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Volumn 194, Issue 2, 2003, Pages 139-154

Biochemical aspects of telomerase function

Author keywords

Aging; Cancer; DNA replication; End replication; G rich overhang; Reverse transcriptase; Telomerase; Telomerase reverse transcriptase; Telomeres; Template RNA; Transformation; Tumor; Tumorigenesis

Indexed keywords

DNA; DNA PRIMASE; DYSKERIN; KU ANTIGEN; NUCLEOTIDE; PROTEIN EST1P; PROTEIN EST3P; PROTEIN L22; PROTEIN MTR10P; PROTEIN P23; PROTEIN P43; PROTEIN P80; PROTEIN SM; PROTEIN STAU; PROTEIN TEP1; RIBONUCLEOPROTEIN; RNA; RNA BINDING PROTEIN; RNA DIRECTED DNA POLYMERASE; SINGLE STRANDED DNA; TELOMERASE; UNCLASSIFIED DRUG;

EID: 0038701907     PISSN: 03043835     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-3835(02)00701-2     Document Type: Article
Times cited : (88)

References (235)
  • 2
    • 0000075523 scopus 로고
    • The behavior of successive nuclear divisions of a chromosome broken at meiosis
    • McClintock B. The behavior of successive nuclear divisions of a chromosome broken at meiosis. Proc. Natl Acad. Sci. USA. 24:1939;404-416.
    • (1939) Proc. Natl Acad. Sci. USA , vol.24 , pp. 404-416
    • McClintock, B.1
  • 3
    • 0001294157 scopus 로고
    • The stability of broken ends of chromosomes in zea mays
    • McClintock B. The stability of broken ends of chromosomes in zea mays. Genetics. 26:1941;234-282.
    • (1941) Genetics , vol.26 , pp. 234-282
    • McClintock, B.1
  • 4
    • 0017833637 scopus 로고
    • A tandomly repeated sequence at the termini of the extrachromosomal ribosomal rna genes in Tetrahymena
    • Blackburn E.H., Gall J. A tandomly repeated sequence at the termini of the extrachromosomal ribosomal rna genes in Tetrahymena. J. Mol. Biol. 120:1978;33-53.
    • (1978) J. Mol. Biol. , vol.120 , pp. 33-53
    • Blackburn, E.H.1    Gall, J.2
  • 5
    • 0021346699 scopus 로고
    • Elaboration of telomeres in yeast: Recognition and modification of termini from oxytricha macronuclear DNA
    • Pluta A.F., Dani G.M., Spear B.B., Zakian V.A. Elaboration of telomeres in yeast: recognition and modification of termini from oxytricha macronuclear DNA. Proc. Natl Acad. Sci. USA. 81:1984;1475-1479.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 1475-1479
    • Pluta, A.F.1    Dani, G.M.2    Spear, B.B.3    Zakian, V.A.4
  • 6
    • 0021234973 scopus 로고
    • DNA sequences of telomeres maintained in yeast
    • Shampay J., Szostak J.W., Blackburn E.H. DNA sequences of telomeres maintained in yeast. Nature. 310:1984;154-157.
    • (1984) Nature , vol.310 , pp. 154-157
    • Shampay, J.1    Szostak, J.W.2    Blackburn, E.H.3
  • 7
    • 0019949718 scopus 로고
    • Cloning yeast telomeres on linear plasmid vectors
    • Szostak J.W., Blackburn E.H. Cloning yeast telomeres on linear plasmid vectors. Cell. 29:1982;245-255.
    • (1982) Cell , vol.29 , pp. 245-255
    • Szostak, J.W.1    Blackburn, E.H.2
  • 8
    • 0020583113 scopus 로고
    • Growth of chromosomal ends in multiplying trypanosomes
    • Bernards A., Michels P.A.M., Lincke C.R., Borst P. Growth of chromosomal ends in multiplying trypanosomes. Nature. 303:1983;592-597.
    • (1983) Nature , vol.303 , pp. 592-597
    • Bernards, A.1    Michels, P.A.M.2    Lincke, C.R.3    Borst, P.4
  • 9
    • 0023669250 scopus 로고
    • Dynamics of telomere length variation in Tetrahymena thermophila
    • Larson D.D., Spangler E.A., Blackburn E.H. Dynamics of telomere length variation in Tetrahymena thermophila. Cell. 50:1987;477-483.
    • (1987) Cell , vol.50 , pp. 477-483
    • Larson, D.D.1    Spangler, E.A.2    Blackburn, E.H.3
  • 10
    • 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. 43:1985;405-413.
    • (1985) Cell , vol.43 , pp. 405-413
    • Greider, C.W.1    Blackburn, E.H.2
  • 11
    • 0023663881 scopus 로고
    • The telomere terminal transferase of Tetrahymena is a ribonucleoprotein enzyme with two kinds of primer specificity
    • Greider C.W., Blackburn E.H. The telomere terminal transferase of Tetrahymena is a ribonucleoprotein enzyme with two kinds of primer specificity. Cell. 51:1987;887-898.
    • (1987) Cell , vol.51 , pp. 887-898
    • Greider, C.W.1    Blackburn, E.H.2
  • 12
    • 0024978857 scopus 로고
    • A telomeric sequence in the rna of Tetrahymena telomerase required for telomere repeat synthesis
    • Greider C.W., Blackburn E.H. A telomeric sequence in the rna of Tetrahymena telomerase required for telomere repeat synthesis. Nature. 337:1989;331-337.
    • (1989) Nature , vol.337 , pp. 331-337
    • Greider, C.W.1    Blackburn, E.H.2
  • 13
    • 0025021235 scopus 로고
    • Functional evidence for an rna template in telomerase
    • Shippen-Lentz D., Blackburn E.H. Functional evidence for an rna template in telomerase. Science. 247:1990;546-552.
    • (1990) Science , vol.247 , pp. 546-552
    • Shippen-Lentz, D.1    Blackburn, E.H.2
  • 14
  • 15
    • 0024677875 scopus 로고
    • Telomere terminal transferase activity from euplotes crassus adds large numbers of tttgggg repeats onto telomeric primers
    • Shippen-Lentz D., Blackburn E.H. Telomere terminal transferase activity from euplotes crassus adds large numbers of tttgggg repeats onto telomeric primers. Mol. Biol. Cell. 9:1989;2761-2764.
    • (1989) Mol. Biol. Cell , vol.9 , pp. 2761-2764
    • Shippen-Lentz, D.1    Blackburn, E.H.2
  • 16
    • 0024325562 scopus 로고
    • The human telomere terminal transferase enzyme is a ribonucleoprotein that synthesizes ttaggg repeats
    • Morin G.B. The human telomere terminal transferase enzyme is a ribonucleoprotein that synthesizes ttaggg repeats. Cell. 59:1989;521-529.
    • (1989) Cell , vol.59 , pp. 521-529
    • Morin, G.B.1
  • 17
    • 0027467847 scopus 로고
    • Identification of a nonprocessive telomerase activity from mouse cells
    • Prowse K.R., Avilion A.A., Greider C.W. Identification of a nonprocessive telomerase activity from mouse cells. Proc. Natl Acad. Sci. USA. 90:1993;1493-1497.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 1493-1497
    • Prowse, K.R.1    Avilion, A.A.2    Greider, C.W.3
  • 18
    • 0029155795 scopus 로고
    • Telomerase in yeast
    • Cohn M., Blackburn E.H. Telomerase in yeast. Science. 269:1995;396-400.
    • (1995) Science , vol.269 , pp. 396-400
    • Cohn, M.1    Blackburn, E.H.2
  • 19
    • 0028356319 scopus 로고
    • Telomerase activity in germline and embryonic cells of xenopus
    • Mantell L.L., Greider C.W. Telomerase activity in germline and embryonic cells of xenopus. EMBO J. 13:1994;3211-3217.
    • (1994) EMBO J. , vol.13 , pp. 3211-3217
    • Mantell, L.L.1    Greider, C.W.2
  • 20
    • 0029955901 scopus 로고    scopus 로고
    • Characterization and developmental patterns of telomerase expression in plants
    • Fitzgerald M.S., McKnight T.D., Shippen D.E. Characterization and developmental patterns of telomerase expression in plants. Proc. Natl Acad. Sci. USA. 93:1996;14422-14427.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14422-14427
    • Fitzgerald, M.S.1    McKnight, T.D.2    Shippen, D.E.3
  • 25
    • 0033406877 scopus 로고    scopus 로고
    • Telomeres of polytene chromosomes in a ciliated protozoan terminate in duplex DNA loops
    • Murti K., Prescott D. Telomeres of polytene chromosomes in a ciliated protozoan terminate in duplex DNA loops. Proc. Natl Acad. Sci. USA. 96:1999;14436-14439.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 14436-14439
    • Murti, K.1    Prescott, D.2
  • 26
    • 0029894237 scopus 로고    scopus 로고
    • Telomere length regulation
    • Greider C.W. Telomere length regulation. Annu. Rev. Biochem. 65:1996;337-365.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 337-365
    • Greider, C.W.1
  • 27
    • 0029763191 scopus 로고    scopus 로고
    • Purification of telomerase from euplotes aediculatus: Requirement of a primer 3′ overhang
    • Lingner J., Cech T.R. Purification of telomerase from euplotes aediculatus: requirement of a primer 3′ overhang. Proc. Natl Acad. Sci. USA. 93:1996;10712-10717.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 10712-10717
    • Lingner, J.1    Cech, T.R.2
  • 28
    • 0025743438 scopus 로고
    • Telomerase primer specificity and chromosome healing
    • Harrington L.A., Greider C.W. Telomerase primer specificity and chromosome healing. Nature. 353:1991;451-454.
    • (1991) Nature , vol.353 , pp. 451-454
    • Harrington, L.A.1    Greider, C.W.2
  • 29
    • 0032481419 scopus 로고    scopus 로고
    • A novel specificity for the primer-template pairing requirement in Tetrahymena telomerase
    • Wang H., Gilley D., Blackburn E.H. A novel specificity for the primer-template pairing requirement in Tetrahymena telomerase. EMBO J. 17:1998;1152-1160.
    • (1998) EMBO J. , vol.17 , pp. 1152-1160
    • Wang, H.1    Gilley, D.2    Blackburn, E.H.3
  • 30
    • 0025808098 scopus 로고
    • Recognition of a chromosome truncation site associated with alpha-thalassaemia by human telomerase
    • Morin G.B. Recognition of a chromosome truncation site associated with alpha-thalassaemia by human telomerase. Nature. 353:1991;454-456.
