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Volumn 37, Issue 15, 2009, Pages 5019-5031

The Myb/SANT domain of the telomere-binding protein TRF2 alters chromatin structure

Author keywords

[No Author keywords available]

Indexed keywords

MICROCOCCAL NUCLEASE; PROTEIN MYB; TELOMERIC REPEAT BINDING FACTOR 2;

EID: 69849107002     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkp515     Document Type: Article
Times cited : (25)

References (58)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger,K., Mader,A.W., Richmond,R.K., Sargent,D.F. and Richmond,T.J. (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature, 389, 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 3
    • 55949109034 scopus 로고    scopus 로고
    • Telomeric chromatin: Roles in aging, cancer and hereditary disease
    • McCord,R.A. and Broccoli,D. (2008) Telomeric chromatin: Roles in aging, cancer and hereditary disease. Mutat. Res., 647, 86-93.
    • (2008) Mutat. Res , vol.647 , pp. 86-93
    • McCord, R.A.1    Broccoli, D.2
  • 4
    • 0029780764 scopus 로고    scopus 로고
    • Condensation of rat telomere-specific nucleosomal arrays containing unusually short DNA repeats and histone H1
    • Bedoyan,J.K., Lejnine,S., Makarov,V.L. and Langmore,J.P. (1996) Condensation of rat telomere-specific nucleosomal arrays containing unusually short DNA repeats and histone H1. J. Biol. Chem., 271 18485-18493.
    • (1996) J. Biol. Chem , vol.271 , pp. 18485-18493
    • Bedoyan, J.K.1    Lejnine, S.2    Makarov, V.L.3    Langmore, J.P.4
  • 5
    • 0027212790 scopus 로고
    • Nucleosomal organization of telomere-specific chromatin in rat
    • Makarov,V.L., Lejnine,S., Bedoyan,J. and Langmore,J.P. (1993) Nucleosomal organization of telomere-specific chromatin in rat. Cell 73, 775-787.
    • (1993) Cell , vol.73 , pp. 775-787
    • Makarov, V.L.1    Lejnine, S.2    Bedoyan, J.3    Langmore, J.P.4
  • 6
    • 51349167747 scopus 로고    scopus 로고
    • No overt nucleosome eviction at deprotected telomeres
    • Wu,P. and de Lange,T. (2008) No overt nucleosome eviction at deprotected telomeres. Mol. Cell Biol., 28, 5724-5735.
    • (2008) Mol. Cell Biol , vol.28 , pp. 5724-5735
    • Wu, P.1    de Lange, T.2
  • 8
    • 0347988045 scopus 로고    scopus 로고
    • Epigenetic regulation of telomere length in mammalian cells by the Suv39h1 and Suv39h2 histone methyltransferases
    • Garcia-Cao,M., O'Sullivan,R., Peters,A.H., Jenuwein,T. and Blasco,M.A. (2004) Epigenetic regulation of telomere length in mammalian cells by the Suv39h1 and Suv39h2 histone methyltransferases. Nat. Genet., 36, 94-99.
    • (2004) Nat. Genet , vol.36 , pp. 94-99
    • Garcia-Cao, M.1    O'Sullivan, R.2    Peters, A.H.3    Jenuwein, T.4    Blasco, M.A.5
  • 11
    • 10944240539 scopus 로고    scopus 로고
    • Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins
    • Liu,D., O'Connor,M.S., Qin,J. and 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
  • 12
    • 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
  • 13
    • 0033605145 scopus 로고    scopus 로고
    • p53- and ATM-dependent apoptosis induced by telomeres lacking TRF2
    • Karlseder,J., Broccoli,D., Dai,Y., Hardy,S. and de Lange,T. (1999) p53- and ATM-dependent apoptosis induced by telomeres lacking TRF2. Science, 283, 1321-1325.
    • (1999) Science , vol.283 , pp. 1321-1325
    • Karlseder, J.1    Broccoli, D.2    Dai, Y.3    Hardy, S.4    de Lange, T.5
  • 14
    • 0032489012 scopus 로고    scopus 로고
    • TRF2 protects human telomeres from end-to-end fusions
    • van Steensel,B., Smogorzewska,A. and 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
  • 15
    • 0037192462 scopus 로고    scopus 로고
    • Senescence induced by altered telomere state, not telomere loss
    • Karlseder,J., Smogorzewska,A. and 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
  • 17
    • 0035476710 scopus 로고    scopus 로고
    • T-loop assembly in vitro involves binding of TRF2 near the 3′ telomeric overhang
    • Stansel,R.M., de Lange,T. and Griffith,J.D. (2001) T-loop assembly in vitro involves binding of TRF2 near the 3′ telomeric overhang. EMBO J., 20, 5532-5540.
