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Volumn 10, Issue 21, 2011, Pages 3652-3657

Regulating the levels of key factors in cell cycle and DNA repair: New pathways revealed by lamins

Author keywords

A type lamins; Cell cycle; DNA repair; Proteases; Vitamin D

Indexed keywords

53BP1 PROTEIN; BRCA1 PROTEIN; CALCITRIOL; CATHEPSIN L; COLECALCIFEROL; HISTONE H2AX; HISTONE H3; LAMIN A; LAMIN C; OXYGENASE; PROTEIN P53; RAD51 PROTEIN; RETINOID X RECEPTOR; UNCLASSIFIED DRUG; VITAMIN D;

EID: 80655140622     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.10.21.18201     Document Type: Review
Times cited : (36)

References (51)
  • 1
    • 33745915850 scopus 로고    scopus 로고
    • Nuclear lamins: Laminopathies and their role in premature ageing
    • PMID:16816143; DOI:10.1152/phys-rev. 00047.2005
    • Broers JL, Ramaekers FC, Bonne G, Yaou RB, Hutchison CJ. Nuclear lamins: laminopathies and their role in premature ageing. Physiol Rev 2006; 86:967-1008; PMID:16816143; DOI:10.1152/phys-rev. 00047.2005.
    • (2006) Physiol Rev , vol.86 , pp. 967-1008
    • Broers, J.L.1    Ramaekers, F.C.2    Bonne, G.3    Yaou, R.B.4    Hutchison, C.J.5
  • 3
    • 10744229294 scopus 로고    scopus 로고
    • Lamin a truncation in Hutchinson-Gilford progeria
    • PMID:12702809; DOI:10.1126/science. 1084125
    • De Sandre-Giovannoli A, Bernard R, Cau P, Navarro C, Amiel J, Boccaccio I, et al. Lamin a truncation in Hutchinson-Gilford progeria. Science 2003; 300:2055; PMID:12702809; DOI:10.1126/science. 1084125.
    • (2003) Science , vol.300 , pp. 2055
    • De Sandre-Giovannoli, A.1    Bernard, R.2    Cau, P.3    Navarro, C.4    Amiel, J.5    Boccaccio, I.6
  • 4
    • 0037673950 scopus 로고    scopus 로고
    • Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome
    • PMID:12714972; DOI:10.1038/nature01629
    • Eriksson M, Brown WT, Gordon LB, Glynn MW, Singer J, Scott L, et al. Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome. Nature 2003; 423:293-8; PMID:12714972; DOI:10.1038/nature01629.
    • (2003) Nature , vol.423 , pp. 293-298
    • Eriksson, M.1    Brown, W.T.2    Gordon, L.B.3    Glynn, M.W.4    Singer, J.5    Scott, L.6
  • 5
    • 2942643923 scopus 로고    scopus 로고
    • Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson-Gilford progeria syndrome
    • PMID:15184648; DOI:10.1073/pnas.0402943101
    • Goldman RD, Shumaker DK, Erdos MR, Eriksson M, Goldman AE, Gordon LB, et al. Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson-Gilford progeria syndrome. Proc Natl Acad Sci USA 2004; 101:8963-8; PMID:15184648; DOI:10.1073/pnas.0402943101.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8963-8968
    • Goldman, R.D.1    Shumaker, D.K.2    Erdos, M.R.3    Eriksson, M.4    Goldman, A.E.5    Gordon, L.B.6
  • 6
    • 22544466685 scopus 로고    scopus 로고
    • Genomic instability in laminopathy-based premature aging
    • PMID:15980864; DOI:10.1038/nm1266
    • Liu B, Wang J, Chan KM, Tjia WM, Deng W, Guan X, et al. Genomic instability in laminopathy-based premature aging. Nat Med 2005; 11:780-5; PMID:15980864; DOI:10.1038/nm1266.
