메뉴 건너뛰기




Volumn 2016, Issue , 2016, Pages

Histone Deacetylase Inhibitors Increase p27Kip1 by Affecting Its Ubiquitin-Dependent Degradation through Skp2 Downregulation

Author keywords

[No Author keywords available]

Indexed keywords

CELL DEATH; ENZYME INHIBITION; GENE EXPRESSION;

EID: 84949238554     PISSN: 19420900     EISSN: 19420994     Source Type: Journal    
DOI: 10.1155/2016/2481865     Document Type: Article
Times cited : (12)

References (64)
  • 1
    • 34249299791 scopus 로고    scopus 로고
    • The complex language of chromatin regulation during transcription
    • S. L. Berger, "The complex language of chromatin regulation during transcription, " Nature, vol. 447, no. 7143, pp. 407-412, 2007.
    • (2007) Nature , vol.447 , Issue.7143 , pp. 407-412
    • Berger, S.L.1
  • 2
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • T. Kouzarides, "Chromatin modifications and their function, " Cell, vol. 128, no. 4, pp. 693-705, 2007.
    • (2007) Cell , vol.128 , Issue.4 , pp. 693-705
    • Kouzarides, T.1
  • 3
    • 84863621527 scopus 로고    scopus 로고
    • Cancer epigenetics: From mechanism to therapy
    • M. A. Dawson and T. Kouzarides, "Cancer epigenetics: from mechanism to therapy, " Cell, vol. 150, no. 1, pp. 12-27, 2012.
    • (2012) Cell , vol.150 , Issue.1 , pp. 12-27
    • Dawson, M.A.1    Kouzarides, T.2
  • 4
    • 84908265816 scopus 로고    scopus 로고
    • Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders
    • K. J. Falkenberg and R. W. Johnstone, "Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders, " Nature Reviews Drug Discovery, vol. 13, no. 9, pp. 673-691, 2014.
    • (2014) Nature Reviews Drug Discovery , vol.13 , Issue.9 , pp. 673-691
    • Falkenberg, K.J.1    Johnstone, R.W.2
  • 5
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • H. A. Tissenbaum and L. Guarente, "Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans, " Nature, vol. 410, no. 6825, pp. 227-230, 2001.
    • (2001) Nature , vol.410 , Issue.6825 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 7
    • 84892942381 scopus 로고    scopus 로고
    • New and emerging HDAC inhibitors for cancer treatment
    • A. C. West and R. W. Johnstone, "New and emerging HDAC inhibitors for cancer treatment, "The Journal of Clinical Investigation, vol. 124, no. 1, pp. 30-39, 2014.
    • (2014) The Journal of Clinical Investigation , vol.124 , Issue.1 , pp. 30-39
    • West, A.C.1    Johnstone, R.W.2
  • 8
    • 0025104094 scopus 로고
    • Epidermal cell-shape regulation and subpopulation kinetics during butyrate-induced terminal maturation of normal and SV40-transformed human keratinocytes: Epithelial models of differentiation therapy
    • L. Staiano-Coico, M. Steinberg, and P. J. Higgins, "Epidermal cell-shape regulation and subpopulation kinetics during butyrate-induced terminal maturation of normal and SV40-transformed human keratinocytes: epithelial models of differentiation therapy, " International Journal of Cancer, vol. 46, no. 4, pp. 733-738, 1990.
    • (1990) International Journal of Cancer , vol.46 , Issue.4 , pp. 733-738
    • Staiano-Coico, L.1    Steinberg, M.2    Higgins, P.J.3
  • 9
    • 0027485599 scopus 로고
    • Sodium butyrate induces apoptosis in human colonic tumour cell lines in a p53-independent pathway: Implications for the possible role of dietary fibre in the prevention of large-bowel cancer
    • A. Hague, A. M. Manning, K. A. Hanlon, L. I. Huschtscha, D. Hart, and C. Paraskeva, "Sodium butyrate induces apoptosis in human colonic tumour cell lines in a p53-independent pathway: implications for the possible role of dietary fibre in the prevention of large-bowel cancer, " International Journal of Cancer, vol. 55, no. 3, pp. 498-505, 1993.
