메뉴 건너뛰기




Volumn 1830, Issue 11, 2013, Pages 5316-5325

Oxidative stress-induced cyclin D1 depletion and its role in cell cycle processing

Author keywords

Cell cycle; Chk1; Oxidative stress; Proteolysis; Translational repression

Indexed keywords

CHECKPOINT KINASE 1; CYCLIN D1; HYDROGEN PEROXIDE; INITIATION FACTOR 2ALPHA; PHOSPHOTRANSFERASE; PROTEASOME; PROTEIN KINASE PERK; UNCLASSIFIED DRUG;

EID: 84883526704     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2013.07.030     Document Type: Article
Times cited : (54)

References (70)
  • 1
    • 33847784791 scopus 로고    scopus 로고
    • Multiple levels of cyclin specificity in cell-cycle control
    • J. Bloom, and F.R. Cross Multiple levels of cyclin specificity in cell-cycle control Nat. Rev. Mol. Cell Biol. 8 2007 149 160
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 149-160
    • Bloom, J.1    Cross, F.R.2
  • 2
    • 0029119740 scopus 로고
    • Cell cycle control in mammalian cells: Role of cyclins, cyclin dependent kinases (CDKs), growth suppressor genes and cyclin-dependent kinase inhibitors (CKIs)
    • X. Grana, and E.P. Reddy Cell cycle control in mammalian cells: role of cyclins, cyclin dependent kinases (CDKs), growth suppressor genes and cyclin-dependent kinase inhibitors (CKIs) Oncogene 11 1995 211 219
    • (1995) Oncogene , vol.11 , pp. 211-219
    • Grana, X.1    Reddy, E.P.2
  • 3
    • 0031466305 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Engines, clocks, and microprocessors
    • D.O. Morgan Cyclin-dependent kinases: engines, clocks, and microprocessors Annu. Rev. Cell Dev. Biol. 13 1997 261 291
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 261-291
    • Morgan, D.O.1
  • 4
    • 69249230769 scopus 로고    scopus 로고
    • Mammalian cell-cycle regulation: Several Cdks, numerous cyclins and diverse compensatory mechanisms
    • A. Satyanarayana, and P. Kaldis Mammalian cell-cycle regulation: several Cdks, numerous cyclins and diverse compensatory mechanisms Oncogene 28 2009 2925 2939
    • (2009) Oncogene , vol.28 , pp. 2925-2939
    • Satyanarayana, A.1    Kaldis, P.2
  • 5
    • 0032491579 scopus 로고    scopus 로고
    • Cyclin D expression is controlled post-transcriptionally via a phosphatidylinositol 3-kinase/Akt-dependent pathway
    • R.C. Muise-Helmericks, H.L. Grimes, A. Bellacosa, S.E. Malstrom, P.N. Tsichlis, and N. Rosen Cyclin D expression is controlled post-transcriptionally via a phosphatidylinositol 3-kinase/Akt-dependent pathway J. Biol. Chem. 273 1998 29864 29872
    • (1998) J. Biol. Chem. , vol.273 , pp. 29864-29872
    • Muise-Helmericks, R.C.1    Grimes, H.L.2    Bellacosa, A.3    Malstrom, S.E.4    Tsichlis, P.N.5    Rosen, N.6
  • 6
    • 70349799010 scopus 로고    scopus 로고
    • The cell cycle is a redox cycle: Linking phase-specific targets to cell fate
    • N.H. Heintz, and W.C. Burhans The cell cycle is a redox cycle: linking phase-specific targets to cell fate Free Radic. Biol. Med. 47 2009 1282 1293
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 1282-1293
    • Heintz, N.H.1    Burhans, W.C.2
  • 7
    • 0037366104 scopus 로고    scopus 로고
    • Oxidative stress, cell cycle, and neurodegeneration
    • J.A. Klein, and S.L. Ackerman Oxidative stress, cell cycle, and neurodegeneration J. Clin. Invest. 111 2003 785 794
    • (2003) J. Clin. Invest. , vol.111 , pp. 785-794
    • Klein, J.A.1    Ackerman, S.L.2
  • 8
    • 0027154638 scopus 로고
