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Volumn 34, Issue 12, 2014, Pages 2162-2175

Unraveling the complexities of DNA-dependent protein kinase autophosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

CISPLATIN; DNA BASE; DNA DEPENDENT PROTEIN KINASE;

EID: 84901334194     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01554-13     Document Type: Article
Times cited : (61)

References (54)
  • 1
    • 0042632901 scopus 로고    scopus 로고
    • Pathways of DNAdouble-strand break repair during the mammalian cell cycle
    • Rothkamm K, Kruger I, Thompson LH, Lobrich M. 2003. Pathways of DNAdouble-strand break repair during the mammalian cell cycle. Mol. Cell. Biol. 23:5706-5715. http://dx.doi.org/10.1128/MCB.23.16.5706-5715.2003.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5706-5715
    • Rothkamm, K.1    Kruger, I.2    Thompson, L.H.3    Lobrich, M.4
  • 2
    • 38049115657 scopus 로고    scopus 로고
    • The mechanism of human nonhomologous DNA end joining
    • Lieber MR. 2008. The mechanism of human nonhomologous DNA end joining. J. Biol. Chem. 283:1-5. http://dx.doi.org/10.1074/jbc.R700039200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1-5
    • Lieber, M.R.1
  • 5
    • 78649446475 scopus 로고    scopus 로고
    • A structural model for regulation of NHEJ by DNA-PKcs autophosphorylation
    • Dobbs TA, Tainer JA, Lees-Miller SP. 2010. A structural model for regulation of NHEJ by DNA-PKcs autophosphorylation. DNA Repair (Amst.) 9:1307-1314. http://dx.doi.org/10.1016/j.dnarep.2010.09.019.
    • (2010) DNA Repair (Amst.) , vol.9 , pp. 1307-1314
    • Dobbs, T.A.1    Tainer, J.A.2    Lees-Miller, S.P.3
  • 6
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse.
    • Hornbeck PV, Kornhauser JM, Tkachev S, Zhang B, Skrzypek E, Murray B, Latham V, Sullivan M. 2012. PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res. 40:D261-270. http://dx.doi.org/10.1093/nar/gkr1122.
    • (2012) Nucleic Acids Res. , vol.40
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5    Murray, B.6    Latham, V.7    Sullivan, M.8
  • 7
    • 0037106180 scopus 로고    scopus 로고
    • Autophosphorylation of the DNA-dependent protein kinase catalytic subunit is required for rejoining of DNA double-strand breaks
    • Chan DW, Chen BP, Prithivirajsingh S, Kurimasa A, Story MD, Qin J, Chen DJ. 2002. Autophosphorylation of the DNA-dependent protein kinase catalytic subunit is required for rejoining of DNA double-strand breaks. Genes Dev. 16:2333-2338. http://dx.doi.org/10.1101/gad.1015202.