    • (1993) International Journal of Cancer , vol.55 , Issue.3 , pp. 498-505
    • Hague, A.1    Manning, A.M.2    Hanlon, K.A.3    Huschtscha, L.I.4    Hart, D.5    Paraskeva, C.6
  • 10
    • 0028286187 scopus 로고
    • Potentiation by specific short-chain fatty acids of differentiation and apoptosis in human colonic carcinoma cell lines
    • B. G. Heerdt, M. A. Houston, and L. H. Augenlicht, "Potentiation by specific short-chain fatty acids of differentiation and apoptosis in human colonic carcinoma cell lines, " Cancer Research, vol. 54, no. 12, pp. 3288-3293, 1994.
    • (1994) Cancer Research , vol.54 , Issue.12 , pp. 3288-3293
    • Heerdt, B.G.1    Houston, M.A.2    Augenlicht, L.H.3
  • 11
    • 84901490188 scopus 로고    scopus 로고
    • Butyrate impairs atherogenesis by reducing plaque inflammation and vulnerability and decreasing NFB activation
    • E. C. Aguilar, A. J. Leonel, L. G. Teixeira et al., "Butyrate impairs atherogenesis by reducing plaque inflammation and vulnerability and decreasing NFB activation, " Nutrition, Metabolism and Cardiovascular Diseases, vol. 24, no. 6, pp. 606-613, 2014.
    • (2014) Nutrition, Metabolism and Cardiovascular Diseases , vol.24 , Issue.6 , pp. 606-613
    • Aguilar, E.C.1    Leonel, A.J.2    Teixeira, L.G.3
  • 12
    • 0021956121 scopus 로고
    • Delay in the fetal globin switch in infants of diabetic mothers
    • S. P. Perrine, M. F. Greene, and D. V. Faller, "Delay in the fetal globin switch in infants of diabetic mothers, " The New England Journal of Medicine, vol. 312, no. 6, pp. 334-338, 1985.
    • (1985) The New England Journal of Medicine , vol.312 , Issue.6 , pp. 334-338
    • Perrine, S.P.1    Greene, M.F.2    Faller, D.V.3
  • 14
    • 0027078611 scopus 로고
    • Ashort-termtrial of butyrate to stimulate fetal-globin-gene expression in the -globin disorders
    • S. P. Perrine, G. D. Ginder, D. V. Faller et al., "Ashort-termtrial of butyrate to stimulate fetal-globin-gene expression in the -globin disorders, "TheNewEngland Journal ofMedicine, vol. 328, no. 2, pp. 81-86, 1993.
    • (1993) TheNewEngland Journal OfMedicine , vol.328 , Issue.2 , pp. 81-86
    • Perrine, S.P.1    Ginder, G.D.2    Faller, D.V.3
  • 15
    • 0029257858 scopus 로고
    • Butyrate in the treatment of sickle cell disease and -thalassemia
    • D. V. Faller and S. P. Perrine, "Butyrate in the treatment of sickle cell disease and -thalassemia, " CurrentOpinion inHematology, vol. 2, no. 2, pp. 109-117, 1995.
    • (1995) CurrentOpinion InHematology , vol.2 , Issue.2 , pp. 109-117
    • Faller, D.V.1    Perrine, S.P.2
  • 16
    • 33947275876 scopus 로고    scopus 로고
    • A phase 1/2 trial of arginine butyrate and ganciclovir in patients with Epstein-Barr virus-associated lymphoid malignancies
    • S. P. Perrine, O. Hermine, T. Small et al., "A phase 1/2 trial of arginine butyrate and ganciclovir in patients with Epstein-Barr virus-associated lymphoid malignancies, " Blood, vol. 109, no. 6, pp. 2571-2578, 2007.
    • (2007) Blood , vol.109 , Issue.6 , pp. 2571-2578
    • Perrine, S.P.1    Hermine, O.2    Small, T.3
  • 18
    • 18244383806 scopus 로고    scopus 로고
    • Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells
    • M. Göttlicher, S. Minucci, P. Zhu et al., "Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells, " The EMBO Journal, vol. 20, no. 24, pp. 6969-6978, 2001.
    • (2001) The EMBO Journal , vol.20 , Issue.24 , pp. 6969-6978
    • Göttlicher, M.1    Minucci, S.2    Zhu, P.3
  • 19
    • 38849187293 scopus 로고    scopus 로고
    • CDK inhibitors: Cell cycle regulators and beyond
    • A. Besson, S. F. Dowdy, and J. M. Roberts, "CDK inhibitors: cell cycle regulators and beyond, " Developmental Cell, vol. 14, no. 2, pp. 159-169, 2008.
