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Volumn 5, Issue 8, 2010, Pages

The protein network surrounding the human telomere repeat binding factors TRF1, TRF2, and POT1

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; PROTEIN POT1; TELOMERIC REPEAT BINDING FACTOR 1; TELOMERIC REPEAT BINDING FACTOR 2; UNCLASSIFIED DRUG; POT1 PROTEIN, HUMAN; TELOMERE BINDING PROTEIN;

EID: 77957881251     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0012407     Document Type: Article
Times cited : (49)

References (75)
  • 1
    • 0030060521 scopus 로고    scopus 로고
    • Telomeres, telomerase and cancer
    • Greider CW, Blackburn EH (1996) Telomeres, telomerase and cancer. Sci Am 274: 92-97.
    • (1996) Sci Am , vol.274 , pp. 92-97
    • Greider, C.W.1    Blackburn, E.H.2
  • 3
    • 3543056880 scopus 로고    scopus 로고
    • Functional links between telomeres and proteins of the DNA-damage response
    • d'Adda di Fagagna F, Teo SH, Jackson SP (2004) Functional links between telomeres and proteins of the DNA-damage response. Genes Dev 18: 1781-1799.
    • (2004) Genes Dev , vol.18 , pp. 1781-1799
    • d'Adda di Fagagna, F.1    Teo, S.H.2    Jackson, S.P.3
  • 4
    • 24944460598 scopus 로고    scopus 로고
    • Shelterin: The protein complex that shapes and safeguards human telomeres
    • de Lange T (2005) Shelterin: the protein complex that shapes and safeguards human telomeres. Genes Dev 19: 2100-2110.
    • (2005) Genes Dev , vol.19 , pp. 2100-2110
    • de Lange, T.1
  • 5
    • 10944240539 scopus 로고    scopus 로고
    • Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins
    • Liu D, O'Connor MS, Qin J, Songyang Z (2004) Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins. J Biol Chem 279: 51338-51342.
    • (2004) J Biol Chem , vol.279 , pp. 51338-51342
    • Liu, D.1    O'Connor, M.S.2    Qin, J.3    Songyang, Z.4
  • 6
    • 46249125488 scopus 로고    scopus 로고
    • How shelterin protects mammalian telomeres
    • Palm W, de Lange T (2008) How shelterin protects mammalian telomeres. Annu Rev Genet 42: 301-334.
    • (2008) Annu Rev Genet , vol.42 , pp. 301-334
    • Palm, W.1    de Lange, T.2
  • 7
    • 58849150874 scopus 로고    scopus 로고
    • The telosome/shelterin complex and its functions
    • Xin H, Liu D, Songyang Z (2008) The telosome/shelterin complex and its functions. Genome Biol 9: 232.
    • (2008) Genome Biol , vol.9 , pp. 232
    • Xin, H.1    Liu, D.2    Songyang, Z.3
  • 9
    • 84984754548 scopus 로고    scopus 로고
    • Telomeric localization of TRF2, a novel human telobox protein
    • Bilaud T, Brun C, Ancelin K, Koering CE, Laroche T, et al. (1997) Telomeric localization of TRF2, a novel human telobox protein. Nat Genet 17: 236-239.
    • (1997) Nat Genet , vol.17 , pp. 236-239
    • Bilaud, T.1    Brun, C.2    Ancelin, K.3    Koering, C.E.4    Laroche, T.5
  • 10
    • 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 (1997) Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2. Nat Genet 17: 231-235.
    • (1997) Nat Genet , vol.17 , pp. 231-235
    • Broccoli, D.1    Smogorzewska, A.2    Chong, L.3    de Lange, T.4
  • 11
    • 0035844082 scopus 로고    scopus 로고
    • Pot1, the putative telomere end-binding protein in fission yeast and humans
    • Baumann P, Cech TR (2001) Pot1, the putative telomere end-binding protein in fission yeast and humans. Science 292: 1171-1175.
