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Volumn 45, Issue 1, 2006, Pages 94-101

SIRT1 top 40 hits: Use of one-bead, one-compound acetyl-peptide libraries and quantum dots to probe deacetylase specificity

Author keywords

[No Author keywords available]

Indexed keywords

BIOASSAY; CATALYSIS; FLUORESCENCE; MASS SPECTROMETRY; SEMICONDUCTOR QUANTUM DOTS; SUBSTRATES;

EID: 30144435945     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052015l     Document Type: Article
Times cited : (58)

References (51)
  • 1
    • 2942564591 scopus 로고    scopus 로고
    • Sirtuins: Sir2-related NAD-dependent protein deacetylases
    • North, B. J., and Verdin, E. (2004) Sirtuins: Sir2-related NAD-dependent protein deacetylases, GenomeBiology 5, 224.
    • (2004) GenomeBiology , vol.5 , pp. 224
    • North, B.J.1    Verdin, E.2
  • 2
    • 25144496904 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Denu, J. M. (2005) The Sir2 family of protein deacetylases, Curr. Opin. Chem. Biol.
    • (2005) Curr. Opin. Chem. Biol.
    • Denu, J.M.1
  • 3
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander, G., and Guarente, L. (2004) The Sir2 family of protein deacetylases, Annu. Rev. Biochem. 73, 417-435.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 4
    • 0036532026 scopus 로고    scopus 로고
    • Histone modifications in transcriptional regulation
    • Berger, S. L. (2002) Histone modifications in transcriptional regulation, Curr. Opin. Genet. Dev. 12, 142-148.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 142-148
    • Berger, S.L.1
  • 5
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai, S., Armstrong, C. M., Kaeberlein, M., and Guarente, L. (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase, Nature 403, 795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 6
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • Starai, V. J., Celic, I., Cole, R. N., Boeke, J. D., and Escalante-Semerena, J. C. (2002) Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine, Science 298, 2390-2392.
    • (2002) Science , vol.298 , pp. 2390-2392
    • Starai, V.J.1    Celic, I.2    Cole, R.N.3    Boeke, J.D.4    Escalante-Semerena, J.C.5
  • 7
    • 0037166269 scopus 로고    scopus 로고
    • +-dependent histone/protein deacetylases
    • +-dependent histone/protein deacetylases, J. Biol. Chem. 277, 18535-18544.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18535-18544
    • Jackson, M.D.1    Denu, J.M.2
  • 9
    • 0028841317 scopus 로고
    • The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability
    • Brachmann, C. B., Sherman, J. M., Devine, S. E., Cameron, E. E., Pillus, L., and Boeke, J. D. (1995) The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability, Genes Dev. 9, 2888-2902.
    • (1995) Genes Dev. , vol.9 , pp. 2888-2902
    • Brachmann, C.B.1    Sherman, J.M.2    Devine, S.E.3    Cameron, E.E.4    Pillus, L.5    Boeke, J.D.6
  • 10
    • 0033600176 scopus 로고    scopus 로고
    • Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity
    • Frye, R. A. (1999) Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity, Biochem. Biophys. Res. Commun. 260, 273-279.
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 273-279
    • Frye, R.A.1
  • 11
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye, R. A. (2000) Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins, Biochem. Biophys. Res. Commun. 273, 793-798.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 13
    • 15444377466 scopus 로고    scopus 로고
    • SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1
    • Bouras, T., Fu, M., Sauve, A. A., Wang, F., Quong, A. A., Perkins, N. D., Hay, R. T., Gu, W., and Pestell, R. G. (2005) SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1, J. Biol. Chem. 280, 10264-10276.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10264-10276
    • Bouras, T.1    Fu, M.2    Sauve, A.A.3    Wang, F.4    Quong, A.A.5    Perkins, N.D.6    Hay, R.T.7    Gu, W.8    Pestell, R.G.9
  • 14
    • 0035868764 scopus 로고    scopus 로고
    • Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription
    • Muth, V., Nadaud, S., Grummt, I., and Voit, R. (2001) Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription, EMBO J. 20, 1353-1362.
    • (2001) EMBO J. , vol.20 , pp. 1353-1362
    • Muth, V.1    Nadaud, S.2    Grummt, I.3    Voit, R.4
  • 16
