Y., Vujcic, M. & Kowalski, D. DNA replication forks pause at silent origins near the HML locus in budding yeast. Mol. Cell. Biol. 21, 4938-4948 (2001).
    • (2001) Mol. Cell. Biol , vol.21 , pp. 4938-4948
    • Wang, Y.1    Vujcic, M.2    Kowalski, D.3
  • 30
    • 4444227318 scopus 로고    scopus 로고
    • Asynchronous replication timing of telomeres at opposite arms of mammalian chromosomes
    • Zou, Y., Gryaznov, S. M., Shay, J. W., Wright, W. E. & Cornforth, M. N. Asynchronous replication timing of telomeres at opposite arms of mammalian chromosomes. Proc. Natl Acad. Sci. USA 101, 12928-12933 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 12928-12933
    • Zou, Y.1    Gryaznov, S.M.2    Shay, J.W.3    Wright, W.E.4    Cornforth, M.N.5
  • 31
    • 0038538374 scopus 로고    scopus 로고
    • Origin usage during Euplotes ribosomal DNA amplification
    • Tan, M., Jahn, C. L. & Price, C. M. Origin usage during Euplotes ribosomal DNA amplification. Eukaryot. Cell 2, 115-122 (2003).
    • (2003) Eukaryot. Cell , vol.2 , pp. 115-122
    • Tan, M.1    Jahn, C.L.2    Price, C.M.3
  • 32
    • 0033568014 scopus 로고    scopus 로고
    • Normal human telomeres are not late replicating
    • Wright, W. E., Tesmer, V. M., Liao, M. L. & Shay, J. W. Normal human telomeres are not late replicating. Exp. Cell Res. 251, 492-499 (1999).
    • (1999) Exp. Cell Res , vol.251 , pp. 492-499
    • Wright, W.E.1    Tesmer, V.M.2    Liao, M.L.3    Shay, J.W.4
  • 33
    • 0035842522 scopus 로고    scopus 로고
    • Replication timing of human telomeric DNA and other repetitive sequences analyzed by fluorescence in situ hybridization and flow cytometry
    • Hultdin, M. et al. Replication timing of human telomeric DNA and other repetitive sequences analyzed by fluorescence in situ hybridization and flow cytometry. Exp. Cell Res. 271, 223-229 (2001).
    • (2001) Exp. Cell Res , vol.271 , pp. 223-229
    • Hultdin, M.1
  • 35
    • 0033564210 scopus 로고    scopus 로고
    • Progressive cis- inhibition of telomerase upon telomere elongation
    • Marcand, S., Brevet, V. & Gilson, E. Progressive cis- inhibition of telomerase upon telomere elongation. EMBO J. 18, 3509-3519 (1999).
    • (1999) EMBO J , vol.18 , pp. 3509-3519
    • Marcand, S.1    Brevet, V.2    Gilson, E.3
  • 36
    • 2042534735 scopus 로고    scopus 로고
    • Teixeira, M. T., Arneric, M., Sperisen, P. & Lingner, J. Telomere length homeostasis is achieved via a switch between telomerase-extendible and -nonextendible states. Cell 117, 323-335 (2004). Shows that telomerase does not act on every telomere in each cell cycle and that it exhibits a preference for short telomeres.
    • Teixeira, M. T., Arneric, M., Sperisen, P. & Lingner, J. Telomere length homeostasis is achieved via a switch between telomerase-extendible and -nonextendible states. Cell 117, 323-335 (2004). Shows that telomerase does not act on every telomere in each cell cycle and that it exhibits a preference for short telomeres.
  • 37
    • 33947308706 scopus 로고    scopus 로고
    • Early replication of short telomeres in budding yeast
    • Bianchi, A. & Shore, D. Early replication of short telomeres in budding yeast. Cell 128, 1051-1062 (2007).
    • (2007) Cell , vol.128 , pp. 1051-1062
    • Bianchi, A.1    Shore, D.2
  • 38
    • 0032497548 scopus 로고    scopus 로고
    • Regulation of DNA-replication origins during cell-cycle progression
    • Shirahige, K. et al. Regulation of DNA-replication origins during cell-cycle progression. Nature 395, 618-621 (1998).
    • (1998) Nature , vol.395 , pp. 618-621
    • Shirahige, K.1
  • 39
    • 0032497529 scopus 로고    scopus 로고
    • Santocanale, C. & Diffley, J. F. A Mec1- and Rad53-dependent checkpoint controls late-firing origins of DNA replication. Nature 395, 615-618 (1998).
    • Santocanale, C. & Diffley, J. F. A Mec1- and Rad53-dependent checkpoint controls late-firing origins of DNA replication. Nature 395, 615-618 (1998).
  • 40
    • 33645152790 scopus 로고    scopus 로고
    • Genomic mapping of single-stranded DNA in hydroxyurea-challenged yeasts identifies origins of replication
    • Feng, W. et al. Genomic mapping of single-stranded DNA in hydroxyurea-challenged yeasts identifies origins of replication. Nature Cell Biol. 8, 148-155 (2006).
    • (2006) Nature Cell Biol , vol.8 , pp. 148-155
    • Feng, W.1
  • 41
    • 0033870408 scopus 로고    scopus 로고
    • Checkpoint proteins influence telomeric silencing and length maintenance in budding yeast
    • Longhese, M. P., Paciotti, V., Neecke, H. & Lucchini, G. Checkpoint proteins influence telomeric silencing and length maintenance in budding yeast. Genetics 155, 1577-1591 (2000).
    • (2000) Genetics , vol.155 , pp. 1577-1591
    • Longhese, M.P.1    Paciotti, V.2    Neecke, H.3    Lucchini, G.4
  • 42
    • 10344256183 scopus 로고    scopus 로고
    • Crabbe, L., Verdun, R. E., Haggblom, C. I. & Karlseder, J. Defective telomere lagging strand synthesis in cells lacking WRN helicase activity. Science 306, 1951-1953 (2004). Reports that cells that lack WRN show deletion of telomeres that were replicated by lagging-strand synthesis, suggesting that WRN is necessary for the efficient replication of G-rich telomeric DNA.
    • Crabbe, L., Verdun, R. E., Haggblom, C. I. & Karlseder, J. Defective telomere lagging strand synthesis in cells lacking WRN helicase activity. Science 306, 1951-1953 (2004). Reports that cells that lack WRN show deletion of telomeres that were replicated by lagging-strand synthesis, suggesting that WRN is necessary for the efficient replication of G-rich telomeric DNA.
  • 43
    • 0041324850 scopus 로고    scopus 로고
    • Telomere instability in a human tumor cell line expressing a dominant-negative WRN protein
    • Bai, Y. & Murnane, J. P. Telomere instability in a human tumor cell line expressing a dominant-negative WRN protein. Hum. Genet. 113, 337-347 (2003).
    • (2003) Hum. Genet , vol.113 , pp. 337-347
    • Bai, Y.1    Murnane, J.P.2
  • 44
    • 0035880025 scopus 로고    scopus 로고
    • Unwinding the molecular basis of the Werner syndrome
    • Shen, J. & Loeb, L. A. Unwinding the molecular basis of the Werner syndrome. Mech. Ageing Dev. 122, 921-944 (2001).
    • (2001) Mech. Ageing Dev , vol.122 , pp. 921-944
    • Shen, J.1    Loeb, L.A.2
  • 45
    • 4544301617 scopus 로고    scopus 로고
    • Telomere shortening exposes functions for the mouse Werner and Bloom syndrome genes
    • Du, X. et al. Telomere shortening exposes functions for the mouse Werner and Bloom syndrome genes. Mol. Cell. Biol. 24, 8437-8446 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 8437-8446
    • Du, X.1
  • 46
    • 3543043128 scopus 로고    scopus 로고
    • Essential role of limiting telomeres in the pathogenesis of Werner syndrome
    • Chang, S. et al. Essential role of limiting telomeres in the pathogenesis of Werner syndrome. Nature Genet. 36, 877-882 (2004).
    • (2004) Nature Genet , vol.36 , pp. 877-882
    • Chang, S.1
  • 47
    • 33749991551 scopus 로고    scopus 로고
    • Unexpected twist: Harnessing the energy in positive supercoils to control telomere resolution
    • Bankhead, T., Kobryn, K. & Chaconas, G. Unexpected twist: harnessing the energy in positive supercoils to control telomere resolution. Mol. Microbiol. 62, 895-905 (2006).