    • (1991) Nature , vol.353 , pp. 454-456
    • Morin, G.B.1
  • 31
    • 0028856541 scopus 로고
    • Utilization of ribonucleotides and rna primers by Tetrahymena telomerase
    • Collins K., Greider C.W. Utilization of ribonucleotides and rna primers by Tetrahymena telomerase. EMBO J. 14:1995;5422-5432.
    • (1995) EMBO J. , vol.14 , pp. 5422-5432
    • Collins, K.1    Greider, C.W.2
  • 32
    • 0034604578 scopus 로고    scopus 로고
    • A mutant of Tetrahymena telomerase reverse transcriptase with increased processivity
    • Bryan T.M., Goodrich K.J., Cech T.R. A mutant of Tetrahymena telomerase reverse transcriptase with increased processivity. J. Biol. Chem. 275:2000;24199-24207.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24199-24207
    • Bryan, T.M.1    Goodrich, K.J.2    Cech, T.R.3
  • 33
    • 0027275438 scopus 로고
    • Tetrahymena telomerase catalyzes nucleolytic cleavage and nonprocessive elongation
    • Collins K., Greider C.W. Tetrahymena telomerase catalyzes nucleolytic cleavage and nonprocessive elongation. Genes Dev. 7:1993;1364-1376.
    • (1993) Genes Dev. , vol.7 , pp. 1364-1376
    • Collins, K.1    Greider, C.W.2
  • 34
    • 0035895954 scopus 로고    scopus 로고
    • Requirements for the dgtp-dependent repeat addition processivity of recombinant Tetrahymena telomerase
    • Hardy C.D., Schultz C.S., Collins K. Requirements for the dgtp-dependent repeat addition processivity of recombinant Tetrahymena telomerase. J. Biol. Chem. 276:2001;4863-4871.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4863-4871
    • Hardy, C.D.1    Schultz, C.S.2    Collins, K.3
  • 35
    • 0030850982 scopus 로고    scopus 로고
    • Dgtp-dependent processivity and possible template switching of euplotes telomerase
    • Hammond P.W., Cech T.R. Dgtp-dependent processivity and possible template switching of euplotes telomerase. Nucleic Acids Res. 25:1997;3698-3704.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3698-3704
    • Hammond, P.W.1    Cech, T.R.2
  • 36
    • 0032515965 scopus 로고    scopus 로고
    • Euplotes telomerase: Evidence for limited base-pairing during primer elongation and dgtp as an effector of translocation
    • Hammond P.W., Cech T.R. Euplotes telomerase: evidence for limited base-pairing during primer elongation and dgtp as an effector of translocation. Biochemistry. 37:1998;5162-5172.
    • (1998) Biochemistry , vol.37 , pp. 5162-5172
    • Hammond, P.W.1    Cech, T.R.2
  • 37
    • 0031026387 scopus 로고    scopus 로고
    • The anchor site of telomerase from euplotes aediculatus revealed by photo-cross-linking to single- and double-stranded DNA primers
    • Hammond P.W., Lively T.N., Cech T.R. The anchor site of telomerase from euplotes aediculatus revealed by photo-cross-linking to single- and double-stranded DNA primers. Mol. Cell. Biol. 17:1997;296-308.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 296-308
    • Hammond, P.W.1    Lively, T.N.2    Cech, T.R.3
  • 38
    • 0031053530 scopus 로고    scopus 로고
    • De novo telomere addition by Tetrahymena telomerase in vitro
    • Wang H., Blackburn E.H. De novo telomere addition by Tetrahymena telomerase in vitro. EMBO J. 16:1997;866-879.
    • (1997) EMBO J. , vol.16 , pp. 866-879
    • Wang, H.1    Blackburn, E.H.2
  • 39
    • 0027486026 scopus 로고
    • Sequence-specific DNA primer effects on telomerase polymerization activity
    • Lee M.S., Blackburn E.H. Sequence-specific DNA primer effects on telomerase polymerization activity. Mol. Cell. Biol. 13:1993;6586-6599.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6586-6599
    • Lee, M.S.1    Blackburn, E.H.2
  • 40
    • 0025914141 scopus 로고
    • Telomerase is processive
    • Greider C.W. Telomerase is processive. Mol. Cell. Biol. 11:1991;4572-4580.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4572-4580
    • Greider, C.W.1
  • 41
    • 0030781067 scopus 로고    scopus 로고
    • Functionally interacting telomerase rnas in the yeast telomerase complex
    • Prescott J., Blackburn E.H. Functionally interacting telomerase rnas in the yeast telomerase complex. Genes Dev. 11:1997;2790-2800.
    • (1997) Genes Dev. , vol.11 , pp. 2790-2800
    • Prescott, J.1    Blackburn, E.H.2
  • 42
    • 0034662244 scopus 로고    scopus 로고
    • Telomerase-dependent repeat divergence at the 3′ ends of yeast telomeres
    • Forstemann K., Hoss M., Lingner J. Telomerase-dependent repeat divergence at the 3′ ends of yeast telomeres. Nucleic Acids Res. 28:2000;2690-2694.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2690-2694
    • Forstemann, K.1    Hoss, M.2    Lingner, J.3
  • 44
    • 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. 18:1999;3509-3519.
    • (1999) EMBO J. , vol.18 , pp. 3509-3519
    • Marcand, S.1    Brevet, V.2    Gilson, E.3
  • 45
    • 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. 275:1997;986-990.
    • (1997) Science , vol.275 , pp. 986-990
    • Marcand, S.1    Gilson, E.2    Shore, D.3
  • 46
    • 0024535634 scopus 로고
    • Introduction of extra telomeric DNA sequences into Saccharomyces cerevisiae results in telomere elongation
    • Runge K.W., Zakian V.A. Introduction of extra telomeric DNA sequences into Saccharomyces cerevisiae results in telomere elongation. Mol. Cell. Biol. 9:1989;1488-1497.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1488-1497
    • Runge, K.W.1    Zakian, V.A.2
  • 47
    • 0031910824 scopus 로고    scopus 로고
    • The c terminus of the major yeast telomere binding protein rap1p enhances telomere formation
    • Ray A., Runge K.W. The c terminus of the major yeast telomere binding protein rap1p enhances telomere formation. Mol. Cell. Biol. 18:1998;1284-1295.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1284-1295
    • Ray, A.1    Runge, K.W.2
  • 48
    • 0033592935 scopus 로고    scopus 로고
    • Varying the number of telomere-bound proteins does not alter telomere length in tel1delta cells
    • Ray A., Runge K.W. Varying the number of telomere-bound proteins does not alter telomere length in tel1delta cells. Proc. Natl Acad. Sci. USA. 96:1999;15044-15049.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 15044-15049
    • Ray, A.1    Runge, K.W.2
  • 49
    • 0032913466 scopus 로고    scopus 로고
    • The yeast telomere length counting machinery is sensitive to sequences at the telomere-nontelomere junction
    • Ray A., Runge K.W. The yeast telomere length counting machinery is sensitive to sequences at the telomere-nontelomere junction. Mol. Cell. Biol. 19:1999;31-45.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 31-45
    • Ray, A.1    Runge, K.W.2
  • 50
    • 0030995534 scopus 로고    scopus 로고
    • A novel rap1p-interacting factor, rif2p, cooperates with rif1p to regulate telomere length in Saccharomyces cerevisiae
    • Wotton D., Shore D. A novel rap1p-interacting factor, rif2p, cooperates with rif1p to regulate telomere length in Saccharomyces cerevisiae. Genes Dev. 11:1997;748-760.
    • (1997) Genes Dev. , vol.11 , pp. 748-760
    • Wotton, D.1    Shore, D.2
  • 51
    • 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. 21:2001;8117-8128.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8117-8128
    • Grossi, S.1    Bianchi, A.2    Damay, P.3    Shore, D.4
  • 52
    • 0031027618 scopus 로고    scopus 로고
    • Control of telomere length by the human telomeric protein trf1
    • van Steensel B., de Lange T. Control of telomere length by the human telomeric protein trf1. Nature. 385:1997;740-743.
    • (1997) Nature , vol.385 , pp. 740-743
    • Van Steensel, B.1    De Lange, T.2
  • 54
    • 0035929353 scopus 로고    scopus 로고
    • Switching and signaling at the telomere
    • Blackburn E.H. Switching and signaling at the telomere. Cell. 106:2001;661-673.
    • (2001) Cell , vol.106 , pp. 661-673
    • Blackburn, E.H.1
  • 55
    • 0028917465 scopus 로고
    • Gel shift and uv cross-linking analysis of Tetrahymena telomerase
    • Harrington L., Hull C., Crittenden J., Greider C. Gel shift and uv cross-linking analysis of Tetrahymena telomerase. J. Biol. Chem. 270:1995;8893-8901.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8893-8901
    • Harrington, L.1    Hull, C.2    Crittenden, J.3    Greider, C.4
  • 57
    • 0030977010 scopus 로고    scopus 로고
    • Developmentally regulated initiation of DNA synthesis by telomerase: Evidence for factor-assisted de novo telomere formation
    • Bednenko J., Melek M., Greene E.C., Shippen D.E. Developmentally regulated initiation of DNA synthesis by telomerase: Evidence for factor-assisted de novo telomere formation. EMBO J. 16:1997;2507-2518.
    • (1997) EMBO J. , vol.16 , pp. 2507-2518
    • Bednenko, J.1    Melek, M.2    Greene, E.C.3    Shippen, D.E.4
  • 58
    • 0029895352 scopus 로고    scopus 로고
    • Processing of nontelomeric 3′ ends by telomerase: Default template alignment and endonucleolytic cleavage
    • Melek M., Greene E.C., Shippen D.E. Processing of nontelomeric 3′ ends by telomerase: default template alignment and endonucleolytic cleavage. Mol. Cell. Biol. 16:1996;3437-3445.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3437-3445
    • Melek, M.1    Greene, E.C.2    Shippen, D.E.3
  • 59
    • 0032555261 scopus 로고    scopus 로고
    • The reverse transcriptase component of the Tetrahymena telomerase ribonucleoprotein complex
    • Collins K., Gandhi L. The reverse transcriptase component of the Tetrahymena telomerase ribonucleoprotein complex. Proc. Natl Acad. Sci. USA. 95:1998;8485-8490.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8485-8490
    • Collins, K.1    Gandhi, L.2
  • 60
    • 0033816358 scopus 로고    scopus 로고
    • Characterization of the interaction between the nuclease and reverse transcriptase activity of the yeast telomerase complex
    • Niu H., Xia J., Lue N.F. Characterization of the interaction between the nuclease and reverse transcriptase activity of the yeast telomerase complex. Mol. Cell. Biol. 20:2000;6806-6815.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6806-6815
    • Niu, H.1    Xia, J.2    Lue, N.F.3
  • 61
    • 0027944347 scopus 로고
    • Tlc1: Template rna component of Saccharomyces cerevisiae telomerase
    • Singer M.S., Gottschling D.E. Tlc1: template rna component of Saccharomyces cerevisiae telomerase. Science. 266:1994;404-409.