    • Cyclin D1 is a nuclear protein required for cell cycle progression in G1
    • V. Baldin, J. Lukas, M.J. Marcote, M. Pagano, and G. Draetta Cyclin D1 is a nuclear protein required for cell cycle progression in G1 Genes Dev. 7 1993 812 821
    • (1993) Genes Dev. , vol.7 , pp. 812-821
    • Baldin, V.1    Lukas, J.2    Marcote, M.J.3    Pagano, M.4    Draetta, G.5
  • 9
    • 0028128954 scopus 로고
    • Differential expression and regulation of Cyclin D1 protein in normal and tumor human cells: Association with Cdk4 is required for Cyclin D1 function in G1 progression
    • S.W. Tam, A.M. Theodoras, J.W. Shay, G.F. Draetta, and M. Pagano Differential expression and regulation of Cyclin D1 protein in normal and tumor human cells: association with Cdk4 is required for Cyclin D1 function in G1 progression Oncogene 9 1994 2663 2674
    • (1994) Oncogene , vol.9 , pp. 2663-2674
    • Tam, S.W.1    Theodoras, A.M.2    Shay, J.W.3    Draetta, G.F.4    Pagano, M.5
  • 10
    • 0027288908 scopus 로고
    • Direct binding of cyclin D to the retinoblastoma gene product (pRb) and pRb phosphorylation by the cyclin D-dependent kinase CDK4
    • J. Kato, H. Matsushime, S.W. Hiebert, M.E. Ewen, and C.J. Sherr Direct binding of cyclin D to the retinoblastoma gene product (pRb) and pRb phosphorylation by the cyclin D-dependent kinase CDK4 Genes Dev. 7 1993 331 342
    • (1993) Genes Dev. , vol.7 , pp. 331-342
    • Kato, J.1    Matsushime, H.2    Hiebert, S.W.3    Ewen, M.E.4    Sherr, C.J.5
  • 11
    • 79960053984 scopus 로고    scopus 로고
    • Three observations that have changed our understanding of cyclin D1 and p27 in cell cycle control
    • D.W. Stacey Three observations that have changed our understanding of cyclin D1 and p27 in cell cycle control Genes Cancer 1 2010 1189 1199
    • (2010) Genes Cancer , vol.1 , pp. 1189-1199
    • Stacey, D.W.1
  • 12
    • 84862874781 scopus 로고    scopus 로고
    • Nitric oxide-donating aspirin induces G2/M phase cell cycle arrest in human cancer cells by regulating phase transition proteins
    • L. Gao, and J.L. Williams Nitric oxide-donating aspirin induces G2/M phase cell cycle arrest in human cancer cells by regulating phase transition proteins Int. J. Oncol. 41 2012 325 330
    • (2012) Int. J. Oncol. , vol.41 , pp. 325-330
    • Gao, L.1    Williams, J.L.2
  • 13
    • 0037376168 scopus 로고    scopus 로고
    • Cyclin D1 serves as a cell cycle regulatory switch in actively proliferating cells
    • D.W. Stacey Cyclin D1 serves as a cell cycle regulatory switch in actively proliferating cells Curr. Opin. Cell Biol. 15 2003 158 163
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 158-163
    • Stacey, D.W.1
  • 14
    • 13944249549 scopus 로고    scopus 로고
    • Destabilization of cyclin D1 message plays a critical role in cell cycle exit upon mitogen withdrawal
    • Y. Guo, J. Harwalkar, D.W. Stacey, and M. Hitomi Destabilization of cyclin D1 message plays a critical role in cell cycle exit upon mitogen withdrawal Oncogene 24 2005 1032 1042
    • (2005) Oncogene , vol.24 , pp. 1032-1042
    • Guo, Y.1    Harwalkar, J.2    Stacey, D.W.3    Hitomi, M.4
  • 15
    • 0030916209 scopus 로고    scopus 로고
    • Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway
    • J.A. Diehl, F. Zindy, and C.J. Sherr Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway Genes Dev. 11 1997 957 972
    • (1997) Genes Dev. , vol.11 , pp. 957-972
    • Diehl, J.A.1    Zindy, F.2    Sherr, C.J.3
  • 16