    • (2005) Nat Med , vol.11 , pp. 780-785
    • Liu, B.1    Wang, J.2    Chan, K.M.3    Tjia, W.M.4    Deng, W.5    Guan, X.6
  • 7
    • 33646745137 scopus 로고    scopus 로고
    • Lamin A-dependent nuclear defects in human aging
    • PMID:16645051; DOI:10.1126/science.1127168
    • Scaffidi P, Misteli T. Lamin A-dependent nuclear defects in human aging. Science 2006; 312:1059-63; PMID:16645051; DOI:10.1126/science.1127168.
    • (2006) Science , vol.312 , pp. 1059-1063
    • Scaffidi, P.1    Misteli, T.2
  • 8
    • 13944249618 scopus 로고    scopus 로고
    • DNA repair, genome stability and aging
    • PMID:15734682; DOI:10.1016/j.cell.2005.01.028
    • Lombard DB, Chua KF, Mostoslavsky R, Franco S, Gostissa M, Alt FW. DNA repair, genome stability and aging. Cell 2005; 120:497-512; PMID:15734682; DOI:10.1016/j.cell.2005.01.028.
    • (2005) Cell , vol.120 , pp. 497-512
    • Lombard, D.B.1    Chua, K.F.2    Mostoslavsky, R.3    Franco, S.4    Gostissa, M.5    Alt, F.W.6
  • 9
    • 69949144385 scopus 로고    scopus 로고
    • Genomic instability and DNA damage responses in progeria arising from defective maturation of prelamin A
    • (Albany NY) PMID:19851476
    • Musich PR, Zou Y. Genomic instability and DNA damage responses in progeria arising from defective maturation of prelamin A. Aging (Albany NY) 2009; 1:28-37; PMID:19851476.
    • (2009) Aging , vol.1 , pp. 28-37
    • Musich, P.R.1    Zou, Y.2
  • 10
    • 38949190562 scopus 로고    scopus 로고
    • Involvement of xeroderma pigmentosum group A (XPA) in progeria arising from defective maturation of prelamin A
    • PMID:17848622; DOI:10.1096/fj.07-8598com
    • Liu Y, Wang Y, Rusinol AE, Sinensky MS, Liu J, Shell SM, et al. Involvement of xeroderma pigmentosum group A (XPA) in progeria arising from defective maturation of prelamin A. FASEB J 2008; 22:603-11; PMID:17848622; DOI:10.1096/fj.07-8598com.
    • (2008) FASEB J , vol.22 , pp. 603-611
    • Liu, Y.1    Wang, Y.2    Rusinol, A.E.3    Sinensky, M.S.4    Liu, J.5    Shell, S.M.6
  • 11
    • 79954626173 scopus 로고    scopus 로고
    • Recapitulation of premature ageing with iPSCs from Hutchinson-Gilford progeria syndrome
    • PMID:21346760; DOI:10.1038/ nature09879
    • Liu GH, Barkho BZ, Ruiz S, Diep D, Qu J, Yang SL, et al. Recapitulation of premature ageing with iPSCs from Hutchinson-Gilford progeria syndrome. Nature 2011; 472:221-5; PMID:21346760; DOI:10.1038/ nature09879.
    • (2011) Nature , vol.472 , pp. 221-225
    • Liu, G.H.1    Barkho, B.Z.2    Ruiz, S.3    Diep, D.4    Qu, J.5    Yang, S.L.6
  • 12
    • 70350088548 scopus 로고    scopus 로고
    • Mechanisms of double-strand break repair in somatic mammalian cells
    • PMID:19772495; DOI:10.1042/BJ20090942
    • Hartlerode AJ, Scully R. Mechanisms of double-strand break repair in somatic mammalian cells. Biochem J 2009; 423:157-68; PMID:19772495; DOI:10.1042/BJ20090942.
    • (2009) Biochem J , vol.423 , pp. 157-168
    • Hartlerode, A.J.1    Scully, R.2
  • 13
    • 70350504453 scopus 로고    scopus 로고
    • The DNA-damage response in human biology and disease
    • PMID:19847258; DOI:10.1038/nature08467
    • Jackson SP, Bartek J. The DNA-damage response in human biology and disease. Nature 2009; 461:1071-8; PMID:19847258; DOI:10.1038/nature08467.