    • (1994) Science , vol.266 , pp. 404-409
    • Singer, M.S.1    Gottschling, D.E.2
  • 62
    • 0029154735 scopus 로고
    • Functional characterization and developmental regulation of mouse telomerase rna
    • Blasco M.A., Funk W., Villeponteau B., Greider C.W. Functional characterization and developmental regulation of mouse telomerase rna. Science. 269:1995;1267-1270.
    • (1995) Science , vol.269 , pp. 1267-1270
    • Blasco, M.A.1    Funk, W.2    Villeponteau, B.3    Greider, C.W.4
  • 65
    • 0028029818 scopus 로고
    • Architecture of telomerase rna
    • Bhattacharyya A., Blackburn E.H. Architecture of telomerase rna. EMBO J. 13:1994;5721-5723.
    • (1994) EMBO J. , vol.13 , pp. 5721-5723
    • Bhattacharyya, A.1    Blackburn, E.H.2
  • 66
    • 0028106199 scopus 로고
    • Telomerase rnas of different ciliates have a common secondary structure and a permuted template
    • Lingner J., Hendrick L.L., Cech T.R. Telomerase rnas of different ciliates have a common secondary structure and a permuted template. Genes Dev. 8:1994;1984-1998.
    • (1994) Genes Dev. , vol.8 , pp. 1984-1998
    • Lingner, J.1    Hendrick, L.L.2    Cech, T.R.3
  • 67
    • 0025944831 scopus 로고
    • A conserved secondary structure for telomerase rna
    • Romero D.P., Blackburn E.H. A conserved secondary structure for telomerase rna. Cell. 67:1991;343-353.
    • (1991) Cell , vol.67 , pp. 343-353
    • Romero, D.P.1    Blackburn, E.H.2
  • 68
  • 70
    • 0034598919 scopus 로고    scopus 로고
    • Secondary structure of vertebrate telomerase rna
    • Chen J.L., Blasco M.A., Greider C.W. Secondary structure of vertebrate telomerase rna. Cell. 100:2000;503-514.
    • (2000) Cell , vol.100 , pp. 503-514
    • Chen, J.L.1    Blasco, M.A.2    Greider, C.W.3
  • 71
    • 0028269621 scopus 로고
    • Functional reconstitution of wild-type and mutant Tetrahymena telomerase
    • Autexier C., Greider C.W. Functional reconstitution of wild-type and mutant Tetrahymena telomerase. Genes Dev. 8:1994;563-575.
    • (1994) Genes Dev. , vol.8 , pp. 563-575
    • Autexier, C.1    Greider, C.W.2
  • 72
    • 0029128539 scopus 로고
    • Boundary elements of the Tetrahymena telomerase rna template and alignment domains
    • Autexier C., Greider C.W. Boundary elements of the Tetrahymena telomerase rna template and alignment domains. Genes Dev. 9:1995;2227-2239.
    • (1995) Genes Dev. , vol.9 , pp. 2227-2239
    • Autexier, C.1    Greider, C.W.2
  • 73
    • 0029958047 scopus 로고    scopus 로고
    • Reconstitution of human telomerase activity and identification of a minimal functional region of the human telomerase rna
    • Autexier C., Pruzan R., Funk W.D., Greider C.W. Reconstitution of human telomerase activity and identification of a minimal functional region of the human telomerase rna. EMBO J. 15:1996;5928-5935.
    • (1996) EMBO J. , vol.15 , pp. 5928-5935
    • Autexier, C.1    Pruzan, R.2    Funk, W.D.3    Greider, C.W.4
  • 74
    • 0033562332 scopus 로고    scopus 로고
    • Tetrahymena telomerase ribonucleoprotein rna-protein interactions
    • Autexier C., Triki I. Tetrahymena telomerase ribonucleoprotein rna-protein interactions. Nucleic Acids Res. 27:1999;2227-2234.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2227-2234
    • Autexier, C.1    Triki, I.2
  • 75
  • 77
    • 0033790120 scopus 로고    scopus 로고
    • Polymerization defects within human telomerase are distinct from telomerase rna and tep1 binding
    • Beattie T.L., Zhou W., Robinson M.O., Harrington L. Polymerization defects within human telomerase are distinct from telomerase rna and tep1 binding. Mol. Biol. Cell. 11:2000;3329-3340.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3329-3340
    • Beattie, T.L.1    Zhou, W.2    Robinson, M.O.3    Harrington, L.4
  • 78
    • 0035723994 scopus 로고    scopus 로고
    • Functional multimerization of the human telomerase reverse transcriptase
    • Beattie T.L., Zhou W., Robinson M.O., Harrington L. Functional multimerization of the human telomerase reverse transcriptase. Mol. Cell. Biol. 21:2001;6151-6160.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6151-6160
    • Beattie, T.L.1    Zhou, W.2    Robinson, M.O.3    Harrington, L.4
  • 80
    • 0035912746 scopus 로고    scopus 로고
    • A stem-loop of Tetrahymena telomerase rna distant from the template potentiates rna folding and telomerase activity
    • Sperger J.M., Cech T.R. A stem-loop of Tetrahymena telomerase rna distant from the template potentiates rna folding and telomerase activity. Biochemistry. 40:2001;7005-7016.
    • (2001) Biochemistry , vol.40 , pp. 7005-7016
    • Sperger, J.M.1    Cech, T.R.2
  • 81
    • 0032004614 scopus 로고    scopus 로고
    • Mutational analysis of the Tetrahymena telomerase rna: Identification of residues affecting telomerase activity in vitro
    • Autexier C., Greider C.W. Mutational analysis of the Tetrahymena telomerase rna: identification of residues affecting telomerase activity in vitro. Nucleic Acids Res. 26:1998;787-795.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 787-795
    • Autexier, C.1    Greider, C.W.2
  • 82
    • 0033134835 scopus 로고    scopus 로고
    • Telomerase rna function in recombinant Tetrahymena telomerase
    • Licht J.D., Collins K. Telomerase rna function in recombinant Tetrahymena telomerase. Genes Dev. 13:1999;1116-1125.
    • (1999) Genes Dev. , vol.13 , pp. 1116-1125
    • Licht, J.D.1    Collins, K.2
  • 83
    • 0037083759 scopus 로고    scopus 로고
    • Template boundary definition in Tetrahymena telomerase
    • Lai C.K., Miller M.C., Collins K. Template boundary definition in Tetrahymena telomerase. Genes Dev. 16:2002;415-420.
    • (2002) Genes Dev. , vol.16 , pp. 415-420
    • Lai, C.K.1    Miller, M.C.2    Collins, K.3
  • 84
    • 0033535962 scopus 로고    scopus 로고
    • The telomerase rna pseudoknot is critical for the stable assembly of a catalytically active ribonucleoprotein
    • Gilley D., Blackburn E.H. The telomerase rna pseudoknot is critical for the stable assembly of a catalytically active ribonucleoprotein. Proc. Natl Acad. Sci. USA. 96:1999;6621-6625.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6621-6625
    • Gilley, D.1    Blackburn, E.H.2
  • 85
    • 0029144984 scopus 로고
    • Altering specific telomerase rna template residues affects active site function
    • Gilley D., Lee M.S., Blackburn E.H. Altering specific telomerase rna template residues affects active site function. Genes Dev. 9:1995;2214-2226.
    • (1995) Genes Dev. , vol.9 , pp. 2214-2226
    • Gilley, D.1    Lee, M.S.2    Blackburn, E.H.3
  • 86
    • 0029655261 scopus 로고    scopus 로고
    • Specific rna residue interactions required for enzymatic functions of Tetrahymena telomerase
    • Gilley D., Blackburn E.H. Specific rna residue interactions required for enzymatic functions of Tetrahymena telomerase. Mol. Cell. Biol. 16:1996;66-75.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 66-75
    • Gilley, D.1    Blackburn, E.H.2
  • 87
    • 0034608073 scopus 로고    scopus 로고
    • Template boundary in a yeast telomerase specified by rna structure
    • Tzfati Y., Fulton T.B., Roy J., Blackburn E.H. Template boundary in a yeast telomerase specified by rna structure. Science. 288:2000;863-867.
    • (2000) Science , vol.288 , pp. 863-867
    • Tzfati, Y.1    Fulton, T.B.2    Roy, J.3    Blackburn, E.H.4
  • 88
    • 0037076276 scopus 로고    scopus 로고
    • Telomerase recognizes its template by using an adjacent rna motif
    • Miller M.C., Collins K. Telomerase recognizes its template by using an adjacent rna motif. Proc. Natl Acad. Sci. USA. 99:2002;6585-6590.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 6585-6590
    • Miller, M.C.1    Collins, K.2
  • 89
    • 0032532428 scopus 로고    scopus 로고
    • Specific telomerase rna residues distant from the template are essential for telomerase function
    • Roy J., Fulton T.B., Blackburn E.H. Specific telomerase rna residues distant from the template are essential for telomerase function. Genes Dev. 12:1998;3286-3300.
