메뉴 건너뛰기




Volumn 350, Issue 5, 2005, Pages 938-952

Binding linkage in a telomere DNA-protein complex at the ends of Oxytricha nova chromosomes

Author keywords

Binding linkage; Protein engineering; Protein DNA interactions; Protein protein interactions; Telomere binding protein

Indexed keywords

HYBRID PROTEIN; SINGLE STRANDED DNA; TELOMERE BINDING PROTEIN;

EID: 21744446086     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.05.040     Document Type: Article
Times cited : (6)

References (65)
  • 1
    • 0025731583 scopus 로고
    • Structure and function of telomeres
    • E.H. Blackburn Structure and function of telomeres Nature 350 1991 569 573
    • (1991) Nature , vol.350 , pp. 569-573
    • Blackburn, E.H.1
  • 2
    • 0032055375 scopus 로고    scopus 로고
    • Telomerase and chromosome end maintenance
    • J. Lingner, and T.R. Cech Telomerase and chromosome end maintenance Curr. Opin. Genet. Dev. 8 1998 226 232
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 226-232
    • Lingner, J.1    Cech, T.R.2
  • 3
    • 0019568388 scopus 로고
    • All gene-sized DNA molecules in four species of hypotrichs have the same terminal sequence and an unusual 3′ terminus
    • L.A. Klobutcher, M.T. Swanton, P. Donini, and D.M. Prescott All gene-sized DNA molecules in four species of hypotrichs have the same terminal sequence and an unusual 3′ terminus Proc. Natl Acad. Sci. USA 78 1981 3015 3019
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 3015-3019
    • Klobutcher, L.A.1    Swanton, M.T.2    Donini, P.3    Prescott, D.M.4
  • 4
    • 0024573115 scopus 로고
    • An overhanging 3′ terminus is a conserved feature of telomeres
    • E.R. Henderson, and E.H. Blackburn An overhanging 3′ terminus is a conserved feature of telomeres Mol. Cell Biol. 9 1989 345 348
    • (1989) Mol. Cell Biol. , vol.9 , pp. 345-348
    • Henderson, E.R.1    Blackburn, E.H.2
  • 5
    • 0030982721 scopus 로고    scopus 로고
    • The terminal DNA structure of mammalian chromosomes
    • R. McElligott, and R.J. Wellinger The terminal DNA structure of mammalian chromosomes EMBO J. 16 1997 3705 3714
    • (1997) EMBO J. , vol.16 , pp. 3705-3714
    • McElligott, R.1    Wellinger, R.J.2
  • 6
    • 0027326367 scopus 로고
    • RAP1 and telomere structure regulate telomere position effects in Saccharomyces cerevisiae
    • G. Kyrion, K. Liu, C. Liu, and A.J. Lustig RAP1 and telomere structure regulate telomere position effects in Saccharomyces cerevisiae Genes Dev. 7 1993 1146 1159
    • (1993) Genes Dev. , vol.7 , pp. 1146-1159
    • Kyrion, G.1    Liu, K.2    Liu, C.3    Lustig, A.J.4
  • 7
    • 0032514694 scopus 로고    scopus 로고
    • Rap1 protein regulates telomere turnover in yeast
    • A. Krauskopf, and E.H. Blackburn Rap1 protein regulates telomere turnover in yeast Proc. Natl Acad. Sci. USA 95 1998 12486 12491
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12486-12491
    • Krauskopf, A.1    Blackburn, E.H.2
  • 8
    • 0034660252 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae RAP1 binds to telomeric sequences with spatial flexibility
    • J. Wahlin, and M. Cohn Saccharomyces cerevisiae RAP1 binds to telomeric sequences with spatial flexibility Nucl. Acids Res. 28 2000 2292 2301
    • (2000) Nucl. Acids Res. , vol.28 , pp. 2292-2301
    • Wahlin, J.1    Cohn, M.2
  • 9
    • 0034716904 scopus 로고    scopus 로고
    • Identification of human Rap1: Implications for telomere evolution
    • B. Li, S. Oestreich, and T. de Lange Identification of human Rap1: implications for telomere evolution Cell 101 2000 471 483
    • (2000) Cell , vol.101 , pp. 471-483
    • Li, B.1    Oestreich, S.2    De Lange, T.3
