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Volumn 5, Issue 5, 2006, Pages 534-543

γH2AX and MDC1: Anchoring the DNA-damage-response machinery to broken chromosomes

Author keywords

Chromatin; DNA damage checkpoint; DNA double strand breaks; DNA repair; Foci; Genome stability; Histone H2AX; MDC1

Indexed keywords

ATM PROTEIN; ATR PROTEIN; DEOXYRIBONUCLEOPROTEIN; DNA DEPENDENT PROTEIN KINASE; DOUBLE STRANDED DNA; HISTONE H2AX; MEDIATOR OF DNA DAMAGE CHECKPOINT PROTEIN 1; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN GAMMA H2AX; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; GAMMAH2AX PROTEIN, S CEREVISIAE; HISTONE; MDC1 PROTEIN, HUMAN; NUCLEAR PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; TRANSACTIVATOR PROTEIN;

EID: 33646106590     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2006.01.012     Document Type: Review
Times cited : (341)

References (71)
  • 1
    • 0034707047 scopus 로고    scopus 로고
    • The DNA damage response: putting checkpoints in perspective
    • Zhou B.-B.S., and Elledge S.J. The DNA damage response: putting checkpoints in perspective. Nature 408 (2000) 433-439
    • (2000) Nature , vol.408 , pp. 433-439
    • Zhou, B.-B.S.1    Elledge, S.J.2
  • 2
    • 0037178748 scopus 로고    scopus 로고
    • Interfaces between the detection, signaling, and repair of DNA damage
    • Rouse J., and Jackson S.P. Interfaces between the detection, signaling, and repair of DNA damage. Science 297 (2002) 547-551
    • (2002) Science , vol.297 , pp. 547-551
    • Rouse, J.1    Jackson, S.P.2
  • 3
    • 0035093737 scopus 로고    scopus 로고
    • DNA double-strand breaks: signaling, repair and the cancer connection
    • Khanna K.K., and Jackson S.P. DNA double-strand breaks: signaling, repair and the cancer connection. Nat. Genet. 27 (2001) 247-254
    • (2001) Nat. Genet. , vol.27 , pp. 247-254
    • Khanna, K.K.1    Jackson, S.P.2
  • 4
    • 3242881500 scopus 로고    scopus 로고
    • The cellular response to general and programmed DNA double strand breaks
    • Bassing C.H., and Alt F.W. The cellular response to general and programmed DNA double strand breaks. DNA Repair (Amst.) 3 (2004) 781-796
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 781-796
    • Bassing, C.H.1    Alt, F.W.2
  • 5
    • 0141740426 scopus 로고    scopus 로고
    • Focusing on foci: H2AX and the recruitment of DNA-damage response factors
    • Fernandez-Capetillo O., Celeste A., and Nussenzweig A. Focusing on foci: H2AX and the recruitment of DNA-damage response factors. Cell Cycle 2 (2003) 426-427
    • (2003) Cell Cycle , vol.2 , pp. 426-427
    • Fernandez-Capetillo, O.1    Celeste, A.2    Nussenzweig, A.3
  • 7
    • 0032489520 scopus 로고    scopus 로고
    • DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
    • Rogakou E.P., Pilch D.R., Orr A.H., Ivanova V.S., and Bonner W.M. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J. Biol. Chem. 273 (1998) 5858-5868
    • (1998) J. Biol. Chem. , vol.273 , pp. 5858-5868
    • Rogakou, E.P.1    Pilch, D.R.2    Orr, A.H.3    Ivanova, V.S.4    Bonner, W.M.5
  • 10
    • 0035289717 scopus 로고    scopus 로고
    • Chromosomal stability and the DNA double-stranded break connection
    • van Gent D.C., Hoeijmakers J.H., and Kanaar R. Chromosomal stability and the DNA double-stranded break connection. Nat. Rev. Genet. 2 (2001) 196-206
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 196-206
    • van Gent, D.C.1    Hoeijmakers, J.H.2    Kanaar, R.3
  • 13
    • 0032861343 scopus 로고    scopus 로고
    • Megabase chromatin domains involved in DNA double-strand breaks in vivo
    • Rogakou E.P., Boon C., Redon C., and Bonner W.M. Megabase chromatin domains involved in DNA double-strand breaks in vivo. J. Cell Biol. 146 (1999) 905-916
    • (1999) J. Cell Biol. , vol.146 , pp. 905-916
    • Rogakou, E.P.1    Boon, C.2    Redon, C.3    Bonner, W.M.4
  • 14