    • (2002) Genes Dev. , vol.16 , pp. 2333-2338
    • Chan, D.W.1    Chen, B.P.2    Prithivirajsingh, S.3    Kurimasa, A.4    Story, M.D.5    Qin, J.6    Chen, D.J.7
  • 9
    • 0043133778 scopus 로고    scopus 로고
    • Autophosphorylation of the catalytic subunit of the DNA-dependent protein kinase is required for efficient end processing during DNA double-strand break repair
    • Ding Q, Reddy YV, Wang W, Woods T, Douglas P, Ramsden DA, Lees-Miller SP, Meek K. 2003. Autophosphorylation of the catalytic subunit of the DNA-dependent protein kinase is required for efficient end processing during DNA double-strand break repair. Mol. Cell. Biol. 23: 5836-5848. http://dx.doi.org/10.1128/MCB.23.16.5836-5848.2003.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5836-5848
    • Ding, Q.1    Reddy, Y.V.2    Wang, W.3    Woods, T.4    Douglas, P.5    Ramsden, D.A.6    Lees-Miller, S.P.7    Meek, K.8
  • 10
    • 28544448011 scopus 로고    scopus 로고
    • Autophosphorylation of DNA-dependent protein kinase regulates DNA end processing and may also alter double-strand break repair pathway choice
    • Cui X, Yu Y, Gupta S, Cho YM, Lees-Miller SP, Meek K. 2005. Autophosphorylation of DNA-dependent protein kinase regulates DNA end processing and may also alter double-strand break repair pathway choice. Mol. Cell. Biol. 25:10842-10852. http://dx.doi.org/10.1128/MCB.25.24.10842-10852.2005.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10842-10852
    • Cui, X.1    Yu, Y.2    Gupta, S.3    Cho, Y.M.4    Lees-Miller, S.P.5    Meek, K.6
  • 11
    • 79953134635 scopus 로고    scopus 로고
    • Inhibition of homologous recombination by DNA-dependent protein kinase requires kinase activity, is titratable, and is modulated by autophosphorylation
    • Neal JA, Dang V, Douglas P, Wold MS, Lees-Miller SP, Meek K. 2011. Inhibition of homologous recombination by DNA-dependent protein kinase requires kinase activity, is titratable, and is modulated by autophosphorylation. Mol. Cell. Biol. 31:1719-1733. http://dx.doi.org/10.1128/MCB.01298-10.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 1719-1733
    • Neal, J.A.1    Dang, V.2    Douglas, P.3    Wold, M.S.4    Lees-Miller, S.P.5    Meek, K.6
  • 12
    • 79956220705 scopus 로고    scopus 로고
    • Choosing the right path: does DNA-PK help make the decision? Mutat
    • Neal JA, Meek K. 2011. Choosing the right path: does DNA-PK help make the decision? Mutat. Res. 711:73- 86. http://dx.doi.org/10.1016/j.mrfmmm.2011.02.010.
    • (2011) Res. , vol.711 , pp. 73-86
    • Neal, J.A.1    Meek, K.2
  • 13
    • 0037444375 scopus 로고    scopus 로고
    • Threonines 2638/2647 in DNA-PK are essential for cellular resistance to ionizing radiation.
    • Soubeyrand S, Pope L, Pakuts B, Hache RJ. 2003. Threonines 2638/2647 in DNA-PK are essential for cellular resistance to ionizing radiation. Cancer Res. 63:1198-1201.
    • (2003) Cancer Res , vol.63 , pp. 1198-1201
    • Soubeyrand, S.1    Pope, L.2    Pakuts, B.3    Hache, R.J.4
  • 14
    • 4043073590 scopus 로고    scopus 로고
    • Autophosphorylation-dependent remodeling of the DNAdependent protein kinase catalytic subunit regulates ligation ofDNAends
    • Block WD, Yu Y, Merkle D, Gifford JL, Ding Q, Meek K, Lees-Miller SP. 2004. Autophosphorylation-dependent remodeling of the DNAdependent protein kinase catalytic subunit regulates ligation ofDNAends. Nucleic Acids Res. 32:4351-4357. http://dx.doi.org/10.1093/nar/gkh761.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 4351-4357
    • Block, W.D.1    Yu, Y.2    Merkle, D.3    Gifford, J.L.4    Ding, Q.5    Meek, K.6    Lees-Miller, S.P.7
  • 15
    • 4544295689 scopus 로고    scopus 로고
    • Nonhomologous end joining requires that the DNA-PK complex undergo an autophosphorylation-dependent rearrangement atDNAends