  • 10
    • 0032489012 scopus 로고    scopus 로고
    • TRF2 protects human telomeres from end-to-end fusions
    • B. van Steensel, A. Smogorzewska, and T. de Lange TRF2 protects human telomeres from end-to-end fusions Cell 92 1998 401 413
    • (1998) Cell , vol.92 , pp. 401-413
    • Van Steensel, B.1    Smogorzewska, A.2    De Lange, T.3
  • 11
    • 84984775429 scopus 로고    scopus 로고
    • Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2
    • D. Broccoli, A. Smogorzewska, L. Chong, and T. de Lange Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2 Nature Genet. 17 1997 231 235
    • (1997) Nature Genet. , vol.17 , pp. 231-235
    • Broccoli, D.1    Smogorzewska, A.2    Chong, L.3    De Lange, T.4
  • 13
    • 0023037564 scopus 로고
    • Telomere proteins: Specific recognition and protection of the natural termini of Oxytricha macronuclear DNA
    • D.E. Gottschling, and V.A. Zakian Telomere proteins: specific recognition and protection of the natural termini of Oxytricha macronuclear DNA Cell 47 1986 195 205
    • (1986) Cell , vol.47 , pp. 195-205
    • Gottschling, D.E.1    Zakian, V.A.2
  • 14
    • 0023433713 scopus 로고
    • Telomeric DNA-protein interactions of Oxytricha macronuclear DNA
    • C.M. Price, and T.R. Cech Telomeric DNA-protein interactions of Oxytricha macronuclear DNA Genes Dev. 1 1987 783 793
    • (1987) Genes Dev. , vol.1 , pp. 783-793
    • Price, C.M.1    Cech, T.R.2
  • 15
    • 0030447657 scopus 로고    scopus 로고
    • The Saccharomyces CDC13 protein is a single-strand TG1-3 telomeric DNA-binding protein in vitro that affects telomere behavior in vivo
    • J.J. Lin, and V.A. Zakian The Saccharomyces CDC13 protein is a single-strand TG1-3 telomeric DNA-binding protein in vitro that affects telomere behavior in vivo Proc. Natl Acad. Sci. USA 93 1996 13760 13765
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13760-13765
    • Lin, J.J.1    Zakian, V.A.2
  • 16
    • 0035844082 scopus 로고    scopus 로고
    • Pot1, the putative telomere end-binding protein in fission yeast and humans
    • P. Baumann, and T.R. Cech Pot1, the putative telomere end-binding protein in fission yeast and humans Science 292 2001 1171 1175
    • (2001) Science , vol.292 , pp. 1171-1175
    • Baumann, P.1    Cech, T.R.2
  • 17
    • 0024843757 scopus 로고
    • Telomeric DNA dimerizes by formation of guanine tetrads between hairpin loops
    • W.I. Sundquist, and A. Klug Telomeric DNA dimerizes by formation of guanine tetrads between hairpin loops Nature 342 1989 825 829
    • (1989) Nature , vol.342 , pp. 825-829
    • Sundquist, W.I.1    Klug, A.2
  • 18
    • 0037142071 scopus 로고    scopus 로고
    • Crystal structure of parallel quadruplexes from human telomeric DNA
    • G.N. Parkinson, M.P. Lee, and S. Neidle Crystal structure of parallel quadruplexes from human telomeric DNA Nature 417 2002 876 880
    • (2002) Nature , vol.417 , pp. 876-880
    • Parkinson, G.N.1    Lee, M.P.2    Neidle, S.3
  • 21
    • 3342974395 scopus 로고    scopus 로고
    • Closed chromatin loops at the ends of chromosomes
    • T. Nikitina, and C.L. Woodcock Closed chromatin loops at the ends of chromosomes J. Cell Biol. 166 2004 161 165
    • (2004) J. Cell Biol. , vol.166 , pp. 161-165
    • Nikitina, T.1    Woodcock, C.L.2
  • 22
    • 1842683257 scopus 로고    scopus 로고
    • T-loops and the origin of telomeres
    • T. de Lange T-loops and the origin of telomeres Nature Rev. Mol. Cell Biol. 5 2004 323 329
    • (2004) Nature Rev. Mol. Cell Biol. , vol.5 , pp. 323-329
    • De Lange, T.1
  • 23
    • 0026523228 scopus 로고
