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Volumn 356, Issue 2, 2015, Pages 637-645

AK-1, a specific SIRT2 inhibitor, induces cell cycle arrest by downregulating Snail in HCT116 human colon carcinoma cells

Author keywords

AK 1; Cell cycle; G1 arrest; SIRT2; Snail

Indexed keywords

AK 1; CYCLIN DEPENDENT KINASE INHIBITOR 1A; ENZYME INHIBITOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MESSENGER RNA; PROTEASOME; PROTEIN P53; SIRTUIN 2; SMALL INTERFERING RNA; SULFONAMIDE; TRANSCRIPTION FACTOR SNAIL; UNCLASSIFIED DRUG; ANTINEOPLASTIC AGENT; CDKN1A PROTEIN, HUMAN; SIRT2 PROTEIN, HUMAN; SNAIL FAMILY TRANSCRIPTION FACTORS; TRANSCRIPTION FACTOR;

EID: 84919459426     PISSN: 03043835     EISSN: 18727980     Source Type: Journal    
DOI: 10.1016/j.canlet.2014.10.012     Document Type: Article
Times cited : (61)

References (51)
  • 1
    • 34547875773 scopus 로고    scopus 로고
    • Sirtuins: critical regulators at the crossroads between cancer and aging
    • Saunders L.R., Verdin E. Sirtuins: critical regulators at the crossroads between cancer and aging. Oncogene 2007, 26:5489-5504.
    • (2007) Oncogene , vol.26 , pp. 5489-5504
    • Saunders, L.R.1    Verdin, E.2
  • 2
    • 77149172855 scopus 로고    scopus 로고
    • SIRT2-mediated protein deacetylation: an emerging key regulator in brain physiology and pathology
    • Harting K., Knoll B. SIRT2-mediated protein deacetylation: an emerging key regulator in brain physiology and pathology. Eur. J. Cell Biol 2010, 89:262-269.
    • (2010) Eur. J. Cell Biol , vol.89 , pp. 262-269
    • Harting, K.1    Knoll, B.2
  • 3
    • 84885460070 scopus 로고    scopus 로고
    • Emerging role of sirtuins on tumorigenesis: possible link between aging and cancer
    • Cha Y.I., Kim H.S. Emerging role of sirtuins on tumorigenesis: possible link between aging and cancer. BMB Rep 2013, 46:429-438.
    • (2013) BMB Rep , vol.46 , pp. 429-438
    • Cha, Y.I.1    Kim, H.S.2
  • 5
    • 84962778960 scopus 로고    scopus 로고
    • SIRT2 is a tumor suppressor that connects aging, acetylome, cell cycle signaling, and carcinogenesis
    • Park S.H., Zhu Y., Ozden O., Kim H.S., Jiang H., Deng C.X., et al. SIRT2 is a tumor suppressor that connects aging, acetylome, cell cycle signaling, and carcinogenesis. Transl. Cancer Res 2012, 1:15-21.
    • (2012) Transl. Cancer Res , vol.1 , pp. 15-21
    • Park, S.H.1    Zhu, Y.2    Ozden, O.3    Kim, H.S.4    Jiang, H.5    Deng, C.X.6
  • 6
    • 34547599329 scopus 로고    scopus 로고
    • Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease
    • Outeiro T.F., Kontopoulos E., Altmann S.M., Kufareva I., Strathearn K.E., Amore A.M., et al. Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease. Science 2007, 317:516-519.
    • (2007) Science , vol.317 , pp. 516-519
    • Outeiro, T.F.1    Kontopoulos, E.2    Altmann, S.M.3    Kufareva, I.4    Strathearn, K.E.5    Amore, A.M.6
  • 8
    • 84871706585 scopus 로고    scopus 로고
    • The sirtuin 2 inhibitor AK-7 is neuroprotective in Huntington's disease mouse models
    • Chopra V., Quinti L., Kim J., Vollor L., Narayanan K.L., Edgerly C., et al. The sirtuin 2 inhibitor AK-7 is neuroprotective in Huntington's disease mouse models. Cell Rep 2012, 1492-1497.