    • Reddy YV, Ding Q, Lees-Miller SP, Meek K, Ramsden DA. 2004. Nonhomologous end joining requires that the DNA-PK complex undergo an autophosphorylation-dependent rearrangement atDNAends. J. Biol. Chem. 279:39408-39413. http://dx.doi.org/10.1074/jbc.M406432200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39408-39413
    • Reddy, Y.V.1    Ding, Q.2    Lees-Miller, S.P.3    Meek, K.4    Ramsden, D.A.5
  • 17
    • 33847185190 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase catalytic subunit is phosphorylated in vivo on threonine 3950, a highly conserved amino acid in the protein kinase domain
    • Douglas P, Cui X, Block WD, Yu Y, Gupta S, Ding Q, Ye R, Morrice N, Lees-Miller SP, Meek K. 2007. The DNA-dependent protein kinase catalytic subunit is phosphorylated in vivo on threonine 3950, a highly conserved amino acid in the protein kinase domain. Mol. Cell. Biol. 27:1581- 1591. http://dx.doi.org/10.1128/MCB.01962-06.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1581-1591
    • Douglas, P.1    Cui, X.2    Block, W.D.3    Yu, Y.4    Gupta, S.5    Ding, Q.6    Ye, R.7    Morrice, N.8    Lees-Miller, S.P.9    Meek, K.10
  • 18
    • 34248231265 scopus 로고    scopus 로고
    • trans Autophosphorylation at DNA-dependent protein kinase's two major autophosphorylation site clusters facilitates end processing but not end joining
    • Meek K, Douglas P, Cui X, Ding Q, Lees-Miller SP. 2007. trans Autophosphorylation at DNA-dependent protein kinase's two major autophosphorylation site clusters facilitates end processing but not end joining. Mol. Cell. Biol. 27:3881-3890. http://dx.doi.org/10.1128/MCB.02366-06.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3881-3890
    • Meek, K.1    Douglas, P.2    Cui, X.3    Ding, Q.4    Lees-Miller, S.P.5
  • 19
    • 34247507469 scopus 로고    scopus 로고
    • Ataxia telangiectasia mutated (ATM) is essential for DNA-PKcs phosphorylations at the Thr-2609 cluster upon DNA double strand break
    • Chen BP, Uematsu N, Kobayashi J, Lerenthal Y, Krempler A, Yajima H,Lobrich M, Shiloh Y, Chen DJ. 2007. Ataxia telangiectasia mutated (ATM) is essential for DNA-PKcs phosphorylations at the Thr-2609 cluster upon DNA double strand break. J. Biol. Chem. 282:6582-6587. http://dx.doi.org/10.1074/jbc.M611605200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 6582-6587
    • Chen, B.P.1    Uematsu, N.2    Kobayashi, J.3    Lerenthal, Y.4    Krempler, A.5    Yajima, H.6    Lobrich, M.7    Shiloh, Y.8    Chen, D.J.9
  • 20
    • 33749611701 scopus 로고    scopus 로고
    • ATR-dependent phosphorylation of DNA-dependent protein kinase catalytic subunit in response to UVinduced replication stress
    • Yajima H, Lee KJ, Chen BP. 2006. ATR-dependent phosphorylation of DNA-dependent protein kinase catalytic subunit in response to UVinduced replication stress. Mol. Cell. Biol. 26:7520-7528. http://dx.doi.org/10.1128/MCB.00048-06.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 7520-7528
    • Yajima, H.1    Lee, K.J.2    Chen, B.P.3
  • 22
    • 0034662228 scopus 로고    scopus 로고
    • Both V(D)J,. recombination and radioresistance require DNA-PK kinase activity, though minimal levels suffice for V(D)J. recombination
    • Kienker LJ, Shin EK, Meek K. 2000. Both V(D)J. recombination and radioresistance require DNA-PK kinase activity, though minimal levels suffice for V(D)J. recombination. Nucleic Acids Res. 28:2752-2761. http://dx.doi.org/10.1093/nar/28.14.2752.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2752-2761
    • Kienker, L.J.1    Shin, E.K.2    Meek, K.3
  • 23
    • 0034132349 scopus 로고    scopus 로고
    • Analyses of TCRB rearrangements substantiate a profound deficit in recombination signal sequence joining in SCID foals: implications for the role of DNA-dependent protein kinase in V(D)J. recombination.