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1 alpha and SIRT1
    • Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., and Puigserver, P. (2005) Nutrient control of glucose homeostasis through a complex of PGC-1 alpha and SIRT1, Nature 434, 113-118.
    • (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
  • 17
    • 16344384026 scopus 로고    scopus 로고
    • Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation
    • Yang, Y., Hou, H., Haller, E. M., Nicosia, S. V., and Bai, W. (2005) Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation, EMBO J. 24, 1021-1032.
    • (2005) EMBO J. , vol.24 , pp. 1021-1032
    • Yang, Y.1    Hou, H.2    Haller, E.M.3    Nicosia, S.V.4    Bai, W.5
  • 19
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., and Mayo, M. W. (2004) Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase, EMBO J. 23, 2369-2380.
    • (2004) EMBO J. , vol.23 , 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
  • 22
    • 0242626891 scopus 로고    scopus 로고
    • Structure of the yeast Hst2 protein deacetylase in ternary complex with 2′-O-acetyl ADP ribose and histone peptide
    • Zhao, K., Chai, X., and Marmorstein, R. (2003) Structure of the yeast Hst2 protein deacetylase in ternary complex with 2′-O-acetyl ADP ribose and histone peptide, Structure (London) 11, 1403-1411.
    • (2003) Structure (London) , vol.11 , pp. 1403-1411
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3
  • 25
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., and Verdin, E. (2003) The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase, Mol. Cell 11, 437-444.
    • (2003) Mol. Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 27
    • 0026419328 scopus 로고
    • A new type of synthetic peptide library for identifying ligand-binding activity
    • Lam, K. S., Salmon, S. E., Hersh, E. M., Hruby, V. J., Kazmierski, W. M., and Knapp, R. J. (1991) A new type of synthetic peptide library for identifying ligand-binding activity, Nature 354, 82-84.
    • (1991) Nature , vol.354 , pp. 82-84
    • Lam, K.S.1    Salmon, S.E.2    Hersh, E.M.3    Hruby, V.J.4    Kazmierski, W.M.5    Knapp, R.J.6
  • 28
    • 0025893762 scopus 로고
    • General method for rapid synthesis of multicomponent peptide mixtures
    • Furka, A., Sebestyen, F., Asgedom, M., and Dibo, G. (1991) General method for rapid synthesis of multicomponent peptide mixtures, Int. J. Pept. Protein Res. 37, 487-493.
    • (1991) Int. J. Pept. Protein Res. , vol.37 , pp. 487-493
    • Furka, A.1    Sebestyen, F.2    Asgedom, M.3    Dibo, G.4
  • 29
    • 0033547751 scopus 로고    scopus 로고
    • Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library
    • Hu, Y. J., Wei, Y., Zhou, Y., Rajagopalan, P. T., and Pei, D. (1999) Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library, Biochemistry 38, 643-650.
    • (1999) Biochemistry , vol.38 , pp. 643-650
    • Hu, Y.J.1    Wei, Y.2    Zhou, Y.3    Rajagopalan, P.T.4    Pei, D.5
  • 30
    • 2442711475 scopus 로고    scopus 로고
    • Combinatorial chemistry: Libraries from libraries, the art of the diversity-oriented transformation of resin-bound peptides and chiral polyamides to low molecular weight acyclic and heterocyclic compounds
    • Nefzi, A., Ostresh, J. M., Yu, Y., and Houghten, R. A. (2004) Combinatorial chemistry: libraries from libraries, the art of the diversity-oriented transformation of resin-bound peptides and chiral polyamides to low molecular weight acyclic and heterocyclic compounds, J. Org. Chem. 69, 3603-3609.
    • (2004) J. Org. Chem. , vol.69 , pp. 3603-3609
    • Nefzi, A.1    Ostresh, J.M.2    Yu, Y.3    Houghten, R.A.4
  • 32
    • 0344443721 scopus 로고    scopus 로고
    • Quantum dots as a visual aid for screening bead-bound combinatorial libraries
    • Olivos, H. J., Bachhawat-Sikder, K., and Kodadek, T. (2003) Quantum dots as a visual aid for screening bead-bound combinatorial libraries, ChemBioChem 4, 1242-1245.
    • (2003) ChemBioChem , vol.4 , pp. 1242-1245
    • Olivos, H.J.1    Bachhawat-Sikder, K.2    Kodadek, T.3
  • 33
    • 0032566763 scopus 로고    scopus 로고
    • Quantum dot bioconjugates for ultrasensitive nonisotopic detection
    • Chan, W. C., and Nie, S. (1998) Quantum dot bioconjugates for ultrasensitive nonisotopic detection, Science 281, 2016-2018.
    • (1998) Science , vol.281 , pp. 2016-2018
