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Volumn 4, Issue 10, 2008, Pages 590-597

Chemical probes for histone-modifying enzymes

Author keywords

[No Author keywords available]

Indexed keywords

5' METHYLTHIOADENOSINE PHOSPHORYLASE; ANACARDIC ACID; CURCUMIN; ENZYME INHIBITOR; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; HISTONE DEMETHYLASE; HISTONE METHYLTRANSFERASE; MEPYRAMINE MALEATE; METHYLTRANSFERASE; PARGYLINE; RESVERATROL; SINEFUNGIN; SIRTUIN; TRANYLCYPROMINE; TRICHOSTATIN A; UNCLASSIFIED DRUG; VORINOSTAT;

EID: 51949111451     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.111     Document Type: Review
Times cited : (214)

References (101)
  • 1
    • 33847047461 scopus 로고    scopus 로고
    • Epigenetics: A landscape takes shape
    • Goldberg, A.D., Allis, C.D. & Bernstein, E. Epigenetics: a landscape takes shape. Cell 128, 635-638 (2007).
    • (2007) Cell , vol.128 , pp. 635-638
    • Goldberg, A.D.1    Allis, C.D.2    Bernstein, E.3
  • 3
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey, V.G., Faulkner, R. & Mirsky, A.E. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc. Natl. Acad. Sci. USA 51, 786-794 (1964).
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 4
    • 33947482638 scopus 로고
    • The occurrence of e-N-methyl lysine in histones
    • Murray, K. The occurrence of e-N-methyl lysine in histones. Biochemistry 3, 10-15 (1964).
    • (1964) Biochemistry , vol.3 , pp. 10-15
    • Murray, K.1
  • 5
    • 0014409959 scopus 로고
    • Chemical studies of histone acetylation. The occurrence of ε-N-acetyllysine in the f2a1 histone
    • Gershey, E.L., Vidali, G. & Allfrey, V.G. Chemical studies of histone acetylation. The occurrence of ε-N-acetyllysine in the f2a1 histone. J. Biol. Chem. 243, 5018-5022 (1968).
    • (1968) J. Biol. Chem , vol.243 , pp. 5018-5022
    • Gershey, E.L.1    Vidali, G.2    Allfrey, V.G.3
  • 6
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. Chromatin modifications and their function. Cell 128, 693-705 (2007).
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 7
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell, J.E. et al. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84, 843-851 (1996).
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1
  • 8
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J., Hassig, C.A. & Schreiber, S.L. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272, 408-411 (1996).
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 9
    • 9744255506 scopus 로고    scopus 로고
    • Structure and functions of the GNAT superfamily of acetyltransferases
    • Vetting, M.W. et al. Structure and functions of the GNAT superfamily of acetyltransferases. Arch. Biochem. Biophys. 433, 212-226 (2005).
    • (2005) Arch. Biochem. Biophys , vol.433 , pp. 212-226
    • Vetting, M.W.1
  • 10
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase in vivo and in vitro by trichostatin A
    • Yoshida, M., Kijima, M., Akita, M. & Beppu, T. Potent and specific inhibition of mammalian histone deacetylase in vivo and in vitro by trichostatin A. J. Biol. Chem. 265, 17174-17179 (1990).
    • (1990) J. Biol. Chem , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 11
    • 0027378351 scopus 로고
    • Trapoxin, an antitumor cyclic tetrapeptide, is an inhibitor of mammalian histone deacetylase
    • Kijima, M., Yoshida, M., Sugita, K., Horinouchi, S. & Beppu, T. Trapoxin, an antitumor cyclic tetrapeptide, is an inhibitor of mammalian histone deacetylase. J. Biol. Chem. 268, 22429-22435 (1993).
    • (1993) J. Biol. Chem , vol.268 , pp. 22429-22435
    • Kijima, M.1    Yoshida, M.2    Sugita, K.3    Horinouchi, S.4    Beppu, T.5
  • 12
    • 0033539092 scopus 로고    scopus 로고
    • Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
    • Finnin, M.S. et al. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 401, 188-193 (1999).