    • Shin EK, Rijkers T, Pastink A, Meek K. 2000. Analyses of TCRB rearrangements substantiate a profound deficit in recombination signal sequence joining in SCID foals: implications for the role of DNA-dependent protein kinase in V(D)J. recombination. J. Immunol. 164:1416-1424.
    • (2000) J. Immunol. , vol.164 , pp. 1416-1424
    • Shin, E.K.1    Rijkers, T.2    Pastink, A.3    Meek, K.4
  • 24
    • 14844292557 scopus 로고    scopus 로고
    • DNA-dependent protein kinase and XRCC4-DNA ligase IV mobilization in the cell in response toDNAdouble strand breaks
    • Drouet J, Delteil C, Lefrancois J, Concannon P, Salles B, Calsou P. 2005. DNA-dependent protein kinase and XRCC4-DNA ligase IV mobilization in the cell in response toDNAdouble strand breaks. J. Biol. Chem. 280:7060-7069. http://dx.doi.org/10.1074/jbc.M410746200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 7060-7069
    • Drouet, J.1    Delteil, C.2    Lefrancois, J.3    Concannon, P.4    Salles, B.5    Calsou, P.6
  • 25
    • 0023659483 scopus 로고
    • Extrachromosomal DNA substrates in pre-B cells undergo inversion or deletion at immunoglobulin V-(D)-J
    • Hesse JE, Lieber MR, Gellert M, Mizuuchi K. 1987. Extrachromosomal DNA substrates in pre-B cells undergo inversion or deletion at immunoglobulin V-(D)-J. joining signals. Cell 49:775-783. http://dx.doi.org/10.1016/0092-8674(87)90615-5.
    • (1987) joining signals. Cell , vol.49 , pp. 775-783
    • Hesse, J.E.1    Lieber, M.R.2    Gellert, M.3    Mizuuchi, K.4
  • 27
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin LJ, Bryson K, Jones DT. 2000. The PSIPRED protein structure prediction server. Bioinformatics 16:404-405. http://dx.doi.org/10.1093/bioinformatics/16.4.404.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 28
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction.
    • Soding J, Biegert A, Lupas AN. 2005. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33:W244-W248. http://dx.doi.org/10.1093/nar/gki408.
    • (2005) Nucleic Acids Res. , vol.33
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3
  • 29
    • 73849140503 scopus 로고    scopus 로고
    • Crystal structure of DNA-PKcs reveals a large open-ring cradle comprised of HEAT repeats
    • Sibanda BL, Chirgadze DY, Blundell TL. 2010. Crystal structure of DNA-PKcs reveals a large open-ring cradle comprised of HEAT repeats. Nature 463:118-121. http://dx.doi.org/10.1038/nature08648.
    • (2010) Nature , vol.463 , pp. 118-121
    • Sibanda, B.L.1    Chirgadze, D.Y.2    Blundell, T.L.3
  • 31
    • 0035866764 scopus 로고    scopus 로고
    • Severe combined immunodeficient cells expressing mutant hRAD54 exhibit a marked DNA double- strand break repair and error-prone chromosome repair defect.
    • Pluth JM, Fried LM, Kirchgessner CU. 2001. Severe combined immunodeficient cells expressing mutant hRAD54 exhibit a marked DNA double- strand break repair and error-prone chromosome repair defect. Cancer Res. 61:2649-2655.
    • (2001) Cancer Res , vol.61 , pp. 2649-2655
    • Pluth, J.M.1    Fried, L.M.2    Kirchgessner, C.U.3
  • 33
    • 0029763211 scopus 로고    scopus 로고
    • DNA-dependent protein kinase is a target for a CPP32-like apoptotic protease
    • Han Z, Malik N, Carter T, Reeves WH, Wyche JH, Hendrickson EA. 1996. DNA-dependent protein kinase is a target for a CPP32-like apoptotic protease. J. Biol. Chem. 271:25035-25040. http://dx.doi.org/10.1074/jbc.271.40.25035.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25035-25040
    • Han, Z.1    Malik, N.2    Carter, T.3    Reeves, W.H.4    Wyche, J.H.5    Hendrickson, E.A.6
  • 34
    • 1942421722 scopus 로고    scopus 로고
    • RAG proteins shepherd double-strand breaks to a specific pathway, suppressing error-prone repair, butRAGnicking initiates homologous recombination.