    • (2012) Cell Rep , pp. 1492-1497
    • Chopra, V.1    Quinti, L.2    Kim, J.3    Vollor, L.4    Narayanan, K.L.5    Edgerly, C.6
  • 9
    • 79961053798 scopus 로고    scopus 로고
    • A brain-permeable small molecule reduces neuronal cholesterol by inhibiting activity of sirtuin 2 deacetylase
    • Taylor D.M., Balabadra U., Xiang Z., Woodman B., Meade S., Amore A., et al. A brain-permeable small molecule reduces neuronal cholesterol by inhibiting activity of sirtuin 2 deacetylase. ACS Chem. Biol 2011, 6:540-546.
    • (2011) ACS Chem. Biol , vol.6 , pp. 540-546
    • Taylor, D.M.1    Balabadra, U.2    Xiang, Z.3    Woodman, B.4    Meade, S.5    Amore, A.6
  • 10
    • 84865987956 scopus 로고    scopus 로고
    • Inhibition of sirtuin 2 with sulfobenzoic acid derivative AK1 is non-toxic and potentially neuroprotective in a mouse model of frontotemporal dementia
    • Spires-Jones T.L., Fox L.M., Rozkalne A., Pitstick R., Carlson G.A., Kazantsev A.G. Inhibition of sirtuin 2 with sulfobenzoic acid derivative AK1 is non-toxic and potentially neuroprotective in a mouse model of frontotemporal dementia. Front. Pharmacol 2012, 3:42.
    • (2012) Front. Pharmacol , vol.3 , pp. 42
    • Spires-Jones, T.L.1    Fox, L.M.2    Rozkalne, A.3    Pitstick, R.4    Carlson, G.A.5    Kazantsev, A.G.6
  • 11
    • 80054769188 scopus 로고    scopus 로고
    • SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity
    • Kim H.S., Vassilopoulos A., Wang R.H., Lahusen T., Xiao Z., Xu X., et al. SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity. Cancer Cell 2011, 20:487-499.
    • (2011) Cancer Cell , vol.20 , pp. 487-499
    • Kim, H.S.1    Vassilopoulos, A.2    Wang, R.H.3    Lahusen, T.4    Xiao, Z.5    Xu, X.6
  • 12
    • 84875309392 scopus 로고    scopus 로고
    • The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation
    • Serrano L., Martinez-Redondo P., Marazuela-Duque A., Vazquez B.N., Dooley S.J., Voigt P., et al. The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation. Genes Dev 2013, 27:639-653.
    • (2013) Genes Dev , vol.27 , pp. 639-653
    • Serrano, L.1    Martinez-Redondo, P.2    Marazuela-Duque, A.3    Vazquez, B.N.4    Dooley, S.J.5    Voigt, P.6
  • 13
    • 84884414960 scopus 로고    scopus 로고
    • Regulation of SIRT2 levels for human non-small cell lung cancer therapy
    • Li Z., Xie Q.R., Chen Z., Lu S., Xia W. Regulation of SIRT2 levels for human non-small cell lung cancer therapy. Lung Cancer 2013, 82:9-15.
    • (2013) Lung Cancer , vol.82 , pp. 9-15
    • Li, Z.1    Xie, Q.R.2    Chen, Z.3    Lu, S.4    Xia, W.5
  • 14
    • 84888294166 scopus 로고    scopus 로고
    • Sirt2 suppresses glioma cell growth through targeting NF-kappaB-miR-21 axis
    • Li Y., Dai D., Lu Q., Fei M., Li M., Wu X. Sirt2 suppresses glioma cell growth through targeting NF-kappaB-miR-21 axis. Biochem. Biophys. Res. Commun 2013, 441:661-667.
    • (2013) Biochem. Biophys. Res. Commun , vol.441 , pp. 661-667
    • Li, Y.1    Dai, D.2    Lu, Q.3    Fei, M.4    Li, M.5    Wu, X.6
  • 15
    • 78650638268 scopus 로고    scopus 로고
    • SIRT2 down-regulation in HeLa can induce p53 accumulation via p38 MAPK activation-dependent p300 decrease, eventually leading to apoptosis
    • Li Y., Matsumori H., Nakayama Y., Osaki M., Kojima H., Kurimasa A., et al. SIRT2 down-regulation in HeLa can induce p53 accumulation via p38 MAPK activation-dependent p300 decrease, eventually leading to apoptosis. Genes Cells 2011, 16:34-45.
