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Volumn 60, Issue , 2013, Pages 441-450

Identification of benzofuran-3-yl(phenyl)methanones as novel SIRT1 inhibitors: Binding mode, inhibitory mechanism and biological action

Author keywords

Benzofuran 3 yl(phenyl)methanones; Binding mode; Deacetylation; Inhibitor; SIRT1

Indexed keywords

(2 HYDROXY 5 METHOXYPHENYL)(5 HYDROXYBENZOFURAN 3 YL)METHANONE; (2,5 DIHYDROXYPHENYL)(5 HYDROXY 1 BENZOFURAN 3 YL)METHANONE; (2,5 DIMETHOXYPHENYL)(5 HYDROXYBENZOFURAN 3 YL)METHANONE; (4 BROMOPHENYL)(5 HYDROXY 2 METHYLBENZOFURAN 3 YL)METHANONE; (4 BROMOPHENYL)(5 HYDROXYBENZOFURAN 3 YL)METHANONE; (4 BROMOPHENYL)(5 HYDROXYNAPHTHO[1,2 B]FURAN 3 YL)METHANONE; (4 CHLOROPHENYL)(5 HYDROXYNAPHTHO[1,2 B]FURAN 3 YL)METHANONE; (4,6 DIBROMO 5 HYDROXYBENZOFURAN 3 YL)(PHENYL)METHANONE; (5 HYDROXY 2 METHOXYPHENYL)(5 HYDROXYBENZOFURAN 3 YL)METHANONE; (5 HYDROXYBENZOFURAN 3 YL)(2 HYDROXYPHENYL)METHANONE; (5 HYDROXYBENZOFURAN 3 YL)(3 HYDROXYPHENYL)METHANONE; (5 HYDROXYNAPHTHO[1,2 B]FURAN 3 YL)(4 METHOXYPHENYL)METHANONE; HYDROLASE INHIBITOR; NICOTINAMIDE; PROTEIN P53; SIRTUIN 1; UNCLASSIFIED DRUG;

EID: 84872129954     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2012.12.026     Document Type: Article
Times cited : (22)