    • (2001) Science , vol.292 , pp. 1171-1175
    • Baumann, P.1    Cech, T.R.2
  • 12
    • 3142679378 scopus 로고    scopus 로고
    • POT1-interacting protein PIP1: A telomere length regulator that recruits POT1 to the TIN2/TRF1 complex
    • Ye JZ, Hockemeyer D, Krutchinsky AN, Loayza D, Hooper SM, et al. (2004) POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex. Genes Dev 18: 1649-1654.
    • (2004) Genes Dev , vol.18 , pp. 1649-1654
    • Ye, J.Z.1    Hockemeyer, D.2    Krutchinsky, A.N.3    Loayza, D.4    Hooper, S.M.5
  • 13
    • 12844254472 scopus 로고    scopus 로고
    • POT1 and TRF2 cooperate to maintain telomeric integrity
    • Yang Q, Zheng YL, Harris CC (2005) POT1 and TRF2 cooperate to maintain telomeric integrity. Mol Cell Biol 25: 1070-1080.
    • (2005) Mol Cell Biol , vol.25 , pp. 1070-1080
    • Yang, Q.1    Zheng, Y.L.2    Harris, C.C.3
  • 15
    • 2642535870 scopus 로고    scopus 로고
    • TIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length control complex
    • Ye JZ, de Lange T (2004) TIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length control complex. Nat Genet 36: 618-623.
    • (2004) Nat Genet , vol.36 , pp. 618-623
    • Ye, J.Z.1    de Lange, T.2
  • 16
    • 4544258775 scopus 로고    scopus 로고
    • A dynamic molecular link between the telomere length regulator TRF1 and the chromosome end protector TRF2
    • Houghtaling BR, Cuttonaro L, Chang W, Smith S (2004) A dynamic molecular link between the telomere length regulator TRF1 and the chromosome end protector TRF2. Curr Biol 14: 1621-1631.
    • (2004) Curr Biol , vol.14 , pp. 1621-1631
    • Houghtaling, B.R.1    Cuttonaro, L.2    Chang, W.3    Smith, S.4
  • 17
    • 3242680818 scopus 로고    scopus 로고
    • PTOP interacts with POT1 and regulates its localization to telomeres
    • Liu D, Safari A, O'Connor MS, Chan DW, Laegeler A, et al. (2004) PTOP interacts with POT1 and regulates its localization to telomeres. Nat Cell Biol 6: 673-680.
    • (2004) Nat Cell Biol , vol.6 , pp. 673-680
    • Liu, D.1    Safari, A.2    O'Connor, M.S.3    Chan, D.W.4    Laegeler, A.5
  • 18
    • 0034716904 scopus 로고    scopus 로고
    • Identification of human Rap1: Implications for telomere evolution
    • Li B, Oestreich S, de Lange T (2000) Identification of human Rap1: implications for telomere evolution. Cell 101: 471-483.
    • (2000) Cell , vol.101 , pp. 471-483
    • Li, B.1    Oestreich, S.2    de Lange, T.3
  • 19
    • 3142616449 scopus 로고    scopus 로고
    • The human Rap1 protein complex and modulation of telomere length
    • O'Connor MS, Safari A, Liu D, Qin J, Songyang Z (2004) The human Rap1 protein complex and modulation of telomere length. J Biol Chem 279: 28585-28591.
    • (2004) J Biol Chem , vol.279 , pp. 28585-28591
    • O'Connor, M.S.1    Safari, A.2    Liu, D.3    Qin, J.4    Songyang, Z.5
  • 20
    • 38349073475 scopus 로고    scopus 로고
    • DNA damage response at functional and dysfunctional telomeres
    • Longhese MP (2008) DNA damage response at functional and dysfunctional telomeres. Genes Dev 22: 125-140.
    • (2008) Genes Dev , vol.22 , pp. 125-140
    • Longhese, M.P.1
  • 21
    • 70350020161 scopus 로고    scopus 로고
    • Conservation of telomere protein complexes: Shuffling through evolution
    • Linger BR, Price CM (2009) Conservation of telomere protein complexes: shuffling through evolution. Crit Rev Biochem Mol Biol 44: 434-446.