    • (2011) Genes Cells , vol.16 , pp. 34-45
    • Li, Y.1    Matsumori, H.2    Nakayama, Y.3    Osaki, M.4    Kojima, H.5    Kurimasa, A.6
  • 16
  • 18
    • 84874542679 scopus 로고    scopus 로고
    • Inhibition of the NAD-dependent protein deacetylase SIRT2 induces granulocytic differentiation in human leukemia cells
    • Sunami Y., Araki M., Hironaka Y., Morishita S., Kobayashi M., Liew E.L., et al. Inhibition of the NAD-dependent protein deacetylase SIRT2 induces granulocytic differentiation in human leukemia cells. PLoS ONE 2013, 8:e57633.
    • (2013) PLoS ONE , vol.8 , pp. e57633
    • Sunami, Y.1    Araki, M.2    Hironaka, Y.3    Morishita, S.4    Kobayashi, M.5    Liew, E.L.6
  • 19
    • 84859447698 scopus 로고    scopus 로고
    • The role of Sirtuin 2 activation by nicotinamide phosphoribosyltransferase in the aberrant proliferation and survival of myeloid leukemia cells
    • Dan L., Klimenkova O., Klimiankou M., Klusmann J.H., van den Heuvel-Eibrink M.M., Reinhardt D., et al. The role of Sirtuin 2 activation by nicotinamide phosphoribosyltransferase in the aberrant proliferation and survival of myeloid leukemia cells. Haematologica 2012, 97:551-559.
    • (2012) Haematologica , vol.97 , pp. 551-559
    • Dan, L.1    Klimenkova, O.2    Klimiankou, M.3    Klusmann, J.H.4    van den Heuvel-Eibrink, M.M.5    Reinhardt, D.6
  • 20
    • 84894490851 scopus 로고    scopus 로고
    • A novel sirtuin 2 (SIRT2) inhibitor with p53-dependent pro-apoptotic activity in non-small cell lung cancer
    • Hoffmann G., Breitenbucher F., Schuler M., Ehrenhofer-Murray A.E. A novel sirtuin 2 (SIRT2) inhibitor with p53-dependent pro-apoptotic activity in non-small cell lung cancer. J. Biol. Chem 2014, 289:5208-5216.
    • (2014) J. Biol. Chem , vol.289 , pp. 5208-5216
    • Hoffmann, G.1    Breitenbucher, F.2    Schuler, M.3    Ehrenhofer-Murray, A.E.4
  • 22
    • 84883555139 scopus 로고    scopus 로고
    • HDAC6 and SIRT2 regulate the acetylation state and oncogenic activity of mutant K-RAS
    • Yang M.H., Laurent G., Bause A.S., Spang R., German N., Haigis M.C., et al. HDAC6 and SIRT2 regulate the acetylation state and oncogenic activity of mutant K-RAS. Mol. Cancer Res 2013, 11:1072-1077.
    • (2013) Mol. Cancer Res , vol.11 , pp. 1072-1077
    • Yang, M.H.1    Laurent, G.2    Bause, A.S.3    Spang, R.4    German, N.5    Haigis, M.C.6
  • 24
    • 84879081348 scopus 로고    scopus 로고
    • SIRT2 overexpression in hepatocellular carcinoma mediates epithelial to mesenchymal transition by protein kinase B/glycogen synthase kinase-3beta/beta-catenin signaling
    • Chen J., Chan A.W., To K.F., Chen W., Zhang Z., Ren J., et al. SIRT2 overexpression in hepatocellular carcinoma mediates epithelial to mesenchymal transition by protein kinase B/glycogen synthase kinase-3beta/beta-catenin signaling. Hepatology 2013, 57:2287-2298.
    • (2013) Hepatology , vol.57 , pp. 2287-2298
    • Chen, J.1    Chan, A.W.2    To, K.F.3    Chen, W.4    Zhang, Z.5    Ren, J.6
  • 25
    • 84863033018 scopus 로고    scopus 로고
    • HDAC6 and SIRT2 promote bladder cancer cell migration and invasion by targeting cortactin
    • Zuo Q., Wu W., Li X., Zhao L., Chen W. HDAC6 and SIRT2 promote bladder cancer cell migration and invasion by targeting cortactin. Oncol. Rep 2012, 27:819-824.