    • (2009) Nature , vol.461 , pp. 1071-1078
    • Jackson, S.P.1    Bartek, J.2
  • 14
    • 52049098230 scopus 로고    scopus 로고
    • Comparison of nonhomologous end joining and homologous recombination in human cells
    • (Amst) PMID:18675941; DOI:10.1016/j.dnarep.2008.06.018
    • Mao Z, Bozzella M, Seluanov A, Gorbunova V. Comparison of nonhomologous end joining and homologous recombination in human cells. DNA Repair (Amst) 2008; 7:1765-71; PMID:18675941; DOI:10.1016/j.dnarep.2008.06.018.
    • (2008) DNA Repair , vol.7 , pp. 1765-1771
    • Mao, Z.1    Bozzella, M.2    Seluanov, A.3    Gorbunova, V.4
  • 16
    • 2642570858 scopus 로고    scopus 로고
    • Mechanisms of DNA double strand break repair and chromosome aberration formation
    • PMID:15162010; DOI:10.1159/000077461
    • Iliakis G, Wang H, Perrault AR, Boecker W, Rosidi B, Windhofer F, et al. Mechanisms of DNA double strand break repair and chromosome aberration formation. Cytogenet Genome Res 2004; 104:14-20; PMID:15162010; DOI:10.1159/000077461.
    • (2004) Cytogenet Genome Res , vol.104 , pp. 14-20
    • Iliakis, G.1    Wang, H.2    Perrault, A.R.3    Boecker, W.4    Rosidi, B.5    Windhofer, F.6
  • 17
    • 33845657443 scopus 로고    scopus 로고
    • PARP-1 and Ku compete for repair of DNA double strand breaks by distinct NHEJ pathways
    • PMID:17088286; DOI:10.1093/nar/gkl840
    • Wang M, Wu W, Wu W, Rosidi B, Zhang L, Wang H, et al. PARP-1 and Ku compete for repair of DNA double strand breaks by distinct NHEJ pathways. Nucleic Acids Res 2006; 34:6170-82; PMID:17088286; DOI:10.1093/nar/gkl840.
    • (2006) Nucleic Acids Res , vol.34 , pp. 6170-6182
    • Wang, M.1    Wu, W.2    Wu, W.3    Rosidi, B.4    Zhang, L.5    Wang, H.6
  • 18
    • 69249222566 scopus 로고    scopus 로고
    • Novel roles for A-type lamins in telomere biology and the DNA damage response pathway
    • PMID:19629036; DOI:10.1038/emboj.2009.196
    • Gonzalez-Suarez I, Redwood AB, Perkins SM, Vermolen B, Lichtensztejin D, Grotsky DA, et al. Novel roles for A-type lamins in telomere biology and the DNA damage response pathway. EMBO J 2009; 28:2414-27; PMID:19629036; DOI:10.1038/emboj.2009.196.
    • (2009) EMBO J , vol.28 , pp. 2414-2427
    • Gonzalez-Suarez, I.1    Redwood, A.B.2    Perkins, S.M.3    Vermolen, B.4    Lichtensztejin, D.5    Grotsky, D.A.6
  • 19
    • 79961121348 scopus 로고    scopus 로고
    • A dual role for A-type lamins in DNA double-strand breaks repair
    • PMID:21701264; DOI:10.4161/cc.10.15.16531
    • Redwood AB, Perkins SM, Vanderwaal RP, Feng Z, Biehl KJ, Gonzalez-Suarez I, et al. A dual role for A-type lamins in DNA double-strand breaks repair. Cell Cycle 2011; 10:2549-60; PMID:21701264; DOI:10.4161/cc.10.15.16531.
    • (2011) Cell Cycle , vol.10 , pp. 2549-2560
    • Redwood, A.B.1    Perkins, S.M.2    Vanderwaal, R.P.3    Feng, Z.4    Biehl, K.J.5    Gonzalez-Suarez, I.6
  • 20
    • 59649119501 scopus 로고    scopus 로고
    • Crosstalk between chromatin structure, nuclear compartmentalization and telomere biology
    • PMID:19188688; DOI:10.1159/000167805
    • Gonzalez-Suarez I, Gonzalo S. Crosstalk between chromatin structure, nuclear compartmentalization and telomere biology. Cytogenet Genome Res 2008; 122:202-10; PMID:19188688; DOI:10.1159/000167805.