    • (2009) Crit Rev Biochem Mol Biol , vol.44 , pp. 434-446
    • Linger, B.R.1    Price, C.M.2
  • 22
    • 0031027618 scopus 로고    scopus 로고
    • Control of telomere length by the human telomeric protein TRF1
    • van Steensel B, de Lange T (1997) Control of telomere length by the human telomeric protein TRF1. Nature 385: 740-743.
    • (1997) Nature , vol.385 , pp. 740-743
    • van Steensel, B.1    de Lange, T.2
  • 23
    • 0032489012 scopus 로고    scopus 로고
    • TRF2 protects human telomeres from end-to-end fusions
    • van Steensel B, Smogorzewska A, de Lange T (1998) TRF2 protects human telomeres from end-to-end fusions. Cell 92: 401-413.
    • (1998) Cell , vol.92 , pp. 401-413
    • van Steensel, B.1    Smogorzewska, A.2    de Lange, T.3
  • 25
    • 0034687248 scopus 로고    scopus 로고
    • Tankyrase promotes telomere elongation in human cells
    • Smith S, de Lange T (2000) Tankyrase promotes telomere elongation in human cells. Curr Biol 10: 1299-1302.
    • (2000) Curr Biol , vol.10 , pp. 1299-1302
    • Smith, S.1    de Lange, T.2
  • 26
    • 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, Brunori M, Bauwens S, Koering CE, Brun C, et al. (2002) 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) Mol Cell Biol , vol.22 , pp. 3474-3487
    • Ancelin, K.1    Brunori, M.2    Bauwens, S.3    Koering, C.E.4    Brun, C.5
  • 27
    • 33846691378 scopus 로고    scopus 로고
    • The POT1-TPP1 telomere complex is a telomerase processivity factor
    • Wang F, Podell ER, Zaug AJ, Yang Y, Baciu P, et al. (2007) The POT1-TPP1 telomere complex is a telomerase processivity factor. Nature 445: 506-510.
    • (2007) Nature , vol.445 , pp. 506-510
    • Wang, F.1    Podell, E.R.2    Zaug, A.J.3    Yang, Y.4    Baciu, P.5
  • 28
    • 33846692105 scopus 로고    scopus 로고
    • TPP1 is a homologue of ciliate TEBP-beta and interacts with POT1 to recruit telomerase
    • Xin H, Liu D, Wan M, Safari A, Kim H, et al. (2007) TPP1 is a homologue of ciliate TEBP-beta and interacts with POT1 to recruit telomerase. Nature 445: 559-562.
    • (2007) Nature , vol.445 , pp. 559-562
    • Xin, H.1    Liu, D.2    Wan, M.3    Safari, A.4    Kim, H.5
  • 29
    • 47549086947 scopus 로고    scopus 로고
    • How telomerase reaches its end: Mechanism of telomerase regulation by the telomeric complex
    • Bianchi A, Shore D (2008) How telomerase reaches its end: mechanism of telomerase regulation by the telomeric complex. Mol Cell 31: 153-165.
    • (2008) Mol Cell , vol.31 , pp. 153-165
    • Bianchi, A.1    Shore, D.2
  • 31
    • 58149171995 scopus 로고    scopus 로고
    • Involvement of human ORC and TRF2 in pre-replication complex assembly at telomeres
    • Tatsumi Y, Ezura K, Yoshida K, Yugawa T, Narisawa-Saito M, et al. (2008) Involvement of human ORC and TRF2 in pre-replication complex assembly at telomeres. Genes Cells 13: 1045-1059.
    • (2008) Genes Cells , vol.13 , pp. 1045-1059
    • Tatsumi, Y.1    Ezura, K.2    Yoshida, K.3    Yugawa, T.4    Narisawa-Saito, M.5
  • 32
    • 69749092744 scopus 로고    scopus 로고
    • Increased telomere fragility and fusions resulting from TRF1 deficiency lead to degenerative pathologies and increased cancer in mice
    • Martinez P, Thanasoula M, Munoz P, Liao C, Tejera A, et al. (2009) Increased telomere fragility and fusions resulting from TRF1 deficiency lead to degenerative pathologies and increased cancer in mice. Genes Dev 23: 2060-2075.