    • (2012) Oncol. Rep , vol.27 , pp. 819-824
    • Zuo, Q.1    Wu, W.2    Li, X.3    Zhao, L.4    Chen, W.5
  • 26
    • 84890448078 scopus 로고    scopus 로고
    • The sirtuins promote Dishevelled-1 scaffolding of TIAM1, Rac activation and cell migration
    • E-pub
    • Saxena M., Dykes S.S., Malyarchuk S., Wang A.E., Cardelli J.A., Pruitt K. The sirtuins promote Dishevelled-1 scaffolding of TIAM1, Rac activation and cell migration. Oncogene 2013, E-pub. 10.1038/onc.2013.549.
    • (2013) Oncogene
    • Saxena, M.1    Dykes, S.S.2    Malyarchuk, S.3    Wang, A.E.4    Cardelli, J.A.5    Pruitt, K.6
  • 27
    • 0041829415 scopus 로고    scopus 로고
    • Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene
    • Hiratsuka M., Inoue T., Toda T., Kimura N., Shirayoshi Y., Kamitani H., et al. Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene. Biochem. Biophys. Res. Commun 2003, 309:558-566.
    • (2003) Biochem. Biophys. Res. Commun , vol.309 , pp. 558-566
    • Hiratsuka, M.1    Inoue, T.2    Toda, T.3    Kimura, N.4    Shirayoshi, Y.5    Kamitani, H.6
  • 28
    • 33847053144 scopus 로고    scopus 로고
    • SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress
    • Inoue T., Hiratsuka M., Osaki M., Yamada H., Kishimoto I., Yamaguchi S., et al. SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress. Oncogene 2007, 26:945-957.
    • (2007) Oncogene , vol.26 , pp. 945-957
    • Inoue, T.1    Hiratsuka, M.2    Osaki, M.3    Yamada, H.4    Kishimoto, I.5    Yamaguchi, S.6
  • 29
    • 84878721346 scopus 로고    scopus 로고
    • Altered expression of SIRT gene family in head and neck squamous cell carcinoma
    • Lai C.C., Lin P.M., Lin S.F., Hsu C.H., Lin H.C., Hu M.L., et al. Altered expression of SIRT gene family in head and neck squamous cell carcinoma. Tumour Biol 2013, 34:1847-1854.
    • (2013) Tumour Biol , vol.34 , pp. 1847-1854
    • Lai, C.C.1    Lin, P.M.2    Lin, S.F.3    Hsu, C.H.4    Lin, H.C.5    Hu, M.L.6
  • 30
    • 84876523738 scopus 로고    scopus 로고
    • Three-gene immunohistochemical panel adds to clinical staging algorithms to predict prognosis for patients with esophageal adenocarcinoma
    • Ong C.A., Shapiro J., Nason K.S., Davison J.M., Liu X., Ross-Innes C., et al. Three-gene immunohistochemical panel adds to clinical staging algorithms to predict prognosis for patients with esophageal adenocarcinoma. J. Clin. Oncol 2013, 31:1576-1582.
    • (2013) J. Clin. Oncol , vol.31 , pp. 1576-1582
    • Ong, C.A.1    Shapiro, J.2    Nason, K.S.3    Davison, J.M.4    Liu, X.5    Ross-Innes, C.6
  • 31
    • 48149115853 scopus 로고    scopus 로고
    • High histone deacetylase 7 (HDAC7) expression is significantly associated with adenocarcinomas of the pancreas
    • Ouaissi M., Sielezneff I., Silvestre R., Sastre B., Bernard J.P., Lafontaine J.S., et al. High histone deacetylase 7 (HDAC7) expression is significantly associated with adenocarcinomas of the pancreas. Ann. Surg. Oncol 2008, 15:2318-2328.
    • (2008) Ann. Surg. Oncol , vol.15 , pp. 2318-2328
    • Ouaissi, M.1    Sielezneff, I.2    Silvestre, R.3    Sastre, B.4    Bernard, J.P.5    Lafontaine, J.S.6
  • 32
    • 84859447698 scopus 로고    scopus 로고
    • The role of sirtuin 2 activation by nicotinamide phosphoribosyltransferase in the aberrant proliferation and survival of myeloid leukemia cells
    • Dan L., Klimenkova O., Klimiankou M., Klusman J.H., van den Heuvel-Eibrink M.M., Reinhardt D., et al. The role of sirtuin 2 activation by nicotinamide phosphoribosyltransferase in the aberrant proliferation and survival of myeloid leukemia cells. Haematologica 2012, 97:551-559.