    • (2001) EMBO J , vol.20 , pp. 5532-5540
    • Stansel, R.M.1    de Lange, T.2    Griffith, J.D.3
  • 19
    • 21444444520 scopus 로고    scopus 로고
    • How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: A view from high-resolution crystal structures
    • Court,R., Chapman,L., Fairall,L. and Rhodes,D. (2005) How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: A view from high-resolution crystal structures. EMBO Rep., 6, 39-45.
    • (2005) EMBO Rep , vol.6 , pp. 39-45
    • Court, R.1    Chapman, L.2    Fairall, L.3    Rhodes, D.4
  • 20
    • 43249105463 scopus 로고    scopus 로고
    • Cell cycle control of telomere protection and NHEJ revealed by a ts mutation in the DNA-binding domain of TRF2
    • Konishi,A. and de Lange,T. (2008) Cell cycle control of telomere protection and NHEJ revealed by a ts mutation in the DNA-binding domain of TRF2. Genes Dev., 22, 1221-1230.
    • (2008) Genes Dev , vol.22 , pp. 1221-1230
    • Konishi, A.1    de Lange, T.2
  • 21
    • 3342974395 scopus 로고    scopus 로고
    • Closed chromatin loops at the ends of chromosomes
    • Nikitina,T. and Woodcock,C.L. (2004) Closed chromatin loops at the ends of chromosomes. J. Cell Biol., 166, 161-165.
    • (2004) J. Cell Biol , vol.166 , pp. 161-165
    • Nikitina, T.1    Woodcock, C.L.2
  • 22
    • 0035830960 scopus 로고    scopus 로고
    • Specific interactions of the telomeric protein Rap1p with nucleosomal binding sites
    • Rossetti,L., Cacchione,S., De Menna,A., Chapman,L., Rhodes,D. and Savino,M. (2001) Specific interactions of the telomeric protein Rap1p with nucleosomal binding sites. J. Mol. Biol., 306, 903-913.
    • (2001) J. Mol. Biol , vol.306 , pp. 903-913
    • Rossetti, L.1    Cacchione, S.2    De Menna, A.3    Chapman, L.4    Rhodes, D.5    Savino, M.6
  • 23
    • 33745226438 scopus 로고    scopus 로고
    • The human telomeric protein TRF1 specifically recognizes nucleosomal binding sites and alters nucleosome structure
    • Galati,A., Rossetti,L., Pisano,S., Chapman,L., Rhodes,D., Savino,M. and Cacchione,S. (2006) The human telomeric protein TRF1 specifically recognizes nucleosomal binding sites and alters nucleosome structure. J. Mol. Biol., 360, 377-385.
    • (2006) J. Mol. Biol , vol.360 , pp. 377-385
    • Galati, A.1    Rossetti, L.2    Pisano, S.3    Chapman, L.4    Rhodes, D.5    Savino, M.6    Cacchione, S.7
  • 24
    • 0028331878 scopus 로고
    • Quantitative agarose gel electrophoresis of chromatin: Nucleosome-dependent changes in charge, sharp, and deformability at low ionic strength
    • Fletcher,T.M., Krishnan,U., Serwer,P. and Hansen,J.C. (1994) Quantitative agarose gel electrophoresis of chromatin: nucleosome-dependent changes in charge, sharp, and deformability at low ionic strength. Biochemistry, 33, 2226-2233.
    • (1994) Biochemistry , vol.33 , pp. 2226-2233
    • Fletcher, T.M.1    Krishnan, U.2    Serwer, P.3    Hansen, J.C.4
  • 25
    • 0033291649 scopus 로고    scopus 로고
    • Quantitative analysis of chromatin higher-order organization using agarose gel electrophoresis
    • Hansen,J.C., Fletcher,T.M. and Kreider,J.I. (1999) Quantitative analysis of chromatin higher-order organization using agarose gel electrophoresis. Methods Mol. Biol., 119, 113-125.
    • (1999) Methods Mol. Biol , vol.119 , pp. 113-125
    • Hansen, J.C.1    Fletcher, T.M.2    Kreider, J.I.3
  • 26
    • 0028074481 scopus 로고
    • Quantitative analysis of macromolecular conformational changes using agarose gel electrophoresis: Application to chromatin folding
    • Fletcher,T.M., Serwer,P. and Hansen,J.C. (1994) Quantitative analysis of macromolecular conformational changes using agarose gel electrophoresis: application to chromatin folding. Biochemistry, 33, 10859-10863.