    • (2006) Mol. Microbiol , vol.62 , pp. 895-905
    • Bankhead, T.1    Kobryn, K.2    Chaconas, G.3
  • 48
    • 0036792653 scopus 로고    scopus 로고
    • To fire or not to fire: Origin activation in Saccharomyces cerevisiae ribosomal DNA
    • Ivessa, A. S. & Zakian, V. A. To fire or not to fire: origin activation in Saccharomyces cerevisiae ribosomal DNA. Genes Dev. 16, 2459-2464 (2002).
    • (2002) Genes Dev , vol.16 , pp. 2459-2464
    • Ivessa, A.S.1    Zakian, V.A.2
  • 49
    • 33751237066 scopus 로고    scopus 로고
    • Azvolinsky, A., Dunaway, S., Torres, J. Z., Bessler, J. B. & Zakian, V. A. The S. cerevisiae Rrm3p DNA helicase moves with the replication fork and affects replication of all yeast chromosomes. Genes Dev. 20, 3104-3116 (2006).
    • Azvolinsky, A., Dunaway, S., Torres, J. Z., Bessler, J. B. & Zakian, V. A. The S. cerevisiae Rrm3p DNA helicase moves with the replication fork and affects replication of all yeast chromosomes. Genes Dev. 20, 3104-3116 (2006).
  • 50
    • 33845335815 scopus 로고    scopus 로고
    • Suppression of spontaneous genome rearrangements in yeast DNA helicase mutants
    • Schmidt, K. H. & Kolodner, R. D. Suppression of spontaneous genome rearrangements in yeast DNA helicase mutants. Proc. Natl Acad. Sci. USA 103, 18196-18201 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 18196-18201
    • Schmidt, K.H.1    Kolodner, R.D.2
  • 51
    • 2942637828 scopus 로고    scopus 로고
    • The Werner syndrome helicase and exonuclease cooperate to resolve telomeric D loops in a manner regulated by TRF1 and TRF2
    • Opresko, P. L. et al. The Werner syndrome helicase and exonuclease cooperate to resolve telomeric D loops in a manner regulated by TRF1 and TRF2. Mol. Cell 14, 763-74 (2004).
    • (2004) Mol. Cell , vol.14 , pp. 763-774
    • Opresko, P.L.1
  • 52
    • 0031000884 scopus 로고    scopus 로고
    • Long G tails at both ends of human chromosomes suggest a C strand degradation mechanism for telomere shortening
    • Makarov, V. L., Hirose, Y. & Langmore, J. P. Long G tails at both ends of human chromosomes suggest a C strand degradation mechanism for telomere shortening. Cell 88, 657-666 (1997).
    • (1997) Cell , vol.88 , pp. 657-666
    • Makarov, V.L.1    Hirose, Y.2    Langmore, J.P.3
  • 53
    • 0030460748 scopus 로고    scopus 로고
    • Dionne, I. & Wellinger, R. J. Cell cycle-regulated generation of single-stranded G-rich DNA in the absence of telomerase. Proc. Natl Acad. Sci. USA 93, 13902-13907 (1996).
    • Dionne, I. & Wellinger, R. J. Cell cycle-regulated generation of single-stranded G-rich DNA in the absence of telomerase. Proc. Natl Acad. Sci. USA 93, 13902-13907 (1996).
  • 54
    • 0019568388 scopus 로고
    • All gene-sized DNA molecules in four species of hypotrichs have the same terminal sequence and an unusual 3′ terminus
    • Klobutcher, L. A., Swanton, M. T., Donini, P. & Prescott, D. M. All gene-sized DNA molecules in four species of hypotrichs have the same terminal sequence and an unusual 3′ terminus. Proc. Natl Acad. Sci. USA 78, 3015-3019 (1981).
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 3015-3019
    • Klobutcher, L.A.1    Swanton, M.T.2    Donini, P.3    Prescott, D.M.4
  • 55
    • 2942644725 scopus 로고    scopus 로고
    • Larrivee, M., LeBel, C. & Wellinger, R. J. The generation of proper constitutive G-tails on yeast telomeres is dependent on the MRX complex. Genes Dev. 18, 1391-1396 (2004). Demonstrates that G-tails are present outside S phase on normal yeast telomeres, and that Mre11 is essential to form this constitutive end structure.
    • Larrivee, M., LeBel, C. & Wellinger, R. J. The generation of proper constitutive G-tails on yeast telomeres is dependent on the MRX complex. Genes Dev. 18, 1391-1396 (2004). Demonstrates that G-tails are present outside S phase on normal yeast telomeres, and that Mre11 is essential to form this constitutive end structure.
  • 56
    • 31544466516 scopus 로고    scopus 로고
    • Chai, W., Du, Q., Shay, J. W. & Wright, W. E. Human telomeres have different overhang sizes at leading versus lagging strands. Mol. Cell 21, 427-435 (2006). Shows that human diploid cells have longer G overhangs at telomeres generated by lagging-strand synthesis than by leading-strand synthesis, which suggests that leading and lagging daughter telomeres are generated differently.
    • Chai, W., Du, Q., Shay, J. W. & Wright, W. E. Human telomeres have different overhang sizes at leading versus lagging strands. Mol. Cell 21, 427-435 (2006). Shows that human diploid cells have longer G overhangs at telomeres generated by lagging-strand synthesis than by leading-strand synthesis, which suggests that leading and lagging daughter telomeres are generated differently.
  • 57
    • 0032403147 scopus 로고    scopus 로고
    • Processing of telomeric DNA ends requires the passage of a replication fork
    • Dionne, I. & Wellinger, R. J. Processing of telomeric DNA ends requires the passage of a replication fork. Nucleic Acids Res. 26, 5365-5371 (1998).
    • (1998) Nucleic Acids Res , vol.26 , pp. 5365-5371
    • Dionne, I.1    Wellinger, R.J.2
  • 58
    • 0033569847 scopus 로고    scopus 로고
    • G-strand overhangs on telomeres in telomerase-deficient mouse cells
    • Hemann, M. T. & Greider, C. W. G-strand overhangs on telomeres in telomerase-deficient mouse cells. Nucleic Acids Res. 27, 3964-3969 (1999).
    • (1999) Nucleic Acids Res , vol.27 , pp. 3964-3969
    • Hemann, M.T.1    Greider, C.W.2
  • 59
    • 0034899458 scopus 로고    scopus 로고
    • In vitro reconstitution of the end replication problem
    • Ohki, R., Tsurimoto, T. & Ishikawa, F. In vitro reconstitution of the end replication problem. Mol. Cell. Biol. 21, 5753-5766 (2001).
    • (2001) Mol. Cell. Biol , vol.21 , pp. 5753-5766
    • Ohki, R.1    Tsurimoto, T.2    Ishikawa, F.3
  • 60
    • 7244220162 scopus 로고    scopus 로고
    • DNA end resection, homologous recombination and DNA damage checkpoint activation require CDK1
    • Ira, G. et al. DNA end resection, homologous recombination and DNA damage checkpoint activation require CDK1. Nature 431, 1011-1017 (2004).
    • (2004) Nature , vol.431 , pp. 1011-1017
    • Ira, G.1
  • 61
    • 33750431337 scopus 로고    scopus 로고
    • Regulation of telomere elongation by the cyclin-dependent kinase CDK1
    • Frank, C. J., Hyde, M. & Greider, C. W. Regulation of telomere elongation by the cyclin-dependent kinase CDK1. Mol. Cell 24, 423-432 (2006).
    • (2006) Mol. Cell , vol.24 , pp. 423-432
    • Frank, C.J.1    Hyde, M.2    Greider, C.W.3
  • 62
    • 33749059184 scopus 로고    scopus 로고
    • Vodenicharov, M. D. & Wellinger, R. J. DNA degradation at unprotected telomeres in yeast is regulated by the CDK1 (Cdc28/Clb) cell-cycle kinase. Mol. Cell 24, 127-137 (2006). References 61 and 62 report evidence that cyclin-dependent kinase Cdk1/Cdc28 activity is required for the generation of 3′ single-strand overhangs at telomeres in S. cerevisiae.