    • 28444483130 scopus 로고    scopus 로고
    • gamma-H2AX dephosphorylation by protein phosphatase 2A facilitates DNA double-strand break repair
    • Chowdhury D., Keogh M.C., Ishii H., Peterson C.L., Buratowski S., and Lieberman J. gamma-H2AX dephosphorylation by protein phosphatase 2A facilitates DNA double-strand break repair. Mol. Cell 20 (2005) 801-809
    • (2005) Mol. Cell , vol.20 , pp. 801-809
    • Chowdhury, D.1    Keogh, M.C.2    Ishii, H.3    Peterson, C.L.4    Buratowski, S.5    Lieberman, J.6
  • 16
    • 0034700511 scopus 로고    scopus 로고
    • A role for Saccharomyces cerevisiae histone H2A in DNA repair
    • Downs J.A., Lowndes N.F., and Jackson S.P. A role for Saccharomyces cerevisiae histone H2A in DNA repair. Nature 408 (2000) 1001-1004
    • (2000) Nature , vol.408 , pp. 1001-1004
    • Downs, J.A.1    Lowndes, N.F.2    Jackson, S.P.3
  • 18
    • 10944233962 scopus 로고    scopus 로고
    • Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair
    • van Attikum H., Fritsch O., Hohn B., and Gasser S.M. Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair. Cell 119 (2004) 777-788
    • (2004) Cell , vol.119 , pp. 777-788
    • van Attikum, H.1    Fritsch, O.2    Hohn, B.3    Gasser, S.M.4
  • 19
  • 22
    • 0038143321 scopus 로고    scopus 로고
    • Accumulation of checkpoint protein 53BP1 at DNA breaks involves its binding to phosphorylated histone H2AX
    • Ward I.M., Minn K., Jorda K.G., and Chen J. Accumulation of checkpoint protein 53BP1 at DNA breaks involves its binding to phosphorylated histone H2AX. J. Biol. Chem. 278 (2003) 19579-19582
    • (2003) J. Biol. Chem. , vol.278 , pp. 19579-19582
    • Ward, I.M.1    Minn, K.2    Jorda, K.G.3    Chen, J.4
  • 24
    • 22144448593 scopus 로고    scopus 로고
    • Histone H2A phosphorylation in DNA double-strand break repair
    • Foster E.R., and Downs J.A. Histone H2A phosphorylation in DNA double-strand break repair. FEBS J. 272 (2005) 3231-3240
    • (2005) FEBS J. , vol.272 , pp. 3231-3240
    • Foster, E.R.1    Downs, J.A.2
  • 26
    • 0142240342 scopus 로고    scopus 로고
    • BRCT repeats as phosphopeptide-binding modules involved in protein targeting
    • Manke I.A., Lowery D.M., Nguyen A., and Yaffe M.B. BRCT repeats as phosphopeptide-binding modules involved in protein targeting. Science 302 (2003) 636-639
    • (2003) Science , vol.302 , pp. 636-639
    • Manke, I.A.1    Lowery, D.M.2    Nguyen, A.3    Yaffe, M.B.4
  • 27
    • 0142147272 scopus 로고    scopus 로고
    • The BRCT domain is a phospho-protein binding domain
    • Yu X., Chini C.C., He M., Mer G., and Chen J. The BRCT domain is a phospho-protein binding domain. Science 302 (2003) 639-642
    • (2003) Science , vol.302 , pp. 639-642
    • Yu, X.1    Chini, C.C.2    He, M.3    Mer, G.4    Chen, J.5
  • 29
    • 2542490186 scopus 로고    scopus 로고
    • Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1
    • Williams R.S., Lee M.S., Hau D.D., and Glover J.N. Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1. Nat. Struct. Mol. Biol. 11 (2004) 519-525
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 519-525
    • Williams, R.S.1    Lee, M.S.2    Hau, D.D.3    Glover, J.N.4
  • 30
    • 0030850047 scopus 로고    scopus 로고
    • Dynamic changes of BRCA1 subnuclear location and phosphorylation state are initiated by DNA damage
    • Scully R., Chen J., Ochs R.L., Keegan K., Hoekstra M., Feunteun J., and Livingston D.M. Dynamic changes of BRCA1 subnuclear location and phosphorylation state are initiated by DNA damage. Cell 90 (1997) 425-435
    • (1997) Cell , vol.90 , pp. 425-435
    • Scully, R.1    Chen, J.2    Ochs, R.L.3    Keegan, K.4    Hoekstra, M.5    Feunteun, J.6    Livingston, D.M.7
  • 31
    • 0034739853 scopus 로고    scopus 로고
    • p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks
    • Schultz L.B., Chehab N.H., Malikzay A., and Halazonetis T.D. p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks. J. Cell Biol. 151 (2000) 1381-1390