    • (1994) Biochemistry , vol.33 , pp. 10859-10863
    • Fletcher, T.M.1    Serwer, P.2    Hansen, J.C.3
  • 27
    • 0028858566 scopus 로고
    • Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organization through distinct molecular mechanisms
    • Fletcher,T.M. and Hansen,J.C. (1995) Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organization through distinct molecular mechanisms. J. Biol. Chem., 270, 25359-25362.
    • (1995) J. Biol. Chem , vol.270 , pp. 25359-25362
    • Fletcher, T.M.1    Hansen, J.C.2
  • 28
    • 0032514742 scopus 로고    scopus 로고
    • Enhanced transcription factor access to arrays of histone H3/H4 tetramer.DNA complexes in vitro: Implications for replication and transcription
    • Tse,C., Fletcher,T.M. and Hansen,J.C. (1998) Enhanced transcription factor access to arrays of histone H3/H4 tetramer.DNA complexes in vitro: Implications for replication and transcription. Proc. Natl Acad. Sci. USA, 95, 12169-12173.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12169-12173
    • Tse, C.1    Fletcher, T.M.2    Hansen, J.C.3
  • 29
    • 0032553013 scopus 로고    scopus 로고
    • Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: Mechanistic ramifications for higher-order chromatin folding
    • Carruthers,L.M., Bednar,J., Woodcock,C.L. and Hansen,J.C. (1998) Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: Mechanistic ramifications for higher-order chromatin folding. Biochemistry, 37, 14776-14787.
    • (1998) Biochemistry , vol.37 , pp. 14776-14787
    • Carruthers, L.M.1    Bednar, J.2    Woodcock, C.L.3    Hansen, J.C.4
  • 30
    • 0038677661 scopus 로고    scopus 로고
    • Formation of higher-order secondary and tertiary chromatin structures by genomic mouse mammary tumor virus promoters
    • Georgel,P.T., Fletcher,T.M., Hager,G.L. and Hansen,J.C. (2003) Formation of higher-order secondary and tertiary chromatin structures by genomic mouse mammary tumor virus promoters. Genes Dev., 17, 1617-1629.
    • (2003) Genes Dev , vol.17 , pp. 1617-1629
    • Georgel, P.T.1    Fletcher, T.M.2    Hager, G.L.3    Hansen, J.C.4
  • 32
    • 0024468871 scopus 로고
    • Homogeneous reconstituted oligonucleosomes, evidence for salt-dependent folding in the absence of histone H1
    • Hansen,J.C., Ausio,J., Stanik,V.H. and van Holde,K.E. (1989) Homogeneous reconstituted oligonucleosomes, evidence for salt-dependent folding in the absence of histone H1. Biochemistry, 28, 9129-9136.
    • (1989) Biochemistry , vol.28 , pp. 9129-9136
    • Hansen, J.C.1    Ausio, J.2    Stanik, V.H.3    van Holde, K.E.4
  • 34
    • 12844270590 scopus 로고    scopus 로고
    • DNA structure-dependent recruitment of telomeric proteins to single-stranded/double-stranded DNA junctions
    • Yanez,G.H., Khan,S.J., Locovei,A.M., Pedroso,I.M. and Fletcher,T.M. (2005) DNA structure-dependent recruitment of telomeric proteins to single-stranded/double-stranded DNA junctions. Biochem. Biophys. Res. Commun., 328, 49-56.
    • (2005) Biochem. Biophys. Res. Commun , vol.328 , pp. 49-56
    • Yanez, G.H.1    Khan, S.J.2    Locovei, A.M.3    Pedroso, I.M.4    Fletcher, T.M.5
  • 35
    • 77957027468 scopus 로고
    • Basic analysis of transcription factor binding to nucleosomes
    • Côté,J., Utley,R.T. and Workman,J.L. (1995) Basic analysis of transcription factor binding to nucleosomes. Methods Mol. Genet., 6, 108-128.
    • (1995) Methods Mol. Genet , vol.6 , pp. 108-128
    • Côté, J.1    Utley, R.T.2    Workman, J.L.3
  • 36
    • 0018531367 scopus 로고
    • Acidic polypeptides can assemble both histones and chromatin in vitro at physiological ionic strength
    • Stein,A., Whitlock,J.P. Jr. and Bina,M. (1979) Acidic polypeptides can assemble both histones and chromatin in vitro at physiological ionic strength. Proc. Natl Acad. Sci. USA, 76, 5000-5004.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 5000-5004
    • Stein, A.1    Whitlock Jr., J.P.2    Bina, M.3
  • 37
    • 0025091721 scopus 로고
    • In vitro evidence that transcription-induced stress causes nucleosome dissolution and regeneration
    • Pfaffle,P., Gerlach,V., Bunzel,L. and Jackson,V. (1990) In vitro evidence that transcription-induced stress causes nucleosome dissolution and regeneration. J. Biol. Chem., 265, 16830-16840.