    • Vodenicharov, M. D. & Wellinger, R. J. DNA degradation at unprotected telomeres in yeast is regulated by the CDK1 (Cdc28/Clb) cell-cycle kinase. Mol. Cell 24, 127-137 (2006). References 61 and 62 report evidence that cyclin-dependent kinase Cdk1/Cdc28 activity is required for the generation of 3′ single-strand overhangs at telomeres in S. cerevisiae.
  • 63
    • 33846970933 scopus 로고    scopus 로고
    • DNA breaks are masked by multiple Rap1 binding in yeast: Implications for telomere capping and telomerase regulation
    • Negrini, S., Ribaud, V., Bianchi, A. & Shore, D. DNA breaks are masked by multiple Rap1 binding in yeast: implications for telomere capping and telomerase regulation. Genes Dev. 21, 292-302 (2007).
    • (2007) Genes Dev , vol.21 , pp. 292-302
    • Negrini, S.1    Ribaud, V.2    Bianchi, A.3    Shore, D.4
  • 64
    • 13944265075 scopus 로고    scopus 로고
    • Late S phasespecific recruitment of Mre11 complex triggers hierarchical assembly of telomere replication proteins in Saccharomyces cerevisiae
    • Takata, H., Tanaka, Y. & Matsuura, A. Late S phasespecific recruitment of Mre11 complex triggers hierarchical assembly of telomere replication proteins in Saccharomyces cerevisiae. Mol. Cell 17, 573-583 (2005).
    • (2005) Mol. Cell , vol.17 , pp. 573-583
    • Takata, H.1    Tanaka, Y.2    Matsuura, A.3
  • 65
    • 33745652501 scopus 로고    scopus 로고
    • Apollo, an Artemis-related nuclease, interacts with TRF2 and protects human telomeres in S phase
    • van Overbeek, M. & de Lange, T. Apollo, an Artemis-related nuclease, interacts with TRF2 and protects human telomeres in S phase. Curr. Biol. 16, 1295-1302 (2006).
    • (2006) Curr. Biol , vol.16 , pp. 1295-1302
    • van Overbeek, M.1    de Lange, T.2
  • 66
    • 33745651993 scopus 로고    scopus 로고
    • The Apollo 5′ exonuclease functions together with TRF2 to protect telomeres from DNA repair
    • Lenain, C. et al. The Apollo 5′ exonuclease functions together with TRF2 to protect telomeres from DNA repair. Curr. Biol. 16, 1303-1310 (2006).
    • (2006) Curr. Biol , vol.16 , pp. 1303-1310
    • Lenain, C.1
  • 67
    • 0032974345 scopus 로고    scopus 로고
    • Accumulation of single-stranded DNA and destabilization of telomeric repeats in yeast mutant strains carrying a deletion of RAD27
    • Parenteau, J. & Wellinger, R. J. Accumulation of single-stranded DNA and destabilization of telomeric repeats in yeast mutant strains carrying a deletion of RAD27. Mol. Cell. Biol. 19, 4143-4152 (1999).
    • (1999) Mol. Cell. Biol , vol.19 , pp. 4143-4152
    • Parenteau, J.1    Wellinger, R.J.2
  • 68
    • 0033982575 scopus 로고    scopus 로고
    • The function of DNA polymerase α at telomeric G tails is important for telomere homeostasis
    • Adams Martin, A., Dionne, I., Wellinger, R. J. & Holm, C. The function of DNA polymerase α at telomeric G tails is important for telomere homeostasis. Mol. Cell. Biol. 20, 786-796 (2000).
    • (2000) Mol. Cell. Biol , vol.20 , pp. 786-796
    • Adams Martin, A.1    Dionne, I.2    Wellinger, R.J.3    Holm, C.4
  • 69
    • 6344284126 scopus 로고    scopus 로고
    • Fission yeast Dna2 is required for generation of the telomeric single-strand overhang
    • Tomita, K. et al. Fission yeast Dna2 is required for generation of the telomeric single-strand overhang. Mol. Cell. Biol. 24, 9557-9567 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 9557-9567
    • Tomita, K.1
  • 71
    • 0034661246 scopus 로고
    • The Saccharomyces telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase α and the telomerase-associated est1 protein
    • 88
    • Qi, H. & Zakian, V. A. The Saccharomyces telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase α and the telomerase-associated est1 protein. Genes Dev. 14, 1777-88 (2000).
    • (1777) Genes Dev , vol.14
    • Qi, H.1    Zakian, V.A.2
  • 72
    • 2442564703 scopus 로고    scopus 로고
    • Pol12, the B subunit of DNA polymerase α, functions in both telomere capping and length regulation
    • Grossi, S., Puglisi, A., Dmitriev, P. V., Lopes, M. & Shore, D. Pol12, the B subunit of DNA polymerase α, functions in both telomere capping and length regulation. Genes Dev. 18, 992-1006 (2004).
    • (2004) Genes Dev , vol.18 , pp. 992-1006
    • Grossi, S.1    Puglisi, A.2    Dmitriev, P.V.3    Lopes, M.4    Shore, D.5
  • 73
    • 0022387528 scopus 로고
    • CDC17: An essential gene that prevents telomere elongation in yeast
    • Carson, M. J. & Hartwell, L. CDC17: an essential gene that prevents telomere elongation in yeast. Cell 42, 249-257 (1985).
    • (1985) Cell , vol.42 , pp. 249-257
    • Carson, M.J.1    Hartwell, L.2
  • 75
    • 0141868298 scopus 로고    scopus 로고
    • The Ku heterodimer performs separable activities at double-strand breaks and chromosome termini
    • Bertuch, A. A. & Lundblad, V. The Ku heterodimer performs separable activities at double-strand breaks and chromosome termini. Mol. Cell. Biol. 23, 8202-8215 (2003).
    • (2003) Mol. Cell. Biol , vol.23 , pp. 8202-8215
    • Bertuch, A.A.1    Lundblad, V.2
  • 76
    • 33748656958 scopus 로고    scopus 로고
    • Vertebrate POT1 restricts G-overhang length and prevents activation of a telomeric DNA damage checkpoint but is dispensable for overhang protection
    • Churikov, D., Wei, C. & Price, C. M. Vertebrate POT1 restricts G-overhang length and prevents activation of a telomeric DNA damage checkpoint but is dispensable for overhang protection. Mol. Cell. Biol. 26, 6971-6982 (2006).
    • (2006) Mol. Cell. Biol , vol.26 , pp. 6971-6982
    • Churikov, D.1    Wei, C.2    Price, C.M.3
  • 77
    • 33745699389 scopus 로고    scopus 로고
    • Are mouse telomeres going to pot?
    • Baumann, P. Are mouse telomeres going to pot? Cell 126, 33-36 (2006).
    • (2006) Cell , vol.126 , pp. 33-36
    • Baumann, P.1
  • 78
    • 0347416975 scopus 로고    scopus 로고
    • ERCC1/XPF removes the 3′ overhang from uncapped telomeres and represses formation of telomeric DNA-containing double minute chromosomes
    • Zhu, X. D. et al. ERCC1/XPF removes the 3′ overhang from uncapped telomeres and represses formation of telomeric DNA-containing double minute chromosomes. Mol. Cell 12, 1489-1498 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 1489-1498
    • Zhu, X.D.1
  • 79
    • 22144490491 scopus 로고    scopus 로고
    • DNA processing is not required for ATM-mediated telomere damage response after TRF2 deletion
    • Celli, G. B. & de Lange, T. DNA processing is not required for ATM-mediated telomere damage response after TRF2 deletion. Nature Cell Biol. 7, 712-718 (2005).
    • (2005) Nature Cell Biol , vol.7 , pp. 712-718
    • Celli, G.B.1    de Lange, T.2
  • 80
    • 33644633822 scopus 로고    scopus 로고
    • Lagging strand replication proteins in genome stability and DNA repair
    • Rossi, M. L., Purohit, V., Brandt, P. D. & Bambara, R. A. Lagging strand replication proteins in genome stability and DNA repair. Chem. Rev. 106, 453-473 (2006).
    • (2006) Chem. Rev , vol.106 , pp. 453-473
    • Rossi, M.L.1    Purohit, V.2    Brandt, P.D.3    Bambara, R.A.4
  • 81
    • 33645215616 scopus 로고    scopus 로고
    • Evidence suggesting that Pif1 helicase functions in DNA replication with the Dna2 helicase/nuclease and DNA polymerase δ
    • Budd, M. E., Reis, C. C., Smith, S., Myung, K. & Campbell, J. L. Evidence suggesting that Pif1 helicase functions in DNA replication with the Dna2 helicase/nuclease and DNA polymerase δ. Mol. Cell. Biol. 26, 2490-2500 (2006).
