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Volumn 12, Issue 14, 2013, Pages 2233-2240

Carboxamide SIRT1 inhibitors block DBC1 binding via an acetylation- independent mechanism

Author keywords

DBC1; DBC1 acetylation; DBC1 localization; SIRT1 inhibitors; SIRT1 DBC1 complex regulation

Indexed keywords

DELETED BREAST CANCER 1; EX 527; SELISISTAT; SIRTUIN 1; SMALL MOLECULE TRANSPORT AGENT; TUMOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84880444482     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.25268     Document Type: Article
Times cited : (19)

References (56)
  • 2
    • 43049121395 scopus 로고    scopus 로고
    • Glucose Restriction Inhibits Skeletal Myoblast Differentiation by Activating SIRT1 through AMPK-Mediated Regulation of Nampt
    • DOI 10.1016/j.devcel.2008.02.004, PII S1534580708000749
    • Fulco M, Cen Y, Zhao P, Hoffman EP, McBurney MW, Sauve AA, et al. Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt. Dev Cell 2008; 14:661-73; PMID:18477450; http://dx.doi.org/10.1016/j.devcel.2008.02.004 (Pubitemid 351622608)
    • (2008) Developmental Cell , vol.14 , Issue.5 , pp. 661-673
    • Fulco, M.1    Cen, Y.2    Zhao, P.3    Hoffman, E.P.4    McBurney, M.W.5    Sauve, A.A.6    Sartorelli, V.7
  • 5
    • 84874721105 scopus 로고    scopus 로고
    • Evidence for a common mechanism of SIRT1 regulation by allosteric activators
    • PMID:23471411
    • Hubbard BP, Gomes AP, Dai H, Li J, Case AW, Considine T, et al. Evidence for a common mechanism of SIRT1 regulation by allosteric activators. Science 2013; 339:1216-9; PMID:23471411; http://dx.doi.org/10.1126/science.1231097
    • (2013) Science , vol.339 , pp. 1216-1219
    • Hubbard, B.P.1    Gomes, A.P.2    Dai, H.3    Li, J.4    Case, A.W.5    Considine, T.6
  • 6
    • 63849252078 scopus 로고    scopus 로고
    • Therapeutic potential of SIRT1 and NAMPT-mediated NAD biosynthesis in type 2 diabetes
    • PMID:19273250
    • Imai S, Kiess W. Therapeutic potential of SIRT1 and NAMPT-mediated NAD biosynthesis in type 2 diabetes. Front Biosci 2009; 14:2983-95; PMID:19273250; http://dx.doi.org/10.2741/3428
    • (2009) Front Biosci , vol.14 , pp. 2983-2995
    • Imai, S.1    Kiess, W.2
  • 8
    • 84873674760 scopus 로고    scopus 로고
    • Analysis of 41 cancer cell lines reveals excessive allelic loss and novel mutations in the SIRT1 gene
    • PMID:23255128
    • Han J, Hubbard BP, Lee J, Montagna C, Lee HW, Sinclair DA, et al. Analysis of 41 cancer cell lines reveals excessive allelic loss and novel mutations in the SIRT1 gene. Cell Cycle 2013; 12:263-70; PMID:23255128; http://dx.doi.org/10.4161/cc.23056
    • (2013) Cell Cycle , vol.12 , pp. 263-270
    • Han, J.1    Hubbard, B.P.2    Lee, J.3    Montagna, C.4    Lee, H.W.5    Sinclair, D.A.6
  • 9
    • 44849096876 scopus 로고    scopus 로고
    • The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth
    • PMID:18414679
    • Firestein R, Blander G, Michan S, Oberdoerffer P, Ogino S, Campbell J, et al. The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth. PLoS One 2008; 3:e2020; PMID:18414679; http://dx.doi.org/10.1371/ journal.pone.0002020
    • (2008) PLoS One , vol.3
    • Firestein, R.1    Blander, G.2    Michan, S.3    Oberdoerffer, P.4    Ogino, S.5    Campbell, J.6
  • 11
    • 62149085241 scopus 로고    scopus 로고
    • Pharmaceutical strategies for activating sirtuins
    • PMID:19149602