    • Telomere shortening associated with chromosome instability is arrested in immortal cells which express telomerase activity
    • C.M. Counter, A.A. Avilion, C.E. LeFeuvre, N.G. Stewart, C.W. Greider, C.B. Harley, and S. Bacchetti Telomere shortening associated with chromosome instability is arrested in immortal cells which express telomerase activity EMBO J. 11 1992 1921 1929
    • (1992) EMBO J. , vol.11 , pp. 1921-1929
    • Counter, C.M.1    Avilion, A.A.2    Lefeuvre, C.E.3    Stewart, N.G.4    Greider, C.W.5    Harley, C.B.6    Bacchetti, S.7
  • 24
    • 0010045614 scopus 로고    scopus 로고
    • Extension of life-span by introduction of telomerase into normal human cells
    • A.G. Bodnar, M. Ouellette, M. Frolkis, S.E. Holt, C.P. Chiu, and G.B. Morin Extension of life-span by introduction of telomerase into normal human cells Science 279 1998 349 352
    • (1998) Science , vol.279 , pp. 349-352
    • Bodnar, A.G.1    Ouellette, M.2    Frolkis, M.3    Holt, S.E.4    Chiu, C.P.5    Morin, G.B.6
  • 25
    • 0037192462 scopus 로고    scopus 로고
    • Senescence induced by altered telomere state, not telomere loss
    • J. Karlseder, A. Smogorzewska, and T. de Lange Senescence induced by altered telomere state, not telomere loss Science 295 2002 2446 2449
    • (2002) Science , vol.295 , pp. 2446-2449
    • Karlseder, J.1    Smogorzewska, A.2    De Lange, T.3
  • 26
    • 0034597794 scopus 로고    scopus 로고
    • Telomere states and cell fates
    • E.H. Blackburn Telomere states and cell fates Nature 408 2000 53 56
    • (2000) Nature , vol.408 , pp. 53-56
    • Blackburn, E.H.1
  • 27
    • 0030271719 scopus 로고    scopus 로고
    • The roles of telomeres and telomerase in cell life span
    • C.M. Counter The roles of telomeres and telomerase in cell life span Mutat. Res. 366 1996 45 63
    • (1996) Mutat. Res. , vol.366 , pp. 45-63
    • Counter, C.M.1
  • 29
    • 0025984268 scopus 로고
    • Cloning and expression of genes for the Oxytricha telomere-binding protein: Specific subunit interactions in the telomeric complex
    • J.T. Gray, D.W. Celander, C.M. Price, and T.R. Cech Cloning and expression of genes for the Oxytricha telomere-binding protein: specific subunit interactions in the telomeric complex Cell 67 1991 807 814
    • (1991) Cell , vol.67 , pp. 807-814
    • Gray, J.T.1    Celander, D.W.2    Price, C.M.3    Cech, T.R.4
  • 30
    • 0027163938 scopus 로고
    • Oxytricha telomere-binding protein: DNA-dependent dimerization of the alpha and beta subunits
    • G. Fang, and T.R. Cech Oxytricha telomere-binding protein: DNA-dependent dimerization of the alpha and beta subunits Proc. Natl Acad. Sci. USA 90 1993 6056 6060
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6056-6060
    • Fang, G.1    Cech, T.R.2
  • 31
    • 0027168268 scopus 로고
    • Oxytricha telomere-binding protein: Separable DNA-binding and dimerization domains of the alpha-subunit
    • G. Fang, J.T. Gray, and T.R. Cech Oxytricha telomere-binding protein: separable DNA-binding and dimerization domains of the alpha-subunit Genes Dev. 7 1993 870 882
    • (1993) Genes Dev. , vol.7 , pp. 870-882
    • Fang, G.1    Gray, J.T.2    Cech, T.R.3
  • 32
    • 0032431057 scopus 로고    scopus 로고
    • Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA
    • M.P. Horvath, V.L. Schweiker, J.M. Bevilacqua, J.A. Ruggles, and S.C. Schultz Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA Cell 95 1998 963 974
    • (1998) Cell , vol.95 , pp. 963-974
    • Horvath, M.P.1    Schweiker, V.L.2    Bevilacqua, J.M.3    Ruggles, J.A.4    Schultz, S.C.5
  • 33
    • 0035861983 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of Oxytricha nova telomere end-binding protein alpha subunit both uncomplexed and complexed with telomeric ssDNA