    • (1998) Genes Dev. , vol.12 , pp. 3286-3300
    • Roy, J.1    Fulton, T.B.2    Blackburn, E.H.3
  • 90
    • 0036118479 scopus 로고    scopus 로고
    • Essential regions of Saccharomyces cerevisiae telomerase rna: Separate elements for est1p and est2p interaction
    • Livengood A.J., Zaug A.J., Cech T.R. Essential regions of Saccharomyces cerevisiae telomerase rna: separate elements for est1p and est2p interaction. Mol. Cell. Biol. 22:2002;2366-2374.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2366-2374
    • Livengood, A.J.1    Zaug, A.J.2    Cech, T.R.3
  • 92
    • 0037082416 scopus 로고    scopus 로고
    • Analysis of the structure of human telomerase rna in vivo
    • Antal M., Boros E., Solymosy F., Kiss T. Analysis of the structure of human telomerase rna in vivo. Nucleic Acids Res. 30:2002;912-920.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 912-920
    • Antal, M.1    Boros, E.2    Solymosy, F.3    Kiss, T.4
  • 93
    • 0035137710 scopus 로고    scopus 로고
    • Functional regions of human telomerase reverse transcriptase and human telomerase rna required for telomerase activity and rna-protein interactions
    • Bachand F., Autexier C. Functional regions of human telomerase reverse transcriptase and human telomerase rna required for telomerase activity and rna-protein interactions. Mol. Cell. Biol. 21:2001;1888-1897.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1888-1897
    • Bachand, F.1    Autexier, C.2
  • 94
    • 0035937133 scopus 로고    scopus 로고
    • Identification of functional domains and dominant negative mutations in vertebrate telomerase rna using an in vivo reconstitution system
    • Martin-Rivera L., Blasco M.A. Identification of functional domains and dominant negative mutations in vertebrate telomerase rna using an in vivo reconstitution system. J. Biol. Chem. 276:2001;5856-5865.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5856-5865
    • Martin-Rivera, L.1    Blasco, M.A.2
  • 95
    • 0033636897 scopus 로고    scopus 로고
    • Human telomerase activation requires two independent interactions between telomerase rna and telomerase reverse transcriptase
    • Mitchell J.R., Collins K. Human telomerase activation requires two independent interactions between telomerase rna and telomerase reverse transcriptase. Mol. Cell. 6:2000;361-371.
    • (2000) Mol. Cell , vol.6 , pp. 361-371
    • Mitchell, J.R.1    Collins, K.2
  • 96
    • 0037079673 scopus 로고    scopus 로고
    • A critical stem-loop structure in the cr4-cr5 domain of mammalian telomerase rna
    • Chen J.L., Opperman K.K., Greider C.W. A critical stem-loop structure in the cr4-cr5 domain of mammalian telomerase rna. Nucleic Acids Res. 30:2002;592-597.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 592-597
    • Chen, J.L.1    Opperman, K.K.2    Greider, C.W.3
  • 97
  • 98
    • 0030721677 scopus 로고    scopus 로고
    • Polyadenylation of telomerase rna in budding yeast
    • Chapon C., Cech T.R., Zaug A.J. Polyadenylation of telomerase rna in budding yeast. RNA. 3:1997;1337-1351.
    • (1997) RNA , vol.3 , pp. 1337-1351
    • Chapon, C.1    Cech, T.R.2    Zaug, A.J.3
  • 99
    • 0033539171 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae telomerase is a small nuclear ribonucleoprotein particle
    • Seto A.G., Zaug A.J., Sobel S.G., Wolin S.L., Cech T.R. Saccharomyces cerevisiae telomerase is a small nuclear ribonucleoprotein particle. Nature. 401:1999;177-180.
    • (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
  • 101
    • 0029866229 scopus 로고    scopus 로고
    • Method for determining rna 3′ ends and application to human telomerase rna
    • Zaug A.J., Linger J., Cech T.R. Method for determining rna 3′ ends and application to human telomerase rna. Nucleic Acids Res. 24:1996;532-533.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 532-533
    • Zaug, A.J.1    Linger, J.2    Cech, T.R.3
  • 102
    • 0036734655 scopus 로고    scopus 로고
    • The product of the survival of motor neuron (smn) gene is a human telomerase-associated protein
    • Bachand F., Boisvert F.M., Cote J., Richard S., Autexier C. The product of the survival of motor neuron (smn) gene is a human telomerase-associated protein. Mol. Biol. Cell. 13:2002;3192-3202.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3192-3202
    • Bachand, F.1    Boisvert, F.M.2    Cote, J.3    Richard, S.4    Autexier, C.5
  • 105
    • 0034933876 scopus 로고    scopus 로고
    • A low threshold level of expression of mutant-template telomerase rna inhibits human tumor cell proliferation
    • Kim M.M., Rivera M.A., Botchkina I.L., Shalaby R., Thor A.D., Blackburn E.H. A low threshold level of expression of mutant-template telomerase rna inhibits human tumor cell proliferation. Proc. Natl Acad Sci. USA. 98:2001;7982-7987.
    • (2001) Proc. Natl Acad Sci. USA , vol.98 , pp. 7982-7987
    • Kim, M.M.1    Rivera, M.A.2    Botchkina, I.L.3    Shalaby, R.4    Thor, A.D.5    Blackburn, E.H.6
  • 106
    • 0035825601 scopus 로고    scopus 로고
    • Expression of mutant telomerase in immortal telomerase-negative human cells results in cell cycle deregulation, nuclear and chromosomal abnormalities and rapid loss of viability
    • Guiducci C., Cerone M.A., Bacchetti S. Expression of mutant telomerase in immortal telomerase-negative human cells results in cell cycle deregulation, nuclear and chromosomal abnormalities and rapid loss of viability. Oncogene. 20:2001;714-725.
    • (2001) Oncogene , vol.20 , pp. 714-725
    • Guiducci, C.1    Cerone, M.A.2    Bacchetti, S.3
  • 107
    • 0035325159 scopus 로고    scopus 로고
    • Transient expression of wild-type or biologically inactive telomerase allows the formation of artificial telomeres in mortal human cells
    • Guiducci C., Anglana M., Wang A., Bacchetti S. Transient expression of wild-type or biologically inactive telomerase allows the formation of artificial telomeres in mortal human cells. Exp. Cell Res. 265:2001;304-311.
    • (2001) Exp. Cell Res. , vol.265 , pp. 304-311
    • Guiducci, C.1    Anglana, M.2    Wang, A.3    Bacchetti, S.4
  • 108
    • 0031047642 scopus 로고    scopus 로고
    • Block in anaphase chromosome separation caused by a telomerase template mutation
    • Kirk K.E., Harmon B.P., Reichardt I.K., Sedat J.W., Blackburn E.H. Block in anaphase chromosome separation caused by a telomerase template mutation. Science. 275:1997;1478-1481.
    • (1997) Science , vol.275 , pp. 1478-1481
    • Kirk, K.E.1    Harmon, B.P.2    Reichardt, I.K.3    Sedat, J.W.4    Blackburn, E.H.5
  • 109
    • 0029743764 scopus 로고    scopus 로고
    • Control of telomere growth by interactions of rap1 with the most distal telomeric repeats
    • Krauskopf A., Blackburn E.H. Control of telomere growth by interactions of rap1 with the most distal telomeric repeats. Nature. 383:1996;354-357.
    • (1996) Nature , vol.383 , pp. 354-357
    • Krauskopf, A.1    Blackburn, E.H.2
  • 110
    • 0029102354 scopus 로고
    • Runaway telomere elongation caused by telomerase rna gene mutations
    • McEachern M.J., Blackburn E.H. Runaway telomere elongation caused by telomerase rna gene mutations. Nature. 376:1995;403-409.
    • (1995) Nature , vol.376 , pp. 403-409
    • McEachern, M.J.1    Blackburn, E.H.2
  • 111
    • 0025279059 scopus 로고
    • In vivo alteration of telomere sequences and senescence caused by mutated Tetrahymena telomerase rnas
    • Yu G.L., Bradley J.D., Attardi L.D., Blackburn E.H. In vivo alteration of telomere sequences and senescence caused by mutated Tetrahymena telomerase rnas. Nature. 344:1990;126-132.
    • (1990) Nature , vol.344 , pp. 126-132
    • Yu, G.L.1    Bradley, J.D.2    Attardi, L.D.3    Blackburn, E.H.4
  • 113
    • 0345643517 scopus 로고    scopus 로고
    • Uncapping and deregulation of telomeres lead to detrimental cellular consequences in yeast
    • Smith C.D., Blackburn E.H. Uncapping and deregulation of telomeres lead to detrimental cellular consequences in yeast. J. Cell Biol. 145:1999;203-214.
    • (1999) J. Cell Biol. , vol.145 , pp. 203-214
    • Smith, C.D.1    Blackburn, E.H.2
  • 114
    • 0036333825 scopus 로고    scopus 로고
    • Biogenesis of yeast telomerase depends on the importin mtr10
    • Ferrezuelo F., Steiner B., Aldea M., Futcher B. Biogenesis of yeast telomerase depends on the importin mtr10. Mol. Cell. Biol. 22:2002;6046-6055.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6046-6055
    • Ferrezuelo, F.1    Steiner, B.2    Aldea, M.3    Futcher, B.4
  • 115
    • 0343183144 scopus 로고    scopus 로고
    • In vitro assembly of human h/aca small nucleolar rnps reveals unique features of u17 and telomerase rnas
    • Dragon F., Pogacic V., Filipowicz W. In vitro assembly of human h/aca small nucleolar rnps reveals unique features of u17 and telomerase rnas. Mol. Cell. Biol. 20:2000;3037-3048.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3037-3048
    • Dragon, F.1    Pogacic, V.2    Filipowicz, W.3
  • 116
    • 0032961170 scopus 로고    scopus 로고
    • A box h/aca small nucleolar rna-like domain at the human telomerase rna 3′ end
    • Mitchell J.R., Cheng J., Collins K. A box h/aca small nucleolar rna-like domain at the human telomerase rna 3′ end. Mol. Cell. Biol. 19:1999;567-576.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 567-576
    • Mitchell, J.R.1    Cheng, J.2    Collins, K.3
  • 117
    • 0035670851 scopus 로고    scopus 로고
    • The snorna domain of vertebrate telomerase rna functions to localize the rna within the nucleus
    • Lukowiak A.A., Narayanan A., Li Z.H., Terns R.M., Terns M.P. The snorna domain of vertebrate telomerase rna functions to localize the rna within the nucleus. RNA. 7:2001;1833-1844.
    • (2001) RNA , vol.7 , pp. 1833-1844
    • Lukowiak, A.A.1    Narayanan, A.2    Li, Z.H.3    Terns, R.M.4    Terns, M.P.5
  • 118
    • 0035960043 scopus 로고    scopus 로고
    • The rna component of telomerase is mutated in autosomal dominant dyskeratosis congenita
    • Vulliamy T., Marrone A., Goldman F., Dearlove A., Bessler M., Mason P.J., Dokal I. The rna component of telomerase is mutated in autosomal dominant dyskeratosis congenita. Nature. 413:2001;432-435.
    • (2001) Nature , vol.413 , pp. 432-435
    • Vulliamy, T.1    Marrone, A.2    Goldman, F.3    Dearlove, A.4    Bessler, M.5    Mason, P.J.6    Dokal, I.7
  • 119
    • 0034966374 scopus 로고    scopus 로고
    • Very short telomeres in the peripheral blood of patients with x-linked and autosomal dyskeratosis congenita
    • Vulliamy T.J., Knight S.W., Mason P.J., Dokal I. Very short telomeres in the peripheral blood of patients with x-linked and autosomal dyskeratosis congenita. Blood Cells Mol. Dis. 27:2001;353-357.