    • (2008) Developmental Cell , vol.14 , Issue.2 , pp. 159-169
    • Besson, A.1    Dowdy, S.F.2    Roberts, J.M.3
  • 21
    • 79955859448 scopus 로고    scopus 로고
    • Targeting p27Kip1 protein: Its relevance in the therapy of human cancer
    • A. Borriello, D. Bencivenga, M. Criscuolo et al., "Targeting p27Kip1 protein: its relevance in the therapy of human cancer, " Expert Opinion on Therapeutic Targets, vol. 15, no. 6, pp. 677-693, 2011.
    • (2011) Expert Opinion on Therapeutic Targets , vol.15 , Issue.6 , pp. 677-693
    • Borriello, A.1    Bencivenga, D.2    Criscuolo, M.3
  • 22
    • 0042520999 scopus 로고    scopus 로고
    • 211 gene expression is modulated by Egr1: A novel regulatory mechanism involved in the resveratrol antiproliferative effect
    • F. Della Ragione, V. Cucciolla, V. Criniti, S. Indaco, A. Borriello, and V. Zappia, "211 gene expression is modulated by Egr1: A novel regulatory mechanism involved in the resveratrol antiproliferative effect, " Journal of Biological Chemistry, vol. 278, no. 26, pp. 23360-23368, 2003.
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23360-23368
    • Della Ragione, F.1    Cucciolla, V.2    Criniti, V.3    Indaco, S.4    Borriello, A.5    Zappia, V.6
  • 23
    • 0034610545 scopus 로고    scopus 로고
    • P27Kip1 accumulation is associated with retinoic-induced neuroblastoma differentiation: Evidence of a decreased proteasome-dependent degradation
    • A. Borriello, V. Della Pietra, M. Criscuolo et al., "p27Kip1 accumulation is associated with retinoic-induced neuroblastoma differentiation: evidence of a decreased proteasome-dependent degradation, " Oncogene, vol. 19, no. 1, pp. 51-60, 2000.
    • (2000) Oncogene , vol.19 , Issue.1 , pp. 51-60
    • Borriello, A.1    Della Pietra, V.2    Criscuolo, M.3
  • 24
    • 40949083876 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors upregulate p57Kip2 level by enhancing its expression through Sp1 transcription factor
    • V. Cucciolla, A. Borriello, M. Criscuolo et al., "Histone deacetylase inhibitors upregulate p57Kip2 level by enhancing its expression through Sp1 transcription factor, " Carcinogenesis, vol. 29, no. 3, pp. 560-567, 2008.
    • (2008) Carcinogenesis , vol.29 , Issue.3 , pp. 560-567
    • Cucciolla, V.1    Borriello, A.2    Criscuolo, M.3
  • 25
    • 84920597046 scopus 로고    scopus 로고
    • P27Kip1 serine 10 phosphorylation determines its metabolism and interaction with cyclin-dependent kinases
    • D. Bencivenga, A. Tramontano, A. Borgia et al., "p27Kip1 serine 10 phosphorylation determines its metabolism and interaction with cyclin-dependent kinases, " Cell Cycle, vol. 13, no. 23, pp. 3768-3782, 2014.
    • (2014) Cell Cycle , vol.13 , Issue.23 , pp. 3768-3782
    • Bencivenga, D.1    Tramontano, A.2    Borgia, A.3
  • 26
    • 33646248087 scopus 로고    scopus 로고
    • Retinoic acid induces p27 Kip1 nuclear accumulation by modulating its phosphorylation
    • A. Borriello, V. Cucciolla, M. Criscuolo et al., "Retinoic acid induces p27 Kip1 nuclear accumulation by modulating its phosphorylation, " Cancer Research, vol. 66, no. 8, pp. 4240-4248, 2006.
    • (2006) Cancer Research , vol.66 , Issue.8 , pp. 4240-4248
    • Borriello, A.1    Cucciolla, V.2    Criscuolo, M.3
  • 28
    • 80054699958 scopus 로고    scopus 로고
    • P57Kip2 and cancer: Time for a critical appraisal
    • A. Borriello, I. Caldarelli, D. Bencivenga et al., "p57Kip2 and cancer: Time for a critical appraisal, "Molecular Cancer Research, vol. 9, no. 10, pp. 1269-1284, 2011.