    • S. Classen, J.A. Ruggles, and S.C. Schultz Crystal structure of the N-terminal domain of Oxytricha nova telomere end-binding protein alpha subunit both uncomplexed and complexed with telomeric ssDNA J. Mol. Biol. 314 2001 1113 1125
    • (2001) J. Mol. Biol. , vol.314 , pp. 1113-1125
    • Classen, S.1    Ruggles, J.A.2    Schultz, S.C.3
  • 34
    • 0036176232 scopus 로고    scopus 로고
    • Dimeric structure of the Oxytricha nova telomere end-binding protein alpha-subunit bound to ssDNA
    • O.B. Peersen, J.A. Ruggles, and S.C. Schultz Dimeric structure of the Oxytricha nova telomere end-binding protein alpha-subunit bound to ssDNA Nature Struct. Biol. 9 2002 182 187
    • (2002) Nature Struct. Biol. , vol.9 , pp. 182-187
    • Peersen, O.B.1    Ruggles, J.A.2    Schultz, S.C.3
  • 35
    • 0027717964 scopus 로고
    • Photocrosslinking of 5-iodouracil-substituted RNA and DNA to proteins
    • M.C. Willis, B.J. Hicke, O.C. Uhlenbeck, T.R. Cech, and T.H. Koch Photocrosslinking of 5-iodouracil-substituted RNA and DNA to proteins Science 262 1993 1255 1257
    • (1993) Science , vol.262 , pp. 1255-1257
    • Willis, M.C.1    Hicke, B.J.2    Uhlenbeck, O.C.3    Cech, T.R.4    Koch, T.H.5
  • 36
    • 0028323417 scopus 로고
    • Telomeric protein-DNA point contacts identified by photo-cross-linking using 5-bromodeoxyuridine
    • B.J. Hicke, M.C. Willis, T.H. Koch, and T.R. Cech Telomeric protein-DNA point contacts identified by photo-cross-linking using 5-bromodeoxyuridine Biochemistry 33 1994 3364 3373
    • (1994) Biochemistry , vol.33 , pp. 3364-3373
    • Hicke, B.J.1    Willis, M.C.2    Koch, T.H.3    Cech, T.R.4
  • 37
    • 0030747732 scopus 로고    scopus 로고
    • Solution conformations and interactions of alpha and beta subunits of the Oxytricha nova telomere binding protein: Investigation by Raman spectroscopy
    • L. Laporte, J. Stultz, and G.J. Thomas Jr Solution conformations and interactions of alpha and beta subunits of the Oxytricha nova telomere binding protein: investigation by Raman spectroscopy Biochemistry 36 1997 8053 8059
    • (1997) Biochemistry , vol.36 , pp. 8053-8059
    • Laporte, L.1    Stultz, J.2    Thomas Jr., G.J.3
  • 38
    • 0023055086 scopus 로고
    • Correlation between sites of limited proteolysis and segmental mobility in thermolysin
    • A. Fontana, G. Fassina, C. Vita, D. Dalzoppo, M. Zamai, and M. Zambonin Correlation between sites of limited proteolysis and segmental mobility in thermolysin Biochemistry 25 1986 1847 1851
    • (1986) Biochemistry , vol.25 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzoppo, D.4    Zamai, M.5    Zambonin, M.6
  • 39
    • 0025912338 scopus 로고
    • Molecular recognition. Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors
    • S.J. Hubbard, S.F. Campbell, and J.M. Thornton Molecular recognition. Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors J. Mol. Biol. 220 1991 507 530
    • (1991) J. Mol. Biol. , vol.220 , pp. 507-530
    • Hubbard, S.J.1    Campbell, S.F.2    Thornton, J.M.3
  • 40
    • 0028336661 scopus 로고
    • Modeling studies of the change in conformation required for cleavage of limited proteolytic sites
    • S.J. Hubbard, F. Eisenmenger, and J.M. Thornton Modeling studies of the change in conformation required for cleavage of limited proteolytic sites Protein Sci. 3 1994 757 768
    • (1994) Protein Sci. , vol.3 , pp. 757-768
    • Hubbard, S.J.1    Eisenmenger, F.2    Thornton, J.M.3
  • 41
    • 0026554887 scopus 로고
    • Quadruplex structure of Oxytricha telomeric DNA oligonucleotides