    • (2000) J. Cell Biol. , vol.151 , pp. 1381-1390
    • Schultz, L.B.1    Chehab, N.H.2    Malikzay, A.3    Halazonetis, T.D.4
  • 33
    • 0037468232 scopus 로고    scopus 로고
    • MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways
    • Lou Z., Minter-Dykhouse K., Wu X., and Chen J. MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways. Nature 421 (2003) 957-961
    • (2003) Nature , vol.421 , pp. 957-961
    • Lou, Z.1    Minter-Dykhouse, K.2    Wu, X.3    Chen, J.4
  • 34
    • 0032076248 scopus 로고    scopus 로고
    • The hMre11/hRad50 protein complex and Nijmegen breakage syndrome: linkage of double-strand break repair to the cellular DNA damage response
    • Carney J.P., Maser R.S., Olivares H., Davis E.M., Le Beau M., Yates III J.R., Hays L., Morgan W.F., and Petrini J.H. The hMre11/hRad50 protein complex and Nijmegen breakage syndrome: linkage of double-strand break repair to the cellular DNA damage response. Cell 93 (1998) 477-486
    • (1998) Cell , vol.93 , pp. 477-486
    • Carney, J.P.1    Maser, R.S.2    Olivares, H.3    Davis, E.M.4    Le Beau, M.5    Yates III, J.R.6    Hays, L.7    Morgan, W.F.8    Petrini, J.H.9
  • 35
    • 4544269236 scopus 로고    scopus 로고
    • Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1
    • Xu X., Lee J., and Stern D.F. Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. J. Biol. Chem. 279 (2004) 34091-34094
    • (2004) J. Biol. Chem. , vol.279 , pp. 34091-34094
    • Xu, X.1    Lee, J.2    Stern, D.F.3
  • 36
    • 11244300690 scopus 로고    scopus 로고
    • Human PTIP facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation
    • Jowsey P.A., Doherty A.J., and Rouse J. Human PTIP facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. J. Biol. Chem. 279 (2004) 55562-55569
    • (2004) J. Biol. Chem. , vol.279 , pp. 55562-55569
    • Jowsey, P.A.1    Doherty, A.J.2    Rouse, J.3
  • 37
    • 0036134979 scopus 로고    scopus 로고
    • A DNA damage-regulated BRCT-containing protein, TopBP1, is required for cell survival
    • Yamane K., Wu X., and Chen J. A DNA damage-regulated BRCT-containing protein, TopBP1, is required for cell survival. Mol. Cell Biol. 22 (2002) 555-566
    • (2002) Mol. Cell Biol. , vol.22 , pp. 555-566
    • Yamane, K.1    Wu, X.2    Chen, J.3
  • 38
    • 0346101743 scopus 로고    scopus 로고
    • Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains
    • Rodriguez M., Yu X., Chen J., and Songyang Z. Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains. J. Biol. Chem. 278 (2003) 52914-52918
    • (2003) J. Biol. Chem. , vol.278 , pp. 52914-52918
    • Rodriguez, M.1    Yu, X.2    Chen, J.3    Songyang, Z.4
  • 40
    • 29244434544 scopus 로고    scopus 로고
    • MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks
    • Stucki M., Clapperton J.A., Mohammad D., Yaffe M.B., Smerdon S.J., and Jackson S.P. MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. Cell 123 (2005) 1213-1226
    • (2005) Cell , vol.123 , pp. 1213-1226
    • Stucki, M.1    Clapperton, J.A.2    Mohammad, D.3    Yaffe, M.B.4    Smerdon, S.J.5    Jackson, S.P.6
  • 41
    • 6344287454 scopus 로고    scopus 로고
    • Interactions between BRCT repeats and phosphoproteins: tangled up in two
    • Glover J.N., Williams R.S., and Lee M.S. Interactions between BRCT repeats and phosphoproteins: tangled up in two. Trends Biochem. Sci. 29 (2004) 579-585
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 579-585
    • Glover, J.N.1    Williams, R.S.2    Lee, M.S.3
  • 42
    • 25444465151 scopus 로고    scopus 로고
    • Structure of the BRCT repeat domain of MDC1 and its specificity for the free COOH-terminal end of the gamma-H2AX histone tail
    • Epub 32005 Jul 32027
    • Lee M.S., Edwards R.A., Thede G.L., and Glover J.N. Structure of the BRCT repeat domain of MDC1 and its specificity for the free COOH-terminal end of the gamma-H2AX histone tail. J. Biol. Chem. 280 (2005) 32053-32056 Epub 32005 Jul 32027