    • (2008) Cytogenet Genome Res , vol.122 , pp. 202-210
    • Gonzalez-Suarez, I.1    Gonzalo, S.2
  • 21
    • 74849107200 scopus 로고    scopus 로고
    • Loss of A-type lamins and genomic instability
    • PMID:19901537; DOI:10.4161/cc.8.23.10092
    • Gonzalez-Suarez I, Redwood AB, Gonzalo S. Loss of A-type lamins and genomic instability. Cell Cycle 2009; 8:3860-5; PMID:19901537; DOI:10.4161/cc.8.23.10092.
    • (2009) Cell Cycle , vol.8 , pp. 3860-3865
    • Gonzalez-Suarez, I.1    Redwood, A.B.2    Gonzalo, S.3
  • 22
    • 57049124828 scopus 로고    scopus 로고
    • 53BP1 facilitates long-range DNA end-joining during V(D)J recombination
    • PMID:18931658; DOI:10.1038/nature07476
    • Difilippantonio S, Gapud E, Wong N, Huang CY, Mahowald G, Chen HT, et al. 53BP1 facilitates long-range DNA end-joining during V(D)J recombination. Nature 2008; 456:529-33; PMID:18931658; DOI:10.1038/nature07476.
    • (2008) Nature , vol.456 , pp. 529-533
    • Difilippantonio, S.1    Gapud, E.2    Wong, N.3    Huang, C.Y.4    Mahowald, G.5    Chen, H.T.6
  • 23
    • 2442707746 scopus 로고    scopus 로고
    • 53BP1 links DNA damage-response pathways to immunoglobulin heavy chain class-switch recombination
    • PMID:15077110; DOI:10.1038/ni1067
    • Manis JP, Morales JC, Xia Z, Kutok JL, Alt FW, Carpenter PB. 53BP1 links DNA damage-response pathways to immunoglobulin heavy chain class-switch recombination. Nat Immunol 2004; 5:481-7; PMID:15077110; DOI:10.1038/ni1067.
    • (2004) Nat Immunol , vol.5 , pp. 481-487
    • Manis, J.P.1    Morales, J.C.2    Xia, Z.3    Kutok, J.L.4    Alt, F.W.5    Carpenter, P.B.6
  • 24
    • 2542463148 scopus 로고    scopus 로고
    • 53BP1 is required for class switch recombination
    • PMID:15159415; DOI:10.1083/jcb.200403021
    • Ward IM, Reina-San-Martin B, Olaru A, Minn K, Tamada K, Lau JS, et al. 53BP1 is required for class switch recombination. J Cell Biol 2004; 165:459-64; PMID:15159415; DOI:10.1083/jcb.200403021.
    • (2004) J Cell Biol , vol.165 , pp. 459-464
    • Ward, I.M.1    Reina-San-Martin, B.2    Olaru, A.3    Minn, K.4    Tamada, K.5    Lau, J.S.6
  • 25
    • 57049132043 scopus 로고    scopus 로고
    • 53BP1 promotes nonhomologous end joining of telomeres by increasing chromatin mobility
    • PMID:18931659; DOI:10.1038/nature07433
    • Dimitrova N, Chen YC, Spector DL, de Lange T. 53BP1 promotes nonhomologous end joining of telomeres by increasing chromatin mobility. Nature 2008; 456:524-8; PMID:18931659; DOI:10.1038/nature07433.
    • (2008) Nature , vol.456 , pp. 524-528
    • Dimitrova, N.1    Chen, Y.C.2    Spector, D.L.3    De Lange, T.4
  • 26
    • 77951057068 scopus 로고    scopus 로고
    • 53BP1 regulates DNA resection and the choice between classical and alternative end joining during class switch recombination
    • PMID:20368578; DOI:10.1084/jem.20100244
    • Bothmer A, Robbiani DF, Feldhahn N, Gazumyan A, Nussenzweig A, Nussenzweig MC. 53BP1 regulates DNA resection and the choice between classical and alternative end joining during class switch recombination. J Exp Med 2010; 207:855-65; PMID:20368578; DOI:10.1084/jem.20100244.