    • (2001) Blood Cells Mol. Dis. , vol.27 , pp. 353-357
    • Vulliamy, T.J.1    Knight, S.W.2    Mason, P.J.3    Dokal, I.4
  • 120
    • 0028990123 scopus 로고
    • Purification of Tetrahymena telomerase and cloning of genes encoding the two protein components of the enzyme
    • Collins K., Kobayashi R., Greider C.W. Purification of Tetrahymena telomerase and cloning of genes encoding the two protein components of the enzyme. Cell. 81:1995;677-686.
    • (1995) Cell , vol.81 , pp. 677-686
    • Collins, K.1    Kobayashi, R.2    Greider, C.W.3
  • 121
    • 0030455861 scopus 로고    scopus 로고
    • Senescence mutants of Saccharomyces cerevisiae with a defect in telomere replication identify three additional est genes
    • Lendvay T.S., Morris D.K., Sah J., Balasubramanian B., Lundblad V. Senescence mutants of Saccharomyces cerevisiae with a defect in telomere replication identify three additional est genes. Genetics. 144:1996;1399-1412.
    • (1996) Genetics , vol.144 , pp. 1399-1412
    • Lendvay, T.S.1    Morris, D.K.2    Sah, J.3    Balasubramanian, B.4    Lundblad, V.5
  • 129
    • 0034872133 scopus 로고    scopus 로고
    • Two telomerase reverse transcriptases (terts) expressed in Candida albicans
    • Metz A.M., Love R.A., Strobel G.A., Long D.M. Two telomerase reverse transcriptases (terts) expressed in Candida albicans. Biotechnol. Appl. Biochem. 34:2001;47-54.
    • (2001) Biotechnol. Appl. Biochem. , vol.34 , pp. 47-54
    • Metz, A.M.1    Love, R.A.2    Strobel, G.A.3    Long, D.M.4
  • 130
    • 0032555275 scopus 로고    scopus 로고
    • Telomerase reverse transcriptase genes identified in Tetrahymena thermophila and oxytricha trifallax
    • Bryan T.M., Sperger J.M., Chapman K.B., Cech T.R. Telomerase reverse transcriptase genes identified in Tetrahymena thermophila and oxytricha trifallax. Proc. Natl Acad. Sci. USA. 95:1998;8479-8484.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8479-8484
    • Bryan, T.M.1    Sperger, J.M.2    Chapman, K.B.3    Cech, T.R.4
  • 131
    • 0033593035 scopus 로고    scopus 로고
    • Disruption of the telomerase catalytic subunit gene from arabidopsis inactivates telomerase and leads to a slow loss of telomeric DNA
    • Fitzgerald M.S., Riha K., Gao F., Ren S., McKnight T.D., Shippen D.E. Disruption of the telomerase catalytic subunit gene from arabidopsis inactivates telomerase and leads to a slow loss of telomeric DNA. Proc. Natl Acad. Sci. USA. 96:1999;14813-14818.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 14813-14818
    • Fitzgerald, M.S.1    Riha, K.2    Gao, F.3    Ren, S.4    McKnight, T.D.5    Shippen, D.E.6
  • 132
    • 0032168370 scopus 로고    scopus 로고
    • Expression of mouse telomerase catalytic subunit in embryos and adult tissues
    • Martin-Rivera L., Herrera E., Albar J.P., Blasco M.A. Expression of mouse telomerase catalytic subunit in embryos and adult tissues. Proc. Natl Acad. Sci. USA. 95:1998;10471-10476.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 10471-10476
    • Martin-Rivera, L.1    Herrera, E.2    Albar, J.P.3    Blasco, M.A.4
  • 133
    • 0034720806 scopus 로고    scopus 로고
    • Putative telomerase catalytic subunits from Giardia lamblia and Caenorhabditis elegans
    • Malik H.S., Burke W.D., Eickbush T.H. Putative telomerase catalytic subunits from Giardia lamblia and Caenorhabditis elegans. Gene. 251:2000;101-108.
    • (2000) Gene , vol.251 , pp. 101-108
    • Malik, H.S.1    Burke, W.D.2    Eickbush, T.H.3
  • 136
    • 0037133668 scopus 로고    scopus 로고
    • Preferential maintenance of critically short telomeres in mammalian cells heterozygous for mtert
    • Liu Y., Kha H., Ungrin M., Robinson M.O., Harrington L. Preferential maintenance of critically short telomeres in mammalian cells heterozygous for mtert. Proc. Natl Acad. Sci. USA. 99:2002;3597-3602.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 3597-3602
    • Liu, Y.1    Kha, H.2    Ungrin, M.3    Robinson, M.O.4    Harrington, L.5
  • 137
    • 0032962953 scopus 로고    scopus 로고
    • The human telomerase catalytic subunit htert: Organization of the gene and characterization of the promoter
    • Cong Y.S., Wen J., Bacchetti S. The human telomerase catalytic subunit htert: organization of the gene and characterization of the promoter. Hum. Mol. Genet. 8:1999;137-142.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 137-142
    • Cong, Y.S.1    Wen, J.2    Bacchetti, S.3
  • 143
    • 0032530136 scopus 로고    scopus 로고
    • Telomerase activity in human development is regulated by human telomerase reverse transcriptase (htert) transcription and by alternate splicing of htert transcripts
    • Ulaner G.A., Hu J.F., Vu T.H., Giudice L.C., Hoffman A.R. Telomerase activity in human development is regulated by human telomerase reverse transcriptase (htert) transcription and by alternate splicing of htert transcripts. Cancer Res. 58:1998;4168-4172.
    • (1998) Cancer Res. , vol.58 , pp. 4168-4172
    • Ulaner, G.A.1    Hu, J.F.2    Vu, T.H.3    Giudice, L.C.4    Hoffman, A.R.5
  • 144
    • 0033988011 scopus 로고    scopus 로고
    • Regulation of telomerase by alternate splicing of human telomerase reverse transcriptase (htert) in normal and neoplastic ovary endometrium and myometrium
    • Ulaner G.A., Hu J.F., Vu T.H., Oruganti H., Giudice L.C., Hoffman A.R. Regulation of telomerase by alternate splicing of human telomerase reverse transcriptase (htert) in normal and neoplastic ovary endometrium and myometrium. Int. J. Cancer. 85:2000;330-335.
    • (2000) Int. J. Cancer , vol.85 , pp. 330-335
    • Ulaner, G.A.1    Hu, J.F.2    Vu, T.H.3    Oruganti, H.4    Giudice, L.C.5    Hoffman, A.R.6
  • 145
    • 0035283896 scopus 로고    scopus 로고
    • Tissue-specific alternate splicing of human telomerase reverse transcriptase (htert) influences telomere lengths during human development
    • Ulaner G.A., Hu J.F., Vu T.H., Giudice L.C., Hoffman A.R. Tissue-specific alternate splicing of human telomerase reverse transcriptase (htert) influences telomere lengths during human development. Int. J. Cancer. 91:2001;644-649.
    • (2001) Int. J. Cancer , vol.91 , pp. 644-649
    • Ulaner, G.A.1    Hu, J.F.2    Vu, T.H.3    Giudice, L.C.4    Hoffman, A.R.5
  • 148
    • 0035886806 scopus 로고    scopus 로고
    • Regulation of human telomerase activity: Repression by normal chromosome 3 abolishes nuclear telomerase reverse transcriptase transcripts but does not affect c-myc activity
    • Ducrest A.L., Amacker M., Mathieu Y.D., Cuthbert A.P., Trott D.A., Newbold R.F., Nabholz M., Lingner J. Regulation of human telomerase activity: repression by normal chromosome 3 abolishes nuclear telomerase reverse transcriptase transcripts but does not affect c-myc activity. Cancer Res. 61:2001;7594-7602.
    • (2001) Cancer Res. , vol.61 , pp. 7594-7602
    • Ducrest, A.L.1    Amacker, M.2    Mathieu, Y.D.3    Cuthbert, A.P.4    Trott, D.A.5    Newbold, R.F.6    Nabholz, M.7    Lingner, J.8
  • 149
    • 0037148401 scopus 로고    scopus 로고
    • Regulation of the human telomerase reverse transcriptase gene
    • Ducrest A.L., Szutorisz H., Lingner J., Nabholz M. Regulation of the human telomerase reverse transcriptase gene. Oncogene. 21:2002;541-552.
    • (2002) Oncogene , vol.21 , pp. 541-552
    • Ducrest, A.L.1    Szutorisz, H.2    Lingner, J.3    Nabholz, M.4
  • 150
    • 0034680840 scopus 로고    scopus 로고
    • Histone deacetylation is involved in the transcriptional repression of htert in normal human cells
    • Cong Y.S., Bacchetti S. Histone deacetylation is involved in the transcriptional repression of htert in normal human cells. J. Biol. Chem. 275:2000;35665-35668.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35665-35668
    • Cong, Y.S.1    Bacchetti, S.2
  • 151
    • 0034234575 scopus 로고    scopus 로고
    • Identification and characterization of negative regulatory elements of the human telomerase catalytic subunit (htert) gene promoter: Possible role of mzf-2 in transcriptional repression of htert
    • Fujimoto K., Kyo S., Takakura M., Kanaya T., Kitagawa Y., Itoh H., Takahashi M., Inoue M. Identification and characterization of negative regulatory elements of the human telomerase catalytic subunit (htert) gene promoter: possible role of mzf-2 in transcriptional repression of htert. Nucleic Acids Res. 28:2000;2557-2562.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2557-2562
    • Fujimoto, K.1    Kyo, S.2    Takakura, M.3    Kanaya, T.4    Kitagawa, Y.5    Itoh, H.6    Takahashi, M.7    Inoue, M.8
  • 152
    • 0033082526 scopus 로고    scopus 로고
    • Cloning of human telomerase catalytic subunit (htert) gene promoter and identification of proximal core promoter sequences essential for transcriptional activation in immortalized and cancer cells
    • Takakura M., Kyo S., Kanaya T., Hirano H., Takeda J., Yutsudo M., Inoue M. Cloning of human telomerase catalytic subunit (htert) gene promoter and identification of proximal core promoter sequences essential for transcriptional activation in immortalized and cancer cells. Cancer Res. 59:1999;551-557.