    • Lee GS, Neiditch MB, Salus SS, Roth DB. 2004. RAG proteins shepherd double-strand breaks to a specific pathway, suppressing error-prone repair, butRAGnicking initiates homologous recombination. Cell 117:171-184.http://dx.doi.org/10.1016/S0092-8674(04)00301-0.
    • (2004) Cell , vol.117 , pp. 171-184
    • Lee, G.S.1    Neiditch, M.B.2    Salus, S.S.3    Roth, D.B.4
  • 35
    • 31144478506 scopus 로고    scopus 로고
    • The leucine rich region of DNA-PKcs contributes to its innate DNA affinity
    • Gupta S, Meek K. 2005. The leucine rich region of DNA-PKcs contributes to its innate DNA affinity. Nucleic Acids Res. 33:6972-6981. http://dx.doi.org/10.1093/nar/gki990.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 6972-6981
    • Gupta, S.1    Meek, K.2
  • 36
    • 2242484657 scopus 로고    scopus 로고
    • Identification of in vitro and in vivo phosphorylation sites in the catalytic subunit of the DNAdependent protein kinase
    • Douglas P, Sapkota GP, Morrice N, Yu Y, Goodarzi AA, Merkle D, Meek K, Alessi DR, Lees-Miller SP. 2002. Identification of in vitro and in vivo phosphorylation sites in the catalytic subunit of the DNAdependent protein kinase. Biochem. J. 368:243-251. http://dx.doi.org/10.1042/BJ20020973.
    • (2002) Biochem. J. , vol.368 , pp. 243-251
    • Douglas, P.1    Sapkota, G.P.2    Morrice, N.3    Yu, Y.4    Goodarzi, A.A.5    Merkle, D.6    Meek, K.7    Alessi, D.R.8    Lees-Miller, S.P.9
  • 37
    • 33646714595 scopus 로고    scopus 로고
    • Threedimensional structure of the human DNA-PKcs/Ku70/Ku80 complex assembled on DNA and its implications for DNA DSB repair
    • Spagnolo L, Rivera-Calzada A, Pearl LH, Llorca O. 2006. Threedimensional structure of the human DNA-PKcs/Ku70/Ku80 complex assembled on DNA and its implications for DNA DSB repair. Mol. Cell 22:511-519. http://dx.doi.org/10.1016/j.molcel.2006.04.013.
    • (2006) Mol. Cell , vol.22 , pp. 511-519
    • Spagnolo, L.1    Rivera-Calzada, A.2    Pearl, L.H.3    Llorca, O.4
  • 38
    • 13844253934 scopus 로고    scopus 로고
    • Three-dimensional structure and regulation of the DNA-dependent protein kinase catalytic subunit (DNA-PKcs)
    • Rivera-Calzada A, Maman JD, Spagnolo L, Pearl LH, Llorca O. 2005. Three-dimensional structure and regulation of the DNA-dependent protein kinase catalytic subunit (DNA-PKcs). Structure 13:243-255. http://dx.doi.org/10.1016/j.str.2004.12.006.
    • (2005) Structure , vol.13 , pp. 243-255
    • Rivera-Calzada, A.1    Maman, J.D.2    Spagnolo, L.3    Pearl, L.H.4    Llorca, O.5
  • 39
    • 3543077621 scopus 로고    scopus 로고
    • Electron microscopy studies on DNA recognition by DNA-PK
    • Llorca O, Pearl LH. 2004. Electron microscopy studies on DNA recognition by DNA-PK. Micron 35:625-633. http://dx.doi.org/10.1016/j.micron.2004.05.004.