    • (1999) Nature , vol.401 , pp. 188-193
    • Finnin, M.S.1
  • 13
    • 42049118549 scopus 로고    scopus 로고
    • Isoform-selective histone deacetylase inhibitors
    • Itoh, Y., Suzuki, T. & Miyata, N. Isoform-selective histone deacetylase inhibitors. Curr. Pharm. Des. 14, 529-544 (2008).
    • (2008) Curr. Pharm. Des , vol.14 , pp. 529-544
    • Itoh, Y.1    Suzuki, T.2    Miyata, N.3
  • 14
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longetivity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai, S., Armstrong, C.M., Kaeberlein, M. & Guarente, L. Transcriptional silencing and longetivity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403, 795-800 (2000).
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 15
    • 0033598942 scopus 로고    scopus 로고
    • An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing
    • Tanny, J.C., Dowd, G.J., Huang, J., Hilz, H. & Moazed, D. An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing. Cell 99, 735-745 (1999).
    • (1999) Cell , vol.99 , pp. 735-745
    • Tanny, J.C.1    Dowd, G.J.2    Huang, J.3    Hilz, H.4    Moazed, D.5
  • 16
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander, G. & Guarente, L. The Sir2 family of protein deacetylases. Annu. Rev. Biochem. 73, 417-435 (2004).
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 17
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • Rea, S. et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 406, 593-599 (2000).
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1
  • 18
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin, C. & Zhang, Y. The diverse functions of histone lysine methylation. Nat. Rev. Mol. Cell Biol. 6, 838-849 (2005).
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 19
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Shi, Y. et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119, 941-953 (2004).
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1
  • 20
    • 32844454603 scopus 로고    scopus 로고
    • Histone demethylation by a family of JmjC domain-containing proteins
    • Tsukada, Y. et al. Histone demethylation by a family of JmjC domain-containing proteins. Nature 439, 811-816 (2006).
    • (2006) Nature , vol.439 , pp. 811-816
    • Tsukada, Y.1
  • 21
    • 35348812522 scopus 로고    scopus 로고
    • LSD1 and the chemistry of histone demethylation
    • Culhane, J.C. & Cole, P.A. LSD1 and the chemistry of histone demethylation. Curr. Opin. Chem. Biol. 11, 561-568 (2007).
    • (2007) Curr. Opin. Chem. Biol , vol.11 , pp. 561-568
    • Culhane, J.C.1    Cole, P.A.2
  • 22
    • 41149089267 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: From bench to clinic
    • Paris, M., Porcelloni, M., Binaschi, M. & Fattori, D. Histone deacetylase inhibitors: from bench to clinic. J. Med. Chem. 51, 1505-1529 (2008).
    • (2008) J. Med. Chem , vol.51 , pp. 1505-1529
    • Paris, M.1    Porcelloni, M.2    Binaschi, M.3    Fattori, D.4
  • 23
    • 6344222799 scopus 로고    scopus 로고
    • Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor
    • Vannini, A. et al. Crystal structure of a eukaryotic zinc-dependent histone deacetylase, human HDAC8, complexed with a hydroxamic acid inhibitor. Proc. Natl. Acad. Sci. USA 101, 15064-15069 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15064-15069
    • Vannini, A.1
  • 24
    • 45549095066 scopus 로고    scopus 로고
    • Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity
    • Schuetz, A. et al. Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity. J. Biol. Chem. 283, 11355-11363 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 11355-11363
    • Schuetz, A.1
  • 25
    • 33847065486 scopus 로고    scopus 로고
    • The epigenomics of cancer
    • Jones, P.A. & Baylin, S.B. The epigenomics of cancer. Cell 128, 683-692 (2007).