    • (2006) Mol. Cell. Biol , vol.26 , pp. 2490-2500
    • Budd, M.E.1    Reis, C.C.2    Smith, S.3    Myung, K.4    Campbell, J.L.5
  • 82
    • 0033512305 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae RNase H(35) functions in RNA primer removal during lagging-strand DNA synthesis, most efficiently in cooperation with Rad27 nuclease
    • Qiu, J., Qian, Y., Frank, P., Wintersberger, U. & Shen, B. Saccharomyces cerevisiae RNase H(35) functions in RNA primer removal during lagging-strand DNA synthesis, most efficiently in cooperation with Rad27 nuclease. Mol. Cell. Biol. 19, 8361-8371 (1999).
    • (1999) Mol. Cell. Biol , vol.19 , pp. 8361-8371
    • Qiu, J.1    Qian, Y.2    Frank, P.3    Wintersberger, U.4    Shen, B.5
  • 84
    • 0030999605 scopus 로고    scopus 로고
    • Reveal, P. M., Henkels, K. M. & Turchi, J. J. Synthesis of the mammalian telomere lagging strand in vitro. J. Biol. Chem. 272, 11678-11681 (1997).
    • Reveal, P. M., Henkels, K. M. & Turchi, J. J. Synthesis of the mammalian telomere lagging strand in vitro. J. Biol. Chem. 272, 11678-11681 (1997).
  • 85
    • 0030807761 scopus 로고    scopus 로고
    • Coordinate regulation of G- and C strand length during new telomere synthesis
    • Fan, X. & Price, C. M. Coordinate regulation of G- and C strand length during new telomere synthesis. Mol. Biol. Cell 8, 2145-2155 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2145-2155
    • Fan, X.1    Price, C.M.2
  • 86
    • 0037623348 scopus 로고    scopus 로고
    • Generation of telomeric G strand overhangs involves both G and C strand cleavage
    • Jacob, N. K., Kirk, K. E. & Price, C. M. Generation of telomeric G strand overhangs involves both G and C strand cleavage. Mol. Cell 11, 1021-1032 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 1021-1032
    • Jacob, N.K.1    Kirk, K.E.2    Price, C.M.3
  • 87
    • 15944368044 scopus 로고    scopus 로고
    • Telomere-end processing the terminal nucleotides of human chromosomes
    • Sfeir, A. J., Chai, W., Shay, J. W. & Wright, W. E. Telomere-end processing the terminal nucleotides of human chromosomes. Mol. Cell 18, 131-138 (2005).
    • (2005) Mol. Cell , vol.18 , pp. 131-138
    • Sfeir, A.J.1    Chai, W.2    Shay, J.W.3    Wright, W.E.4
  • 88
    • 23044500389 scopus 로고    scopus 로고
    • POT1 protects telomeres from a transient DNA damage response and determines how human chromosomes end
    • Hockemeyer, D., Sfeir, A. J., Shay, J. W., Wright, W. E. & de Lange, T. POT1 protects telomeres from a transient DNA damage response and determines how human chromosomes end. EMBO J. 24, 2667-2678 (2005).
    • (2005) EMBO J , vol.24 , pp. 2667-2678
    • Hockemeyer, D.1    Sfeir, A.J.2    Shay, J.W.3    Wright, W.E.4    de Lange, T.5
  • 89
    • 0035476710 scopus 로고    scopus 로고
    • T-loop assembly in vitro involves binding of TRF2 near the 3′ telomeric overhang
    • Stansel, R. M., de Lange, T. & Griffith, J. D. T-loop assembly in vitro involves binding of TRF2 near the 3′ telomeric overhang. EMBO J. 20, 5532-5540 (2001).
    • (2001) EMBO J , vol.20 , pp. 5532-5540
    • Stansel, R.M.1    de Lange, T.2    Griffith, J.D.3
  • 90
    • 33845987076 scopus 로고    scopus 로고
    • The basic domain of TRF2 directs binding to DNA junctions irrespective of the presence of TTAGGG repeats
    • Fouche, N. et al. The basic domain of TRF2 directs binding to DNA junctions irrespective of the presence of TTAGGG repeats. J. Biol. Chem. 281, 37486-37495 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 37486-37495
    • Fouche, N.1
  • 91
    • 0035964864 scopus 로고    scopus 로고
    • Strand-specific postreplicative processing of mammalian telomeres
    • Bailey, S. M., Cornforth, M. N., Kurimasa, A., Chen, D. J. & Goodwin, E. H. Strand-specific postreplicative processing of mammalian telomeres. Science 293, 2462-2465 (2001).
    • (2001) Science , vol.293 , pp. 2462-2465
    • Bailey, S.M.1    Cornforth, M.N.2    Kurimasa, A.3    Chen, D.J.4    Goodwin, E.H.5
  • 92
    • 7044232011 scopus 로고    scopus 로고
    • Homologous recombination generates T-loop-sized deletions at human telomeres
    • Wang, R. C., Smogorzewska, A. & de Lange, T. Homologous recombination generates T-loop-sized deletions at human telomeres. Cell 119, 355-368 (2004).
    • (2004) Cell , vol.119 , pp. 355-368
    • Wang, R.C.1    Smogorzewska, A.2    de Lange, T.3
  • 93
    • 0029820640 scopus 로고    scopus 로고
    • The clustering of telomeres and colocalization with Rap1, Sir3, and Sir4 proteins in wild-type Saccharomyces cerevisiae
    • Gotta, M. et al. The clustering of telomeres and colocalization with Rap1, Sir3, and Sir4 proteins in wild-type Saccharomyces cerevisiae. J. Cell Biol. 134, 1349-1363 (1996).
    • (1996) J. Cell Biol , vol.134 , pp. 1349-1363
    • Gotta, M.1
  • 94
    • 0035824395 scopus 로고    scopus 로고
    • Chromosome dynamics in the yeast interphase nucleus
    • Heun, P., Laroche, T., Shimada, K., Furrer, P. & Gasser, S. M. Chromosome dynamics in the yeast interphase nucleus. Science 294, 2181-2186 (2001).
    • (2001) Science , vol.294 , pp. 2181-2186
    • Heun, P.1    Laroche, T.2    Shimada, K.3    Furrer, P.4    Gasser, S.M.5
  • 95
    • 0034175814 scopus 로고    scopus 로고
    • Marcand, S., Brevet, V., Mann, C. & Gilson, E. Cell cycle restriction of telomere elongation. Curr. Biol. 10, 487-490 (2000). Shows that in budding yeast cells that progress synchronously through the cell cycle, telomere elongation coincides with the time of telomere replication.
    • Marcand, S., Brevet, V., Mann, C. & Gilson, E. Cell cycle restriction of telomere elongation. Curr. Biol. 10, 487-490 (2000). Shows that in budding yeast cells that progress synchronously through the cell cycle, telomere elongation coincides with the time of telomere replication.
  • 96
    • 0033598944 scopus 로고    scopus 로고
    • Diede, S. J. & Gottschling, D. E. Telomerase-mediated telomere addition in vivo requires DNA primase and DNA polymerases α and δ. Cell 99, 723-733 (1999). Shows that the essential DNA polymerase-α and -δ and DNA primase are required for telomerase function, indicating that telomeric DNA synthesis by telomerase is tightly coregulated with the production of the opposite strand.
    • Diede, S. J. & Gottschling, D. E. Telomerase-mediated telomere addition in vivo requires DNA primase and DNA polymerases α and δ. Cell 99, 723-733 (1999). Shows that the essential DNA polymerase-α and -δ and DNA primase are required for telomerase function, indicating that telomeric DNA synthesis by telomerase is tightly coregulated with the production of the opposite strand.
  • 97
    • 0037047643 scopus 로고    scopus 로고
    • Taggart, A. K., Teng, S. C. & Zakian, V. A. Est1p as a cell cycle-regulated activator of telomere-bound telomerase. Science 297, 1023-1026 (2002). This study correlates the timing of telomere elongation in budding yeast with the binding at the telomeres of several proteins that are involved in telomere elongation, including the telomerase holoenzyme.