    • (2011) Molecular Cancer Research , vol.9 , Issue.10 , pp. 1269-1284
    • Borriello, A.1    Caldarelli, I.2    Bencivenga, D.3
  • 29
    • 42149170586 scopus 로고    scopus 로고
    • P27Kip1 nuclear localization and cyclin-dependent kinase inhibitory activity are regulated by glycogen synthase kinase-3 in human colon cancer cells
    • Q. Wang, Y. Zhou, X. Wang, and B. M. Evers, "p27Kip1 nuclear localization and cyclin-dependent kinase inhibitory activity are regulated by glycogen synthase kinase-3 in human colon cancer cells, " Cell Death and Differentiation, vol. 15, no. 5, pp. 908-919, 2008.
    • (2008) Cell Death and Differentiation , vol.15 , Issue.5 , pp. 908-919
    • Wang, Q.1    Zhou, Y.2    Wang, X.3    Evers, B.M.4
  • 30
    • 84861555689 scopus 로고    scopus 로고
    • Vorinostat enhances protein stability of p27 and p21 through negative regulation of Skp2 and Cks1 in human breast cancer cells
    • N. Uehara, K. Yoshizawa, and A. Tsubura, "Vorinostat enhances protein stability of p27 and p21 through negative regulation of Skp2 and Cks1 in human breast cancer cells, " Oncology Reports, vol. 28, no. 1, pp. 105-110, 2012.
    • (2012) Oncology Reports , vol.28 , Issue.1 , pp. 105-110
    • Uehara, N.1    Yoshizawa, K.2    Tsubura, A.3
  • 31
    • 84863752217 scopus 로고    scopus 로고
    • Dual effects of sodium butyrate on hepatocellular carcinoma cells
    • W. Jiang, Q. Guo, J. Wu et al., "Dual effects of sodium butyrate on hepatocellular carcinoma cells, " Molecular Biology Reports, vol. 39, no. 5, pp. 6235-6242, 2012.
    • (2012) Molecular Biology Reports , vol.39 , Issue.5 , pp. 6235-6242
    • Jiang, W.1    Guo, Q.2    Wu, J.3
  • 32
    • 0344012519 scopus 로고    scopus 로고
    • Vitamin D inhibits G1 to S progression in LNCaP prostate cancer cells through p27Kip1 stabilization and Cdk2 mislocalization to the cytoplasm
    • E. S. Yang and K. L. Burnstein, "Vitamin D inhibits G1 to S progression in LNCaP prostate cancer cells through p27Kip1 stabilization and Cdk2 mislocalization to the cytoplasm, " The Journal of Biological Chemistry, vol. 278, no. 47, pp. 46862-46868, 2003.
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 46862-46868
    • Yang, E.S.1    Burnstein, K.L.2
  • 33
    • 1642378661 scopus 로고    scopus 로고
    • Control of the SCFSkp2?Cks1 ubiquitin ligase by the APC/CCdh1 ubiquitin ligase
    • T. Bashir, N. V. Dorrello, V. Amado, D. Guardavaccaro, and M. Pagano, "Control of the SCFSkp2?Cks1 ubiquitin ligase by the APC/CCdh1 ubiquitin ligase, " Nature, vol. 428, no. 6979, pp. 190-193, 2004.
    • (2004) Nature , vol.428 , Issue.6979 , pp. 190-193
    • Bashir, T.1    Dorrello, N.V.2    Amado, V.3    Guardavaccaro, D.4    Pagano, M.5
  • 34
    • 1642399624 scopus 로고    scopus 로고
    • Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex
    • W. Wei, N. G. Ayad, Y. Wan, G.-J. Zhang, M. W. Kirschner, andW. G. Kaelin Jr., "Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex, " Nature, vol. 428, no. 6979, pp. 194-198, 2004.
    • (2004) Nature , vol.428 , Issue.6979 , pp. 194-198
    • Wei, W.1    Ayad, N.G.2    Wan, Y.3    Zhang, G.-J.4    Kirschner, M.W.5    Kaelin, W.G.6
  • 35
    • 64049087382 scopus 로고    scopus 로고
    • Phosphorylationdependent regulation of cytosolic localization and oncogenic function of Skp2 by Akt/PKB
    • H.-K. Lin, G. Wang, Z. Chen et al., "Phosphorylationdependent regulation of cytosolic localization and oncogenic function of Skp2 by Akt/PKB, " Nature Cell Biology, vol. 11, no. 4, pp. 420-432, 2009.