    • (2009) Genes Dev , vol.23 , pp. 2060-2075
    • Martinez, P.1    Thanasoula, M.2    Munoz, P.3    Liao, C.4    Tejera, A.5
  • 33
    • 67649635974 scopus 로고    scopus 로고
    • Mammalian telomeres resemble fragile sites and require TRF1 for efficient replication
    • Sfeir A, Kosiyatrakul ST, Hockemeyer D, MacRae SL, Karlseder J, et al. (2009) Mammalian telomeres resemble fragile sites and require TRF1 for efficient replication. Cell 138: 90-103.
    • (2009) Cell , vol.138 , pp. 90-103
    • Sfeir, A.1    Kosiyatrakul, S.T.2    Hockemeyer, D.3    Macrae, S.L.4    Karlseder, J.5
  • 34
    • 0037192462 scopus 로고    scopus 로고
    • Senescence induced by altered telomere state, not telomere loss
    • Karlseder J, Smogorzewska A, de Lange T (2002) Senescence induced by altered telomere state, not telomere loss. Science 295: 2446-2449.
    • (2002) Science , vol.295 , pp. 2446-2449
    • Karlseder, J.1    Smogorzewska, A.2    de Lange, T.3
  • 35
    • 23044500389 scopus 로고    scopus 로고
    • POT1 Protects Telomeres From a Transient DNA Damage Response and Determines How Human Chromosomes End
    • Hockemeyer D, Sfeir AJ, Shay JW, Wright WE, de Lange T (2005) POT1 protects telomeres from a transient DNA damage response and determines how human chromosomes end. Embo J 24: 2667-2678.
    • (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
  • 36
    • 33745685066 scopus 로고    scopus 로고
    • Recent expansion of the telomeric complex in rodents: Two distinct POT1 proteins protect mouse telomeres
    • Hockemeyer D, Daniels JP, Takai H, de Lange T (2006) Recent expansion of the telomeric complex in rodents: Two distinct POT1 proteins protect mouse telomeres. Cell 126: 63-77.
    • (2006) Cell , vol.126 , pp. 63-77
    • Hockemeyer, D.1    Daniels, J.P.2    Takai, H.3    de Lange, T.4
  • 37
    • 33745713451 scopus 로고    scopus 로고
    • Pot1 deficiency initiates DNA damage checkpoint activation and aberrant homologous recombination at telomeres
    • Wu L, Multani AS, He H, Cosme-Blanco W, Deng Y, et al. (2006) Pot1 deficiency initiates DNA damage checkpoint activation and aberrant homologous recombination at telomeres. Cell 126: 49-62.
    • (2006) Cell , vol.126 , pp. 49-62
    • Wu, L.1    Multani, A.S.2    He, H.3    Cosme-Blanco, W.4    Deng, Y.5
  • 38
    • 34548317418 scopus 로고    scopus 로고
    • Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1
    • Denchi EL, de Lange T (2007) Protection of telomeres through independent control of ATM and ATR by TRF2 and POT1. Nature 448: 1068-1071.
    • (2007) Nature , vol.448 , pp. 1068-1071
    • Denchi, E.L.1    de Lange, T.2
  • 39
    • 36248952723 scopus 로고    scopus 로고
    • Dysfunctional telomeres activate an ATM-ATR-dependent DNA damage response to suppress tumorigenesis
    • Guo X, Deng Y, Lin Y, Cosme-Blanco W, Chan S, et al. (2007) Dysfunctional telomeres activate an ATM-ATR-dependent DNA damage response to suppress tumorigenesis. Embo J 26: 4709-4719.
    • (2007) Embo J , vol.26 , pp. 4709-4719
    • Guo, X.1    Deng, Y.2    Lin, Y.3    Cosme-Blanco, W.4    Chan, S.5
  • 40
    • 73649113140 scopus 로고    scopus 로고
    • BRCA1 localization to the telomere and its loss from the telomere in response to DNA damage
    • Ballal RD, Saha T, Fan S, Haddad BR, Rosen EM (2009) BRCA1 localization to the telomere and its loss from the telomere in response to DNA damage. J Biol Chem 284: 36083-36098.