    • (2005) J. Biol. Chem. , vol.280 , pp. 32053-32056
    • Lee, M.S.1    Edwards, R.A.2    Thede, G.L.3    Glover, J.N.4
  • 43
    • 3142608985 scopus 로고    scopus 로고
    • Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains
    • Botuyan M.V., Nomine Y., Yu X., Juranic N., Macura S., Chen J., and Mer G. Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains. Structure (Camb.) 12 (2004) 1137-1146
    • (2004) Structure (Camb.) , vol.12 , pp. 1137-1146
    • Botuyan, M.V.1    Nomine, Y.2    Yu, X.3    Juranic, N.4    Macura, S.5    Chen, J.6    Mer, G.7
  • 44
    • 2342484423 scopus 로고    scopus 로고
    • Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling
    • Shiozaki E.N., Gu L., Yan N., and Shi Y. Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling. Mol. Cell 14 (2004) 405-412
    • (2004) Mol. Cell , vol.14 , pp. 405-412
    • Shiozaki, E.N.1    Gu, L.2    Yan, N.3    Shi, Y.4
  • 46
    • 3242885156 scopus 로고    scopus 로고
    • MDC1/NFBD1: a key regulator of the DNA damage response in higher eukaryotes
    • Stucki M., and Jackson S.P. MDC1/NFBD1: a key regulator of the DNA damage response in higher eukaryotes. DNA Repair (Amst.) 3 (2004) 953-957
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 953-957
    • Stucki, M.1    Jackson, S.P.2
  • 48
    • 22944462083 scopus 로고    scopus 로고
    • Dynamic assembly and sustained retention of 53BP1 at the sites of DNA damage are controlled by Mdc1/NFBD1
    • Bekker-Jensen S., Lukas C., Melander F., Bartek J., and Lukas J. Dynamic assembly and sustained retention of 53BP1 at the sites of DNA damage are controlled by Mdc1/NFBD1. J. Cell Biol. 170 (2005) 201-211
    • (2005) J. Cell Biol. , vol.170 , pp. 201-211
    • Bekker-Jensen, S.1    Lukas, C.2    Melander, F.3    Bartek, J.4    Lukas, J.5
  • 51
    • 15844394846 scopus 로고    scopus 로고
    • Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA damage
    • Falck J., Coates J., and Jackson S.P. Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA damage. Nature 434 (2005) 605-611
    • (2005) Nature , vol.434 , pp. 605-611
    • Falck, J.1    Coates, J.2    Jackson, S.P.3
  • 52
    • 20744436198 scopus 로고    scopus 로고
    • ATM activation and its recruitment to damaged DNA require binding to the C terminus of Nbs1
    • You Z., Chahwan C., Bailis J., Hunter T., and Russell P. ATM activation and its recruitment to damaged DNA require binding to the C terminus of Nbs1. Mol. Cell Biol. 25 (2005) 5363-5379
    • (2005) Mol. Cell Biol. , vol.25 , pp. 5363-5379
    • You, Z.1    Chahwan, C.2    Bailis, J.3    Hunter, T.4    Russell, P.5
  • 53
    • 0035930537 scopus 로고    scopus 로고
    • Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress
    • Ward I.M., and Chen J. Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress. J. Biol. Chem. 276 (2001) 47759-47762
    • (2001) J. Biol. Chem. , vol.276 , pp. 47759-47762
    • Ward, I.M.1    Chen, J.2
  • 54
    • 1642280957 scopus 로고    scopus 로고
    • UV-induced ataxia-telangiectasia-mutated and Rad3-related (ATR) activation requires replication stress
    • Ward I.M., Minn K., and Chen J. UV-induced ataxia-telangiectasia-mutated and Rad3-related (ATR) activation requires replication stress. J. Biol. Chem. 279 (2004) 9677-9680
    • (2004) J. Biol. Chem. , vol.279 , pp. 9677-9680
    • Ward, I.M.1    Minn, K.2    Chen, J.3
  • 55
    • 0035834693 scopus 로고    scopus 로고
    • ATM phosphorylates histone H2AX in response to DNA double-strand breaks
    • Burma S., Chen B.P., Murphy M., Kurimasa A., and Chen D.J. ATM phosphorylates histone H2AX in response to DNA double-strand breaks. J. Biol. Chem. 276 (2001) 42462-42467
    • (2001) J. Biol. Chem. , vol.276 , pp. 42462-42467
    • Burma, S.1    Chen, B.P.2    Murphy, M.3    Kurimasa, A.4    Chen, D.J.5