    • (2007) Cell , vol.128 , pp. 683-692
    • Jones, P.A.1    Baylin, S.B.2
  • 26
    • 0038274087 scopus 로고    scopus 로고
    • Structural basis for in-cell histone deacetylase paralog selectivity
    • Wong, J.C., Hong, R. & Schreiber, S.L. Structural basis for in-cell histone deacetylase paralog selectivity. J. Am. Chem. Soc. 125, 5586-5587 (2003).
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 5586-5587
    • Wong, J.C.1    Hong, R.2    Schreiber, S.L.3
  • 27
    • 43949130430 scopus 로고    scopus 로고
    • Structural origin of selectivity in class II-selective histone deacetylase inhibitors
    • Estiu, G. et al. Structural origin of selectivity in class II-selective histone deacetylase inhibitors. J. Med. Chem. 51, 2898-2906 (2008).
    • (2008) J. Med. Chem , vol.51 , pp. 2898-2906
    • Estiu, G.1
  • 28
    • 20844435806 scopus 로고    scopus 로고
    • Small-molecule inhibition of proteasome and aggresome function induces synergistic antitumor activity in multiple myeloma
    • Hideshima, T. et al. Small-molecule inhibition of proteasome and aggresome function induces synergistic antitumor activity in multiple myeloma. Proc. Natl. Acad. Sci. USA 102, 8567-8572 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8567-8572
    • Hideshima, T.1
  • 29
    • 34248213405 scopus 로고    scopus 로고
    • DAC6 deacetylation of tubulin modulates dynamics of cellular adhesions
    • Tran, A.D. et al. DAC6 deacetylation of tubulin modulates dynamics of cellular adhesions. J. Cell Sci. 120, 1469-1479 (2007).
    • (2007) J. Cell Sci , vol.120 , pp. 1469-1479
    • Tran, A.D.1
  • 30
    • 39549102872 scopus 로고    scopus 로고
    • Optimization of activity-based probes for proteomic profiling of histone deacetylase complexes
    • Salisbury, C.M. & Cravatt, B.F. Optimization of activity-based probes for proteomic profiling of histone deacetylase complexes. J. Am. Chem. Soc. 130, 2184-2194 (2008).
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 2184-2194
    • Salisbury, C.M.1    Cravatt, B.F.2
  • 31
    • 13944253348 scopus 로고    scopus 로고
    • Calorie restriction-the SIR2 connection
    • Guarente, L. & Picard, F. Calorie restriction-the SIR2 connection. Cell 120, 473-482 (2005).
    • (2005) Cell , vol.120 , pp. 473-482
    • Guarente, L.1    Picard, F.2
  • 33
    • 85029150992 scopus 로고    scopus 로고
    • Wade, N. New hints seen that red wine may slow aging. New York Times 4, June 2008A1.
    • Wade, N. New hints seen that red wine may slow aging. New York Times 4, June 2008A1.
  • 34
    • 0141719702 scopus 로고    scopus 로고
    • Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
    • Howitz, K.T. et al. Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature 425, 191-196 (2003).
    • (2003) Nature , vol.425 , pp. 191-196
    • Howitz, K.T.1
  • 35
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SirT1 activation by resveratrol
    • Borra, M.T., Smith, B.C. & Denu, J.M. Mechanism of human SirT1 activation by resveratrol. J. Biol. Chem. 280, 17187-17195 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 36
    • 20444431507 scopus 로고    scopus 로고
    • Substrate-specific activation of sirtuins by resveratrol
    • Kaeberlein, M. et al. Substrate-specific activation of sirtuins by resveratrol. J. Biol. Chem. 280, 17038-17045 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 17038-17045
    • Kaeberlein, M.1
  • 37
    • 33845399894 scopus 로고    scopus 로고
    • Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1alpha
    • Lagouge, M. et al. Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1alpha. Cell 127, 1109-1122 (2006).
    • (2006) Cell , vol.127 , pp. 1109-1122
    • Lagouge, M.1
  • 38
    • 12944300930 scopus 로고    scopus 로고
    • Vinferin formation by COX-1: Evidence for radical intermediates during co-oxidation of resveratrol