    • (2010) J Exp Med , vol.207 , pp. 855-865
    • Bothmer, A.1    Robbiani, D.F.2    Feldhahn, N.3    Gazumyan, A.4    Nussenzweig, A.5    Nussenzweig, M.C.6
  • 27
    • 77950958141 scopus 로고    scopus 로고
    • 53BP1 inhibits homologous recombination in Brca1-deficient cells by blocking resection of DNA breaks
    • PMID:20362325; DOI:10.1016/j.cell.2010.03.012
    • Bunting SF, Callen E, Wong N, Chen HT, Polato F, Gunn A, et al. 53BP1 inhibits homologous recombination in Brca1-deficient cells by blocking resection of DNA breaks. Cell 2010; 141:243-54; PMID:20362325; DOI:10.1016/j.cell.2010. 03.012.
    • (2010) Cell , vol.141 , pp. 243-254
    • Bunting, S.F.1    Callen, E.2    Wong, N.3    Chen, H.T.4    Polato, F.5    Gunn, A.6
  • 28
    • 33646777783 scopus 로고    scopus 로고
    • Genetic dissection of vertebrate 53BP1: A major role in nonhomologous end joining of DNA double strand breaks
    • (Amst) PMID:16644291; DOI:10.1016/j.dnarep.2006.03.008
    • Nakamura K, Sakai W, Kawamoto T, Bree RT, Lowndes NF, Takeda S, et al. Genetic dissection of vertebrate 53BP1: a major role in nonhomologous end joining of DNA double strand breaks. DNA Repair (Amst) 2006; 5:741-9; PMID:16644291; DOI:10.1016/j.dnarep.2006.03.008.
    • (2006) DNA Repair , vol.5 , pp. 741-749
    • Nakamura, K.1    Sakai, W.2    Kawamoto, T.3    Bree, R.T.4    Lowndes, N.F.5    Takeda, S.6
  • 29
    • 0037772381 scopus 로고    scopus 로고
    • Role for the BRCA1 C-terminal repeats (BRCT) protein 53BP1 in maintaining genomic stability
    • PMID:12578828; DOI:10.1074/jbc.M212484200
    • Morales JC, Xia Z, Lu T, Aldrich MB, Wang B, Rosales C, et al. Role for the BRCA1 C-terminal repeats (BRCT) protein 53BP1 in maintaining genomic stability. J Biol Chem 2003; 278:14971-7; PMID:12578828; DOI:10.1074/jbc. M212484200.
    • (2003) J Biol Chem , vol.278 , pp. 14971-14977
    • Morales, J.C.1    Xia, Z.2    Lu, T.3    Aldrich, M.B.4    Wang, B.5    Rosales, C.6
  • 30
    • 0037378527 scopus 로고    scopus 로고
    • p53 Binding protein 53BP1 is required for DNA damage responses and tumor suppression in mice
    • PMID:12640136; DOI:10.1128/MCB.23.7.2556-63.2003
    • Ward IM, Minn K, van Deursen J, Chen J. p53 Binding protein 53BP1 is required for DNA damage responses and tumor suppression in mice. Mol Cell Biol 2003; 23:2556-63; PMID:12640136; DOI:10.1128/MCB.23.7.2556-63.2003.
    • (2003) Mol Cell Biol , vol.23 , pp. 2556-2563
    • Ward, I.M.1    Minn, K.2    Van Deursen, J.3    Chen, J.4
  • 31
    • 0037112212 scopus 로고    scopus 로고
    • 53BP1, a mediator of the DNA damage checkpoint
    • PMID:12364621; DOI:10.1126/science.1076182
    • Wang B, Matsuoka S, Carpenter PB, Elledge SJ. 53BP1, a mediator of the DNA damage checkpoint. Science 2002; 298:1435-8; PMID:12364621; DOI:10.1126/science.1076182.