    • (2009) Nature Cell Biology , vol.11 , Issue.4 , pp. 420-432
    • Lin, H.-K.1    Wang, G.2    Chen, Z.3
  • 36
    • 64049086572 scopus 로고    scopus 로고
    • Phosphorylation by Akt1 promotes cytoplasmic localization of Skp2 and impairs APCCdh1-mediated Skp2 destruction
    • D. Gao, H. Inuzuka, A. Tseng, R. Y. Chin, A. Toker, andW. Wei, "Phosphorylation by Akt1 promotes cytoplasmic localization of Skp2 and impairs APCCdh1-mediated Skp2 destruction, " Nature Cell Biology, vol. 11, no. 4, pp. 397-408, 2009.
    • (2009) Nature Cell Biology , vol.11 , Issue.4 , pp. 397-408
    • Gao, D.1    Inuzuka, H.2    Tseng, A.3    Chin, R.Y.4    Toker, A.5    Wei, W.6
  • 37
    • 39449106065 scopus 로고    scopus 로고
    • Phosphorylation of Skp2 regulated by CDK2 and Cdc14B protects it from degradation by APCCdh1 in G1 phase
    • G. Rodier, P. Coulombe, P.-L. Tanguay, C. Boutonnet, and S. Meloche, "Phosphorylation of Skp2 regulated by CDK2 and Cdc14B protects it from degradation by APCCdh1 in G1 phase, " The EMBO Journal, vol. 27, no. 4, pp. 679-691, 2008.
    • (2008) The EMBO Journal , vol.27 , Issue.4 , pp. 679-691
    • Rodier, G.1    Coulombe, P.2    Tanguay, P.-L.3    Boutonnet, C.4    Meloche, S.5
  • 38
    • 84876888400 scopus 로고    scopus 로고
    • Sodium butyrate inhibits platelet-derived growth factor-induced proliferation and migration in pulmonary artery smooth muscle cells through Akt inhibition
    • S. Cantoni, M. Galletti, F. Zambelli et al., "Sodium butyrate inhibits platelet-derived growth factor-induced proliferation and migration in pulmonary artery smooth muscle cells through Akt inhibition, " FEBS Journal, vol. 280, no. 9, pp. 2042-2055, 2013.
    • (2013) FEBS Journal , vol.280 , Issue.9 , pp. 2042-2055
    • Cantoni, S.1    Galletti, M.2    Zambelli, F.3
  • 39
    • 33644663872 scopus 로고    scopus 로고
    • Histone acetylation-independent effect of histone deacetylase inhibitors on Akt through the reshuffling of protein phosphatase 1 complexes
    • C.-S. Chen, S.-C. Weng, P.-H. Tseng, H.-P. Lin, and C.-S. Chen, "Histone acetylation-independent effect of histone deacetylase inhibitors on Akt through the reshuffling of protein phosphatase 1 complexes, "The Journal of Biological Chemistry, vol. 280, no. 46, pp. 38879-38887, 2005.
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.46 , pp. 38879-38887
    • Chen, C.-S.1    Weng, S.-C.2    Tseng, P.-H.3    Lin, H.-P.4    Chen, C.-S.5
  • 40
    • 0032587495 scopus 로고    scopus 로고
    • P27kip1: A multifunctional cyclin-dependent kinase inhibitor with prognostic significance in human cancers
    • R. V. Lloyd, L. A. Erickson, L. Jin et al., "p27kip1: A multifunctional cyclin-dependent kinase inhibitor with prognostic significance in human cancers, " The American Journal of Pathology, vol. 154, no. 2, pp. 313-323, 1999.
    • (1999) The American Journal of Pathology , vol.154 , Issue.2 , pp. 313-323
    • Lloyd, R.V.1    Erickson, L.A.2    Jin, L.3
  • 41
    • 0035525781 scopus 로고    scopus 로고
    • Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: A case report
    • R. L. Piekarz, R. Robey, V. Sandor et al., "Inhibitor of histone deacetylation, depsipeptide (FR901228), in the treatment of peripheral and cutaneous T-cell lymphoma: A case report, " Blood, vol. 98, no. 9, pp. 2865-2868, 2001.