    • (1990) J. Biol. Chem , vol.265 , pp. 16830-16840
    • Pfaffle, P.1    Gerlach, V.2    Bunzel, L.3    Jackson, V.4
  • 38
    • 0031194492 scopus 로고    scopus 로고
    • Analysis of transcription factor-mediated remodeling of nucleosomal arrays in a purified system
    • Steger,D.J., Owen-Hughes,T., John,S. and Workman,J.L. (1997) Analysis of transcription factor-mediated remodeling of nucleosomal arrays in a purified system. Methods, 12, 276-285.
    • (1997) Methods , vol.12 , pp. 276-285
    • Steger, D.J.1    Owen-Hughes, T.2    John, S.3    Workman, J.L.4
  • 39
    • 0024720506 scopus 로고
    • The sieving of spheres during agarose gel electrophoresis: Quantitation and modeling
    • Griess,G.A., Moreno,E.T., Easom,R.A. and Serwer,P. (1989) The sieving of spheres during agarose gel electrophoresis: Quantitation and modeling. Biopolymers, 28, 1475-1484.
    • (1989) Biopolymers , vol.28 , pp. 1475-1484
    • Griess, G.A.1    Moreno, E.T.2    Easom, R.A.3    Serwer, P.4
  • 40
    • 0036931098 scopus 로고    scopus 로고
    • Glutaraldehyde modified mica: A new surface for atomic force microscopy of chromatin
    • Wang,H., Bash,R., Yodh,J.G., Hager,G.H., Lohr,D. and Lindsay,S.M. (2002) Glutaraldehyde modified mica: A new surface for atomic force microscopy of chromatin. Biophys. J., 83, 3619-3625.
    • (2002) Biophys. J , vol.83 , pp. 3619-3625
    • Wang, H.1    Bash, R.2    Yodh, J.G.3    Hager, G.H.4    Lohr, D.5    Lindsay, S.M.6
  • 41
    • 63249087946 scopus 로고    scopus 로고
    • The effect of the TRF2 N-terminal and TRFH regions on telomeric G-quadruplex structures
    • Pedroso,I.M., Hayward,W. and Fletcher,T.M. (2009) The effect of the TRF2 N-terminal and TRFH regions on telomeric G-quadruplex structures. Nucleic Acids Res., 37, 1541-1554.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1541-1554
    • Pedroso, I.M.1    Hayward, W.2    Fletcher, T.M.3
  • 42
    • 0031031106 scopus 로고    scopus 로고
    • In vitro low propensity to form nucleosomes of four telomeric sequences
    • Cacchione,S., Cerone,M.A. and Savino,M. (1997) In vitro low propensity to form nucleosomes of four telomeric sequences. FEBS Lett., 400, 37-41.
    • (1997) FEBS Lett , vol.400 , pp. 37-41
    • Cacchione, S.1    Cerone, M.A.2    Savino, M.3
  • 43
  • 44
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8A resolution
    • Luger,K., Mäder,A.W., Richmond,R.K., Sargent,D.F. and Richmond,T.J. (1997) Crystal structure of the nucleosome core particle at 2.8A resolution. Nature, 389, 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 45
    • 0027431478 scopus 로고
    • Topography of the histone octamer surface: Repeating structural motifs utilized in the docking of nucleosomal DNA
    • Arents,G. and Moudrianakis,E.N. (1993) Topography of the histone octamer surface: Repeating structural motifs utilized in the docking of nucleosomal DNA. Proc. Natl Acad. Sci. USA, 90, 10489-10493.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10489-10493
    • Arents, G.1    Moudrianakis, E.N.2
  • 46
    • 0022234831 scopus 로고
    • Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones: A model system for study of higher order structure
    • Simpson,R.T., Thoma,F. and Brubaker,J.M. (1985) Chromatin reconstituted from tandemly repeated cloned DNA fragments and core histones: A model system for study of higher order structure. Cell, 42, 799-808.
    • (1985) Cell , vol.42 , pp. 799-808
    • Simpson, R.T.1    Thoma, F.2    Brubaker, J.M.3
  • 47
    • 33847026837 scopus 로고    scopus 로고
    • Using atomic force microscopy to study chromatin structure and nucleosome remodeling
    • Lohr,D., Bash,R., Wang,H., Yodh,J. and Lindsay,S. (2007) Using atomic force microscopy to study chromatin structure and nucleosome remodeling. Methods, 41, 333-341.