  • 57
    • 11144305946 scopus 로고    scopus 로고
    • Complex H2AX phosphorylation patterns by multiple kinases including ATM and DNA-PK in human cells exposed to ionizing radiation and treated with kinase inhibitors
    • Wang H., Wang M., Bocker W., and Iliakis G. Complex H2AX phosphorylation patterns by multiple kinases including ATM and DNA-PK in human cells exposed to ionizing radiation and treated with kinase inhibitors. J. Cell Physiol. 202 (2005) 492-502
    • (2005) J. Cell Physiol. , vol.202 , pp. 492-502
    • Wang, H.1    Wang, M.2    Bocker, W.3    Iliakis, G.4
  • 58
    • 1942538492 scopus 로고    scopus 로고
    • ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation
    • Stiff T., O'Driscoll M., Rief N., Iwabuchi K., Lobrich M., and Jeggo P.A. ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation. Cancer Res. 64 (2004) 2390-2396
    • (2004) Cancer Res. , vol.64 , pp. 2390-2396
    • Stiff, T.1    O'Driscoll, M.2    Rief, N.3    Iwabuchi, K.4    Lobrich, M.5    Jeggo, P.A.6
  • 59
    • 6044261241 scopus 로고    scopus 로고
    • Effects of novel inhibitors of poly(ADP-ribose) polymerase-1 and the DNA-dependent protein kinase on enzyme activities and DNA repair
    • Veuger S.J., Curtin N.J., Smith G.C., and Durkacz B.W. Effects of novel inhibitors of poly(ADP-ribose) polymerase-1 and the DNA-dependent protein kinase on enzyme activities and DNA repair. Oncogene 23 (2004) 7322-7329
    • (2004) Oncogene , vol.23 , pp. 7322-7329
    • Veuger, S.J.1    Curtin, N.J.2    Smith, G.C.3    Durkacz, B.W.4
  • 63
    • 2442706035 scopus 로고    scopus 로고
    • H2AX may function as an anchor to hold broken chromosomal DNA ends in close proximity
    • Bassing C.H., and Alt F.W. H2AX may function as an anchor to hold broken chromosomal DNA ends in close proximity. Cell Cycle 3 (2004) 149-153
    • (2004) Cell Cycle , vol.3 , pp. 149-153
    • Bassing, C.H.1    Alt, F.W.2
  • 66
    • 30344444484 scopus 로고    scopus 로고
    • Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks
    • Murr R., Loizou J.I., Yang Y.G., Cuenin C., Li H., Wang Z.Q., and Herceg Z. Histone acetylation by Trrap-Tip60 modulates loading of repair proteins and repair of DNA double-strand breaks. Nat. Cell Biol. 8 (2006) 91-99
    • (2006) Nat. Cell Biol. , vol.8 , pp. 91-99
    • Murr, R.1    Loizou, J.I.2    Yang, Y.G.3    Cuenin, C.4    Li, H.5    Wang, Z.Q.6    Herceg, Z.7
  • 67
    • 10944232673 scopus 로고    scopus 로고
    • Post-replicative recruitment of cohesin to double-strand breaks is required for DNA repair
    • Strom L., Lindroos H.B., Shirahige K., and Sjogren C. Post-replicative recruitment of cohesin to double-strand breaks is required for DNA repair. Mol. Cell 16 (2004) 1003-1015
    • (2004) Mol. Cell , vol.16 , pp. 1003-1015
    • Strom, L.1    Lindroos, H.B.2    Shirahige, K.3    Sjogren, C.4
  • 68
    • 10944262393 scopus 로고    scopus 로고
    • DNA damage response pathway uses histone modification to assemble a double-strand break-specific cohesin domain
    • Unal E., Arbel-Eden A., Sattler U., Shroff R., Lichten M., Haber J.E., and Koshland D. DNA damage response pathway uses histone modification to assemble a double-strand break-specific cohesin domain. Mol. Cell 16 (2004) 991-1002
    • (2004) Mol. Cell , vol.16 , pp. 991-1002
    • Unal, E.1    Arbel-Eden, A.2    Sattler, U.3    Shroff, R.4    Lichten, M.5    Haber, J.E.6    Koshland, D.7
  • 69
    • 14044255880 scopus 로고    scopus 로고
    • Activation of the DNA damage response by telomere attrition: a passage to cellular senescence
    • Reaper P.M., di Fagagna F., and Jackson S.P. Activation of the DNA damage response by telomere attrition: a passage to cellular senescence. Cell Cycle 3 (2004) 543-546
    • (2004) Cell Cycle , vol.3 , pp. 543-546
    • Reaper, P.M.1    di Fagagna, F.2    Jackson, S.P.3


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