    • Sauve AA. Pharmaceutical strategies for activating sirtuins. Curr Pharm Des 2009; 15:45-56; PMID:19149602; http://dx.doi.org/10.2174/138161209787185797
    • (2009) Curr Pharm des , vol.15 , pp. 45-56
    • Sauve, A.A.1
  • 12
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast Sir2 and human SIRT1
    • DOI 10.1074/jbc.M205670200
    • Bitterman KJ, Anderson RM, Cohen HY, Latorre- Esteves M, Sinclair DA. Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J Biol Chem 2002; 277:45099-107; PMID:12297502; http://dx.doi.org/10.1074/jbc.M205670200 (Pubitemid 36159111)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 13
    • 35748962613 scopus 로고    scopus 로고
    • SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress
    • DOI 10.1038/ncb1645, PII NCB1645
    • Yang Y, Fu W, Chen J, Olashaw N, Zhang X, Nicosia SV, et al. SIRT1 sumoylation regulates its deacetylase activity and cellular response to genotoxic stress. Nat Cell Biol 2007; 9:1253-62; PMID:17934453; http://dx.doi.org/10.1038/ncb1645 (Pubitemid 350042357)
    • (2007) Nature Cell Biology , vol.9 , Issue.11 , pp. 1253-1262
    • Yang, Y.1    Fu, W.2    Chen, J.3    Olashaw, N.4    Zhang, X.5    Nicosia, S.V.6    Bhalla, K.7    Bai, W.8
  • 15
    • 69949138641 scopus 로고    scopus 로고
    • CK2 is the regulator of SIRT1 substrate-binding affinity, deacetylase activity and cellular response to DNA-damage
    • PMID:19680552
    • Kang H, Jung JW, Kim MK, Chung JH. CK2 is the regulator of SIRT1 substrate-binding affinity, deacetylase activity and cellular response to DNA-damage. PLoS One 2009; 4:e6611; PMID:19680552; http://dx.doi.org/10.1371/ journal.pone.0006611
    • (2009) PLoS One , vol.4
    • Kang, H.1    Jung, J.W.2    Kim, M.K.3    Chung, J.H.4
  • 16
    • 35349011726 scopus 로고    scopus 로고
    • Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity
    • PMID:17964266
    • Kim EJ, Kho JH, Kang MR, Um SJ. Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity. Mol Cell 2007; 28:277-90; PMID:17964266; http://dx.doi.org/10.1016/j.molcel.2007.08.030
    • (2007) Mol Cell , vol.28 , pp. 277-290
    • Kim, E.J.1    Kho, J.H.2    Kang, M.R.3    Um, S.J.4
  • 17
    • 38749132992 scopus 로고    scopus 로고
    • Negative regulation of the deacetylase SIRT1 by DBC1
    • DOI 10.1038/nature06515, PII NATURE06515
    • 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; PMID:18235502; http://dx.doi.org/10.1038/nature06515 (Pubitemid 351186268)
    • (2008) Nature , vol.451 , Issue.7178 , pp. 587-590
    • Zhao, W.1    Kruse, J.-P.2    Tang, Y.3    Jung, S.Y.4    Qin, J.5    Gu, W.6
  • 18
    • 38749088678 scopus 로고    scopus 로고
    • DBC1 is a negative regulator of SIRT1
    • DOI 10.1038/nature06500, PII NATURE06500
    • Kim JE, Chen J, Lou Z. DBC1 is a negative regulator of SIRT1. Nature 2008; 451:583-6; PMID:18235501; http://dx.doi.org/10.1038/nature06500 (Pubitemid 351186264)
    • (2008) Nature , vol.451 , Issue.7178 , pp. 583-586
    • Kim, J.-E.1    Chen, J.2    Lou, Z.3
  • 20
    • 23744485726 scopus 로고    scopus 로고
    • Caspase-dependent processing activates the proapoptotic activity of deleted in breast cancer-1 during tumor necrosis factor-alpha-mediated death signaling
    • DOI 10.1038/sj.onc.1208681
    • Sundararajan R, Chen G, Mukherjee C, White E. Caspase-dependent processing activates the proapoptotic activity of deleted in breast cancer-1 during tumor necrosis factor-alpha-mediated death signaling. Oncogene 2005; 24:4908-20; PMID:15824730; http://dx.doi.org/10.1038/sj.onc.1208681 (Pubitemid 41129095)