    • Taggart, A. K., Teng, S. C. & Zakian, V. A. Est1p as a cell cycle-regulated activator of telomere-bound telomerase. Science 297, 1023-1026 (2002). This study correlates the timing of telomere elongation in budding yeast with the binding at the telomeres of several proteins that are involved in telomere elongation, including the telomerase holoenzyme.
  • 98
    • 0347988057 scopus 로고    scopus 로고
    • Schramke, V. et al. RPA regulates telomerase action by providing Est1p access to chromosome ends. Nature Genet. 36, 46-54 (2004). Shows that in budding yeast, RPA binds to telomeres at the end of S phase and is required for telomerase action.
    • Schramke, V. et al. RPA regulates telomerase action by providing Est1p access to chromosome ends. Nature Genet. 36, 46-54 (2004). Shows that in budding yeast, RPA binds to telomeres at the end of S phase and is required for telomerase action.
  • 99
    • 4944265507 scopus 로고    scopus 로고
    • Delivery of yeast telomerase to a DNA break depends on the recruitment functions of Cdc13 and Est1
    • Bianchi, A., Negrini, S. & Shore, D. Delivery of yeast telomerase to a DNA break depends on the recruitment functions of Cdc13 and Est1. Mol. Cell 16, 139-146 (2004).
    • (2004) Mol. Cell , vol.16 , pp. 139-146
    • Bianchi, A.1    Negrini, S.2    Shore, D.3
  • 100
    • 33746850081 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of Est1p regulates the cell cycle-restricted assembly of telomerase in Saccharomyces cerevisiae
    • Osterhage, J. L., Talley, J. M. & Friedman, K. L. Proteasome-dependent degradation of Est1p regulates the cell cycle-restricted assembly of telomerase in Saccharomyces cerevisiae. Nature Struct. Mol. Biol. 13, 720-728 (2006).
    • (2006) Nature Struct. Mol. Biol , vol.13 , pp. 720-728
    • Osterhage, J.L.1    Talley, J.M.2    Friedman, K.L.3
  • 101
    • 34547813672 scopus 로고    scopus 로고
    • Goudsouzian, L. K., Tuzon, C. T. & Zakian, V. A. S. cerevisiae Tel1p and Mre11p are required for normal levels of Est1p and Est2p telomere association. Mol. Cell 24, 603-610 (2006).
    • Goudsouzian, L. K., Tuzon, C. T. & Zakian, V. A. S. cerevisiae Tel1p and Mre11p are required for normal levels of Est1p and Est2p telomere association. Mol. Cell 24, 603-610 (2006).
  • 102
    • 0141525391 scopus 로고    scopus 로고
    • Ku interacts with telomerase RNA to promote telomere addition at native and broken chromosome ends
    • Stellwagen, A. E., Haimberger, Z. W., Veatch, J. R. & Gottschling, D. E. Ku interacts with telomerase RNA to promote telomere addition at native and broken chromosome ends. Genes Dev. 17, 2384-2395 (2003).
    • (2003) Genes Dev , vol.17 , pp. 2384-2395
    • Stellwagen, A.E.1    Haimberger, Z.W.2    Veatch, J.R.3    Gottschling, D.E.4
  • 103
    • 16544390953 scopus 로고    scopus 로고
    • Cell cycle-dependent regulation of yeast telomerase by Ku
    • Fisher, T. S., Taggart, A. K. & Zakian, V. A. Cell cycle-dependent regulation of yeast telomerase by Ku. Nature Struct. Mol. Biol. 11, 1198-1205 (2004).
    • (2004) Nature Struct. Mol. Biol , vol.11 , pp. 1198-1205
    • Fisher, T.S.1    Taggart, A.K.2    Zakian, V.A.3
  • 104
    • 0033214013 scopus 로고    scopus 로고
    • Est1 and Cdc13 as comediators of telomerase access
    • Evans, S. K. & Lundblad, V. Est1 and Cdc13 as comediators of telomerase access. Science 286, 117-120 (1999).
    • (1999) Science , vol.286 , pp. 117-120
    • Evans, S.K.1    Lundblad, V.2
  • 105
    • 0029845892 scopus 로고    scopus 로고
    • Cdc13p: A single-strand telomeric DNA-binding protein with a dual role in yeast telomere maintenance
    • Nugent, C. I., Hughes, T. R., Lue, N. F. & Lundblad, V. Cdc13p: a single-strand telomeric DNA-binding protein with a dual role in yeast telomere maintenance. Science 274, 249-252 (1996).
    • (1996) Science , vol.274 , pp. 249-252
    • Nugent, C.I.1    Hughes, T.R.2    Lue, N.F.3    Lundblad, V.4
  • 106
    • 0035830494 scopus 로고    scopus 로고
    • Cdc13 delivers separate complexes to the telomere for end protection and replication
    • Pennock, E., Buckley, K. & Lundblad, V. Cdc13 delivers separate complexes to the telomere for end protection and replication. Cell 104, 387-396 (2001).
    • (2001) Cell , vol.104 , pp. 387-396
    • Pennock, E.1    Buckley, K.2    Lundblad, V.3
  • 107
    • 0033766666 scopus 로고    scopus 로고
    • Cdc13 cooperates with the yeast Ku proteins and Stn1 to regulate telomerase recruitment
    • Grandin, N., Damon, C. & Charbonneau, M. Cdc13 cooperates with the yeast Ku proteins and Stn1 to regulate telomerase recruitment. Mol. Cell. Biol. 20, 8397-8408 (2000).
    • (2000) Mol. Cell. Biol , vol.20 , pp. 8397-8408
    • Grandin, N.1    Damon, C.2    Charbonneau, M.3
  • 108
    • 0033539171 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle
    • Seto, A. G., Zaug, A. J., Sobel, S. G., Wolin, S. L. & Cech, T. R. Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle. Nature 401, 177-180 (1999).
    • (1999) Nature , vol.401 , pp. 177-180
    • Seto, A.G.1    Zaug, A.J.2    Sobel, S.G.3    Wolin, S.L.4    Cech, T.R.5
  • 109
    • 0036828725 scopus 로고    scopus 로고
    • A bulged stem tethers Est1p to telomerase RNA in budding yeast
    • Seto, A. G., Livengood, A. J., Tzfati, Y., Blackburn, E. H. & Cech, T. R. A bulged stem tethers Est1p to telomerase RNA in budding yeast. Genes Dev. 16, 2800-2812 (2002).
    • (2002) Genes Dev , vol.16 , pp. 2800-2812
    • Seto, A.G.1    Livengood, A.J.2    Tzfati, Y.3    Blackburn, E.H.4    Cech, T.R.5
  • 110
    • 0035158605 scopus 로고    scopus 로고
    • The function of a stem-loop in telomerase RNA is linked to the DNA repair protein Ku
    • Peterson, S. E. et al. The function of a stem-loop in telomerase RNA is linked to the DNA repair protein Ku. Nature Genet. 27, 64-67 (2001).
    • (2001) Nature Genet , vol.27 , pp. 64-67
    • Peterson, S.E.1
  • 111
    • 3142532677 scopus 로고    scopus 로고
    • A phylogenetically based secondary structure for the yeast telomerase RNA
    • Dandjinou, A. T. et al. A phylogenetically based secondary structure for the yeast telomerase RNA. Curr. Biol. 14, 1148-1158 (2004).
    • (2004) Curr. Biol , vol.14 , pp. 1148-1158
    • Dandjinou, A.T.1
  • 112
    • 3042798454 scopus 로고    scopus 로고
    • Zappulla, D. C. & Cech, T. R. Yeast telomerase RNA: a flexible scaffold for protein subunits. Proc. Natl Acad. Sci. USA 101, 10024-10029 (2004). Based on the interactions of yeast telomerase RNA TLC1 with Est1, Ku and Sm proteins, this study proposes that TLC1 provides a flexible tether for these proteins.
    • Zappulla, D. C. & Cech, T. R. Yeast telomerase RNA: a flexible scaffold for protein subunits. Proc. Natl Acad. Sci. USA 101, 10024-10029 (2004). Based on the interactions of yeast telomerase RNA TLC1 with Est1, Ku and Sm proteins, this study proposes that TLC1 provides a flexible tether for these proteins.