    • (2004) Micron , vol.35 , pp. 625-633
    • Llorca, O.1    Pearl, L.H.2
  • 40
    • 0242576857 scopus 로고    scopus 로고
    • Visualization of DNA-induced conformational changes in the DNA repair kinase DNA-PKcs
    • Boskovic J, Rivera-Calzada A, Maman JD, Chacon P, Willison KR, Pearl LH, Llorca O. 2003. Visualization of DNA-induced conformational changes in the DNA repair kinase DNA-PKcs. EMBO J. 22:5875-5882. http://dx.doi.org/10.1093/emboj/cdg555.
    • (2003) EMBO J. , vol.22 , pp. 5875-5882
    • Boskovic, J.1    Rivera-Calzada, A.2    Maman, J.D.3    Chacon, P.4    Willison, K.R.5    Pearl, L.H.6    Llorca, O.7
  • 42
  • 43
    • 77953148666 scopus 로고    scopus 로고
    • Site-specific phosphorylation dynamics of the nuclear proteome during the DNA damage response
    • Bennetzen MV, Larsen DH, Bunkenborg J, Bartek J, Lukas J, Andersen JS. 2010. Site-specific phosphorylation dynamics of the nuclear proteome during the DNA damage response. Mol. Cell. Proteomics 9:1314-1323. http://dx.doi.org/10.1074/mcp.M900616-MCP200.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1314-1323
    • Bennetzen, M.V.1    Larsen, D.H.2    Bunkenborg, J.3    Bartek, J.4    Lukas, J.5    Andersen, J.S.6
  • 45
    • 0030009738 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit
    • Chan DW, Lees-Miller SP. 1996. The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit. J. Biol. Chem. 271:8936-8941. http://dx.doi.org/10.1074/jbc.271.15.8936.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8936-8941
    • Chan, D.W.1    Lees-Miller, S.P.2
  • 48
    • 84891396638 scopus 로고    scopus 로고
    • DNA-dependent Protein Kinase regulates DNA end resection in concert with the Mre11-Rad50-Nbs1 (MRN) complex and ataxia-telangiectasia-mutated (ATM)
    • Zhou Y, Paull TT. 2013. DNA-dependent Protein Kinase regulates DNA end resection in concert with the Mre11-Rad50-Nbs1 (MRN) complex and ataxia-telangiectasia-mutated (ATM). J. Biol. Chem. 288:37112- 37125. http://dx.doi.org/10.1074/jbc.M113.514398.
    • (2013) J. Biol. Chem. , vol.288 , pp. 37112-37125
    • Zhou, Y.1    Paull, T.T.2
  • 52
    • 0028897304 scopus 로고
    • DNAdependent protein kinase activity is absent in xrs-6 cells: implications for site-specific recombination and DNA double-strand break repair
    • Finnie NJ, Gottlieb TM, Blunt T, Jeggo PA, Jackson SP. 1995. DNAdependent protein kinase activity is absent in xrs-6 cells: implications for site-specific recombination and DNA double-strand break repair. Proc. Natl. Acad. Sci. U. S. A. 92:320-324. http://dx.doi.org/10.1073/pnas.92.1.320.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 320-324
    • Finnie, N.J.1    Gottlieb, T.M.2    Blunt, T.3    Jeggo, P.A.4    Jackson, S.P.5
  • 53
    • 0026687883 scopus 로고
    • Human DNA-activated protein kinase phosphorylates serines 15 and 37 in the amino-terminal transactivation domain of human p53.
    • Lees-Miller SP, Sakaguchi K, Ullrich SJ, Appella E, Anderson CW. 1992. Human DNA-activated protein kinase phosphorylates serines 15 and 37 in the amino-terminal transactivation domain of human p53. Mol. Cell. Biol. 12:5041-5049.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5041-5049
    • Lees-Miller, S.P.1    Sakaguchi, K.2    Ullrich, S.J.3    Appella, E.4    Anderson, C.W.5


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