References (35)
  • 13
    • 79958246421 scopus 로고    scopus 로고
    • Synthesis and biological activity of splitomicin analogs targeted at human NAD(+)-dependent histone deacetylases (sirtuins)
    • M. Freitag, J. Schemies, T. Larsen, K. El Gaghlab, F. Schulz, T. Rumpf, M. Jung, and A. Link Synthesis and biological activity of splitomicin analogs targeted at human NAD(+)-dependent histone deacetylases (sirtuins) Bioorg. Med. Chem. 19 2011 3669 3677
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 3669-3677
    • Freitag, M.1    Schemies, J.2    Larsen, T.3    El Gaghlab, K.4    Schulz, F.5    Rumpf, T.6    Jung, M.7    Link, A.8
  • 14
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of Yeast Sir2 and human SIRT1
    • K.J. Bitterman Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of Yeast Sir2 and human SIRT1 J. Biol. Chem. 277 2002 45099 45107
    • (2002) J. Biol. Chem. , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1
  • 15
    • 33846709501 scopus 로고    scopus 로고
    • Structural basis for nicotinamide inhibition and base exchange in Sir2 enzymes
    • B.D. Sanders, K. Zhao, J.T. Slama, and R. Marmorstein Structural basis for nicotinamide inhibition and base exchange in Sir2 enzymes Mol. Cell 25 2007 463 472
    • (2007) Mol. Cell , vol.25 , pp. 463-472
    • Sanders, B.D.1    Zhao, K.2    Slama, J.T.3    Marmorstein, R.4
  • 16
    • 30544445468 scopus 로고    scopus 로고
    • Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated Ras-MAPK signaling in human cancer cells
    • H. Ota, E. Tokunaga, K. Chang, M. Hikasa, K. Iijima, M. Eto, K. Kozaki, M. Akishita, Y. Ouchi, and M. Kaneki Sirt1 inhibitor, Sirtinol, induces senescence-like growth arrest with attenuated Ras-MAPK signaling in human cancer cells Oncogene 25 2006 176 185
    • (2006) Oncogene , vol.25 , pp. 176-185
    • Ota, H.1    Tokunaga, E.2    Chang, K.3    Hikasa, M.4    Iijima, K.5    Eto, M.6    Kozaki, K.7    Akishita, M.8    Ouchi, Y.9    Kaneki, M.10
  • 17
    • 33645221885 scopus 로고    scopus 로고
    • Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not alter cell survival following DNA damage
    • J.M. Solomon, R. Pasupuleti, L. Xu, T. McDonagh, R. Curtis, P.S. DiStefano, and L.J. Huber Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not alter cell survival following DNA damage Mol. Cell. Biol. 26 2006 28 38
    • (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    Huber, L.J.7
  • 21
    • 15244355745 scopus 로고    scopus 로고
    • Mechanism of sirtuin inhibition by nicotinamide: Altering the NAD+ Cosubstrate Specificity of a Sir2 enzyme
    • J.L. Avalos, K.M. Bever, and C. Wolberger Mechanism of sirtuin inhibition by nicotinamide: altering the NAD+ Cosubstrate Specificity of a Sir2 enzyme Mol. Cell 17 2005 855 868
    • (2005) Mol. Cell , vol.17 , pp. 855-868
    • Avalos, J.L.1    Bever, K.M.2    Wolberger, C.3
  • 23
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • J.U. Bowie, R. Luthy, and D. Eisenberg A method to identify protein sequences that fold into a known three-dimensional structure Science 253 1991 164 170
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 25
    • 84962439356 scopus 로고    scopus 로고
    • Roles of electrostatic interaction in proteins
    • H. Nakamura Roles of electrostatic interaction in proteins Q. Rev. Biophys. 29 1996 1 90
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 1-90
    • Nakamura, H.1
  • 28
    • 70349782222 scopus 로고    scopus 로고
    • A fluorometric assay of SIRT1 deacetylation activity through quantification of nicotinamide adenine dinucleotide
    • Y. Feng, J. Wu, L. Chen, C. Luo, X. Shen, K. Chen, H. Jiang, and D. Liu A fluorometric assay of SIRT1 deacetylation activity through quantification of nicotinamide adenine dinucleotide Anal. Biochem. 395 2009 205 210
    • (2009) Anal. Biochem. , vol.395 , pp. 205-210
    • Feng, Y.1    Wu, J.2    Chen, L.3    Luo, C.4    Shen, X.5    Chen, K.6    Jiang, H.7    Liu, D.8
  • 29
    • 36649031003 scopus 로고    scopus 로고
    • Microwave-enhanced one-pot synthesis of diversified 3-acyl-5- hydroxybenzofurans
    • X.M. Cheng, and X.W. Liu Microwave-enhanced one-pot synthesis of diversified 3-acyl-5-hydroxybenzofurans J. Comb. Chem. 9 2007 906 908
    • (2007) J. Comb. Chem. , vol.9 , pp. 906-908
    • Cheng, X.M.1    Liu, X.W.2
  • 32
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • J. Luo, A.Y. Nikolaev, S. Imai, D. Chen, F. Su, A. Shiloh, L. Guarente, and W. Gu Negative control of p53 by Sir2alpha promotes cell survival under stress Cell 107 2001 137 148
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 34
    • 0035917536 scopus 로고    scopus 로고
    • Crystal structure of a SIR2 homolog-NAD complex
    • J. Min, J. Landry, R. Sternglanz, and R.M. Xu Crystal structure of a SIR2 homolog-NAD complex Cell 105 2001 269 279
    • (2001) Cell , vol.105 , pp. 269-279
    • Min, J.1    Landry, J.2    Sternglanz, R.3    Xu, R.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.