    • (2009) J Biol Chem , vol.284 , pp. 36083-36098
    • Ballal, R.D.1    Saha, T.2    Fan, S.3    Haddad, B.R.4    Rosen, E.M.5
  • 41
    • 41449108060 scopus 로고    scopus 로고
    • Flap endonuclease 1 contributes to telomere stability
    • Saharia A, Guittat L, Crocker S, Lim A, Steffen M, et al. (2008) Flap endonuclease 1 contributes to telomere stability. Curr Biol 18: 496-500.
    • (2008) Curr Biol , vol.18 , pp. 496-500
    • Saharia, A.1    Guittat, L.2    Crocker, S.3    Lim, A.4    Steffen, M.5
  • 42
    • 44349180746 scopus 로고    scopus 로고
    • Topoisomerase IIIalpha is required for normal proliferation and telomere stability in alternative lengthening of telomeres
    • Temime-Smaali N, Guittat L, Wenner T, Bayart E, Douarre C, et al. (2008) Topoisomerase IIIalpha is required for normal proliferation and telomere stability in alternative lengthening of telomeres. Embo J.
    • (2008) Embo J
    • Temime-Smaali, N.1    Guittat, L.2    Wenner, T.3    Bayart, E.4    Douarre, C.5
  • 43
    • 58149351370 scopus 로고    scopus 로고
    • Essential role of Pin1 in the regulation of TRF1 stability and telomere maintenance
    • Lee TH, Tun-Kyi A, Shi R, Lim J, Soohoo C, et al. (2009) Essential role of Pin1 in the regulation of TRF1 stability and telomere maintenance. Nat Cell Biol 11: 97-105.
    • (2009) Nat Cell Biol , vol.11 , pp. 97-105
    • Lee, T.H.1    Tun-Kyi, A.2    Shi, R.3    Lim, J.4    Soohoo, C.5
  • 45
    • 0036867444 scopus 로고    scopus 로고
    • Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity
    • Koering CE, Pollice A, Zibella MP, Bauwens S, Puisieux A, et al. (2002) Human telomeric position effect is determined by chromosomal context and telomeric chromatin integrity. EMBO Rep 3: 1055-1061.
    • (2002) EMBO Rep , vol.3 , pp. 1055-1061
    • Koering, C.E.1    Pollice, A.2    Zibella, M.P.3    Bauwens, S.4    Puisieux, A.5
  • 46
    • 36549030804 scopus 로고    scopus 로고
    • Protein requirements for sister telomere association in human cells
    • Canudas S, Houghtaling BR, Kim JY, Dynek JN, Chang WG, et al. (2007) Protein requirements for sister telomere association in human cells. Embo J 26: 4867-4878.
    • (2007) Embo J , vol.26 , pp. 4867-4878
    • Canudas, S.1    Houghtaling, B.R.2    Kim, J.Y.3    Dynek, J.N.4    Chang, W.G.5
  • 47
    • 34447129654 scopus 로고    scopus 로고
    • The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteins
    • Potts PR, Yu H (2007) The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteins. Nat Struct Mol Biol 14: 581-590.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 581-590
    • Potts, P.R.1    Yu, H.2
  • 48
    • 38849111756 scopus 로고    scopus 로고
    • Developmentally regulated transcription of mammalian telomeres by DNA-dependent RNA polymerase II
    • Schoeftner S, Blasco MA (2008) Developmentally regulated transcription of mammalian telomeres by DNA-dependent RNA polymerase II. Nat Cell Biol 10: 228-236.
    • (2008) Nat Cell Biol , vol.10 , pp. 228-236
    • Schoeftner, S.1    Blasco, M.A.2
  • 49
    • 13944263628 scopus 로고    scopus 로고
    • Human telomeric protein TRF2 associates with genomic double-strand breaks as an early response to DNA damage
    • Bradshaw PS, Stavropoulos DJ, Meyn MS (2005) Human telomeric protein TRF2 associates with genomic double-strand breaks as an early response to DNA damage. Nat Genet 37: 193-197.