    • 0034634574 scopus 로고    scopus 로고
    • Osmotic stress regulates the stability of cyclin D1 in a p38SAPK2-dependent manner
    • O. Casanovas, F. Miro, J.M. Estanyol, E. Itarte, N. Agell, and O. Bachs Osmotic stress regulates the stability of cyclin D1 in a p38SAPK2-dependent manner J. Biol. Chem. 275 2000 35091 35097
    • (2000) J. Biol. Chem. , vol.275 , pp. 35091-35097
    • Casanovas, O.1    Miro, F.2    Estanyol, J.M.3    Itarte, E.4    Agell, N.5    Bachs, O.6
  • 17
    • 50249184808 scopus 로고    scopus 로고
    • Phosphorylation of cyclin D1 regulated by ATM or ATR controls cell cycle progression
    • M. Hitomi, K. Yang, A.W. Stacey, and D.W. Stacey Phosphorylation of cyclin D1 regulated by ATM or ATR controls cell cycle progression Mol. Cell. Biol. 28 2008 5478 5493
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 5478-5493
    • Hitomi, M.1    Yang, K.2    Stacey, A.W.3    Stacey, D.W.4
  • 18
    • 26644457201 scopus 로고    scopus 로고
    • IkappaB kinase alpha regulates subcellular distribution and turnover of cyclin D1 by phosphorylation
    • Y.T. Kwak, R. Li, C.R. Becerra, D. Tripathy, E.P. Frenkel, and U.N. Verma IkappaB kinase alpha regulates subcellular distribution and turnover of cyclin D1 by phosphorylation J. Biol. Chem. 280 2005 33945 33952
    • (2005) J. Biol. Chem. , vol.280 , pp. 33945-33952
    • Kwak, Y.T.1    Li, R.2    Becerra, C.R.3    Tripathy, D.4    Frenkel, E.P.5    Verma, U.N.6
  • 19
    • 41249089202 scopus 로고    scopus 로고
    • PKR and PKR-like endoplasmic reticulum kinase induce the proteasome-dependent degradation of cyclin D1 via a mechanism requiring eukaryotic initiation factor 2 alpha phosphorylation
    • J.F. Raven, D. Baltzis, S. Wang, Z. Mounir, A.I. Papadakis, H.Q. Gao, and A.E. Koromilas PKR and PKR-like endoplasmic reticulum kinase induce the proteasome-dependent degradation of cyclin D1 via a mechanism requiring eukaryotic initiation factor 2 alpha phosphorylation J. Biol. Chem. 283 2008 3097 3108
    • (2008) J. Biol. Chem. , vol.283 , pp. 3097-3108
    • Raven, J.F.1    Baltzis, D.2    Wang, S.3    Mounir, Z.4    Papadakis, A.I.5    Gao, H.Q.6    Koromilas, A.E.7
  • 20
    • 57349191639 scopus 로고    scopus 로고
    • Genotoxic stress-induced cyclin D1 phosphorylation and proteolysis are required for genomic stability
    • L.L. Pontano, P. Aggarwal, O. Barbash, E.J. Brown, C.H. Bassing, and J.A. Diehl Genotoxic stress-induced cyclin D1 phosphorylation and proteolysis are required for genomic stability Mol. Cell. Biol. 28 2008 7245 7258
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 7245-7258
    • Pontano, L.L.1    Aggarwal, P.2    Barbash, O.3    Brown, E.J.4    Bassing, C.H.5    Diehl, J.A.6
  • 21
    • 0242526150 scopus 로고    scopus 로고
    • An alternatively spliced cyclin D1 isoform, cyclin D1b, is a nuclear oncogene
    • F. Lu, A.B. Gladden, and J.A. Diehl An alternatively spliced cyclin D1 isoform, cyclin D1b, is a nuclear oncogene Cancer Res. 63 2003 7056 7061
    • (2003) Cancer Res. , vol.63 , pp. 7056-7061
    • Lu, F.1    Gladden, A.B.2    Diehl, J.A.3
  • 23
    • 43149105398 scopus 로고    scopus 로고
    • Alteration of cyclin D1 transcript elongation by a mutated transcription factor up-regulates the oncogenic D1b splice isoform in cancer
    • G. Sanchez, D. Bittencourt, K. Laud, J. Barbier, O. Delattre, D. Auboeuf, and M. Dutertre Alteration of cyclin D1 transcript elongation by a mutated transcription factor up-regulates the oncogenic D1b splice isoform in cancer Proc. Natl. Acad. Sci. U. S. A. 105 2008 6004 6009