    • (2012) Haematologica , vol.97 , pp. 551-559
    • Dan, L.1    Klimenkova, O.2    Klimiankou, M.3    Klusman, J.H.4    van den Heuvel-Eibrink, M.M.5    Reinhardt, D.6
  • 33
    • 27644534576 scopus 로고    scopus 로고
    • The response of autologous T cells to a human melanoma is dominated by mutated neoantigens
    • Lennerz V., Fatho M., Gentilini C., Frye R.A., Lifke A., Ferel D., et al. The response of autologous T cells to a human melanoma is dominated by mutated neoantigens. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:16013-16018.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 16013-16018
    • Lennerz, V.1    Fatho, M.2    Gentilini, C.3    Frye, R.A.4    Lifke, A.5    Ferel, D.6
  • 34
  • 35
    • 84866526603 scopus 로고    scopus 로고
    • Inhibition of SIRT2 potentiates the anti-motility activity of taxanes: implications for antineoplastic combination therapies
    • Bonezzi K., Belotti D., North B.J., Ghilardi C., Borsotti P., Resovi A., et al. Inhibition of SIRT2 potentiates the anti-motility activity of taxanes: implications for antineoplastic combination therapies. Neoplasia 2012, 14:846-854.
    • (2012) Neoplasia , vol.14 , pp. 846-854
    • Bonezzi, K.1    Belotti, D.2    North, B.J.3    Ghilardi, C.4    Borsotti, P.5    Resovi, A.6
  • 36
    • 84907271009 scopus 로고    scopus 로고
    • SIRT2 interacts with beta-catenin to inhibit Wnt signaling output in response to radiation-induced stress
    • Nguyen P., Lee S., Lorang-Leins D., Trepel J., Smart D.K. SIRT2 interacts with beta-catenin to inhibit Wnt signaling output in response to radiation-induced stress. Mol. Cancer Res 2014, 12:1244-1253.
    • (2014) Mol. Cancer Res , vol.12 , pp. 1244-1253
    • Nguyen, P.1    Lee, S.2    Lorang-Leins, D.3    Trepel, J.4    Smart, D.K.5
  • 37
    • 23844528776 scopus 로고    scopus 로고
    • The Snail genes as inducers of cell movement and survival: implications in development and cancer
    • Barrallo-Gimeno A., Nieto M.A. The Snail genes as inducers of cell movement and survival: implications in development and cancer. Development 2005, 132:3151-3161.
    • (2005) Development , vol.132 , pp. 3151-3161
    • Barrallo-Gimeno, A.1    Nieto, M.A.2
  • 38
    • 5444269904 scopus 로고    scopus 로고
    • Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition
    • Zhou B.P., Deng J., Xia W., Xu J., Li Y.M., Gunduz M., et al. Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition. Nat. Cell Biol 2004, 6:931-940.
    • (2004) Nat. Cell Biol , vol.6 , pp. 931-940
    • Zhou, B.P.1    Deng, J.2    Xia, W.3    Xu, J.4    Li, Y.M.5    Gunduz, M.6
  • 39
    • 65349092794 scopus 로고    scopus 로고
    • Stabilization of snail by NF-kappaB is required for inflammation-induced cell migration and invasion
    • Wu Y., Deng J., Rychahou P.G., Qiu S., Evers B.M., Zhou B.P. Stabilization of snail by NF-kappaB is required for inflammation-induced cell migration and invasion. Cancer Cell 2009, 15:416-428.
    • (2009) Cancer Cell , vol.15 , pp. 416-428
    • Wu, Y.1    Deng, J.2    Rychahou, P.G.3    Qiu, S.4    Evers, B.M.5    Zhou, B.P.6
  • 40
    • 0028986075 scopus 로고
    • Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation
    • Brown K., Gerstberger S., Carlson L., Franzoso G., Siebenlist U. Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation. Science 1995, 267:1485-1488.
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 41
    • 77953571622 scopus 로고    scopus 로고
    • Snail: more than EMT
    • Wu Y., Zhou B.P. Snail: more than EMT. Cell Adh. Migr 2010, 4:199-203.
    • (2010) Cell Adh. Migr , vol.4 , pp. 199-203
    • Wu, Y.1    Zhou, B.P.2
  • 43
    • 84878396726 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase mediates both cell death and ATP decreases in SIRT2 inhibitor AGK2-treated microglial BV2 cells
    • Li Y., Nie H., Wu D., Zhang J., Wei X., Ying W. Poly(ADP-ribose) polymerase mediates both cell death and ATP decreases in SIRT2 inhibitor AGK2-treated microglial BV2 cells. Neurosci. Lett 2013, 544:36-40.