    • (2005) Nat Genet , vol.37 , pp. 193-197
    • Bradshaw, P.S.1    Stavropoulos, D.J.2    Meyn, M.S.3
  • 50
    • 18844396775 scopus 로고    scopus 로고
    • Accumulation and altered localization of telomere-associated protein TRF2 in immortally transformed and tumor-derived human breast cells
    • Nijjar T, Bassett E, Garbe J, Takenaka Y, Stampfer MR, et al. (2005) Accumulation and altered localization of telomere-associated protein TRF2 in immortally transformed and tumor-derived human breast cells. Oncogene 24: 3369-3376.
    • (2005) Oncogene , vol.24 , pp. 3369-3376
    • Nijjar, T.1    Bassett, E.2    Garbe, J.3    Takenaka, Y.4    Stampfer, M.R.5
  • 52
    • 34548737554 scopus 로고    scopus 로고
    • TRF2 is required for repair of nontelomeric DNA double-strand breaks by homologous recombination
    • Mao Z, Seluanov A, Jiang Y, Gorbunova V (2007) TRF2 is required for repair of nontelomeric DNA double-strand breaks by homologous recombination. Proc Natl Acad Sci U S A 104: 13068-13073.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 13068-13073
    • Mao, Z.1    Seluanov, A.2    Jiang, Y.3    Gorbunova, V.4
  • 53
    • 67650096772 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of TRF2 is required for the fast pathway of DNA double-strand break repair
    • Huda N, Tanaka H, Mendonca MS, Gilley D (2009) DNA damage-induced phosphorylation of TRF2 is required for the fast pathway of DNA double-strand break repair. Mol Cell Biol 29: 3597-3604.
    • (2009) Mol Cell Biol , vol.29 , pp. 3597-3604
    • Huda, N.1    Tanaka, H.2    Mendonca, M.S.3    Gilley, D.4
  • 54
    • 53249087743 scopus 로고    scopus 로고
    • Nontelomeric TRF2-REST interaction modulates neuronal gene silencing and fate of tumor and stem cells
    • Zhang P, Pazin MJ, Schwartz CM, Becker KG, Wersto RP, et al. (2008) Nontelomeric TRF2-REST interaction modulates neuronal gene silencing and fate of tumor and stem cells. Curr Biol 18: 1489-1494.
    • (2008) Curr Biol , vol.18 , pp. 1489-1494
    • Zhang, P.1    Pazin, M.J.2    Schwartz, C.M.3    Becker, K.G.4    Wersto, R.P.5
  • 55
    • 0035797910 scopus 로고    scopus 로고
    • A specific interaction between the telomeric protein Pin2/TRF1 and the mitotic spindle
    • Nakamura M, Zhou XZ, Kishi S, Kosugi I, Tsutsui Y, et al. (2001) A specific interaction between the telomeric protein Pin2/TRF1 and the mitotic spindle. Curr Biol 11: 1512-1516.
    • (2001) Curr Biol , vol.11 , pp. 1512-1516
    • Nakamura, M.1    Zhou, X.Z.2    Kishi, S.3    Kosugi, I.4    Tsutsui, Y.5
  • 56
    • 34548668650 scopus 로고    scopus 로고
    • Dualtagging system for the affinity purification of mammalian protein complexes
    • passim
    • Giannone RJ, McDonald WH, Hurst GB, Huang Y, Wu J, et al. (2007) Dualtagging system for the affinity purification of mammalian protein complexes. Biotechniques 43: 296, 298, 300 passim.
    • (2007) Biotechniques , vol.43
    • Giannone, R.J.1    McDonald, W.H.2    Hurst, G.B.3    Huang, Y.4    Wu, J.5
  • 57
    • 33745375693 scopus 로고    scopus 로고
    • PARP1 Is a TRF2-associated poly(ADP-ribose)polymerase and protects eroded telomeres
    • Gomez M, Wu J, Schreiber V, Dunlap J, Dantzer F, et al. (2006) PARP1 Is a TRF2-associated poly(ADP-ribose)polymerase and protects eroded telomeres. Mol Biol Cell 17: 1686-1696.