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 6004-6009
    • Sanchez, G.1    Bittencourt, D.2    Laud, K.3    Barbier, J.4    Delattre, O.5    Auboeuf, D.6    Dutertre, M.7
  • 26
  • 27
    • 0001952829 scopus 로고    scopus 로고
    • Redox signaling: Hydrogen peroxide as intracellular messenger
    • S.G. Rhee Redox signaling: hydrogen peroxide as intracellular messenger Exp. Mol. Med. 31 1999 53 59
    • (1999) Exp. Mol. Med. , vol.31 , pp. 53-59
    • Rhee, S.G.1
  • 28
    • 33646698671 scopus 로고    scopus 로고
    • Hydrogen peroxide: A signaling messenger
    • J.R. Stone, and S. Yang Hydrogen peroxide: a signaling messenger Antioxid. Redox Signal. 8 2006 243 270
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 243-270
    • Stone, J.R.1    Yang, S.2
  • 29
    • 81255200303 scopus 로고    scopus 로고
    • Human cytomegalovirus induces multiple means to combat reactive oxygen species
    • C. Tilton, A.J. Clippinger, T. Maguire, and J.C. Alwine Human cytomegalovirus induces multiple means to combat reactive oxygen species J. Virol. 85 2011 12585 12593
    • (2011) J. Virol. , vol.85 , pp. 12585-12593
    • Tilton, C.1    Clippinger, A.J.2    Maguire, T.3    Alwine, J.C.4
  • 30
    • 77749239882 scopus 로고    scopus 로고
    • Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site
    • J. Ling, and D. Soll Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site Proc. Natl. Acad. Sci. U. S. A. 107 2010 4028 4033
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 4028-4033
    • Ling, J.1    Soll, D.2
  • 31
    • 0033857531 scopus 로고    scopus 로고
    • The missing link: A single unifying mechanism for diabetic complications
    • T. Nishikawa, D. Edelstein, and M. Brownlee The missing link: A single unifying mechanism for diabetic complications Kidney Int. 58 2000 S26 S30
    • (2000) Kidney Int. , vol.58
    • Nishikawa, T.1    Edelstein, D.2    Brownlee, M.3
  • 33
    • 7244260490 scopus 로고    scopus 로고
    • Redox regulation of the calcium/calmodulin-dependent protein kinases
    • C.J. Howe, M.M. Lahair, J.A. McCubrey, and R.A. Franklin Redox regulation of the calcium/calmodulin-dependent protein kinases J. Biol. Chem. 279 2004 44573 44581
    • (2004) J. Biol. Chem. , vol.279 , pp. 44573-44581
    • Howe, C.J.1    Lahair, M.M.2    McCubrey, J.A.3    Franklin, R.A.4
  • 35
    • 0037861837 scopus 로고    scopus 로고
    • UV-induced free radicals in the skin detected by ESR spectroscopy and imaging using nitroxides
    • T. Herrling, J. Fuchs, J. Rehberg, and N. Groth UV-induced free radicals in the skin detected by ESR spectroscopy and imaging using nitroxides Free Radic. Biol. Med. 35 2003 59 67
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 59-67
    • Herrling, T.1    Fuchs, J.2    Rehberg, J.3    Groth, N.4
  • 36
    • 8544224992 scopus 로고    scopus 로고
    • Metal-induced oxidative stress and signal transduction
    • S.S. Leonard, G.K. Harris, and X.L. Shi Metal-induced oxidative stress and signal transduction Free Radic. Biol. Med. 37 2004 1921 1942
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 1921-1942
    • Leonard, S.S.1    Harris, G.K.2    Shi, X.L.3
  • 37
    • 43449100667 scopus 로고    scopus 로고
    • Reactive oxygen species: Current knowledge and applications in cancer research and therapeutic