    • (2005) Oncogene , vol.24 , Issue.31 , pp. 4908-4920
    • Sundararajan, R.1    Chen, G.2    Mukherjee, C.3    White, E.4
  • 21
    • 34347221253 scopus 로고    scopus 로고
    • Modulation of estrogen receptor α protein level and survival function by DBC-1
    • DOI 10.1210/me.2007-0064
    • Trauernicht AM, Kim SJ, Kim NH, Boyer TG. Modulation of estrogen receptor alpha protein level and survival function by DBC-1. Mol Endocrinol 2007; 21:1526-36; PMID:17473282; http://dx.doi.org/10.1210/me.2007-0064 (Pubitemid 47001079)
    • (2007) Molecular Endocrinology , vol.21 , Issue.7 , pp. 1526-1536
    • Trauernicht, A.M.1    Se, J.K.2    Nam, H.K.3    Boyer, T.G.4
  • 22
    • 77953485032 scopus 로고    scopus 로고
    • DBC-1 mediates endocrine resistant breast cancer cell survival
    • PMID:20237431
    • Trauernicht AM, Kim SJ, Kim NH, Clarke R, Boyer TG. DBC-1 mediates endocrine resistant breast cancer cell survival. Cell Cycle 2010; 9:1218-9; PMID:20237431; http://dx.doi.org/10.4161/cc.9.6.11010
    • (2010) Cell Cycle , vol.9 , pp. 1218-1219
    • Trauernicht, A.M.1    Kim, S.J.2    Kim, N.H.3    Clarke, R.4    Boyer, T.G.5
  • 23
    • 84856384698 scopus 로고    scopus 로고
    • The c-MYC oncoprotein, the NAMPT enzyme, the SIRT1-inhibitor DBC1, and the SIRT1 deacetylase form a positive feedback loop
    • PMID:22190494
    • Menssen A, Hydbring P, Kapelle K, Vervoorts J, Diebold J, Lüscher B, et al. The c-MYC oncoprotein, the NAMPT enzyme, the SIRT1-inhibitor DBC1, and the SIRT1 deacetylase form a positive feedback loop. Proc Natl Acad Sci USA 2012; 109:E187-96; PMID:22190494; http://dx.doi.org/10.1073/pnas.1105304109
    • (2012) Proc Natl Acad Sci USA , vol.109
    • Menssen, A.1    Hydbring, P.2    Kapelle, K.3    Vervoorts, J.4    Diebold, J.5    Lüscher, B.6
  • 24
    • 78650411683 scopus 로고    scopus 로고
    • HDAC3 is negatively regulated by the nuclear protein DBC1
    • PMID:21030595
    • Chini CC, Escande C, Nin V, Chini EN. HDAC3 is negatively regulated by the nuclear protein DBC1. J Biol Chem 2010; 285:40830-7; PMID:21030595; http://dx.doi.org/10.1074/jbc.M110.153270
    • (2010) J Biol Chem , vol.285 , pp. 40830-40837
    • Chini, C.C.1    Escande, C.2    Nin, V.3    Chini, E.N.4
  • 25
    • 67449103687 scopus 로고    scopus 로고
    • Inhibition of SUV39H1 methyltransferase activity by DBC1
    • PMID:19218236
    • Li Z, Chen L, Kabra N, Wang C, Fang J, Chen J. Inhibition of SUV39H1 methyltransferase activity by DBC1. J Biol Chem 2009; 284:10361-6; PMID:19218236; http://dx.doi.org/10.1074/jbc. M900956200
    • (2009) J Biol Chem , vol.284 , pp. 10361-10366
    • Li, Z.1    Chen, L.2    Kabra, N.3    Wang, C.4    Fang, J.5    Chen, J.6
  • 26
    • 84876239207 scopus 로고    scopus 로고
    • DBC1 (Deleted in Breast Cancer 1) modulates the stability and function of the nuclear receptor Rev-erbα
    • PMID:23398316
    • Chini CC, Escande C, Nin V, Chini EN. DBC1 (Deleted in Breast Cancer 1) modulates the stability and function of the nuclear receptor Rev-erbα. Biochem J 2013; 451:453-61; PMID:23398316; http://dx.doi.org/10.1042/BJ20121085
    • (2013) Biochem J , vol.451 , pp. 453-461
    • Chini, C.C.1    Escande, C.2    Nin, V.3    Chini, E.N.4
  • 27
    • 84859910490 scopus 로고    scopus 로고