    • (2002) Science , vol.298 , pp. 1435-1438
    • Wang, B.1    Matsuoka, S.2    Carpenter, P.B.3    Elledge, S.J.4
  • 32
    • 80155174987 scopus 로고    scopus 로고
    • A new pathway regulating 53BP1 stability implicates Cathepsin L and vitamin D in DNA repair
    • In press; PMID:21750527; DOI:10.1038/emboj.2011.225
    • Gonzalez-Suarez I, Redwood AB, Grotsky DE, Neumann M, Cheng E, Stewart CL, et al. A new pathway regulating 53BP1 stability implicates Cathepsin L and vitamin D in DNA repair. EMBO J 2011; In press; PMID:21750527; DOI:10.1038/emboj.2011.225.
    • (2011) EMBO J
    • Gonzalez-Suarez, I.1    Redwood, A.B.2    Grotsky, D.E.3    Neumann, M.4    Cheng, E.5    Stewart, C.L.6
  • 33
    • 0024780504 scopus 로고
    • Mechanisms and regulation of lysosomal proteolysis
    • PMID:2700097
    • Katunuma N. Mechanisms and regulation of lysosomal proteolysis. Revis Biol Celular 1989; 20:35-61; PMID:2700097.
    • (1989) Revis Biol Celular , vol.20 , pp. 35-61
    • Katunuma, N.1
  • 34
    • 77957855881 scopus 로고    scopus 로고
    • Specialized roles for cysteine cathepsins in health and disease
    • PMID:20921628; DOI:10.1172/JCI42918
    • Reiser J, Adair B, Reinheckel T. Specialized roles for cysteine cathepsins in health and disease. J Clin Invest 2010; 120:3421-31; PMID:20921628; DOI:10.1172/JCI42918.
    • (2010) J Clin Invest , vol.120 , pp. 3421-3431
    • Reiser, J.1    Adair, B.2    Reinheckel, T.3
  • 35
    • 33846643454 scopus 로고    scopus 로고
    • Cysteine cathepsins and the cutting edge of cancer invasion
    • PMID:17245112; DOI:10.4161/cc.6.1.3669
    • Gocheva V, Joyce JA. Cysteine cathepsins and the cutting edge of cancer invasion. Cell Cycle 2007; 6:60-4; PMID:17245112; DOI:10.4161/cc.6.1.3669.
    • (2007) Cell Cycle , vol.6 , pp. 60-64
    • Gocheva, V.1    Joyce, J.A.2
  • 36
    • 10044296973 scopus 로고    scopus 로고
    • Cysteine cathepsins in human cancer
    • PMID:15576321; DOI:10.1515/BC.2004.132
    • Jedeszko C, Sloane BF. Cysteine cathepsins in human cancer. Biol Chem 2004; 385:1017-27; PMID:15576321; DOI:10.1515/BC.2004.132.
    • (2004) Biol Chem , vol.385 , pp. 1017-1027
    • Jedeszko, C.1    Sloane, B.F.2
  • 37
    • 80053196652 scopus 로고    scopus 로고
    • Cathepsin L is highly expressed in gastrointestinal stromal tumors
    • PMID:21769426
    • Miyamoto K, Iwadate M, Yanagisawa Y, Ito E, Imai J, Yamamoto M, et al. Cathepsin L is highly expressed in gastrointestinal stromal tumors. Int J Oncol 2011; 39:1109-15; PMID:21769426.
    • (2011) Int J Oncol , vol.39 , pp. 1109-1115
    • Miyamoto, K.1    Iwadate, M.2    Yanagisawa, Y.3    Ito, E.4    Imai, J.5    Yamamoto, M.6
  • 38
    • 53549094681 scopus 로고    scopus 로고
    • Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation
    • PMID:18957203; DOI:10.1016/j. cell.2008.09.055
    • Duncan EM, Muratore-Schroeder TL, Cook RG, Garcia BA, Shabanowitz J, Hunt DF, et al. Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation. Cell 2008; 135:284-94; PMID:18957203; DOI:10.1016/j. cell.2008.09.055.
    • (2008) Cell , vol.135 , pp. 284-294
    • Duncan, E.M.1    Muratore-Schroeder, T.L.2    Cook, R.G.3    Garcia, B.A.4    Shabanowitz, J.5    Hunt, D.F.6
  • 39
    • 1942470581 scopus 로고    scopus 로고
    • A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor
    • PMID:15099520; DOI:10.1016/S1097-2765(04)00209-6
    • Goulet B, Baruch A, Moon NS, Poirier M, Sansregret LL, Erickson A, et al. A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Mol Cell 2004; 14:207-19; PMID:15099520; DOI:10.1016/S1097-2765(04)00209-6.