    • (1999) Cancer Res. , vol.59 , pp. 551-557
    • Takakura, M.1    Kyo, S.2    Kanaya, T.3    Hirano, H.4    Takeda, J.5    Yutsudo, M.6    Inoue, M.7
  • 154
    • 0035796403 scopus 로고    scopus 로고
    • Human telomerase contains two cooperating telomerase rna molecules
    • Wenz C., Enenkel B., Amacker M., Kelleher C., Damm K., Lingner J. Human telomerase contains two cooperating telomerase rna molecules. EMBO J. 20:2001;3526-3534.
    • (2001) EMBO J. , vol.20 , pp. 3526-3534
    • Wenz, C.1    Enenkel, B.2    Amacker, M.3    Kelleher, C.4    Damm, K.5    Lingner, J.6
  • 155
    • 0034698133 scopus 로고    scopus 로고
    • Telomerase activity reconstituted in vitro with purified human telomerase reverse transcriptase and human telomerase rna component
    • Masutomi K., Kaneko S., Hayashi N., Yamashita T., Shirota Y., Kobayashi K., Murakami S. Telomerase activity reconstituted in vitro with purified human telomerase reverse transcriptase and human telomerase rna component. J. Biol. Chem. 275:2000;22568-22573.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22568-22573
    • Masutomi, K.1    Kaneko, S.2    Hayashi, N.3    Yamashita, T.4    Shirota, Y.5    Kobayashi, K.6    Murakami, S.7
  • 156
    • 0033621463 scopus 로고    scopus 로고
    • Functional reconstitution of human telomerase expressed in Saccharomyces cerevisiae
    • Bachand F., Autexier C. Functional reconstitution of human telomerase expressed in Saccharomyces cerevisiae. J. Biol. Chem. 274:1999;38027-38031.
    • (1999) J. Biol. Chem. , vol.274 , pp. 38027-38031
    • Bachand, F.1    Autexier, C.2
  • 157
    • 0035144580 scopus 로고    scopus 로고
    • RNA binding domain of telomerase reverse transcriptase
    • Lai C.K., Mitchell J.R., Collins K. RNA binding domain of telomerase reverse transcriptase. Mol. Cell. Biol. 21:2001;990-1000.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 990-1000
    • Lai, C.K.1    Mitchell, J.R.2    Collins, K.3
  • 158
    • 0034612249 scopus 로고    scopus 로고
    • Analysis of telomerase catalytic subunit mutants in vivo and in vitro in schizo Saccharomyces pombe
    • Haering C.H., Nakamura T.M., Baumann P., Cech T.R. Analysis of telomerase catalytic subunit mutants in vivo and in vitro in schizo Saccharomyces pombe. Proc. Natl Acad. Sci. USA. 97:2000;6367-6372.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6367-6372
    • Haering, C.H.1    Nakamura, T.M.2    Baumann, P.3    Cech, T.R.4
  • 159
    • 0034664006 scopus 로고    scopus 로고
    • Template definition by Tetrahymena telomerase reverse transcriptase
    • Miller M.C., Liu J.K., Collins K. Template definition by Tetrahymena telomerase reverse transcriptase. EMBO J. 19:2000;4412-4422.
    • (2000) EMBO J. , vol.19 , pp. 4412-4422
    • Miller, M.C.1    Liu, J.K.2    Collins, K.3
  • 160
    • 0033636319 scopus 로고    scopus 로고
    • Telomerase rna bound by protein motifs specific to telomerase reverse transcriptase
    • Bryan T.M., Goodrich K.J., Cech T.R. Telomerase rna bound by protein motifs specific to telomerase reverse transcriptase. Mol. Cell. 6:2000;493-499.
    • (2000) Mol. Cell , vol.6 , pp. 493-499
    • Bryan, T.M.1    Goodrich, K.J.2    Cech, T.R.3
  • 161
    • 0032699279 scopus 로고    scopus 로고
    • Essential functions of amino-terminal domains in the yeast telomerase catalytic subunit revealed by selection for viable mutants
    • Friedman K.L., Cech T.R. Essential functions of amino-terminal domains in the yeast telomerase catalytic subunit revealed by selection for viable mutants. Genes Dev. 13:1999;2863-2874.
    • (1999) Genes Dev. , vol.13 , pp. 2863-2874
    • Friedman, K.L.1    Cech, T.R.2
  • 162
    • 0034775749 scopus 로고    scopus 로고
    • N-terminal domains of the human telomerase catalytic subunit required for enzyme activity in vivo
    • Armbruster B.N., Banik S.S., Guo C., Smith A.C., Counter C.M. N-terminal domains of the human telomerase catalytic subunit required for enzyme activity in vivo. Mol. Cell. Biol. 21:2001;7775-7786.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7775-7786
    • Armbruster, B.N.1    Banik, S.S.2    Guo, C.3    Smith, A.C.4    Counter, C.M.5
  • 163
    • 0035824558 scopus 로고    scopus 로고
    • Functional analysis of conserved residues in the putative finger domain of telomerase reverse transcriptase
    • Bosoy D., Lue N.F. Functional analysis of conserved residues in the putative finger domain of telomerase reverse transcriptase. J. Biol. Chem. 276:2001;46305-46312.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46305-46312
    • Bosoy, D.1    Lue, N.F.2
  • 164
    • 0033948026 scopus 로고    scopus 로고
    • Identification of functionally important domains in the N-terminal region of telomerase reverse transcriptase
    • Xia J., Peng Y., Mian I.S., Lue N.F. Identification of functionally important domains in the N-terminal region of telomerase reverse transcriptase. Mol. Cell. Biol. 20:2000;5196-5207.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5196-5207
    • Xia, J.1    Peng, Y.2    Mian, I.S.3    Lue, N.F.4
  • 167
    • 0038504649 scopus 로고    scopus 로고
    • Functional analysis of the C-terminal extension of telomerase reverse transcriptase: A putative thumb domain
    • Hossain S., Singh S.M., Lue N.F. Functional analysis of the C-terminal extension of telomerase reverse transcriptase: a putative thumb domain. J. Biol. Chem. 31:2002;31.
    • (2002) J. Biol. Chem. , vol.31 , pp. 31
    • Hossain, S.1    Singh, S.M.2    Lue, N.F.3
  • 169
    • 0034964393 scopus 로고    scopus 로고
    • Analysis of telomerase processivity: Mechanistic similarity to hiv-1 reverse transcriptase and role in telomere maintenance
    • Peng Y., Mian I.S., Lue N.F. Analysis of telomerase processivity: mechanistic similarity to hiv-1 reverse transcriptase and role in telomere maintenance. Mol. Cell. 7:2001;1201-1211.
    • (2001) Mol. Cell. , vol.7 , pp. 1201-1211
    • Peng, Y.1    Mian, I.S.2    Lue, N.F.3
  • 170
    • 0037040990 scopus 로고    scopus 로고
    • Two independent regions of human telomerase reverse transcriptase are important for its oligomerization and telomerase activity
    • Arai K., Masutomi K., Khurts S., Kaneko S., Kobayashi K., Murakami S. Two independent regions of human telomerase reverse transcriptase are important for its oligomerization and telomerase activity. J. Biol. Chem. 277:2002;8538-8544.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8538-8544
    • Arai, K.1    Masutomi, K.2    Khurts, S.3    Kaneko, S.4    Kobayashi, K.5    Murakami, S.6
  • 171
    • 0036150238 scopus 로고    scopus 로고
    • Functional multimerization of human telomerase requires an rna interaction domain in the N terminus of the catalytic subunit
    • Moriarty T.J., Huard S., Dupuis S., Autexier C. Functional multimerization of human telomerase requires an rna interaction domain in the N terminus of the catalytic subunit. Mol. Cell. Biol. 22:2002;1253-1265.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1253-1265
    • Moriarty, T.J.1    Huard, S.2    Dupuis, S.3    Autexier, C.4
  • 172
    • 0032803237 scopus 로고    scopus 로고
    • Two inactive fragments of the integral rna cooperate to assemble active telomerase with the human protein catalytic subunit (htert) in vitro
    • Tesmer V.M., Ford L.P., Holt S.E., Frank B.C., Yi X., Aisner D.L., Ouellette M., Shay J.W., Wright W.E. Two inactive fragments of the integral rna cooperate to assemble active telomerase with the human protein catalytic subunit (htert) in vitro. Mol. Cell. Biol. 19:1999;6207-6216.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6207-6216
    • Tesmer, V.M.1    Ford, L.P.2    Holt, S.E.3    Frank, B.C.4    Yi, X.5    Aisner, D.L.6    Ouellette, M.7    Shay, J.W.8    Wright, W.E.9
  • 173
    • 0032522443 scopus 로고    scopus 로고
    • The telomerase reverse transcriptase: Components and regulation
    • Nugent C.I., Lundblad V. The telomerase reverse transcriptase: components and regulation. Genes Dev. 12:1998;1073-1085.
    • (1998) Genes Dev. , vol.12 , pp. 1073-1085
    • Nugent, C.I.1    Lundblad, V.2
  • 174
    • 0036312043 scopus 로고    scopus 로고
    • Interactions between telomerase and primase physically link the telomere and chromosome replication machinery
    • 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. 22:2002;5859-5868.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5859-5868
    • Ray, S.1    Karamysheva, Z.2    Wang, L.3    Shippen, D.E.4    Price, C.M.5
  • 176
    • 0033638401 scopus 로고    scopus 로고
    • The Tetrahymena p80/p95 complex is required for proper telomere length maintenance and micronuclear genome stability
    • Miller M.C., Collins K. The Tetrahymena p80/p95 complex is required for proper telomere length maintenance and micronuclear genome stability. Mol. Cell. 6:2000;827-837.
    • (2000) Mol. Cell , vol.6 , pp. 827-837
    • Miller, M.C.1    Collins, K.2
  • 177
    • 0032030840 scopus 로고    scopus 로고
    • Interaction of recombinant Tetrahymena telomerase proteins p80 and p95 with telomerase rna and telomeric DNA substrates
    • Gandhi L., Collins K. Interaction of recombinant Tetrahymena telomerase proteins p80 and p95 with telomerase rna and telomeric DNA substrates. Genes Dev. 12:1998;721-733.
    • (1998) Genes Dev. , vol.12 , pp. 721-733
    • Gandhi, L.1    Collins, K.2
  • 178
    • 0035940399 scopus 로고    scopus 로고
    • Tetrahymena proteins p80 and p95 are not core telomerase components
    • Mason D.X., Autexier C., Greider C.W. Tetrahymena proteins p80 and p95 are not core telomerase components. Proc. Natl Acad. Sci. USA. 98:2001;12368-12373.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 12368-12373
    • Mason, D.X.1    Autexier, C.2    Greider, C.W.3
  • 179
    • 0030898989 scopus 로고    scopus 로고
    • Tlp1: A gene encoding a protein component of mammalian telomerase is a novel member of wd repeats family
    • Nakayama J., Saito M., Nakamura H., Matsuura A., Ishikawa F. Tlp1: a gene encoding a protein component of mammalian telomerase is a novel member of wd repeats family. Cell. 88:1997;875-884.
