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Volumn 7, Issue 19, 2008, Pages 3091-3097

JNK2-dependent regulation of SIRT1 protein stability

Author keywords

5 FU; Cancer; JNK2; p53; Phosphorylation; Protein stability; SIRT1

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN JNK2; SERINE; SIRTUIN 1; UNCLASSIFIED DRUG;

EID: 53649100104     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.7.19.6799     Document Type: Article
Times cited : (114)

References (29)
  • 1
    • 2942564591 scopus 로고    scopus 로고
    • Sirtuins: Sir2-related NAD-dependent protein deacetylases
    • North BJ, Verdin E. Sirtuins: Sir2-related NAD-dependent protein deacetylases. Genome Biol 2004; 5:224.
    • (2004) Genome Biol , vol.5 , pp. 224
    • North, B.J.1    Verdin, E.2
  • 2
    • 4944245398 scopus 로고    scopus 로고
    • Human SirT1 interacts with histone H1 and promotes the formation of facultative heterochromatin
    • Vaquero A, Scher M, Lee D, Erdjument-Bromage H, Tempst P, Reinberg D. Human SirT1 interacts with histone H1 and promotes the formation of facultative heterochromatin. Mol Cell 2004; 16:93-105.
    • (2004) Mol Cell , vol.16 , pp. 93-105
    • Vaquero, A.1    Scher, M.2    Lee, D.3    Erdjument-Bromage, H.4    Tempst, P.5    Reinberg, D.6
  • 10
  • 11
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • Rodgers JT, Lerin C, Haas W, Gygi SP, Spiegelman BM, Puigserver P. Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 2005; 434:113-8.
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5    Puigserver, P.6
  • 12
    • 35349011726 scopus 로고    scopus 로고
    • Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppresssion of p53 activity
    • Kim EJ, Kho JH, Kang MR, Um SJ. Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppresssion of p53 activity. Mol Cell 2007; 28:277-90.
    • (2007) Mol Cell , vol.28 , pp. 277-290
    • Kim, E.J.1    Kho, J.H.2    Kang, M.R.3    Um, S.J.4
  • 13
    • 38749088678 scopus 로고    scopus 로고
    • DBC1 is a negative regulator of SIRT1
    • Kim JE, Chen J, Lou Z. DBC1 is a negative regulator of SIRT1. Nature 2008; 451:583-6.
    • (2008) Nature , vol.451 , pp. 583-586
    • Kim, J.E.1    Chen, J.2    Lou, Z.3
  • 14
    • 38749132992 scopus 로고    scopus 로고
    • Negative regulation of the deacetylase SIRT1 by DBC1
    • Zhao W, Kruse JP, Tang Y, Jung SY, Qin J, Gu W. Negative regulation of the deacetylase SIRT1 by DBC1. Nature 2008; 451:587-90.
    • (2008) Nature , vol.451 , pp. 587-590
    • Zhao, W.1    Kruse, J.P.2    Tang, Y.3    Jung, S.Y.4    Qin, J.5    Gu, W.6
  • 16
    • 34247570492 scopus 로고    scopus 로고
    • Strong expression of a longevity-related protein, SIRT1, in Bowen's disease
    • Hida Y, Kubo Y, Murao K, Arase S. Strong expression of a longevity-related protein, SIRT1, in Bowen's disease. Arch Dermatol Res 2007; 299:103-6.
    • (2007) Arch Dermatol Res , vol.299 , pp. 103-106
    • Hida, Y.1    Kubo, Y.2    Murao, K.3    Arase, S.4
  • 19
    • 28544444366 scopus 로고    scopus 로고
    • Cancer-specific functions of SIRT1 enable human epithelial cancer cell growth and survival
    • Ford J, Jiang M, Milner J. Cancer-specific functions of SIRT1 enable human epithelial cancer cell growth and survival. Cancer Res 2005; 65:10457-63.
    • (2005) Cancer Res , vol.65 , pp. 10457-10463
    • Ford, J.1    Jiang, M.2    Milner, J.3
  • 21
    • 27544434763 scopus 로고    scopus 로고
    • Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses
    • Chen WY, Wang DH, Yen RC, Luo J, Gu W, Baylin SB. Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses. Cell 2005; 123:437-48.
    • (2005) Cell , vol.123 , pp. 437-448
    • Chen, W.Y.1    Wang, D.H.2    Yen, R.C.3    Luo, J.4    Gu, W.5    Baylin, S.B.6
  • 24
    • 33745931074 scopus 로고    scopus 로고
    • Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases
    • Hallows WC, Lee S, Denu JM. Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc Natl Acad Sci USA 2006; 103:10230-5.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10230-10235
    • Hallows, W.C.1    Lee, S.2    Denu, J.M.3
  • 25
    • 0038387494 scopus 로고    scopus 로고
    • 5-fluorouracil: Mechanisms of action and clinical strategies
    • Longley DB, Harkin DP, Johnston PG. 5-fluorouracil: mechanisms of action and clinical strategies. Nature Rev Cancer 2003; 3:330-8.
    • (2003) Nature Rev Cancer , vol.3 , pp. 330-338
    • Longley, D.B.1    Harkin, D.P.2    Johnston, P.G.3
  • 28
    • 36849002444 scopus 로고    scopus 로고
    • SIRT3 is pro-apoptotic and participates in distinct basal apoptotic pathways
    • Allison SJ, Milner J. SIRT3 is pro-apoptotic and participates in distinct basal apoptotic pathways. Cell Cycle 2007; 6:2669-78.
    • (2007) Cell Cycle , vol.6 , pp. 2669-2678
    • Allison, S.J.1    Milner, J.2
  • 29
    • 33845327501 scopus 로고    scopus 로고
    • SIRT1: Linking adaptive cellular responses to aging-associated changes in organismal physiology
    • Anastasiou D, Krek W. SIRT1: Linking adaptive cellular responses to aging-associated changes in organismal physiology. Physiology 2006; 21:401-10.
    • (2006) Physiology , vol.21 , pp. 401-410
    • Anastasiou, D.1    Krek, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.