    • DBIRD complex integrates alternative mRNA splicing with RNA polymerase II transcript elongation
    • PMID:22446626
    • Close P, East P, Dirac-Svejstrup AB, Hartmann H, Heron M, Maslen S, et al. DBIRD complex integrates alternative mRNA splicing with RNA polymerase II transcript elongation. Nature 2012; 484:386-9; PMID:22446626; http://dx.doi.org/10.1038/nature10925
    • (2012) Nature , vol.484 , pp. 386-389
    • Close, P.1    East, P.2    Dirac-Svejstrup, A.B.3    Hartmann, H.4    Heron, M.5    Maslen, S.6
  • 28
    • 82455219091 scopus 로고    scopus 로고
    • Peptide switch is essential for Sirt1 deacetylase activity
    • PMID:22017869
    • Kang H, Suh JY, Jung YS, Jung JW, Kim MK, Chung JH. Peptide switch is essential for Sirt1 deacetylase activity. Mol Cell 2011; 44:203-13; PMID:22017869; http://dx.doi.org/10.1016/j.molcel.2011.07.038
    • (2011) Mol Cell , vol.44 , pp. 203-213
    • Kang, H.1    Suh, J.Y.2    Jung, Y.S.3    Jung, J.W.4    Kim, M.K.5    Chung, J.H.6
  • 29
    • 84872507367 scopus 로고    scopus 로고
    • The SIRT1 modulators AROS and DBC1 regulate HSF1 activity and the heat shock response
    • PMID:23349863
    • Raynes R, Pombier KM, Nguyen K, Brunquell J, Mendez JE, Westerheide SD. The SIRT1 modulators AROS and DBC1 regulate HSF1 activity and the heat shock response. PLoS One 2013; 8:e54364; PMID:23349863; http://dx.doi.org/10.1371/ journal. pone.0054364
    • (2013) PLoS One , vol.8
    • Raynes, R.1    Pombier, K.M.2    Nguyen, K.3    Brunquell, J.4    Mendez, J.E.5    Westerheide, S.D.6
  • 30
    • 76649085804 scopus 로고    scopus 로고
    • Deleted in breast cancer-1 regulates SIRT1 activity and contributes to high-fat diet-induced liver steatosis in mice
    • PMID:20071779
    • Escande C, Chini CC, Nin V, Dykhouse KM, Novak CM, Levine J, et al. Deleted in breast cancer-1 regulates SIRT1 activity and contributes to high-fat diet-induced liver steatosis in mice. J Clin Invest 2010; 120:545-58; PMID:20071779; http://dx.doi.org/10.1172/JCI39319
    • (2010) J Clin Invest , vol.120 , pp. 545-558
    • Escande, C.1    Chini, C.C.2    Nin, V.3    Dykhouse, K.M.4    Novak, C.M.5    Levine, J.6
  • 31
    • 84864615516 scopus 로고    scopus 로고
    • Brown remodeling of white adipose tissue by SirT1- dependent deacetylation of Pparγ
    • PMID:22863012
    • Qiang L, Wang L, Kon N, Zhao W, Lee S, Zhang Y, et al. Brown remodeling of white adipose tissue by SirT1- dependent deacetylation of Pparγ. Cell 2012; 150:620-32; PMID:22863012; http://dx.doi.org/10.1016/j.cell.2012.06.027
    • (2012) Cell , vol.150 , pp. 620-632
    • Qiang, L.1    Wang, L.2    Kon, N.3    Zhao, W.4    Lee, S.5    Zhang, Y.6
  • 32
    • 70449748196 scopus 로고    scopus 로고
    • Interactions between DBC1 and SIRT 1 are deregulated in breast cancer cells
    • PMID:19855164
    • Kim JE, Lou Z, Chen J. Interactions between DBC1 and SIRT 1 are deregulated in breast cancer cells. Cell Cycle 2009; 8:3784-5; PMID:19855164; http://dx.doi.org/10.4161/cc.8.22.10055
    • (2009) Cell Cycle , vol.8 , pp. 3784-3785
    • Kim, J.E.1    Lou, Z.2    Chen, J.3
  • 33
    • 84863622561 scopus 로고    scopus 로고
    • Role of deleted in breast cancer 1 (DBC1) protein in SIRT1 deacetylase activation induced by protein kinase A and AMP-activated protein kinase
    • PMID:22553202