    • (1997) Cell , vol.88 , pp. 875-884
    • Nakayama, J.1    Saito, M.2    Nakamura, H.3    Matsuura, A.4    Ishikawa, F.5
  • 182
    • 0035825120 scopus 로고    scopus 로고
    • The telomerase/vault-associated protein tep1 is required for vault rna stability and its association with the vault particle
    • Kickhoefer V.A., Liu Y., Kong L.B., Snow B.E., Stewart P.L., Harrington L., Rome L.H. The telomerase/vault-associated protein tep1 is required for vault rna stability and its association with the vault particle. J. Cell. Biol. 152:2001;157-164.
    • (2001) J. Cell. Biol. , vol.152 , pp. 157-164
    • Kickhoefer, V.A.1    Liu, Y.2    Kong, L.B.3    Snow, B.E.4    Stewart, P.L.5    Harrington, L.6    Rome, L.H.7
  • 184
    • 0034669177 scopus 로고    scopus 로고
    • Euplotes telomerase contains an Ia motif protein produced by apparent translational frameshifting
    • Aigner S., Lingner J., Goodrich K.J., Grosshans C.A., Shevchenko A., Mann M., Cech T.R. Euplotes telomerase contains an Ia motif protein produced by apparent translational frameshifting. EMBO J. 19:2000;6230-6239.
    • (2000) EMBO J. , vol.19 , pp. 6230-6239
    • Aigner, S.1    Lingner, J.2    Goodrich, K.J.3    Grosshans, C.A.4    Shevchenko, A.5    Mann6
  • 185
    • 0034903676 scopus 로고    scopus 로고
    • The Ia antigen associates with the human telomerase ribonucleoprotein and influences telomere length in vivo
    • Ford L.P., Shay J.W., Wright W.E. The Ia antigen associates with the human telomerase ribonucleoprotein and influences telomere length in vivo. RNA. 7:2001;1068-1075.
    • (2001) RNA , vol.7 , pp. 1068-1075
    • Ford, L.P.1    Shay, J.W.2    Wright, W.E.3
  • 186
    • 0031800617 scopus 로고    scopus 로고
    • Telomere elongation by hnrnp a1 and a derivative that interacts with telomeric repeats and telomerase
    • LaBranche H., Dupuis S., Ben-David Y., Bani M.R., Wellinger R.J., Chabot B. Telomere elongation by hnrnp a1 and a derivative that interacts with telomeric repeats and telomerase. Nat. Genet. 19:1998;199-202.
    • (1998) Nat. Genet. , vol.19 , pp. 199-202
    • LaBranche, H.1    Dupuis, S.2    Ben-David, Y.3    Bani, M.R.4    Wellinger, R.J.5    Chabot, B.6
  • 187
    • 0035368412 scopus 로고    scopus 로고
    • Hnrnp a1 may interact simultaneously with telomeric DNA and the human telomerase rna in vitro
    • Fiset S., Chabot B. Hnrnp a1 may interact simultaneously with telomeric DNA and the human telomerase rna in vitro. Nucleic Acids Res. 29:2001;2268-2275.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2268-2275
    • Fiset, S.1    Chabot, B.2
  • 188
    • 0034462197 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoproteins c1 and c2 associate with the rna component of human telomerase
    • Ford L.P., Suh J.M., Wright W.E., Shay J.W. Heterogeneous nuclear ribonucleoproteins c1 and c2 associate with the rna component of human telomerase. Mol. Cell. Biol. 20:2000;9084-9091.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 9084-9091
    • Ford, L.P.1    Suh, J.M.2    Wright, W.E.3    Shay, J.W.4
  • 189
    • 0034640507 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein a1 and up1 protect mammalian telomeric repeats and modulate telomere replication in vitro
    • Dallaire F., Dupuis S., Fiset S., Chabot B. Heterogeneous nuclear ribonucleoprotein a1 and up1 protect mammalian telomeric repeats and modulate telomere replication in vitro. J. Biol. Chem. 275:2000;14509-14516.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14509-14516
    • Dallaire, F.1    Dupuis, S.2    Fiset, S.3    Chabot, B.4
  • 191
    • 0033927902 scopus 로고    scopus 로고
    • In vitro properties of the conserved mammalian protein hnrnp d suggest a role in telomere maintenance
    • Eversole A., Maizels N. In vitro properties of the conserved mammalian protein hnrnp d suggest a role in telomere maintenance. Mol. Cell. Biol. 20:2000;5425-5432.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5425-5432
    • Eversole, A.1    Maizels, N.2
  • 192
    • 0037148269 scopus 로고    scopus 로고
    • A model for heterogeneous nuclear ribonucleoproteins in telomere and telomerase regulation
    • Ford L.P., Wright W.E., Shay J.W. A model for heterogeneous nuclear ribonucleoproteins in telomere and telomerase regulation. Oncogene. 21:2002;580-583.
    • (2002) Oncogene , vol.21 , pp. 580-583
    • Ford, L.P.1    Wright, W.E.2    Shay, J.W.3
  • 193
    • 0034099225 scopus 로고    scopus 로고
    • Identification of two rna-binding proteins associated with human telomerase rna
    • Le S., Sternglanz R., Greider C.W. Identification of two rna-binding proteins associated with human telomerase rna. Mol. Biol. Cell. 11:2000;999-1010.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 999-1010
    • Le, S.1    Sternglanz, R.2    Greider, C.W.3
  • 195
    • 0035844136 scopus 로고    scopus 로고
    • Stable association of hsp90 and p23, but not hsp70, with active human telomerase
    • Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E. Stable association of hsp90 and p23, but not hsp70, with active human telomerase. J. Biol. Chem. 276:2001;15571-15574.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15571-15574
    • Forsythe, H.L.1    Jarvis, J.L.2    Turner, J.W.3    Elmore, L.W.4    Holt, S.E.5
  • 197
    • 0035090016 scopus 로고    scopus 로고
    • Hsp90 levels affect telomere length in yeast
    • Grandin N., Charbonneau M. Hsp90 levels affect telomere length in yeast. Mol. Genet. Genomics. 265:2001;126-134.
    • (2001) Mol. Genet. Genomics , vol.265 , pp. 126-134
    • Grandin, N.1    Charbonneau, M.2
  • 199
    • 85047697807 scopus 로고    scopus 로고
    • Tert regulates cell survival independent of telomerase enzymatic activity
    • Cao Y., Li H., Deb S., Liu J.P. Tert regulates cell survival independent of telomerase enzymatic activity. Oncogene. 21:2002;3130-3138.
    • (2002) Oncogene , vol.21 , pp. 3130-3138
    • Cao, Y.1    Li, H.2    Deb, S.3    Liu, J.P.4
  • 200
    • 0033532056 scopus 로고    scopus 로고
    • Akt protein kinase enhances human telomerase activity through phosphorylation of telomerase reverse transcriptase subunit
    • Kang S.S., Kwon T., Kwon D.Y., Do S.I. Akt protein kinase enhances human telomerase activity through phosphorylation of telomerase reverse transcriptase subunit. J. Biol. Chem. 274:1999;13085-13090.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13085-13090
    • Kang, S.S.1    Kwon, T.2    Kwon, D.Y.3    Do, S.I.4
  • 201
    • 0032509350 scopus 로고    scopus 로고
    • Telomerase is controlled by protein kinase calpha in human breast cancer cells
    • Li H., Zhao L., Yang Z., Funder J.W., Liu J.P. Telomerase is controlled by protein kinase calpha in human breast cancer cells. J. Biol. Chem. 273:1998;33436-33442.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33436-33442
    • Li, H.1    Zhao, L.2    Yang, Z.3    Funder, J.W.4    Liu, J.P.5
  • 202
    • 0033581883 scopus 로고    scopus 로고
    • Molecular interactions between telomerase and the tumor suppressor protein p53 in vitro
    • Li H., Cao Y., Berndt M.C., Funder J.W., Liu J.P. Molecular interactions between telomerase and the tumor suppressor protein p53 in vitro. Oncogene. 18:1999;6785-6794.
    • (1999) Oncogene , vol.18 , pp. 6785-6794
    • Li, H.1    Cao, Y.2    Berndt, M.C.3    Funder, J.W.4    Liu, J.P.5
  • 203
    • 0030755955 scopus 로고    scopus 로고
    • Protein phosphatase 2a inhibits nuclear telomerase activity in human breast cancer cells
    • Li H., Zhao L.L., Funder J.W., Liu J.P. Protein phosphatase 2a inhibits nuclear telomerase activity in human breast cancer cells. J. Biol. Chem. 272:1997;16729-16732.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16729-16732
    • Li, H.1    Zhao, L.L.2    Funder, J.W.3    Liu, J.P.4
  • 204
    • 0035798379 scopus 로고    scopus 로고
    • The pin2/trf1-interacting protein pinx1 is a potent telomerase inhibitor
    • Zhou X.Z., Lu K.P. The pin2/trf1-interacting protein pinx1 is a potent telomerase inhibitor. Cell. 107:2001;347-359.
    • (2001) Cell , vol.107 , pp. 347-359
    • Zhou, X.Z.1    Lu, K.P.2
  • 205
    • 0037490699 scopus 로고    scopus 로고
    • The yeast homolog of human pinx1 is involved in rrna and snorna maturation, not in telomere elongation inhibition
    • Guglielmi B., Werner M. The yeast homolog of human pinx1 is involved in rrna and snorna maturation, not in telomere elongation inhibition. J. Biol. Chem. 9:2002;9.
    • (2002) J. Biol. Chem. , vol.9 , pp. 9
    • Guglielmi, B.1    Werner, M.2
  • 206
    • 0030881688 scopus 로고    scopus 로고
    • Three ever shorter telomere (est) genes are dispensable for in vitro yeast telomerase activity
    • Lingner J., Cech T.R., Hughes T.R., Lundblad V. Three ever shorter telomere (est) genes are dispensable for in vitro yeast telomerase activity. Proc. Natl Acad. Sci. USA. 94:1997;11190-11195.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11190-11195
    • Lingner, J.1    Cech, T.R.2    Hughes, T.R.3    Lundblad, V.4
  • 208
    • 0030462146 scopus 로고    scopus 로고
    • Est1 has the properties of a single-stranded telomere end-binding protein
    • Virta-Pearlman V., Morris D.K., Lundblad V. Est1 has the properties of a single-stranded telomere end-binding protein. Genes Dev. 10:1996;3094-3104.