    • Chan, W.C.1    Nie, S.2
  • 34
    • 0037314241 scopus 로고    scopus 로고
    • Lighting up cells with quantum dots
    • Watson, A., Wu, X., and Bruchez, M. (2003) Lighting up cells with quantum dots, BioTechniques 34, 296-300, 302-293.
    • (2003) BioTechniques , vol.34 , pp. 296-300
    • Watson, A.1    Wu, X.2    Bruchez, M.3
  • 35
    • 0029109073 scopus 로고
    • Generadon and screening of combinatorial peptide libraries designed for rapid sequencing by mass spectrometry
    • Youngquist, R. S., Fuentes, G. R., Lacey, M. P., and Keough, T. (1995) Generadon and screening of combinatorial peptide libraries designed for rapid sequencing by mass spectrometry, J. Am. Chem. Soc. 117, 3900-3906.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3900-3906
    • Youngquist, R.S.1    Fuentes, G.R.2    Lacey, M.P.3    Keough, T.4
  • 36
    • 0028135116 scopus 로고
    • Combinatorial technologies involving reiterative division/coupling/ recombination: Statistical considerations
    • Burgess, K., Liaw, A. I., and Wang, N. (1994) Combinatorial technologies involving reiterative division/coupling/recombination: Statistical considerations, J. Med. Chem. 37, 2985-2987.
    • (1994) J. Med. Chem. , vol.37 , pp. 2985-2987
    • Burgess, K.1    Liaw, A.I.2    Wang, N.3
  • 38
    • 0346435109 scopus 로고    scopus 로고
    • Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases
    • Jackson, M. D., Schmidt, M. T., Oppenheimer, N. J., and Denu, J. M. (2003) Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases, J. Biol. Chem. 278, 50985-50998.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50985-50998
    • Jackson, M.D.1    Schmidt, M.T.2    Oppenheimer, N.J.3    Denu, J.M.4
  • 41
    • 0037826918 scopus 로고    scopus 로고
    • Mutational analysis of the guanylyltransferase component of mammalian mRNA capping enzyme
    • Sawaya, R., and Shuman, S. (2003) Mutational analysis of the guanylyltransferase component of mammalian mRNA capping enzyme, Biochemistry 42, 8240-8249.
    • (2003) Biochemistry , vol.42 , pp. 8240-8249
    • Sawaya, R.1    Shuman, S.2
  • 43
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao, X., and Sudhof, T. C. (2001) A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60, Science 293, 115-120.
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 45
    • 0037185024 scopus 로고    scopus 로고
    • DNA damage-induced translocation of the Werner helicase is regulated by acetylation
    • Blander, G., Zalle, N., Daniely, Y., Taplick, J., Gray, M. D., and Oren, M. (2002) DNA damage-induced translocation of the Werner helicase is regulated by acetylation, J. Biol. Chem. 277, 50934-50940.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50934-50940
    • Blander, G.1    Zalle, N.2    Daniely, Y.3    Taplick, J.4    Gray, M.D.5    Oren, M.6
  • 46
    • 4344649442 scopus 로고    scopus 로고
    • The Werner syndrome protein at the crossroads of DNA repair and apoptosis
    • Comai, L., and Li, B. (2004) The Werner syndrome protein at the crossroads of DNA repair and apoptosis, Mech. Ageing Den. 125, 521-528.
    • (2004) Mech. Ageing Den. , vol.125 , pp. 521-528
    • Comai, L.1    Li, B.2
  • 47
    • 27744569240 scopus 로고    scopus 로고
    • Unstructured conformations are a substrate requirement for the Sir2 family of NAD-dependent protein deacetylases
    • Khan, A. N., and Lewis, P. N. (2005) Unstructured conformations are a substrate requirement for the Sir2 family of NAD-dependent protein deacetylases, J. Biol. Chem.
    • (2005) J. Biol. Chem.
    • Khan, A.N.1    Lewis, P.N.2
  • 49
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT1 activation by resveratrol
    • Borra, M. T., Smith, B. C., and Denu, J. M. (2005) Mechanism of human SIRT1 activation by resveratrol, J. Biol. Chem. 280, 17187-17195.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 51
    • 0025103048 scopus 로고
    • A cleavage method which minimizes side reactions following Fmoc solid-phase peptide synthesis
    • King, D. S., Fields, C. G., and Fields, G. B. (1990) A cleavage method which minimizes side reactions following Fmoc solid-phase peptide synthesis, Int. J. Pept. Protein Res. 36, 255-266.
    • (1990) Int. J. Pept. Protein Res. , vol.36 , pp. 255-266
    • King, D.S.1    Fields, C.G.2    Fields, G.B.3


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