    • Nin V, Escande C, Chini CC, Giri S, Camacho-Pereira J, Matalonga J, et al. Role of deleted in breast cancer 1 (DBC1) protein in SIRT1 deacetylase activation induced by protein kinase A and AMP-activated protein kinase. J Biol Chem 2012; 287:23489-501; PMID:22553202; http://dx.doi.org/10.1074/jbc. M112.365874
    • (2012) J Biol Chem , vol.287 , pp. 23489-23501
    • Nin, V.1    Escande, C.2    Chini, C.C.3    Giri, S.4    Camacho-Pereira, J.5    Matalonga, J.6
  • 34
    • 84859871053 scopus 로고    scopus 로고
    • Regulation of SIRT1 activity by genotoxic stress
    • PMID:22465953
    • Yuan J, Luo K, Liu T, Lou Z. Regulation of SIRT1 activity by genotoxic stress. Genes Dev 2012; 26:791-6; PMID:22465953; http://dx.doi.org/10.1101/gad. 188482.112
    • (2012) Genes Dev , vol.26 , pp. 791-796
    • Yuan, J.1    Luo, K.2    Liu, T.3    Lou, Z.4
  • 35
    • 77953257025 scopus 로고    scopus 로고
    • Aging and disease: Connections to sirtuins
    • PMID:20409078
    • Donmez G, Guarente L. Aging and disease: connections to sirtuins. Aging Cell 2010; 9:285-90; PMID:20409078; http://dx.doi.org/10.1111/j.1474-9726.2010. 00548.x
    • (2010) Aging Cell , vol.9 , pp. 285-290
    • Donmez, G.1    Guarente, L.2
  • 36
    • 33645221885 scopus 로고    scopus 로고
    • Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not alter cell survival following DNA damage
    • PMID:16354677
    • Solomon JM, Pasupuleti R, Xu L, McDonagh T, Curtis R, DiStefano PS, et al. Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not alter cell survival following DNA damage. Mol Cell Biol 2006; 26:28-38; PMID:16354677; http://dx.doi.org/10.1128/MCB.26.1.28-38.2006
    • (2006) Mol Cell Biol , vol.26 , pp. 28-38
    • Solomon, J.M.1    Pasupuleti, R.2    Xu, L.3    McDonagh, T.4    Curtis, R.5    Distefano, P.S.6
  • 37
    • 84877714749 scopus 로고    scopus 로고
    • Discovery of Thieno[3,2-d]pyrimidine-6-carboxamides as Potent Inhibitors of SIRT1, SIRT2, and SIRT3
    • PMID:23570514
    • Disch JS, Evindar G, Chiu CH, Blum CA, Dai H, Jin L, et al. Discovery of Thieno[3,2-d]pyrimidine-6-carboxamides as Potent Inhibitors of SIRT1, SIRT2, and SIRT3. J Med Chem 2013; 56:3666-79; PMID:23570514; http://dx.doi.org/10.1021/ jm400204k
    • (2013) J Med Chem , vol.56 , pp. 3666-3679
    • Disch, J.S.1    Evindar, G.2    Chiu, C.H.3    Blum, C.A.4    Dai, H.5    Jin, L.6
  • 38
    • 0034956304 scopus 로고    scopus 로고
    • Structure of the histone deacetylase SIRT2
    • DOI 10.1038/89668
    • Finnin MS, Donigian JR, Pavletich NP. Structure of the histone deacetylase SIRT2. Nat Struct Biol 2001; 8:621-5; PMID:11427894; http://dx.doi.org/10.1038/89668 (Pubitemid 32613012)
    • (2001) Nature Structural Biology , vol.8 , Issue.7 , pp. 621-625
    • Finnin, M.S.1    Donigian, J.R.2    Pavletich, N.P.3
  • 39
    • 15244355745 scopus 로고    scopus 로고
    • + cosubstrate specificity of a Sir2 enzyme
    • DOI 10.1016/j.molcel.2005.02.022
    • Avalos JL, Bever KM, Wolberger C. Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme. Mol Cell 2005; 17:855-68; PMID:15780941; http://dx.doi.org/10.1016/j.molcel.2005.02. 022 (Pubitemid 40386946)
    • (2005) Molecular Cell , vol.17 , Issue.6 , pp. 855-868
    • Avalos, J.L.1    Bever, K.M.2    Wolberger, C.3
  • 40
    • 33745119442 scopus 로고    scopus 로고
    • The structural basis of sirtuin substrate affinity
    • DOI 10.1021/bi0526332