    • (2006) Mol Biol Cell , vol.17 , pp. 1686-1696
    • Gomez, M.1    Wu, J.2    Schreiber, V.3    Dunlap, J.4    Dantzer, F.5
  • 59
    • 0036684101 scopus 로고    scopus 로고
    • Comparison of three directly coupled HPLC MS/MS strategies for identification of proteins from complex mixtures: Single-dimension LC-MS/MS, 2-phase MudPIT, and 3-phase MudPIT
    • McDonald WH, Ohi R, Miyamoto DT, Mitchison TJ, John R, Yates I (2002) Comparison of three directly coupled HPLC MS/MS strategies for identification of proteins from complex mixtures: single-dimension LC-MS/MS, 2-phase MudPIT, and 3-phase MudPIT. International Journal of Mass Spectrometry 219: 245-251.
    • (2002) International Journal of Mass Spectrometry , vol.219 , pp. 245-251
    • McDonald, W.H.1    Ohi, R.2    Miyamoto, D.T.3    Mitchison, T.J.4    John, R.5    Yates, I.6
  • 60
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb DL, McDonald WH, Yates JR, 3rd (2002) DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J Proteome Res 1: 21-26.
    • (2002) J Proteome Res , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 62
    • 34547900244 scopus 로고    scopus 로고
    • Telomere maintenance through spatial control of telomeric proteins
    • Chen LY, Liu D, Songyang Z (2007) Telomere maintenance through spatial control of telomeric proteins. Mol Cell Biol 27: 5898-5909.
    • (2007) Mol Cell Biol , vol.27 , pp. 5898-5909
    • Chen, L.Y.1    Liu, D.2    Songyang, Z.3
  • 63
    • 34247135913 scopus 로고    scopus 로고
    • Classical nuclear localization signals: Definition, function, and interaction with importin alpha
    • Lange A, Mills RE, Lange CJ, Stewart M, Devine SE, et al. (2007) Classical nuclear localization signals: definition, function, and interaction with importin alpha. J Biol Chem 282: 5101-5105.
    • (2007) J Biol Chem , vol.282 , pp. 5101-5105
    • Lange, A.1    Mills, R.E.2    Lange, C.J.3    Stewart, M.4    Devine, S.E.5
  • 64
    • 0037199488 scopus 로고    scopus 로고
    • Nuclear import pathway of the telomere elongation suppressor TRF1: Inhibition by importin alpha
    • Forwood JK, Jans DA (2002) Nuclear import pathway of the telomere elongation suppressor TRF1: inhibition by importin alpha. Biochemistry 41: 9333-9340.
    • (2002) Biochemistry , vol.41 , pp. 9333-9340
    • Forwood, J.K.1    Jans, D.A.2
  • 65
    • 19344374569 scopus 로고    scopus 로고
    • The telomeric protein TRF2 binds the ATM kinase and can inhibit the ATMdependent DNA damage response
    • Karlseder J, Hoke K, Mirzoeva OK, Bakkenist C, Kastan MB, et al. (2004) The telomeric protein TRF2 binds the ATM kinase and can inhibit the ATMdependent DNA damage response. PLoS Biol 2: E240.
    • (2004) PLoS Biol , vol.2
    • Karlseder, J.1    Hoke, K.2    Mirzoeva, O.K.3    Bakkenist, C.4    Kastan, M.B.5
  • 66
    • 0342561644 scopus 로고    scopus 로고
    • Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres
    • Zhu XD, Kuster B, Mann M, Petrini JH, de Lange T (2000) Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres. Nat Genet 25: 347-352.
    • (2000) Nat Genet , vol.25 , pp. 347-352
    • Zhu, X.D.1    Kuster, B.2    Mann, M.3    Petrini, J.H.4    de Lange, T.5
  • 68
    • 0037610123 scopus 로고    scopus 로고
    • TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
    • Chang W, Dynek JN, Smith S (2003) TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres. Genes Dev 17: 1328-1333.