    • F.W. Smith, and J. Feigon Quadruplex structure of Oxytricha telomeric DNA oligonucleotides Nature 356 1992 164 168
    • (1992) Nature , vol.356 , pp. 164-168
    • Smith, F.W.1    Feigon, J.2
  • 42
    • 0036290781 scopus 로고    scopus 로고
    • Crystal structure of the potassium form of an Oxytricha nova G-quadruplex
    • S. Haider, G.N. Parkinson, and S. Neidle Crystal structure of the potassium form of an Oxytricha nova G-quadruplex J. Mol. Biol. 320 2002 189 200
    • (2002) J. Mol. Biol. , vol.320 , pp. 189-200
    • Haider, S.1    Parkinson, G.N.2    Neidle, S.3
  • 43
    • 0035816210 scopus 로고    scopus 로고
    • DNA G-quartets in a 1.86 Å resolution structure of an Oxytricha nova telomeric protein-DNA complex
    • M.P. Horvath, and S.C. Schultz DNA G-quartets in a 1.86 Å resolution structure of an Oxytricha nova telomeric protein-DNA complex J. Mol. Biol. 310 2001 367 377
    • (2001) J. Mol. Biol. , vol.310 , pp. 367-377
    • Horvath, M.P.1    Schultz, S.C.2
  • 44
    • 84935023004 scopus 로고
    • Ueber einen in biologischer Beziehung wichtigen Einfluss, den die Kohlensaurespannung des Blutes aufdessen Sauerstoffbindung ubt
    • C. Bohr, K.A. Hasselbalch, and A. Krogh Ueber einen in biologischer Beziehung wichtigen Einfluss, den die Kohlensaurespannung des Blutes aufdessen Sauerstoffbindung ubt Skand. Arch. Physiol. 16 1904 402 412
    • (1904) Skand. Arch. Physiol. , vol.16 , pp. 402-412
    • Bohr, C.1    Hasselbalch, K.A.2    Krogh, A.3
  • 45
    • 0016637031 scopus 로고
    • PH dependence of the Adair constants of human hemoglobin. Nonuniform contribution of successive oxygen bindings to the alkaline Bohr effect
    • K. Imai, and T. Yonetani PH dependence of the Adair constants of human hemoglobin. Nonuniform contribution of successive oxygen bindings to the alkaline Bohr effect J. Biol. Chem. 250 1975 2227 2231
    • (1975) J. Biol. Chem. , vol.250 , pp. 2227-2231
    • Imai, K.1    Yonetani, T.2
  • 46
    • 0023819640 scopus 로고
    • Escherichia coli aspartate transcarbamylase: The relation between structure and function
    • E.R. Kantrowitz, and W.N. Lipscomb Escherichia coli aspartate transcarbamylase: the relation between structure and function Science 241 1988 669 674
    • (1988) Science , vol.241 , pp. 669-674
    • Kantrowitz, E.R.1    Lipscomb, W.N.2
  • 49
    • 0027104087 scopus 로고
    • Euplotes crassus has genes encoding telomere-binding proteins and telomere-binding protein homologs
    • W. Wang, R. Skopp, M. Scofield, and C. Price Euplotes crassus has genes encoding telomere-binding proteins and telomere-binding protein homologs Nucl. Acids Res. 20 1992 6621 6629
    • (1992) Nucl. Acids Res. , vol.20 , pp. 6621-6629
    • Wang, W.1    Skopp, R.2    Scofield, M.3    Price, C.4
  • 50
    • 0037058877 scopus 로고    scopus 로고
    • Cooperative binding of single-stranded telomeric DNA by the Pot1 protein of Schizosaccharomyces pombe
    • M. Lei, P. Baumann, and T.R. Cech Cooperative binding of single-stranded telomeric DNA by the Pot1 protein of Schizosaccharomyces pombe Biochemistry 41 2002 14560 14568
    • (2002) Biochemistry , vol.41 , pp. 14560-14568
    • Lei, M.1    Baumann, P.2    Cech, T.R.3
  • 51
    • 1842529179 scopus 로고    scopus 로고
    • DNA binding features of human POT1: A nonamer 5′-TAGGGTTAG-3′ minimal binding site, sequence specificity, and internal binding to multimeric sites
    • D. Loayza, H. Parsons, J. Donigian, K. Hoke, and T. de Lange DNA binding features of human POT1: a nonamer 5′-TAGGGTTAG-3′ minimal binding site, sequence specificity, and internal binding to multimeric sites J. Biol. Chem. 279 2004 13241 13248