    • A.T.Y. Lau, Y. Wang, and J.F. Chiu Reactive oxygen species: current knowledge and applications in cancer research and therapeutic J. Cell. Biochem. 104 2008 657 667
    • (2008) J. Cell. Biochem. , vol.104 , pp. 657-667
    • Lau, A.T.Y.1    Wang, Y.2    Chiu, J.F.3
  • 38
    • 0036910386 scopus 로고    scopus 로고
    • The role of hydrogen peroxide in endothelial proliferative responses
    • J.R. Stone, and T. Collins The role of hydrogen peroxide in endothelial proliferative responses Endothelium 9 2002 231 238
    • (2002) Endothelium , vol.9 , pp. 231-238
    • Stone, J.R.1    Collins, T.2
  • 39
    • 0032694302 scopus 로고    scopus 로고
    • The broad spectrum of responses to oxidants in proliferating cells: A new paradigm for oxidative stress
    • K.J.A. Davies The broad spectrum of responses to oxidants in proliferating cells: a new paradigm for oxidative stress IUBMB Life 48 1999 41 47
    • (1999) IUBMB Life , vol.48 , pp. 41-47
    • Davies, K.J.A.1
  • 40
    • 17844406439 scopus 로고    scopus 로고
    • Ubiquitination and degradation of the Arg tyrosine kinase is regulated by oxidative stress
    • C. Cao, Y. Li, Y. Leng, P. Li, Q. Ma, and D. Kufe Ubiquitination and degradation of the Arg tyrosine kinase is regulated by oxidative stress Oncogene 24 2005 2433 2440
    • (2005) Oncogene , vol.24 , pp. 2433-2440
    • Cao, C.1    Li, Y.2    Leng, Y.3    Li, P.4    Ma, Q.5    Kufe, D.6
  • 41
    • 57649221592 scopus 로고    scopus 로고
    • Hypoxic reactive oxygen species regulate the integrated stress response and cell survival
    • L.P. Liu, D.R. Wise, J.A. Diehl, and M.C. Simon Hypoxic reactive oxygen species regulate the integrated stress response and cell survival J. Biol. Chem. 283 2008 31153 31162
    • (2008) J. Biol. Chem. , vol.283 , pp. 31153-31162
    • Liu, L.P.1    Wise, D.R.2    Diehl, J.A.3    Simon, M.C.4
  • 43
    • 0242668688 scopus 로고    scopus 로고
    • Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation
    • H.A. Woo, H.Z. Chae, S.C. Hwang, K.S. Yang, S.W. Kang, K. Kim, and S.G. Rhee Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation Science 300 2003 653 656
    • (2003) Science , vol.300 , pp. 653-656
    • Woo, H.A.1    Chae, H.Z.2    Hwang, S.C.3    Yang, K.S.4    Kang, S.W.5    Kim, K.6    Rhee, S.G.7
  • 44
    • 0028982274 scopus 로고
    • P21 as a common signaling target of reactive free radicals and cellular redox stress
    • H.M. Lander, J.S. Ogiste, K.K. Teng, and A. Novogrodsky p21 as a common signaling target of reactive free radicals and cellular redox stress J. Biol. Chem. 270 1995 21195 21198
    • (1995) J. Biol. Chem. , vol.270 , pp. 21195-21198
    • Lander, H.M.1    Ogiste, J.S.2    Teng, K.K.3    Novogrodsky, A.4
  • 46
    • 17644373442 scopus 로고    scopus 로고
    • Redox regulation of cell-cycle re-entry: Cyclin D1 as a primary target for the mitogenic effects of reactive oxygen and nitrogen species
    • P.M. Burch, and N.H. Heintz Redox regulation of cell-cycle re-entry: cyclin D1 as a primary target for the mitogenic effects of reactive oxygen and nitrogen species Antioxid. Redox Signal. 7 2005 741 751
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 741-751
    • Burch, P.M.1    Heintz, N.H.2
  • 47
    • 21344440000 scopus 로고    scopus 로고
    • Reactive oxygen species as mediators of cellular senescence
    • R. Colavitti, and T. Finkel Reactive oxygen species as mediators of cellular senescence IUBMB Life 57 2005 277 281
    • (2005) IUBMB Life , vol.57 , pp. 277-281