  • 113
    • 28544450412 scopus 로고    scopus 로고
    • A miniature yeast telomerase RNA functions in vivo and reconstitutes activity in vitro
    • Zappulla, D. C., Goodrich, K. & Cech, T. R. A miniature yeast telomerase RNA functions in vivo and reconstitutes activity in vitro. Nature Struct. Mol. Biol. 12, 1072-1077 (2005).
    • (2005) Nature Struct. Mol. Biol , vol.12 , pp. 1072-1077
    • Zappulla, D.C.1    Goodrich, K.2    Cech, T.R.3
  • 115
    • 0035158136 scopus 로고    scopus 로고
    • Telomere formation by rap1p binding site arrays reveals end-specific length regulation requirements and active telomeric recombination
    • Grossi, S., Bianchi, A., Damay, P. & Shore, D. Telomere formation by rap1p binding site arrays reveals end-specific length regulation requirements and active telomeric recombination. Mol. Cell. Biol. 21, 8117-8128 (2001).
    • (2001) Mol. Cell. Biol , vol.21 , pp. 8117-8128
    • Grossi, S.1    Bianchi, A.2    Damay, P.3    Shore, D.4
  • 116
    • 27744445335 scopus 로고    scopus 로고
    • Boule, J. B., Vega, L. R. & Zakian, V. A. The yeast Pif1p helicase removes telomerase from telomeric DNA. Nature 438, 57-61 (2005). Suggests that Pif1 RNA/DNA helicase activity limits telomerase action by displacing active telomerase from DNA ends.
    • Boule, J. B., Vega, L. R. & Zakian, V. A. The yeast Pif1p helicase removes telomerase from telomeric DNA. Nature 438, 57-61 (2005). Suggests that Pif1 RNA/DNA helicase activity limits telomerase action by displacing active telomerase from DNA ends.
  • 117
    • 33746817406 scopus 로고    scopus 로고
    • The finger subdomain of yeast telomerase cooperates with Pif1p to limit telomere elongation
    • Eugster, A. et al. The finger subdomain of yeast telomerase cooperates with Pif1p to limit telomere elongation. Nature Struct. Mol. Biol. 13, 734-739 (2006).
    • (2006) Nature Struct. Mol. Biol , vol.13 , pp. 734-739
    • Eugster, A.1
  • 118
    • 0031036351 scopus 로고    scopus 로고
    • A protein-counting mechanism for telomere length regulation in yeast
    • Marcand, S., Gilson, E. & Shore, D. A protein-counting mechanism for telomere length regulation in yeast. Science 275, 986-990 (1997).
    • (1997) Science , vol.275 , pp. 986-990
    • Marcand, S.1    Gilson, E.2    Shore, D.3
  • 119
    • 0031686574 scopus 로고    scopus 로고
    • Circular chromosome formation in a fission yeast mutant defective in two ATM homologues
    • Naito, T., Matsuura, A. & Ishikawa, F. Circular chromosome formation in a fission yeast mutant defective in two ATM homologues. Nature Genet. 20, 203-206 (1998).
    • (1998) Nature Genet , vol.20 , pp. 203-206
    • Naito, T.1    Matsuura, A.2    Ishikawa, F.3
  • 120
    • 0035928740 scopus 로고    scopus 로고
    • Altering telomere structure allows telomerase to act in yeast lacking ATM kinases
    • Chan, S. W., Chang, J., Prescott, J. & Blackburn, E. H. Altering telomere structure allows telomerase to act in yeast lacking ATM kinases. Curr. Biol. 11, 1240-1250 (2001).
    • (2001) Curr. Biol , vol.11 , pp. 1240-1250
    • Chan, S.W.1    Chang, J.2    Prescott, J.3    Blackburn, E.H.4
  • 121
    • 0029088371 scopus 로고
    • TEL1, a gene involved in controlling telomere length in S. cerevisiae, is homologous to the human ataxia telangiectasia gene
    • Greenwell, P. W. et al. TEL1, a gene involved in controlling telomere length in S. cerevisiae, is homologous to the human ataxia telangiectasia gene. Cell 82, 823-829 (1995).
    • (1995) Cell , vol.82 , pp. 823-829
    • Greenwell, P.W.1
  • 122
    • 0041468535 scopus 로고    scopus 로고
    • Sudden telomere lengthening triggers a Rad53-dependent checkpoint in Saccharomyces cerevisiae
    • Viscardi, V., Baroni, E., Romano, M., Lucchini, G. & Longhese, M. P. Sudden telomere lengthening triggers a Rad53-dependent checkpoint in Saccharomyces cerevisiae. Mol. Biol. Cell 14, 3126-3143 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3126-3143
    • Viscardi, V.1    Baroni, E.2    Romano, M.3    Lucchini, G.4    Longhese, M.P.5
  • 123
    • 0036670615 scopus 로고    scopus 로고
    • Telomere binding of checkpoint sensor and DNA repair proteins contributes to maintenance of functional fission yeast telomeres
    • Nakamura, T. M., Moser, B. A. & Russell, P. Telomere binding of checkpoint sensor and DNA repair proteins contributes to maintenance of functional fission yeast telomeres. Genetics 161, 1437-1452 (2002).
    • (2002) Genetics , vol.161 , pp. 1437-1452
    • Nakamura, T.M.1    Moser, B.A.2    Russell, P.3
  • 124
    • 34547731434 scopus 로고    scopus 로고
    • Telomerase and Tel1p preferentially associate with short telomeres in S. cerevisiae
    • Sabourin, M., Tuzon, C.T. & Zakian, V.A. Telomerase and Tel1p preferentially associate with short telomeres in S. cerevisiae. Mol. Cell 27, 550-561 (2007).
    • (2007) Mol. Cell , vol.27 , pp. 550-561
    • Sabourin, M.1    Tuzon, C.T.2    Zakian, V.A.3
  • 125
    • 34447532519 scopus 로고    scopus 로고
    • Increased association of telomerase with short telomeres in yeast
    • Bianchi, A. & Shore, D. Increased association of telomerase with short telomeres in yeast. Genes Dev. 21, 1726-1730 (2007).
    • (2007) Genes Dev , vol.21 , pp. 1726-1730
    • Bianchi, A.1    Shore, D.2
  • 126
    • 34548269900 scopus 로고    scopus 로고
    • Tel1p preferentially associates with short telomeres to stimulate their elongation
    • in the press
    • Hector, R.E. et al. Tel1p preferentially associates with short telomeres to stimulate their elongation. Mol. Cell (in the press).
    • Mol. Cell
    • Hector, R.E.1
  • 127
    • 35748941663 scopus 로고    scopus 로고
    • Tel1p kinase and subtelomere bound Tbf1p mediate preferential elongation of short telomeres by telomerase in yeast. EMBO Rep
    • in the press
    • Arneriç, M. & Lingner, J. Tel1p kinase and subtelomere bound Tbf1p mediate preferential elongation of short telomeres by telomerase in yeast. EMBO Rep. (in the press).
    • Arneriç, M.1    Lingner, J.2
  • 128
    • 34948898465 scopus 로고    scopus 로고
    • Telomerase repeat addition processivity is increased at critically short telomeres in a Tel1-dependent manner in Saccharomyces cerevisiae
    • in the press
    • Chang, M., Arneric, M., & Lingner, J. Telomerase repeat addition processivity is increased at critically short telomeres in a Tel1-dependent manner in Saccharomyces cerevisiae. Genes Dev. (in the press).
    • Genes Dev
    • Chang, M.1    Arneric, M.2    Lingner, J.3
  • 129
    • 33644558048 scopus 로고    scopus 로고
    • Subtelomeric proteins negatively regulate telomere elongation in budding yeast
    • Berthiau, A. S. et al. Subtelomeric proteins negatively regulate telomere elongation in budding yeast. EMBO J. 25, 846-856 (2006).
    • (2006) EMBO J , vol.25 , pp. 846-856
    • Berthiau, A.S.1
  • 130
    • 33644530693 scopus 로고    scopus 로고
    • Subtelomeric factors antagonize telomere anchoring and Tel1-independent telomere length regulation
    • Hediger, F., Berthiau, A. S., van Houwe, G., Gilson, E. & Gasser, S. M. Subtelomeric factors antagonize telomere anchoring and Tel1-independent telomere length regulation. EMBO J. 25, 857-867 (2006).