    • (2001) Blood , vol.98 , Issue.9 , pp. 2865-2868
    • Piekarz, R.L.1    Robey, R.2    Sandor, V.3
  • 42
    • 33748451151 scopus 로고    scopus 로고
    • Anticancer activities of histone deacetylase inhibitors
    • J. E. Bolden, M. J. Peart, and R. W. Johnstone, "Anticancer activities of histone deacetylase inhibitors, " Nature Reviews Drug Discovery, vol. 5, no. 9, pp. 769-784, 2006.
    • (2006) Nature Reviews Drug Discovery , vol.5 , Issue.9 , pp. 769-784
    • Bolden, J.E.1    Peart, M.J.2    Johnstone, R.W.3
  • 43
    • 34547683194 scopus 로고    scopus 로고
    • Phase IIBmulticenter trial of vorinostat in patients with persistent, progressive, or treatment refractory cutaneous t-cell lymphoma
    • E. A. Olsen, Y. H. Kim, T. M. Kuzel et al., "Phase IIBmulticenter trial of vorinostat in patients with persistent, progressive, or treatment refractory cutaneous t-cell lymphoma, " Journal of Clinical Oncology, vol. 25, no. 21, pp. 3109-3115, 2007.
    • (2007) Journal of Clinical Oncology , vol.25 , Issue.21 , pp. 3109-3115
    • Olsen, E.A.1    Kim, Y.H.2    Kuzel, T.M.3
  • 44
    • 77954879663 scopus 로고    scopus 로고
    • Final results from a multicenter, international, pivotal study of romidepsin in refractory cutaneous T-cell lymphoma
    • S. J. Whittaker, M.-F. Demierre, E. J. Kim et al., "Final results from a multicenter, international, pivotal study of romidepsin in refractory cutaneous T-cell lymphoma, " Journal of Clinical Oncology, vol. 28, no. 29, pp. 4485-4491, 2010.
    • (2010) Journal of Clinical Oncology , vol.28 , Issue.29 , pp. 4485-4491
    • Whittaker, S.J.1    Demierre, M.-F.2    Kim, E.J.3
  • 45
    • 73949149251 scopus 로고    scopus 로고
    • Phase II multiinstitutional trial of the histone deacetylase inhibitor romidepsin as monotherapy for patients with cutaneous T-cell lymphoma
    • R. L. Piekarz, R. Frye, M. Turner et al., "Phase II multiinstitutional trial of the histone deacetylase inhibitor romidepsin as monotherapy for patients with cutaneous T-cell lymphoma, " Journal of Clinical Oncology, vol. 27, no. 32, pp. 5410-5417, 2009.
    • (2009) Journal of Clinical Oncology , vol.27 , Issue.32 , pp. 5410-5417
    • Piekarz, R.L.1    Frye, R.2    Turner, M.3
  • 46
    • 0035694469 scopus 로고    scopus 로고
    • Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases
    • N. A. Barlev, L. Liu, N. H. Chehab et al., "Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases, " Molecular Cell, vol. 8, no. 6, pp. 1243-1254, 2001.
    • (2001) Molecular Cell , vol.8 , Issue.6 , pp. 1243-1254
    • Barlev, N.A.1    Liu, L.2    Chehab, N.H.3
  • 47
    • 27944448727 scopus 로고    scopus 로고
    • Dual regulation of c-Myc by p300 via acetylation-dependent control ofMyc protein turnover and coactivation of Myc-induced transcription
    • F. Faiola, X. Liu, S. Lo et al., "Dual regulation of c-Myc by p300 via acetylation-dependent control ofMyc protein turnover and coactivation of Myc-induced transcription, " Molecular and Cellular Biology, vol. 25, no. 23, pp. 10220-10234, 2005.
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.23 , pp. 10220-10234
    • Faiola, F.1    Liu, X.2    Lo, S.3
  • 49
    • 0032980308 scopus 로고    scopus 로고
    • The prognostic significance of altered cyclin-dependent kinase inhibitors in human cancer
    • J. Tsihlias, L. Kapusta, and J. Slingerland, "The prognostic significance of altered cyclin-dependent kinase inhibitors in human cancer, " Annual Review ofMedicine, vol. 50, pp. 401-423, 1999.