    • Colavitti, R.1    Finkel, T.2
  • 48
    • 70349087001 scopus 로고    scopus 로고
    • Cell cycle arrest induced by hydrogen peroxide is associated with modulation of oxidative stress related genes in breast cancer cells
    • P.J. Chua, G.W. Yip, and B.H. Bay Cell cycle arrest induced by hydrogen peroxide is associated with modulation of oxidative stress related genes in breast cancer cells Exp. Biol. Med. (Maywood) 234 2009 1086 1094
    • (2009) Exp. Biol. Med. (Maywood) , vol.234 , pp. 1086-1094
    • Chua, P.J.1    Yip, G.W.2    Bay, B.H.3
  • 50
    • 69749116302 scopus 로고    scopus 로고
    • A new MIF4G domain-containing protein, CTIF, directs nuclear cap-binding protein CBP80/20-dependent translation
    • K.M. Kim, H. Cho, K. Choi, J. Kim, B.W. Kim, Y.G. Ko, S.K. Jang, and Y.K. Kim A new MIF4G domain-containing protein, CTIF, directs nuclear cap-binding protein CBP80/20-dependent translation Genes Dev. 23 2009 2033 2045
    • (2009) Genes Dev. , vol.23 , pp. 2033-2045
    • Kim, K.M.1    Cho, H.2    Choi, K.3    Kim, J.4    Kim, B.W.5    Ko, Y.G.6    Jang, S.K.7    Kim, Y.K.8
  • 51
    • 0024390302 scopus 로고
    • Nuclear distribution of the Ki-67 antigen during the cell cycle: Comparison with growth fraction in human breast cancer cells
    • J.H. van Dierendonck, R. Keijzer, C.J. van de Velde, and C.J. Cornelisse Nuclear distribution of the Ki-67 antigen during the cell cycle: comparison with growth fraction in human breast cancer cells Cancer Res. 49 1989 2999 3006
    • (1989) Cancer Res. , vol.49 , pp. 2999-3006
    • Van Dierendonck, J.H.1    Keijzer, R.2    Van De Velde, C.J.3    Cornelisse, C.J.4
  • 54
    • 0029825066 scopus 로고    scopus 로고
    • Role of inhibitory CDC2 phosphorylation in radiation-induced G2 arrest in human cells
    • P. Jin, Y. Gu, and D.O. Morgan Role of inhibitory CDC2 phosphorylation in radiation-induced G2 arrest in human cells J. Cell Biol. 134 1996 963 970
    • (1996) J. Cell Biol. , vol.134 , pp. 963-970
    • Jin, P.1    Gu, Y.2    Morgan, D.O.3
  • 56
    • 0031035528 scopus 로고    scopus 로고
    • Chk1 is a wee1 kinase in the G(2) DNA damage checkpoint inhibiting cdc2 by Y15 phosphorylation
    • M.J. O'Connell, J.M. Raleigh, H.M. Verkade, and P. Nurse Chk1 is a wee1 kinase in the G(2) DNA damage checkpoint inhibiting cdc2 by Y15 phosphorylation EMBO J. 16 1997 545 554
    • (1997) EMBO J. , vol.16 , pp. 545-554
    • O'Connell, M.J.1    Raleigh, J.M.2    Verkade, H.M.3    Nurse, P.4
  • 57
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling
    • T. Finkel Oxygen radicals and signaling Curr. Opin. Cell Biol. 10 1998 248 253
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 248-253
    • Finkel, T.1
  • 58
    • 79951518607 scopus 로고    scopus 로고
    • Molecular targets of oxidative stress
    • S.V. Avery Molecular targets of oxidative stress Biochem. J. 434 2011 201 210
    • (2011) Biochem. J. , vol.434 , pp. 201-210
    • Avery, S.V.1
  • 59
    • 79958210838 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases in mammalian oxidative stress responses
    • C. Runchel, A. Matsuzawa, and H. Ichijo Mitogen-activated protein kinases in mammalian oxidative stress responses Antioxid. Redox Signal. 15 2011 205 218
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 205-218
    • Runchel, C.1    Matsuzawa, A.2    Ichijo, H.3
  • 60
    • 33847349283 scopus 로고    scopus 로고
    • Reactive oxygen species: A breath of life or death?
