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Volumn 12, Issue 9, 2002, Pages 404-406

Human Sir2 and the 'silencing' of p53 activity

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE; HISTONE H3; HISTONE H4; NICOTINAMIDE ADENINE DINUCLEOTIDE; PROTEIN P53; REGULATOR PROTEIN; SILENT INFORMATION REGULATOR PROTEIN 2; UNCLASSIFIED DRUG;

EID: 0036709074     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(02)02342-5     Document Type: Review
Times cited : (126)

References (26)
  • 1
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner D.E., Berger S.L. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. 64:2000;435-459.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 2
    • 0035868764 scopus 로고    scopus 로고
    • Acetylation of TAFI68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription
    • Muth V., et al. Acetylation of TAFI68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription. EMBO J. 20:2001;1353-1362.
    • (2001) EMBO J. , vol.20 , pp. 1353-1362
    • Muth, V.1
  • 3
    • 0037093346 scopus 로고    scopus 로고
    • Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence
    • Langley E., et al. Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence. EMBO J. 21:2002;2383-2396.
    • (2002) EMBO J. , vol.21 , pp. 2383-2396
    • Langley, E.1
  • 4
    • 0035913903 scopus 로고    scopus 로고
    • SIRT1 functions as an NAD-dependent p53 deacetylase
    • SIRT1 functions as an NAD-dependent p53 deacetylase. Cell. 107:2001;149-159.
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1
  • 5
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2α promotes cell survival under stress
    • Luo J., et al. Negative control of p53 by Sir2α promotes cell survival under stress. Cell. 107:2001;137-148.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1
  • 6
    • 0035862199 scopus 로고    scopus 로고
    • The human histone deacetylase family
    • Gray S.G., Ekstrom T.J. The human histone deacetylase family. Exp. Cell Res. 262:2001;75-83.
    • (2001) Exp. Cell Res. , vol.262 , pp. 75-83
    • Gray, S.G.1    Ekstrom, T.J.2
  • 7
    • 0035313756 scopus 로고    scopus 로고
    • Enzymatic activities of Sir2 and chromatin silencing
    • Moazed D. Enzymatic activities of Sir2 and chromatin silencing. Curr. Opin. Cell Biol. 13:2001;232-238.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 232-238
    • Moazed, D.1
  • 8
    • 0028841317 scopus 로고
    • The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability
    • Brachmann C.B., et al. The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability. Genes Dev. 9:1995;2888-2902.
    • (1995) Genes Dev. , vol.9 , pp. 2888-2902
    • Brachmann, C.B.1
  • 9
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 273:2000;793-798.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 10
    • 0034705129 scopus 로고    scopus 로고
    • The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases
    • Landry J., et al. The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc. Natl. Acad. Sci. U. S. A. 97:2000;5807-5811.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5807-5811
    • Landry, J.1
  • 11
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S-i., et al. Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature. 403:2000;795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.-I.1
  • 12
    • 12944283150 scopus 로고    scopus 로고
    • +-dependent protein deacetylase activity in the Sir2 protein family
    • +-dependent protein deacetylase activity in the Sir2 protein family. Proc. Natl. Acad. Sci. U. S. A. 97:2000;6658-6663.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6658-6663
    • Smith, J.S.1
  • 13
    • 0035951072 scopus 로고    scopus 로고
    • +-dependent deacetylation reactions
    • +-dependent deacetylation reactions. Biochemistry. 40:2001;15456-15463.
    • (2001) Biochemistry , vol.40 , pp. 15456-15463
    • Sauve, A.A.1
  • 14
    • 0037166269 scopus 로고    scopus 로고
    • +-dependent histone/protein deacetylases
    • +-dependent histone/protein deacetylases. J. Biol. Chem. 277:2002;18535-18544.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18535-18544
    • Jackson, M.D.1    Denu, J.M.2
  • 15
    • 0034687694 scopus 로고    scopus 로고
    • Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-0-acetyl-ADP-ribose