    • (2007) Methods , vol.41 , pp. 333-341
    • Lohr, D.1    Bash, R.2    Wang, H.3    Yodh, J.4    Lindsay, S.5
  • 48
    • 11144223025 scopus 로고    scopus 로고
    • Comparison between TRF2 and TRF1 of their telomeric DNA-bound structures and DNA-binding activities
    • Hanaoka,S., Nagadoi,A. and Nishimura,Y. (2005) Comparison between TRF2 and TRF1 of their telomeric DNA-bound structures and DNA-binding activities. Protein Sci., 14, 119-130.
    • (2005) Protein Sci , vol.14 , pp. 119-130
    • Hanaoka, S.1    Nagadoi, A.2    Nishimura, Y.3
  • 49
    • 0021878850 scopus 로고
    • Theory of gel electrophoresis of DNA
    • Lumpkin,O.J., Dejardin,P. and Zimm,B.H. (1985) Theory of gel electrophoresis of DNA. Biopolymers, 24, 1573-1593.
    • (1985) Biopolymers , vol.24 , pp. 1573-1593
    • Lumpkin, O.J.1    Dejardin, P.2    Zimm, B.H.3
  • 50
    • 0023355867 scopus 로고
    • On the stretching of DNA in the reptation theories of gel electrophoresis
    • Slater,G.W., Rousseau,J. and Noolandi,J. (1987) On the stretching of DNA in the reptation theories of gel electrophoresis. Biopolymers, 26, 863-872.
    • (1987) Biopolymers , vol.26 , pp. 863-872
    • Slater, G.W.1    Rousseau, J.2    Noolandi, J.3
  • 51
    • 0027032561 scopus 로고
    • Polymer dynamics in electrophoresis of DNA
    • Noolandi,J. (1992) Polymer dynamics in electrophoresis of DNA. Annu. Rev. Phys. Chem., 43, 237-256.
    • (1992) Annu. Rev. Phys. Chem , vol.43 , pp. 237-256
    • Noolandi, J.1
  • 52
    • 33750801681 scopus 로고    scopus 로고
    • The DNA damage machinery and homologous recombination pathway act consecutively to protect human telomeres
    • Verdun,R.E. and Karlseder,J. (2006) The DNA damage machinery and homologous recombination pathway act consecutively to protect human telomeres. Cell, 127, 709-720.
    • (2006) Cell , vol.127 , pp. 709-720
    • Verdun, R.E.1    Karlseder, J.2
  • 53
    • 0036809731 scopus 로고    scopus 로고
    • Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes
    • Boyer,L.A., Langer,M.R., Crowley,K.A., Tan,S., Denu,J.M. and Peterson,C.L. (2002) Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes. Mol. Cell., 10, 935-942.
    • (2002) Mol. Cell , vol.10 , pp. 935-942
    • Boyer, L.A.1    Langer, M.R.2    Crowley, K.A.3    Tan, S.4    Denu, J.M.5    Peterson, C.L.6
  • 54
    • 0141922979 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI
    • Grune,T., Brzeski,J., Eberharter,A., Clapier,C.R., Corona,D.F., Becker,P.B. and Muller,C.W. (2003) Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI. Mol. Cell, 12, 449-460.
    • (2003) Mol. Cell , vol.12 , pp. 449-460
    • Grune, T.1    Brzeski, J.2    Eberharter, A.3    Clapier, C.R.4    Corona, D.F.5    Becker, P.B.6    Muller, C.W.7
  • 56
    • 26944472827 scopus 로고    scopus 로고
    • Histone H3 tail positioning and acetylation by the c-Myb but not the v-Myb DNA-binding SANT domain
    • Mo,X., Kowenz-Leutz,E., Laumonnier,Y., Xu,H. and Leutz,A. (2005) Histone H3 tail positioning and acetylation by the c-Myb but not the v-Myb DNA-binding SANT domain. Genes Dev., 19, 2447-2457.
    • (2005) Genes Dev , vol.19 , pp. 2447-2457
    • Mo, X.1    Kowenz-Leutz, E.2    Laumonnier, Y.3    Xu, H.4    Leutz, A.5
  • 58
    • 55849088321 scopus 로고    scopus 로고
    • Role of TRF2 in the assembly of telomeric chromatin
    • Benetti,R., Schoeftner,S., Munoz,P. and Blasco,M.A. (2008) Role of TRF2 in the assembly of telomeric chromatin. Cell Cycle, 7, 3461-3468.
    • (2008) Cell Cycle , vol.7 , pp. 3461-3468
    • Benetti, R.1    Schoeftner, S.2    Munoz, P.3    Blasco, M.A.4


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