    • (1996) Genes Dev. , vol.10 , pp. 3094-3104
    • Virta-Pearlman, V.1    Morris, D.K.2    Lundblad, V.3
  • 209
    • 0033994222 scopus 로고    scopus 로고
    • The est1 subunit of yeast telomerase binds the tlc1 telomerase rna
    • Zhou J., Hidaka K., Futcher B. The est1 subunit of yeast telomerase binds the tlc1 telomerase rna. Mol. Cell. Biol. 20:2000;1947-1955.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1947-1955
    • Zhou, J.1    Hidaka, K.2    Futcher, B.3
  • 210
    • 0029883887 scopus 로고    scopus 로고
    • Association of the est1 protein with telomerase activity in yeast
    • Steiner B.R., Hidaka K., Futcher B. Association of the est1 protein with telomerase activity in yeast. Proc. Natl Acad. Sci. USA. 93:1996;2817-2821.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2817-2821
    • Steiner, B.R.1    Hidaka, K.2    Futcher, B.3
  • 211
    • 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. 104:2001;387-396.
    • (2001) Cell , vol.104 , pp. 387-396
    • Pennock, E.1    Buckley, K.2    Lundblad, V.3
  • 212
    • 0034661246 scopus 로고    scopus 로고
    • The saccharomyces telomere-binding protein cdc13p interacts with both the catalytic subunit of DNA polymerase alpha and the telomerase- associated est1 protein
    • Qi H., Zakian V.A. The saccharomyces telomere-binding protein cdc13p interacts with both the catalytic subunit of DNA polymerase alpha and the telomerase- associated est1 protein. Genes Dev. 14:2000;1777-1788.
    • (2000) Genes Dev. , vol.14 , pp. 1777-1788
    • Qi, H.1    Zakian, V.A.2
  • 213
    • 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. 286:1999;117-120.
    • (1999) Science , vol.286 , pp. 117-120
    • Evans, S.K.1    Lundblad, V.2
  • 214
    • 0031029001 scopus 로고    scopus 로고
    • Stn1, a new Saccharomyces cerevisiae, is implicated in telomere size regulation in association with cdc13
    • Grandin N., Reed S.I., Charbonneau M. Stn1, a new Saccharomyces cerevisiae, is implicated in telomere size regulation in association with cdc13. Genes Dev. 11:1997;512-527.
    • (1997) Genes Dev. , vol.11 , pp. 512-527
    • Grandin, N.1    Reed, S.I.2    Charbonneau, M.3
  • 215
    • 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. 20:2000;8397-8408.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8397-8408
    • Grandin, N.1    Damon, C.2    Charbonneau, M.3
  • 216
    • 0035282781 scopus 로고    scopus 로고
    • Ten1 functions in telomere end protection and length regulation in association with stn1 and cdc13
    • Grandin N., Damon C., Charbonneau M. Ten1 functions in telomere end protection and length regulation in association with stn1 and cdc13. EMBO J. 20:2001;1173-1183.
    • (2001) EMBO J. , vol.20 , pp. 1173-1183
    • Grandin, N.1    Damon, C.2    Charbonneau, M.3
  • 217
    • 0037047643 scopus 로고    scopus 로고
    • Est1p as a cell cycle-regulated activator of telomere-bound telomerase
    • Taggart A.K., Teng S.C., Zakian V.A. Est1p as a cell cycle-regulated activator of telomere-bound telomerase. Science. 297:2002;1023-1026.
    • (2002) Science , vol.297 , pp. 1023-1026
    • Taggart, A.K.1    Teng, S.C.2    Zakian, V.A.3
  • 218
    • 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. 8:1997;2145-2155.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2145-2155
    • Fan, X.1    Price, C.M.2
  • 219
    • 0029772312 scopus 로고    scopus 로고
    • Specific DNA replication mutations affect telomere length in Saccharomyces cerevisiae
    • Adams A.K., Holm C. Specific DNA replication mutations affect telomere length in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:1996;4614-4620.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4614-4620
    • Adams, A.K.1    Holm, C.2
  • 220
    • 0034626734 scopus 로고    scopus 로고
    • Pcna connects DNA replication to epigenetic inheritance in yeast
    • Zhang Z., Shibahara K., Stillman B. Pcna connects DNA replication to epigenetic inheritance in yeast. Nature. 408:2000;221-225.
    • (2000) Nature , vol.408 , pp. 221-225
    • Zhang, Z.1    Shibahara, K.2    Stillman, B.3
  • 221
    • 0033982575 scopus 로고    scopus 로고
    • The function of DNA polymerase alpha at telomeric g tails is important for telomere homeostasis
    • Adams Martin A., Dionne I., Wellinger R.J., Holm C. The function of DNA polymerase alpha at telomeric g tails is important for telomere homeostasis. Mol. Cell. Biol. 20:2000;786-796.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 786-796
    • Adams Martin, A.1    Dionne, I.2    Wellinger, R.J.3    Holm, C.4
  • 222
    • 0033951868 scopus 로고    scopus 로고
    • Characterization of genetic interactions with rfa1: The role of rpa in DNA replication and telomere maintenance
    • Smith J., Zou H., Rothstein R. Characterization of genetic interactions with rfa1: the role of rpa in DNA replication and telomere maintenance. Biochimie. 82:2000;71-78.
    • (2000) Biochimie , vol.82 , pp. 71-78
    • Smith, J.1    Zou, H.2    Rothstein, R.3
  • 223
    • 0033598944 scopus 로고    scopus 로고
    • Telomerase-mediated telomere addition in vivo requires DNA primase and DNA polymerases alpha and delta
    • Diede S.J., Gottschling D.E. Telomerase-mediated telomere addition in vivo requires DNA primase and DNA polymerases alpha and delta. Cell. 99:1999;723-733.
    • (1999) Cell , vol.99 , pp. 723-733
    • Diede, S.J.1    Gottschling, D.E.2
  • 224
    • 0034175814 scopus 로고    scopus 로고
    • Cell cycle restriction of telomere elongation
    • Marcand S., Brevet V., Mann C., Gilson E. Cell cycle restriction of telomere elongation. Curr. Biol. 10:2000;487-490.
    • (2000) Curr. Biol. , vol.10 , pp. 487-490
    • Marcand, S.1    Brevet, V.2    Mann, C.3    Gilson, E.4
  • 225
    • 0027509950 scopus 로고
    • Saccharomyces telomeres acquire single-strand tg1-3 tails late in S phase
    • Wellinger R.J., Wolf A.J., Zakian V.A. Saccharomyces telomeres acquire single-strand tg1-3 tails late in S phase. Cell. 72:1993;51-60.
    • (1993) Cell , vol.72 , pp. 51-60
    • Wellinger, R.J.1    Wolf, A.J.2    Zakian, V.A.3
  • 226
  • 227
    • 0035806955 scopus 로고    scopus 로고
    • Exonuclease activity is required for sequence addition and cdc13p loading at a de novo telomere
    • Diede S.J., Gottschling D.E. Exonuclease activity is required for sequence addition and cdc13p loading at a de novo telomere. Curr. Biol. 11:2001;1336-1340.
    • (2001) Curr. Biol. , vol.11 , pp. 1336-1340
    • Diede, S.J.1    Gottschling, D.E.2
  • 228
    • 0035806977 scopus 로고    scopus 로고
    • The role of the mre11-rad50-xrs2 complex in telomerase-mediated lengthening of Saccharomyces cerevisiae telomeres
    • Tsukamoto Y., Taggart A.K., Zakian V.A. The role of the mre11-rad50-xrs2 complex in telomerase-mediated lengthening of Saccharomyces cerevisiae telomeres. Curr. Biol. 11:2001;1328-1335.
    • (2001) Curr. Biol. , vol.11 , pp. 1328-1335
    • Tsukamoto, Y.1    Taggart, A.K.2    Zakian, V.A.3
  • 229
    • 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. 26:1998;5365-5371.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5365-5371
    • Dionne, I.1    Wellinger, R.J.2
  • 230
    • 0342561644 scopus 로고    scopus 로고
    • Cell-cycle-regulated association of rad50/mre11/nbs1 with trf2 and human telomeres
    • Zhu X.D., Kuster B., Mann M., Petrini J.H., Lange T. Cell-cycle-regulated association of rad50/mre11/nbs1 with trf2 and human telomeres. Nat. Genet. 25:2000;347-352.
    • (2000) Nat. Genet. , vol.25 , pp. 347-352
    • Zhu, X.D.1    Kuster, B.2    Mann, M.3    Petrini, J.H.4    Lange, T.5
  • 231
    • 0032076127 scopus 로고    scopus 로고
    • Yeast ku as a regulator of chromosomal DNA end structure
    • Gravel S., Larrivee M., Labrecque P., Wellinger R.J. Yeast ku as a regulator of chromosomal DNA end structure. Science. 280:1998;741-744.
    • (1998) Science , vol.280 , pp. 741-744
    • Gravel, S.1    Larrivee, M.2    Labrecque, P.3    Wellinger, R.J.4
  • 233
    • 0032536861 scopus 로고    scopus 로고
    • Components of the ku-dependent non-homologous end-joining pathway are involved in telomeric length maintenance and telomeric silencing
    • Boulton S.J., Jackson S.P. Components of the ku-dependent non-homologous end-joining pathway are involved in telomeric length maintenance and telomeric silencing. EMBO J. 17:1998;1819-1828.
    • (1998) EMBO J. , vol.17 , pp. 1819-1828
    • Boulton, S.J.1    Jackson, S.P.2
  • 234
    • 0036119253 scopus 로고    scopus 로고
    • Maintenance of double-stranded telomeric repeats as the critical determinant for cell viability in yeast cells lacking ku
    • Gravel S., Wellinger R.J. Maintenance of double-stranded telomeric repeats as the critical determinant for cell viability in yeast cells lacking ku. Mol. Cell. Biol. 22:2002;2182-2193.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2182-2193
    • Gravel, S.1    Wellinger, R.J.2
  • 235
    • 0033533699 scopus 로고    scopus 로고
    • Yeast ku protein plays a direct role in telomeric silencing and counteracts inhibition by rif proteins
    • Mishra K., Shore D. Yeast ku protein plays a direct role in telomeric silencing and counteracts inhibition by rif proteins. Curr. Biol. 9:1999;1123-1126.
    • (1999) Curr. Biol. , vol.9 , pp. 1123-1126
    • Mishra, K.1    Shore, D.2


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