    • Tanner K.G., et al. Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-0-acetyl-ADP-ribose. Proc. Natl. Acad. Sci. U. S. A. 97:2000;14178-14182.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 14178-14182
    • Tanner, K.G.1
  • 16
    • 0037066738 scopus 로고    scopus 로고
    • +-dependent deacetylases
    • +-dependent deacetylases. J. Biol. Chem. 277:2002;12632-12641.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12632-12641
    • Borra, M.T.1
  • 17
    • 0033610894 scopus 로고    scopus 로고
    • CobB, a new member of the SIR2 family of eucaryotic regulatory proteins, is required to compensate for the lack of nicotinate mononucleotide: 5,6-dimethylbenzimidazole phosphoribosyltransferase activity in cobT mutants during cobalamin biosynthesis in Salmonella typhimurium LT2
    • Tsang A.W., Escalante-Semerena J.C. CobB, a new member of the SIR2 family of eucaryotic regulatory proteins, is required to compensate for the lack of nicotinate mononucleotide: 5,6-dimethylbenzimidazole phosphoribosyltransferase activity in cobT mutants during cobalamin biosynthesis in Salmonella typhimurium LT2. J. Biol. Chem. 273:1998;31788-31794.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31788-31794
    • Tsang, A.W.1    Escalante-Semerena, J.C.2
  • 18
    • 0037154013 scopus 로고    scopus 로고
    • Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism
    • Bryk M., et al. Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism. Curr. Biol. 12:2002;165-170.
    • (2002) Curr. Biol. , vol.12 , pp. 165-170
    • Bryk, M.1
  • 19
    • 0036261650 scopus 로고    scopus 로고
    • Steps in assembly of silent chromatin in yeast: Sir3-independent binding of a sir2/sir4 complex to silencers and role for sir2-dependent deacetylation
    • Hoppe G.J., et al. Steps in assembly of silent chromatin in yeast: sir3-independent binding of a sir2/sir4 complex to silencers and role for sir2-dependent deacetylation. Mol. Cell. Biol. 22:2002;4167-4180.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4167-4180
    • Hoppe, G.J.1
  • 20
    • 0034676439 scopus 로고    scopus 로고
    • Deacetylation of p53 modulates its effect on cell growth and apoptosis
    • Luo J., et al. Deacetylation of p53 modulates its effect on cell growth and apoptosis. Nature. 408:2000;377-381.
    • (2000) Nature , vol.408 , pp. 377-381
    • Luo, J.1
  • 21
    • 0035868964 scopus 로고    scopus 로고
    • P300/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2
    • Ito A., et al. p300/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2. EMBO J. 20:2001;1331-1340.
    • (2001) EMBO J. , vol.20 , pp. 1331-1340
    • Ito, A.1
  • 22
    • 0034626747 scopus 로고    scopus 로고
    • Genetic pathways that regulate ageing in model organisms
    • Guarente L., Kenyon C. Genetic pathways that regulate ageing in model organisms. Nature. 408:2000;255-262.
    • (2000) Nature , vol.408 , pp. 255-262
    • Guarente, L.1    Kenyon, C.2
  • 23
    • 0035913975 scopus 로고    scopus 로고
    • Caenorhabditis elegans p53: Role in apoptosis, meiosis, and stress resistance
    • Derry W.B., et al. Caenorhabditis elegans p53: role in apoptosis, meiosis, and stress resistance. Science. 294:2001;591-595.
    • (2001) Science , vol.294 , pp. 591-595
    • Derry, W.B.1
  • 24
    • 0037011958 scopus 로고    scopus 로고
    • P53 mutant mice that display early ageing-associated phenotypes
    • Tyner S.D., et al. p53 mutant mice that display early ageing-associated phenotypes. Nature. 415:2002;45-53.
    • (2002) Nature , vol.415 , pp. 45-53
    • Tyner, S.D.1
  • 25
    • 0034703217 scopus 로고    scopus 로고
    • Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae
    • Lin S.J., et al. Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science. 289:2000;2126-2128.
    • (2000) Science , vol.289 , pp. 2126-2128
    • Lin, S.J.1
  • 26
    • 0033570901 scopus 로고    scopus 로고
    • Sum1 and Hst1 repress middle sporulation-specific gene expression during mitosis in Saccharomyces cerevisiae
    • Xie J., et al. Sum1 and Hst1 repress middle sporulation-specific gene expression during mitosis in Saccharomyces cerevisiae. EMBO J. 18:1999;6448-6454.
    • (1999) EMBO J. , vol.18 , pp. 6448-6454
    • Xie, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.