    • (2006) EMBO J , vol.25 , pp. 857-867
    • Hediger, F.1    Berthiau, A.S.2    van Houwe, G.3    Gilson, E.4    Gasser, S.M.5
  • 131
    • 27144451010 scopus 로고    scopus 로고
    • Telomere end-binding proteins control the formation of G-quadruplex DNA structures in vivo
    • Paeschke, K., Simonsson, T., Postberg, J., Rhodes, D. & Lipps, H. J. Telomere end-binding proteins control the formation of G-quadruplex DNA structures in vivo. Nature Struct. Mol. Biol. 12, 847-854 (2005).
    • (2005) Nature Struct. Mol. Biol , vol.12 , pp. 847-854
    • Paeschke, K.1    Simonsson, T.2    Postberg, J.3    Rhodes, D.4    Lipps, H.J.5
  • 132
    • 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
    • Loayza, D., Parsons, H., Donigian, J., Hoke, K. & de Lange, T. 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, 13241-13248 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 13241-13248
    • Loayza, D.1    Parsons, H.2    Donigian, J.3    Hoke, K.4    de Lange, T.5
  • 133
    • 3142679378 scopus 로고    scopus 로고
    • POT1-interacting protein PIP1: A telomere length regulator that recruits POT1 to the TIN2/TRF1 complex
    • Ye, J. Z. et al. POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex. Genes Dev. 18, 1649-1654 (2004).
    • (2004) Genes Dev , vol.18 , pp. 1649-1654
    • Ye, J.Z.1
  • 134
    • 0038413786 scopus 로고    scopus 로고
    • Human POT1 facilitates telomere elongation by telomerase
    • Colgin, L. M., Baran, K., Baumann, P., Cech, T. R. & Reddel, R. R. Human POT1 facilitates telomere elongation by telomerase. Curr. Biol. 13, 942-946 (2003).
    • (2003) Curr. Biol , vol.13 , pp. 942-946
    • Colgin, L.M.1    Baran, K.2    Baumann, P.3    Cech, T.R.4    Reddel, R.R.5
  • 135
    • 1842557510 scopus 로고    scopus 로고
    • Rescue of an hTERT mutant defective in telomere elongation by fusion with hPot1
    • Armbruster, B. N. et al. Rescue of an hTERT mutant defective in telomere elongation by fusion with hPot1. Mol. Cell. Biol. 24, 3552-3561 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 3552-3561
    • Armbruster, B.N.1
  • 136
    • 11844280894 scopus 로고    scopus 로고
    • Human protection of telomeres 1 (POT1) is a negative regulator of telomerase activity in vitro
    • Kelleher, C., Kurth, I. & Lingner, J. Human protection of telomeres 1 (POT1) is a negative regulator of telomerase activity in vitro. Mol. Cell. Biol. 25, 808-818 (2005).
    • (2005) Mol. Cell. Biol , vol.25 , pp. 808-818
    • Kelleher, C.1    Kurth, I.2    Lingner, J.3
  • 137
    • 20144382152 scopus 로고    scopus 로고
    • Switching human telomerase on and off with hPOT1 protein in vitro
    • Lei, M., Zaug, A. J., Podell, E. R. & Cech, T. R. Switching human telomerase on and off with hPOT1 protein in vitro. J. Biol. Chem. 280, 20449-20456 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 20449-20456
    • Lei, M.1    Zaug, A.J.2    Podell, E.R.3    Cech, T.R.4
  • 138
    • 6344289975 scopus 로고    scopus 로고
    • TIN2 mediates functions of TRF2 at human telomeres
    • Kim, S. H. et al. TIN2 mediates functions of TRF2 at human telomeres. J. Biol. Chem. 279, 43799-43804 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 43799-43804
    • Kim, S.H.1
  • 139
    • 3242680818 scopus 로고    scopus 로고
    • PTOP interacts with POT1 and regulates its localization to telomeres
    • Liu, D. et al. PTOP interacts with POT1 and regulates its localization to telomeres. Nature Cell Biol. 6, 673-680 (2004).
    • (2004) Nature Cell Biol , vol.6 , pp. 673-680
    • Liu, D.1
  • 140
    • 6944232071 scopus 로고    scopus 로고
    • TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 complex on telomeres
    • Ye, J. Z. et al. TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 complex on telomeres. J. Biol. Chem. 279, 47264-47271 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 47264-47271
    • Ye, J.Z.1
  • 141
    • 33747051742 scopus 로고    scopus 로고
    • A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly
    • O'Connor, M. S., Safari, A., Xin, H., Liu, D. & Songyang, Z. A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly. Proc. Natl Acad. Sci. USA 103, 11874-11879 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 11874-11879
    • O'Connor, M.S.1    Safari, A.2    Xin, H.3    Liu, D.4    Songyang, Z.5
  • 142
    • 4544258775 scopus 로고    scopus 로고
    • A dynamic molecular link between the telomere length regulator TRF1 and the chromosome end protector TRF2
    • Houghtaling, B. R., Cuttonaro, L., Chang, W. & Smith, S. A dynamic molecular link between the telomere length regulator TRF1 and the chromosome end protector TRF2. Curr. Biol. 14, 1621-1631 (2004).
    • (2004) Curr. Biol , vol.14 , pp. 1621-1631
    • Houghtaling, B.R.1    Cuttonaro, L.2    Chang, W.3    Smith, S.4
  • 143
    • 0027479161 scopus 로고
    • (oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin, A. G. OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J. 12, 861-867 (1993).
    • (1993) EMBO J , vol.12 , pp. 861-867
    • Murzin, A.G.O.1
  • 144
    • 33846691378 scopus 로고    scopus 로고
    • The POT1-TPP1 telomere complex is a telomerase processivity factor
    • Wang, F. et al. The POT1-TPP1 telomere complex is a telomerase processivity factor. Nature 445, 506-510 (2007).
    • (2007) Nature , vol.445 , pp. 506-510
    • Wang, F.1
  • 145
    • 33846692105 scopus 로고    scopus 로고
    • Xin, H. et al. TPP1 is a homologue of ciliate TEBP-β and interacts with POT1 to recruit telomerase. Nature 445, 559-562 (2007). References 144 and 145 show that the human telomeric proteins TPP1 and POT1 form a complex that regulates telomerase access to the telomere and increases the processivity of the telomerase core enzyme.
    • Xin, H. et al. TPP1 is a homologue of ciliate TEBP-β and interacts with POT1 to recruit telomerase. Nature 445, 559-562 (2007). References 144 and 145 show that the human telomeric proteins TPP1 and POT1 form a complex that regulates telomerase access to the telomere and increases the processivity of the telomerase core enzyme.
  • 146
    • 0036241994 scopus 로고    scopus 로고
    • Targeting assay to study the cis functions of human telomeric proteins: Evidence for inhibition of telomerase by TRF1 and for activation of telomere degradation by TRF2
    • Ancelin, K. et al. Targeting assay to study the cis functions of human telomeric proteins: evidence for inhibition of telomerase by TRF1 and for activation of telomere degradation by TRF2. Mol. Cell. Biol. 22, 3474-3487 (2002).
    • (2002) Mol. Cell. Biol , vol.22 , pp. 3474-3487
    • Ancelin, K.1
  • 147
    • 0038451396 scopus 로고    scopus 로고
    • POT1 as a terminal transducer of TRF1 telomere length control
    • Loayza, D. & De Lange, T. POT1 as a terminal transducer of TRF1 telomere length control. Nature 423, 1013-1018 (2003).
    • (2003) Nature , vol.423 , pp. 1013-1018
    • Loayza, D.1    De Lange, T.2
  • 148
    • 0021232048 scopus 로고
    • Chromatin structure of the molecular ends of Oxytricha macronuclear DNA: Phased nucleosomes and a telomeric complex
    • Gottschling, D. E. & Cech, T. R. Chromatin structure of the molecular ends of Oxytricha macronuclear DNA: phased nucleosomes and a telomeric complex. Cell 38, 501-510 (1984).
    • (1984) Cell , vol.38 , pp. 501-510
    • Gottschling, D.E.1    Cech, T.R.2
  • 149
    • 0026563895 scopus 로고
    • Saccharomyces telomeres assume a non-nucleosomal chromatin structure
    • Wright, J. H., Gottschling, D. E. & Zakian, V. A. Saccharomyces telomeres assume a non-nucleosomal chromatin structure. Genes Dev. 6, 197-210 (1992).