    • (2004) J. Biol. Chem. , vol.279 , pp. 13241-13248
    • Loayza, D.1    Parsons, H.2    Donigian, J.3    Hoke, K.4    De Lange, T.5
  • 52
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • A.G. Murzin OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences EMBO J. 12 1993 861 867
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 53
    • 12844265975 scopus 로고    scopus 로고
    • Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection
    • M. Lei, E.R. Podell, and T.R. Cech Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection Nature Struct. Mol. Biol. 11 2004 1223 1229
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 1223-1229
    • Lei, M.1    Podell, E.R.2    Cech, T.R.3
  • 54
    • 0345304903 scopus 로고    scopus 로고
    • DNA self-recognition in the structure of Pot1 bound to telomeric single-stranded DNA
    • M. Lei, E.R. Podell, P. Baumann, and T.R. Cech DNA self-recognition in the structure of Pot1 bound to telomeric single-stranded DNA Nature 426 2003 198 203
    • (2003) Nature , vol.426 , pp. 198-203
    • Lei, M.1    Podell, E.R.2    Baumann, P.3    Cech, T.R.4
  • 56
    • 4644220875 scopus 로고    scopus 로고
    • Prediction of multiple tandem OB-fold domains in telomere end-binding proteins Pot1 and Cdc13
    • D.L. Theobald, and D.S. Wuttke Prediction of multiple tandem OB-fold domains in telomere end-binding proteins Pot1 and Cdc13 Structure (Camb) 12 2004 1877 1879
    • (2004) Structure (Camb) , vol.12 , pp. 1877-1879
    • Theobald, D.L.1    Wuttke, D.S.2
  • 58
    • 0038451396 scopus 로고    scopus 로고
    • POT1 as a terminal transducer of TRF1 telomere length control
    • D. Loayza, and T. De Lange POT1 as a terminal transducer of TRF1 telomere length control Nature 423 2003 1013 1018
    • (2003) Nature , vol.423 , pp. 1013-1018
    • Loayza, D.1    De Lange, T.2
  • 60
    • 0035476710 scopus 로고    scopus 로고
    • T-loop assembly in vitro involves binding of TRF2 near the 3′ telomeric overhang
    • R.M. Stansel, T. de Lange, and J.D. Griffith T-loop assembly in vitro involves binding of TRF2 near the 3′ telomeric overhang EMBO J 20 2001 5532 5540
    • (2001) EMBO J , vol.20 , pp. 5532-5540
    • Stansel, R.M.1    De Lange, T.2    Griffith, J.D.3
  • 61
    • 7044232011 scopus 로고    scopus 로고
    • Homologous recombination generates T-loop-sized deletions at human telomeres
    • R.C. Wang, A. Smogorzewska, and T. de Lange Homologous recombination generates T-loop-sized deletions at human telomeres Cell 119 2004 355 368
    • (2004) Cell , vol.119 , pp. 355-368
    • Wang, R.C.1    Smogorzewska, A.2    De Lange, T.3
  • 62
    • 12844254472 scopus 로고    scopus 로고
    • POT1 and TRF2 cooperate to maintain telomeric integrity
    • Q. Yang, Y.L. Zheng, and C.C. Harris POT1 and TRF2 cooperate to maintain telomeric integrity Mol. Cell Biol. 25 2005 1070 1080
    • (2005) Mol. Cell Biol. , vol.25 , pp. 1070-1080
    • Yang, Q.1    Zheng, Y.L.2    Harris, C.C.3
  • 63
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 64
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • H. Schagger, and G. von Jagow Tricine-sodium dodecyl sulfate- polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Anal. Biochem. 166 1987 368 379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 65
    • 0000169232 scopus 로고
    • An algorithm for least-squares estimation of non-linear parameters
    • D.W. Marquardt An algorithm for least-squares estimation of non-linear parameters J. Soc. Ind. Appl. Math. 11 1963 431 441
    • (1963) J. Soc. Ind. Appl. Math. , vol.11 , pp. 431-441
    • Marquardt, D.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.