    • Cosgrove MS, Bever K, Avalos JL, Muhammad S, Zhang X, Wolberger C. The structural basis of sirtuin substrate affinity. Biochemistry 2006; 45:7511-21; PMID:16768447; http://dx.doi.org/10.1021/bi0526332 (Pubitemid 43894945)
    • (2006) Biochemistry , vol.45 , Issue.24 , pp. 7511-7521
    • Cosgrove, M.S.1    Bever, K.2    Avalos, J.L.3    Muhammad, S.4    Zhang, X.5    Wolberger, C.6
  • 41
    • 78751663378 scopus 로고    scopus 로고
    • SIRT1 modulation as a novel approach to the treatment of diseases of aging
    • PMID:21080630
    • Blum CA, Ellis JL, Loh C, Ng PY, Perni RB, Stein RL. SIRT1 modulation as a novel approach to the treatment of diseases of aging. J Med Chem 2011; 54:417-32; PMID:21080630; http://dx.doi.org/10.1021/jm100861p
    • (2011) J Med Chem , vol.54 , pp. 417-432
    • Blum, C.A.1    Ellis, J.L.2    Loh, C.3    Ng, P.Y.4    Perni, R.B.5    Stein, R.L.6
  • 42
    • 20144372893 scopus 로고    scopus 로고
    • SIRT1 regulates HIV transcription via Tat deacetylation
    • PMID:15719057
    • Pagans S, Pedal A, North BJ, Kaehlcke K, Marshall BL, Dorr A, et al. SIRT1 regulates HIV transcription via Tat deacetylation. PLoS Biol 2005; 3:e41; PMID:15719057; http://dx.doi.org/10.1371/journal. pbio.0030041
    • (2005) PLoS Biol , vol.3
    • Pagans, S.1    Pedal, A.2    North, B.J.3    Kaehlcke, K.4    Marshall, B.L.5    Dorr, A.6
  • 44
    • 65649111534 scopus 로고    scopus 로고
    • Novel cambinol analogs as sirtuin inhibitors: Synthesis, biological evaluation, and rationalization of activity
    • PMID:19419202
    • Medda F, Russell RJ, Higgins M, McCarthy AR, Campbell J, Slawin AM, et al. Novel cambinol analogs as sirtuin inhibitors: synthesis, biological evaluation, and rationalization of activity. J Med Chem 2009; 52:2673-82; PMID:19419202; http://dx.doi.org/10.1021/jm8014298
    • (2009) J Med Chem , vol.52 , pp. 2673-2682
    • Medda, F.1    Russell, R.J.2    Higgins, M.3    McCarthy, A.R.4    Campbell, J.5    Slawin, A.M.6
  • 45
    • 84868113308 scopus 로고    scopus 로고
    • Discovery and validation of SIRT2 inhibitors based on tenovin-6: Use of a 1H-NMR method to assess deacetylase activity
    • PMID:23079492
    • Pirrie L, McCarthy AR, Major LL, Morkunaite V, Zubriene A, Matulis D, et al. Discovery and validation of SIRT2 inhibitors based on tenovin-6: use of a 1H-NMR method to assess deacetylase activity. Molecules 2012; 17:12206-24; PMID:23079492; http://dx.doi.org/10.3390/molecules171012206
    • (2012) Molecules , vol.17 , pp. 12206-12224
    • Pirrie, L.1    McCarthy, A.R.2    Major, L.L.3    Morkunaite, V.4    Zubriene, A.5    Matulis, D.6
  • 46
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-κB-dependent transcription and cell survival by the SIRT1 deacetylase
    • DOI 10.1038/sj.emboj.7600244
    • Yeung F, Hoberg JE, Ramsey CS, Keller MD, Jones DR, Frye RA, et al. Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase. EMBO J 2004; 23:2369-80; PMID:15152190; http://dx.doi.org/10.1038/ sj.emboj.7600244 (Pubitemid 38954844)
    • (2004) EMBO Journal , vol.23 , Issue.12 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3    Keller, M.D.4    Jones, D.R.5    Frye, R.A.6    Mayo, M.W.7
  • 48
    • 33751208345 scopus 로고    scopus 로고
    • A highly sensitive protein-protein interaction assay based on Gaussia luciferase
    • DOI 10.1038/nmeth979, PII NMETH979
    • Remy I, Michnick SW. A highly sensitive proteinprotein interaction assay based on Gaussia luciferase. Nat Methods 2006; 3:977-9; PMID:17099704; http://dx.doi.org/10.1038/nmeth979 (Pubitemid 44782695)