    • (2004) Mol Cell , vol.14 , pp. 207-219
    • Goulet, B.1    Baruch, A.2    Moon, N.S.3    Poirier, M.4    Sansregret, L.L.5    Erickson, A.6
  • 40
    • 25644440744 scopus 로고    scopus 로고
    • Accelerated ageing in mice deficient in Zmpste24 protease is linked to p53 signalling activation
    • PMID:16079796; DOI:10.1038/nature04019
    • Varela I, Cadinanos J, Pendas AM, Gutierrez-Fernandez A, Folgueras AR, Sanchez LM, et al. Accelerated ageing in mice deficient in Zmpste24 protease is linked to p53 signalling activation. Nature 2005; 437:564-8; PMID:16079796; DOI:10.1038/nature04019.
    • (2005) Nature , vol.437 , pp. 564-568
    • Varela, I.1    Cadinanos, J.2    Pendas, A.M.3    Gutierrez-Fernandez, A.4    Folgueras, A.R.5    Sanchez, L.M.6
  • 41
    • 77953291328 scopus 로고    scopus 로고
    • 53BP1 loss rescues BRCA1 deficiency and is associated with triplenegative and BRCA-mutated breast cancers
    • PMID:20453858; DOI:10.1038/nsmb.1831
    • Bouwman P, Aly A, Escandell JM, Pieterse M, Bartkova J, van der Gulden H, et al. 53BP1 loss rescues BRCA1 deficiency and is associated with triplenegative and BRCA-mutated breast cancers. Nat Struct Mol Biol 2010; 17:688-95; PMID:20453858; DOI:10.1038/nsmb.1831.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 688-695
    • Bouwman, P.1    Aly, A.2    Escandell, J.M.3    Pieterse, M.4    Bartkova, J.5    Van Der Gulden, H.6
  • 42
    • 34047112221 scopus 로고    scopus 로고
    • Repression of RAD51 gene expression by E2F4/p130 complexes in hypoxia
    • PMID:17001309; DOI:10.1038/sj.onc.1210001
    • Bindra RS, Glazer PM. Repression of RAD51 gene expression by E2F4/p130 complexes in hypoxia. Oncogene 2007; 26:2048-57; PMID:17001309; DOI:10.1038/sj.onc.1210001.
    • (2007) Oncogene , vol.26 , pp. 2048-2057
    • Bindra, R.S.1    Glazer, P.M.2
  • 43
    • 76649094290 scopus 로고    scopus 로고
    • Inhibition of poly(ADP-ribose) polymerase downregulates BRCA1 and RAD51 in a pathway mediated by E2F4 and p130
    • PMID:20133863; DOI:10.1073/pnas.0904783107
    • Hegan DC, Lu Y, Stachelek GC, Crosby ME, Bindra RS, Glazer PM. Inhibition of poly(ADP-ribose) polymerase downregulates BRCA1 and RAD51 in a pathway mediated by E2F4 and p130. Proc Natl Acad Sci USA 2010; 107:2201-6; PMID:20133863; DOI:10.1073/pnas.0904783107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2201-2206
    • Hegan, D.C.1    Lu, Y.2    Stachelek, G.C.3    Crosby, M.E.4    Bindra, R.S.5    Glazer, P.M.6
  • 44
    • 3042829496 scopus 로고    scopus 로고
    • A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteasomal degradation
    • PMID:15210943; DOI:10.1073/pnas.0403250101
    • Johnson BR, Nitta RT, Frock RL, Mounkes L, Barbie DA, Stewart CL, et al. A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteasomal degradation. Proc Natl Acad Sci USA 2004; 101:9677-82; PMID:15210943; DOI:10.1073/pnas.0403250101.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9677-9682
    • Johnson, B.R.1    Nitta, R.T.2    Frock, R.L.3    Mounkes, L.4    Barbie, D.A.5    Stewart, C.L.6
  • 45
    • 33745838652 scopus 로고    scopus 로고
    • Stabilization of the retinoblastoma protein by A-type nuclear lamins is required for INK4A-mediated cell cycle arrest
    • PMID:16809772; DOI:10.1128/MCB.02464-05
    • Nitta RT, Jameson SA, Kudlow BA, Conlan LA, Kennedy BK. Stabilization of the retinoblastoma protein by A-type nuclear lamins is required for INK4A-mediated cell cycle arrest. Mol Cell Biol 2006; 26:5360-72; PMID:16809772; DOI:10.1128/MCB.02464-05.