    • (2003) Genes Dev , vol.17 , pp. 1328-1333
    • Chang, W.1    Dynek, J.N.2    Smith, S.3
  • 69
    • 0242331744 scopus 로고    scopus 로고
    • Telomere repeat binding factors TRF1, TRF2, and hRAP1 modulate replication of Epstein-Barr virus OriP
    • Deng Z, Atanasiu C, Burg JS, Broccoli D, Lieberman PM (2003) Telomere repeat binding factors TRF1, TRF2, and hRAP1 modulate replication of Epstein-Barr virus OriP. J Virol 77: 11992-12001.
    • (2003) J Virol , vol.77 , pp. 11992-12001
    • Deng, Z.1    Atanasiu, C.2    Burg, J.S.3    Broccoli, D.4    Lieberman, P.M.5
  • 70
    • 1842424729 scopus 로고    scopus 로고
    • Resolution of sister telomere association is required for progression through mitosis
    • Dynek JN, Smith S (2004) Resolution of sister telomere association is required for progression through mitosis. Science 304: 97-100.
    • (2004) Science , vol.304 , pp. 97-100
    • Dynek, J.N.1    Smith, S.2
  • 71
    • 33947317206 scopus 로고    scopus 로고
    • The epigenetic regulation of mammalian telomeres
    • Blasco MA (2007) The epigenetic regulation of mammalian telomeres. Nat Rev Genet 8: 299-309.
    • (2007) Nat Rev Genet , vol.8 , pp. 299-309
    • Blasco, M.A.1
  • 72
    • 43349084022 scopus 로고    scopus 로고
    • Important role of Ser 219 phosphorylation of TRF1 in regulation of cell cycle
    • Xu YY, Lan JP, Zhu YY (2007) Important role of Ser 219 phosphorylation of TRF1 in regulation of cell cycle. Zhejiang Da Xue Xue Bao Yi Xue Ban 36: 325-330.
    • (2007) Zhejiang Da Xue Xue Bao Yi Xue Ban , vol.36 , pp. 325-330
    • Xu, Y.Y.1    Lan, J.P.2    Zhu, Y.Y.3
  • 73
    • 33644855565 scopus 로고    scopus 로고
    • The F-box protein FBX4 targets PIN2/TRF1 for ubiquitin-mediated degradation and regulates telomere maintenance
    • Lee TH, Perrem K, Harper JW, Lu KP, Zhou XZ (2006) The F-box protein FBX4 targets PIN2/TRF1 for ubiquitin-mediated degradation and regulates telomere maintenance. J Biol Chem 281: 759-768.
    • (2006) J Biol Chem , vol.281 , pp. 759-768
    • Lee, T.H.1    Perrem, K.2    Harper, J.W.3    Lu, K.P.4    Zhou, X.Z.5
  • 74
    • 33745651993 scopus 로고    scopus 로고
    • The Apollo 5' exonuclease functions together with TRF2 to protect telomeres from DNA repair
    • Lenain C, Bauwens S, Amiard S, Brunori M, Giraud-Panis MJ, et al. (2006) The Apollo 5' exonuclease functions together with TRF2 to protect telomeres from DNA repair. Curr Biol 16: 1303-1310.
    • (2006) Curr Biol , vol.16 , pp. 1303-1310
    • Lenain, C.1    Bauwens, S.2    Amiard, S.3    Brunori, M.4    Giraud-Panis, M.J.5
  • 75
    • 45849131324 scopus 로고    scopus 로고
    • Mutations in Fbx4 inhibit dimerization of the SCF(Fbx4) ligase and contribute to cyclin D1 overexpression in human cancer
    • Barbash O, Zamfirova P, Lin DI, Chen X, Yang K, et al. (2008) Mutations in Fbx4 inhibit dimerization of the SCF(Fbx4) ligase and contribute to cyclin D1 overexpression in human cancer. Cancer Cell 14: 68-78.
    • (2008) Cancer Cell , vol.14 , pp. 68-78
    • Barbash, O.1    Zamfirova, P.2    Lin, D.I.3    Chen, X.4    Yang, K.5


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