    • (1992) Genes Dev , vol.6 , pp. 197-210
    • Wright, J.H.1    Gottschling, D.E.2    Zakian, V.A.3
  • 150
    • 23944502886 scopus 로고    scopus 로고
    • Telomere maintenance, function and evolution: The yeast paradigm
    • Teixeira, M. T. & Gilson, E. Telomere maintenance, function and evolution: the yeast paradigm. Chromosome Res. 13, 535-548 (2005).
    • (2005) Chromosome Res , vol.13 , pp. 535-548
    • Teixeira, M.T.1    Gilson, E.2
  • 151
    • 33947317206 scopus 로고    scopus 로고
    • The epigenetic regulation of mammalian telomeres
    • Blasco, M. A. The epigenetic regulation of mammalian telomeres. Nature Rev. Genet. 8, 299-309 (2007).
    • (2007) Nature Rev. Genet , vol.8 , pp. 299-309
    • Blasco, M.A.1
  • 152
    • 0035874977 scopus 로고    scopus 로고
    • Telomere position effect in human cells
    • Baur, J. A., Zou, Y., Shay, J. W. & Wright, W. E. Telomere position effect in human cells. Science 292, 2075-2077 (2001).
    • (2001) Science , vol.292 , pp. 2075-2077
    • Baur, J.A.1    Zou, Y.2    Shay, J.W.3    Wright, W.E.4
  • 153
    • 0036867444 scopus 로고    scopus 로고
    • Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity
    • 1055-1061
    • Koering, C. E. et al. Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity. EMBO Rep. 3, 1055-1061 (2002).
    • (2002) EMBO Rep , vol.3
    • Koering, C.E.1
  • 154
    • 0029586089 scopus 로고
    • A human telomeric protein
    • Chong, L. et al. A human telomeric protein. Science 270, 1663-1667 (1995).
    • (1995) Science , vol.270 , pp. 1663-1667
    • Chong, L.1
  • 155
    • 84984775429 scopus 로고    scopus 로고
    • Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2
    • Broccoli, D., Smogorzewska, A., Chong, L. & de Lange, T. Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2. Nature Genet. 17, 231-235 (1997).
    • (1997) Nature Genet , vol.17 , pp. 231-235
    • Broccoli, D.1    Smogorzewska, A.2    Chong, L.3    de Lange, T.4
  • 156
    • 84984754548 scopus 로고    scopus 로고
    • Telomeric localization of TRF2, a novel human telobox protein
    • Bilaud, T. et al. Telomeric localization of TRF2, a novel human telobox protein. Nature Genet. 17, 236-239 (1997).
    • (1997) Nature Genet , vol.17 , pp. 236-239
    • Bilaud, T.1
  • 157
    • 0033553536 scopus 로고    scopus 로고
    • Mammalian telomeres end in a large duplex loop
    • Griffith, J. D. et al. Mammalian telomeres end in a large duplex loop. Cell 97, 503-514 (1999).
    • (1999) Cell , vol.97 , pp. 503-514
    • Griffith, J.D.1
  • 158
    • 25444533047 scopus 로고    scopus 로고
    • POT1 stimulates RecQ helicases WRN and BLM to unwind telomeric DNA substrates
    • Opresko, P. L. et al. POT1 stimulates RecQ helicases WRN and BLM to unwind telomeric DNA substrates. J. Biol. Chem. 280, 32069-32080 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 32069-32080
    • Opresko, P.L.1
  • 159
    • 23344451160 scopus 로고    scopus 로고
    • Human POT1 disrupts telomeric G-quadruplexes allowing telomerase extension in vitro
    • Zaug, A. J., Podell, E. R. & Cech, T. R. Human POT1 disrupts telomeric G-quadruplexes allowing telomerase extension in vitro. Proc. Natl Acad. Sci. USA 102, 10864-10869 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 10864-10869
    • Zaug, A.J.1    Podell, E.R.2    Cech, T.R.3
  • 160
    • 0032562649 scopus 로고    scopus 로고
    • TRF1 promotes parallel pairing of telomeric tracts in vitro
    • Griffith, J., Bianchi, A. & de Lange, T. TRF1 promotes parallel pairing of telomeric tracts in vitro. J. Mol. Biol. 278, 79-88 (1998).
    • (1998) J. Mol. Biol , vol.278 , pp. 79-88
    • Griffith, J.1    Bianchi, A.2    de Lange, T.3
  • 161
    • 34247600494 scopus 로고    scopus 로고
    • RAP1/TRF2 complex inhibits nonhomologous end-joining at human telomeric DNA ends
    • Bae, N. S. & Baumann, P. A RAP1/TRF2 complex inhibits nonhomologous end-joining at human telomeric DNA ends. Mol. Cell 26, 323-334 (2007).
    • (2007) Mol. Cell , vol.26 , pp. 323-334
    • Bae, N.S.1    Baumann, P.A.2
  • 162
    • 0030697342 scopus 로고    scopus 로고
    • Evidence for an alternative mechanism for maintaining telomere length in human tumors and tumor-derived cell lines
    • Bryan, T. M., Englezou, A., Dalla-Pozza, L., Dunham, M. A. & Reddel, R. R. Evidence for an alternative mechanism for maintaining telomere length in human tumors and tumor-derived cell lines. Nature Med. 3, 1271-1274 (1997).
    • (1997) Nature Med , vol.3 , pp. 1271-1274
    • Bryan, T.M.1    Englezou, A.2    Dalla-Pozza, L.3    Dunham, M.A.4    Reddel, R.R.5
  • 163
    • 16844379374 scopus 로고    scopus 로고
    • A novel telomere structure in a human alternative lengthening of telomeres cell line
    • Marciniak, R. A. et al. A novel telomere structure in a human alternative lengthening of telomeres cell line. Cancer Res. 65, 2730-2737 (2005).
    • (2005) Cancer Res , vol.65 , pp. 2730-2737
    • Marciniak, R.A.1
  • 164
    • 33745474120 scopus 로고    scopus 로고
    • Break-induced replication and recombinational telomere elongation in yeast
    • McEachern, M. J. & Haber, J. E. Break-induced replication and recombinational telomere elongation in yeast. Annu. Rev. Biochem. 75, 111-135 (2006).
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 111-135
    • McEachern, M.J.1    Haber, J.E.2
  • 165
    • 0030824031 scopus 로고    scopus 로고
    • Telomere maintenance without telomerase
    • Biessmann, H. & Mason, J. M. Telomere maintenance without telomerase. Chromosoma 106, 63-69 (1997).
    • (1997) Chromosoma , vol.106 , pp. 63-69
    • Biessmann, H.1    Mason, J.M.2
  • 166
    • 23944501376 scopus 로고    scopus 로고
    • Two retrotransposons maintain telomeres in Drosophila
    • Pardue, M. L. et al. Two retrotransposons maintain telomeres in Drosophila. Chromosome Res. 13, 443-453 (2005).
    • (2005) Chromosome Res , vol.13 , pp. 443-453
    • Pardue, M.L.1
  • 167
    • 33947128732 scopus 로고    scopus 로고
    • Endonuclease-independent LINE-1 retrotransposition at mammalian telomeres
    • Morrish, T. A. et al. Endonuclease-independent LINE-1 retrotransposition at mammalian telomeres. Nature 446, 208-212 (2007).
    • (2007) Nature , vol.446 , pp. 208-212
    • Morrish, T.A.1
  • 168
    • 33750211081 scopus 로고    scopus 로고
    • Human replication protein A unfolds telomeric G-quadruplexes
    • Salas, T. R. et al. Human replication protein A unfolds telomeric G-quadruplexes. Nucleic Acids Res. 34, 4857-4865 (2006).
    • (2006) Nucleic Acids Res , vol.34 , pp. 4857-4865
    • Salas, T.R.1
  • 169
    • 31544482730 scopus 로고    scopus 로고
    • Telomere repeat binding factor 2 interacts with base excision repair proteins and stimulates DNA synthesis by DNA polymerase β
    • Muftuoglu, M. et al. Telomere repeat binding factor 2 interacts with base excision repair proteins and stimulates DNA synthesis by DNA polymerase β. Cancer Res. 66, 113-124 (2006).
    • (2006) Cancer Res , vol.66 , pp. 113-124
    • Muftuoglu, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.