    • J.P. Fruehauf, and F.L. Meyskens Jr. Reactive oxygen species: a breath of life or death? Clin. Cancer Res. 13 2007 789 794
    • (2007) Clin. Cancer Res. , vol.13 , pp. 789-794
    • Fruehauf, J.P.1    Meyskens, Jr.F.L.2
  • 61
    • 0034616913 scopus 로고    scopus 로고
    • Distinct initiation and maintenance mechanisms cooperate to induce G1 cell cycle arrest in response to DNA damage
    • R. Agami, and R. Bernards Distinct initiation and maintenance mechanisms cooperate to induce G1 cell cycle arrest in response to DNA damage Cell 102 2000 55 66
    • (2000) Cell , vol.102 , pp. 55-66
    • Agami, R.1    Bernards, R.2
  • 62
    • 17844382743 scopus 로고    scopus 로고
    • Phosphorylation of cyclin D1 at Thr 286 during S phase leads to its proteasomal degradation and allows efficient DNA synthesis
    • Y. Guo, K. Yang, J. Harwalkar, J.M. Nye, D.R. Mason, M.D. Garrett, M. Hitomi, and D.W. Stacey Phosphorylation of cyclin D1 at Thr 286 during S phase leads to its proteasomal degradation and allows efficient DNA synthesis Oncogene 24 2005 2599 2612
    • (2005) Oncogene , vol.24 , pp. 2599-2612
    • Guo, Y.1    Yang, K.2    Harwalkar, J.3    Nye, J.M.4    Mason, D.R.5    Garrett, M.D.6    Hitomi, M.7    Stacey, D.W.8
  • 64
    • 84862820415 scopus 로고    scopus 로고
    • Oxidative stress, endogenous antioxidants, alcohol, and hepatitis C: Pathogenic interactions and therapeutic considerations
    • J. Choi Oxidative stress, endogenous antioxidants, alcohol, and hepatitis C: pathogenic interactions and therapeutic considerations Free Radic. Biol. Med. 52 2012 1135 1150
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 1135-1150
    • Choi, J.1
  • 65
    • 33244481730 scopus 로고    scopus 로고
    • Expression of constitutively nuclear cyclin D1 in murine lymphocytes induces B-cell lymphoma
    • A.B. Gladden, R. Woolery, P. Aggarwal, M.A. Wasik, and J.A. Diehl Expression of constitutively nuclear cyclin D1 in murine lymphocytes induces B-cell lymphoma Oncogene 25 2006 998 1007
    • (2006) Oncogene , vol.25 , pp. 998-1007
    • Gladden, A.B.1    Woolery, R.2    Aggarwal, P.3    Wasik, M.A.4    Diehl, J.A.5
  • 66
    • 0037036460 scopus 로고    scopus 로고
    • Redox regulation of Cdc25C
    • P.A. Savitsky, and T. Finkel Redox regulation of Cdc25C J. Biol. Chem. 277 2002 20535 20540
    • (2002) J. Biol. Chem. , vol.277 , pp. 20535-20540
    • Savitsky, P.A.1    Finkel, T.2
  • 68
    • 33744544172 scopus 로고    scopus 로고
    • 14-3-3 proteins in cell cycle regulation
    • H. Hermeking, and A. Benzinger 14-3-3 proteins in cell cycle regulation Semin. Cancer Biol. 16 2006 183 192
    • (2006) Semin. Cancer Biol. , vol.16 , pp. 183-192
    • Hermeking, H.1    Benzinger, A.2
  • 69
    • 0030667428 scopus 로고    scopus 로고
    • Hyperphosphorylation of the N-terminal domain of Cdc25 regulates activity toward cyclin B1/Cdc2 but not cyclin A/Cdk2
    • B.G. Gabrielli, J.M. Clark, A.K. McCormack, and K.A. Ellem Hyperphosphorylation of the N-terminal domain of Cdc25 regulates activity toward cyclin B1/Cdc2 but not cyclin A/Cdk2 J. Biol. Chem. 272 1997 28607 28614
    • (1997) J. Biol. Chem. , vol.272 , pp. 28607-28614
    • Gabrielli, B.G.1    Clark, J.M.2    McCormack, A.K.3    Ellem, K.A.4
  • 70
    • 4344718628 scopus 로고    scopus 로고
    • Cdc25 phosphatases and cancer
    • K. Kristjansdottir, and J. Rudolph Cdc25 phosphatases and cancer Chem. Biol. 11 2004 1043 1051
    • (2004) Chem. Biol. , vol.11 , pp. 1043-1051
    • Kristjansdottir, K.1    Rudolph, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.