    • (2013) Neurosci. Lett , vol.544 , pp. 36-40
    • Li, Y.1    Nie, H.2    Wu, D.3    Zhang, J.4    Wei, X.5    Ying, W.6
  • 44
    • 84891949982 scopus 로고    scopus 로고
    • Inhibition of SIRT2 in merlin/NF2-mutant Schwann cells triggers necrosis
    • Petrilli A., Bott M., Fernandez-Valle C. Inhibition of SIRT2 in merlin/NF2-mutant Schwann cells triggers necrosis. Oncotarget 2013, 4:2354-2365.
    • (2013) Oncotarget , vol.4 , pp. 2354-2365
    • Petrilli, A.1    Bott, M.2    Fernandez-Valle, C.3
  • 45
    • 84896901019 scopus 로고    scopus 로고
    • Sirt2 deacetylase is a novel AKT binding partner critical for AKT activation by insulin
    • Ramakrishnan G., Davaakhuu G., Kaplun L., Chung W.C., Rana A., Atfi A., et al. Sirt2 deacetylase is a novel AKT binding partner critical for AKT activation by insulin. J. Biol. Chem 2014, 289:6054-6066.
    • (2014) J. Biol. Chem , vol.289 , pp. 6054-6066
    • Ramakrishnan, G.1    Davaakhuu, G.2    Kaplun, L.3    Chung, W.C.4    Rana, A.5    Atfi, A.6
  • 46
    • 84885760626 scopus 로고    scopus 로고
    • Activation of GSK3beta by Sirt2 is required for early lineage commitment of mouse embryonic stem cell
    • Si X., Chen W., Guo X., Chen L., Wang G., Xu Y., et al. Activation of GSK3beta by Sirt2 is required for early lineage commitment of mouse embryonic stem cell. PLoS ONE 2013, 8:e76699.
    • (2013) PLoS ONE , vol.8 , pp. e76699
    • Si, X.1    Chen, W.2    Guo, X.3    Chen, L.4    Wang, G.5    Xu, Y.6
  • 47
    • 78649738291 scopus 로고    scopus 로고
    • SIRT2 regulates NF-kappaB dependent gene expression through deacetylation of p65 Lys310
    • Rothgiesser K.M., Erener S., Waibel S., Luscher B., Hottiger M.O. SIRT2 regulates NF-kappaB dependent gene expression through deacetylation of p65 Lys310. J. Cell Sci 2010, 123:4251-4258.
    • (2010) J. Cell Sci , vol.123 , pp. 4251-4258
    • Rothgiesser, K.M.1    Erener, S.2    Waibel, S.3    Luscher, B.4    Hottiger, M.O.5
  • 50
    • 77950835404 scopus 로고    scopus 로고
    • SIRT inhibitors induce cell death and p53 acetylation through targeting both SIRT1 and SIRT2
    • Peck B., Chen C.Y., Ho K.K., Di Fruscia P., Myatt S.S., Coombes R.C., et al. SIRT inhibitors induce cell death and p53 acetylation through targeting both SIRT1 and SIRT2. Mol. Cancer Ther 2010, 9:844-855.
    • (2010) Mol. Cancer Ther , vol.9 , pp. 844-855
    • Peck, B.1    Chen, C.Y.2    Ho, K.K.3    Di Fruscia, P.4    Myatt, S.S.5    Coombes, R.C.6
  • 51
    • 84876473075 scopus 로고    scopus 로고
    • Tenovin-D3, a novel small-molecule inhibitor of sirtuin SirT2, increases p21 (CDKN1A) expression in a p53-independent manner
    • McCarthy A.R., Sachweh M.C., Higgins M., Campbell J., Drummond C.J., van Leeuwen I.M., et al. Tenovin-D3, a novel small-molecule inhibitor of sirtuin SirT2, increases p21 (CDKN1A) expression in a p53-independent manner. Mol. Cancer Ther 2013, 12:352-360.
    • (2013) Mol. Cancer Ther , vol.12 , pp. 352-360
    • McCarthy, A.R.1    Sachweh, M.C.2    Higgins, M.3    Campbell, J.4    Drummond, C.J.5    van Leeuwen, I.M.6


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