    • (1999) Annual Review OfMedicine , vol.50 , pp. 401-423
    • Tsihlias, J.1    Kapusta, L.2    Slingerland, J.3
  • 50
    • 0034011051 scopus 로고    scopus 로고
    • Multiple functions of p27(Kip1) and its alterations in tumor cells: A review
    • A. Sgambato, A. Cittadini, B. Faraglia, and I. B. Weinstein, "Multiple functions of p27(Kip1) and its alterations in tumor cells: A review, " Journal of Cellular Physiology, vol. 183, no. 1, pp. 18-27, 2000.
    • (2000) Journal of Cellular Physiology , vol.183 , Issue.1 , pp. 18-27
    • Sgambato, A.1    Cittadini, A.2    Faraglia, B.3    Weinstein, I.B.4
  • 51
    • 0029024015 scopus 로고
    • Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27
    • M. Pagano, S. W. Tam, A. M. Theodoras et al., "Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27, " Science, vol. 269, no. 5224, pp. 682-685, 1995.
    • (1995) Science , vol.269 , Issue.5224 , pp. 682-685
    • Pagano, M.1    Tam, S.W.2    Theodoras, A.M.3
  • 52
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • A. C. Carrano, E. Eytan, A. Hershko, and M. Pagano, "SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27, " Nature Cell Biology, vol. 1, no. 4, pp. 193-199, 1999.
    • (1999) Nature Cell Biology , vol.1 , Issue.4 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 53
    • 0033174070 scopus 로고    scopus 로고
    • P45SKP2 promotes p27Kip1 degradation and induces S phase in quiescent cells
    • H. Sutterlüty, E. Chatelain, A. Marti et al., "p45SKP2 promotes p27Kip1 degradation and induces S phase in quiescent cells, " Nature Cell Biology, vol. 1, no. 4, pp. 207-214, 1999.
    • (1999) Nature Cell Biology , vol.1 , Issue.4 , pp. 207-214
    • Sutterlüty, H.1    Chatelain, E.2    Marti, A.3
  • 54
    • 0035265829 scopus 로고    scopus 로고
    • A CDKindependent function of mammalian Cks1: Targeting of SCFSkp2 to the CDK inhibitor p27Kip1
    • C. Spruck, H. Strohmaier, M. Watson et al., "A CDKindependent function of mammalian Cks1: Targeting of SCFSkp2 to the CDK inhibitor p27Kip1, " Molecular Cell, vol. 7, no. 3, pp. 639-650, 2001.
    • (2001) Molecular Cell , vol.7 , Issue.3 , pp. 639-650
    • Spruck, C.1    Strohmaier, H.2    Watson, M.3
  • 55
    • 0035966104 scopus 로고    scopus 로고
    • Degradation of p27Kip1 at the G0-G1 transition mediated by a Skp2-independent ubiquitination pathway
    • T. Hara, T. Kamura, K. Nakayama, K. Oshikawa, S. Hatakeyama, and K.-I. Nakayama, "Degradation of p27Kip1 at the G0-G1 transition mediated by a Skp2-independent ubiquitination pathway, " The Journal of Biological Chemistry, vol. 276, no. 52, pp. 48937-48943, 2001.
    • (2001) The Journal of Biological Chemistry , vol.276 , Issue.52 , pp. 48937-48943
    • Hara, T.1    Kamura, T.2    Nakayama, K.3    Oshikawa, K.4    Hatakeyama, S.5    Nakayama, K.-I.6
  • 56
    • 0035921821 scopus 로고    scopus 로고
    • A mouse knock-in model exposes sequential proteolytic pathways that regulate p27Kip1 in G1 and S phase
    • N. P. Malek, H. Sundberg, S. McGrew, K. Nakayama, T. R. Kyriakidis, and J. M. Roberts, "A mouse knock-in model exposes sequential proteolytic pathways that regulate p27Kip1 in G1 and S phase, " Nature, vol. 413, no. 6853, pp. 323-327, 2001.
    • (2001) Nature , vol.413 , Issue.6853 , pp. 323-327
    • Malek, N.P.1    Sundberg, H.2    McGrew, S.3    Nakayama, K.4    Kyriakidis, T.R.5    Roberts, J.M.6
  • 57
    • 10344260649 scopus 로고    scopus 로고
    • Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1) at G1 phase
    • T. Kamura, T. Hara, M. Matsumoto et al., "Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1) at G1 phase, " Nature Cell Biology, vol. 6, no. 12, pp. 1229-1235, 2004.