    • (2006) Mol Cell Biol , vol.26 , pp. 5360-5372
    • Nitta, R.T.1    Jameson, S.A.2    Kudlow, B.A.3    Conlan, L.A.4    Kennedy, B.K.5
  • 46
    • 41449094144 scopus 로고    scopus 로고
    • Evidence that proteasome-dependent degradation of the retinoblastoma protein in cells lacking A-type lamins occurs independently of gankyrin and MDM2
    • PMID:17896003; DOI:10.1371/Journal. pone.0000963
    • Nitta RT, Smith CL, Kennedy BK. Evidence that proteasome-dependent degradation of the retinoblastoma protein in cells lacking A-type lamins occurs independently of gankyrin and MDM2. PLoS ONE 2007; 2:963; PMID:17896003; DOI:10.1371/Journal. pone.0000963.
    • (2007) PLoS ONE , vol.2 , pp. 963
    • Nitta, R.T.1    Smith, C.L.2    Kennedy, B.K.3
  • 47
    • 33744769686 scopus 로고    scopus 로고
    • Mechanism of vitamin D receptor action
    • PMID:16831920; DOI:10.1196/annals.1346.026
    • Demay MB. Mechanism of vitamin D receptor action. Ann NY Acad Sci 2006; 1068:204-13; PMID:16831920; DOI:10.1196/annals.1346.026.
    • (2006) Ann NY Acad Sci , vol.1068 , pp. 204-213
    • Demay, M.B.1
  • 48
    • 78649697894 scopus 로고    scopus 로고
    • Vitamin D, disease and therapeutic opportunities
    • PMID:21119732; DOI:10.1038/nrd3318
    • Plum LA, DeLuca HF. Vitamin D, disease and therapeutic opportunities. Nat Rev Drug Discov 2010; 9:941-55; PMID:21119732; DOI:10.1038/nrd3318.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 941-955
    • Plum, L.A.1    DeLuca, H.F.2
  • 49
    • 68849107323 scopus 로고    scopus 로고
    • Cystatin D is a candidate tumor suppressor gene induced by vitamin D in human colon cancer cells
    • PMID:19662683; DOI:10.1172/JCI37205
    • Alvarez-Díaz S, Valle N, Garcia JM, Pena C, Freije JM, Quesada V, et al. Cystatin D is a candidate tumor suppressor gene induced by vitamin D in human colon cancer cells. J Clin Invest 2009; 119:2343-58; PMID:19662683; DOI:10.1172/JCI37205.
    • (2009) J Clin Invest , vol.119 , pp. 2343-2358
    • Alvarez-Díaz, S.1    Valle, N.2    Garcia, J.M.3    Pena, C.4    Freije, J.M.5    Quesada, V.6
  • 51
    • 0037485699 scopus 로고    scopus 로고
    • Vitamin D growth inhibition of breast cancer cells: Gene expression patterns assessed by cDNA microarray
    • PMID:12889598; DOI:10.1023/A:1024487118457
    • Swami S, Raghavachari N, Muller UR, Bao YP, Feldman D. Vitamin D growth inhibition of breast cancer cells: gene expression patterns assessed by cDNA microarray. Breast Cancer Res Treat 2003; 80:49-62; PMID:12889598; DOI:10.1023/A:1024487118457.
    • (2003) Breast Cancer Res Treat , vol.80 , pp. 49-62
    • Swami, S.1    Raghavachari, N.2    Muller, U.R.3    Bao, Y.P.4    Feldman, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.