    • (2006) Nature Methods , vol.3 , Issue.12 , pp. 977-979
    • Remy, I.1    Michnick, S.W.2
  • 49
    • 20144387545 scopus 로고    scopus 로고
    • Transgenic expression of BACH1 transcription factor results in megakaryocytic impairment
    • PMID:15613547
    • Toki T, Katsuoka F, Kanezaki R, Xu G, Kurotaki H, Sun J, et al. Transgenic expression of BACH1 transcription factor results in megakaryocytic impairment. Blood 2005; 105:3100-8; PMID:15613547; http://dx.doi.org/10.1182/ blood-2004-07-2826
    • (2005) Blood , vol.105 , pp. 3100-3108
    • Toki, T.1    Katsuoka, F.2    Kanezaki, R.3    Xu, G.4    Kurotaki, H.5    Sun, J.6
  • 50
    • 38049184488 scopus 로고    scopus 로고
    • Profiling of UV-induced ATM/ATR signaling pathways
    • PMID:18077418
    • Stokes MP, Rush J, Macneill J, Ren JM, Sprott K, Nardone J, et al. Profiling of UV-induced ATM/ATR signaling pathways. Proc Natl Acad Sci USA 2007; 104:19855-60; PMID:18077418; http://dx.doi.org/10.1073/pnas.0707579104
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19855-19860
    • Stokes, M.P.1    Rush, J.2    Macneill, J.3    Ren, J.M.4    Sprott, K.5    Nardone, J.6
  • 52
    • 84873929641 scopus 로고    scopus 로고
    • The 2.5 Å crystal structure of the SIRT1 catalytic domain bound to nicotinamide adenine dinucleotide (NAD+) and an indole (EX527 analogue) reveals a novel mechanism of histone deacetylase inhibition
    • PMID:23311358
    • Zhao X, Allison D, Condon B, Zhang F, Gheyi T, Zhang A, et al. The 2.5 Å crystal structure of the SIRT1 catalytic domain bound to nicotinamide adenine dinucleotide (NAD+) and an indole (EX527 analogue) reveals a novel mechanism of histone deacetylase inhibition. J Med Chem 2013; 56:963-9; PMID:23311358; http://dx.doi.org/10.1021/jm301431y
    • (2013) J Med Chem , vol.56 , pp. 963-969
    • Zhao, X.1    Allison, D.2    Condon, B.3    Zhang, F.4    Gheyi, T.5    Zhang, A.6
  • 53
    • 77953480631 scopus 로고    scopus 로고
    • Biochemical effects of SIRT1 activators
    • PMID:19897059
    • Baur JA. Biochemical effects of SIRT1 activators. Biochim Biophys Acta 2010; 1804:1626-34; PMID:19897059; http://dx.doi.org/10.1016/j.bbapap.2009.10. 025
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1626-1634
    • Baur, J.A.1
  • 55
    • 13944258164 scopus 로고    scopus 로고
    • Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition
    • DOI 10.1016/j.molcel.2004.12.032
    • Sauve AA, Moir RD, Schramm VL, Willis IM. Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition. Mol Cell 2005; 17:595-601; PMID:15721262; http://dx.doi.org/10.1016/j.molcel.2004.12.032 (Pubitemid 40269123)
    • (2005) Molecular Cell , vol.17 , Issue.4 , pp. 595-601
    • Sauve, A.A.1    Moir, R.D.2    Schramm, V.L.3    Willis, I.M.4
  • 56
    • 78049299600 scopus 로고    scopus 로고
    • Characterization of murine SIRT3 transcript variants and corresponding protein products
    • PMID:20677216
    • Yang Y, Hubbard BP, Sinclair DA, Tong Q. Characterization of murine SIRT3 transcript variants and corresponding protein products. J Cell Biochem 2010; 111:1051-8; PMID:20677216; http://dx.doi.org/10.1002/jcb.22795
    • (2010) J Cell Biochem , vol.111 , pp. 1051-1058
    • Yang, Y.1    Hubbard, B.P.2    Sinclair, D.A.3    Tong, Q.4


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