    • (2004) Nature Cell Biology , vol.6 , Issue.12 , pp. 1229-1235
    • Kamura, T.1    Hara, T.2    Matsumoto, M.3
  • 58
    • 24044555556 scopus 로고    scopus 로고
    • Molecular dissection of the interaction between p27 and Kip1 ubiquitylation-promoting complex, the ubiquitin ligase that regulates proteolysis of p27 in G1 phase
    • S. Kotoshibai, T. Kamura, T. Hara, N. Ishida, and K. I. Nakayama, "Molecular dissection of the interaction between p27 and Kip1 ubiquitylation-promoting complex, the ubiquitin ligase that regulates proteolysis of p27 in G1 phase, " The Journal of Biological Chemistry, vol. 280, no. 18, pp. 17694-17700, 2005.
    • (2005) The Journal of Biological Chemistry , vol.280 , Issue.18 , pp. 17694-17700
    • Kotoshibai, S.1    Kamura, T.2    Hara, T.3    Ishida, N.4    Nakayama, K.I.5
  • 59
    • 29944440513 scopus 로고    scopus 로고
    • A pathway in quiescent cells that controls p271 stability, subcellular localization, and tumor suppression
    • A. Besson, M. Gurian-West, X. Chen, K. S. Kelly-Spratt, C. J. Kemp, and J. M. Roberts, "A pathway in quiescent cells that controls p271 stability, subcellular localization, and tumor suppression, " Genes and Development, vol. 20, no. 1, pp. 47-64, 2006.
    • (2006) Genes and Development , vol.20 , Issue.1 , pp. 47-64
    • Besson, A.1    Gurian-West, M.2    Chen, X.3    Kelly-Spratt, K.S.4    Kemp, C.J.5    Roberts, J.M.6
  • 60
    • 0041633899 scopus 로고    scopus 로고
    • Cell cycledependent regulation of the Skp2 promoter by GA-binding protein
    • H. Imaki, K. Nakayama, S. Delehouzee et al., "Cell cycledependent regulation of the Skp2 promoter by GA-binding protein, " Cancer Research, vol. 63, no. 15, pp. 4607-4613, 2003.
    • (2003) Cancer Research , vol.63 , Issue.15 , pp. 4607-4613
    • Imaki, H.1    Nakayama, K.2    Delehouzee, S.3
  • 61
    • 84863618431 scopus 로고    scopus 로고
    • Acetylationdependent regulation of Skp2 function
    • H. Inuzuka, D. Gao, L. W. S. Finley et al., "Acetylationdependent regulation of Skp2 function, " Cell, vol. 150, no. 1, pp. 179-193, 2012.
    • (2012) Cell , vol.150 , Issue.1 , pp. 179-193
    • Inuzuka, H.1    Gao, D.2    Finley, L.W.S.3
  • 62
    • 44349122993 scopus 로고    scopus 로고
    • Deregulated proteolysis by the Fbox proteins SKP2 and -TrCP: Tipping the scales of cancer
    • D. Frescas and M. Pagano, "Deregulated proteolysis by the Fbox proteins SKP2 and -TrCP: Tipping the scales of cancer, " Nature Reviews Cancer, vol. 8, no. 6, pp. 438-449, 2008.
    • (2008) Nature Reviews Cancer , vol.8 , Issue.6 , pp. 438-449
    • Frescas, D.1    Pagano, M.2
  • 63
    • 41149141967 scopus 로고    scopus 로고
    • Oncogenic properties and prognostic implications of the ubiquitin ligase Skp2 in cancer
    • D. D. Hershko, "Oncogenic properties and prognostic implications of the ubiquitin ligase Skp2 in cancer, " Cancer, vol. 112, no. 7, pp. 1415-1424, 2008.
    • (2008) Cancer , vol.112 , Issue.7 , pp. 1415-1424
    • Hershko, D.D.1
  • 64
    • 0037925520 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor valproic acid selectively induces proteasomal degradation of HDAC2
    • O. H. Krämer, P. Zhu, H. P. Ostendorff et al., "The histone deacetylase inhibitor valproic acid selectively induces proteasomal degradation of HDAC2, " The EMBO Journal, vol. 22, no. 13, pp. 3411-3420, 2003.
    • (2003) The EMBO Journal , vol.22 , Issue.13 , pp. 3411-3420
    • Krämer, O.H.1    Zhu, P.2    Ostendorff, H.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.