    • Szewczuk, L.M., Lee, S.H., Blair, I.A. & Penning, T.M. Vinferin formation by COX-1: evidence for radical intermediates during co-oxidation of resveratrol. J. Nat. Prod. 68, 36-42 (2005).
    • (2005) J. Nat. Prod , vol.68 , pp. 36-42
    • Szewczuk, L.M.1    Lee, S.H.2    Blair, I.A.3    Penning, T.M.4
  • 39
    • 36749087548 scopus 로고    scopus 로고
    • Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
    • Milne, J.C. et al. Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes. Nature 450, 712-716 (2007).
    • (2007) Nature , vol.450 , pp. 712-716
    • Milne, J.C.1
  • 40
    • 33745534953 scopus 로고    scopus 로고
    • Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide
    • Hoff, K.G., Avalos, J.L., Sens, K. & Wolberger, C. Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide. Structure 14, 1231-1240 (2006).
    • (2006) Structure , vol.14 , pp. 1231-1240
    • Hoff, K.G.1    Avalos, J.L.2    Sens, K.3    Wolberger, C.4
  • 41
    • 85029171550 scopus 로고    scopus 로고
    • A fasting inducible acetylase/deacetylase switch modulates gluconeogenesis through activator-coactivator exchange
    • in the press
    • Liu, Y. et al. A fasting inducible acetylase/deacetylase switch modulates gluconeogenesis through activator-coactivator exchange. Nature (in the press).
    • Nature
    • Liu, Y.1
  • 42
    • 4544243684 scopus 로고    scopus 로고
    • Coenzyme specificity of Sir2 protein deacetylases: Implications for physiological regulation
    • Schmidt, M.T., Smith, B.C., Jackson, M.D. & Denu, J.M. Coenzyme specificity of Sir2 protein deacetylases: implications for physiological regulation. J. Biol. Chem. 279, 40122-40129 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 40122-40129
    • Schmidt, M.T.1    Smith, B.C.2    Jackson, M.D.3    Denu, J.M.4
  • 43
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2a promotes cell survival under stress
    • Luo, J. et al. Negative control of p53 by Sir2a promotes cell survival under stress. Cell 107, 137-148 (2001).
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1
  • 44
    • 33746484522 scopus 로고    scopus 로고
    • Ne-thioacetyl-lysine: A multi-facet functional probe for enzymatic protein lysine Ne-deacetylation
    • Fatkins, D.G., Monnot, A.D. & Zheng, W. Ne-thioacetyl-lysine: a multi-facet functional probe for enzymatic protein lysine Ne-deacetylation. Bioorg. Med. Chem. Lett. 16, 3651-3656 (2006).
    • (2006) Bioorg. Med. Chem. Lett , vol.16 , pp. 3651-3656
    • Fatkins, D.G.1    Monnot, A.D.2    Zheng, W.3
  • 45
    • 37549067781 scopus 로고    scopus 로고
    • Acetyl-lysine analog peptides as mechanistic probes of protein deacetylases
    • Smith, B.C. & Denu, J.M. Acetyl-lysine analog peptides as mechanistic probes of protein deacetylases. J. Biol. Chem. 282, 37256-37265 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 37256-37265
    • Smith, B.C.1    Denu, J.M.2
  • 47
    • 0035914304 scopus 로고    scopus 로고
    • Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening
    • Grozinger, C.M., Chao, E.D., Blackwell, H.E., Moazed, D. & Schreiber, S.L. Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening. J. Biol. Chem. 276, 38837-38843 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 38837-38843
    • Grozinger, C.M.1    Chao, E.D.2    Blackwell, H.E.3    Moazed, D.4    Schreiber, S.L.5
  • 48
    • 0346101749 scopus 로고    scopus 로고
    • Identification of selective inhibitors of NAD-dependent deacetylases using phenotypic screens in yeast
    • Hirao, M. et al. Identification of selective inhibitors of NAD-dependent deacetylases using phenotypic screens in yeast. J. Biol. Chem. 278, 52773-52782 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 52773-52782
    • Hirao, M.1
  • 49
    • 0042431612 scopus 로고    scopus 로고
    • Sir1, an upstream component in auxin signaling identified by chemical genetics
    • Zhao, Y., Dai, X., Blackwell, H.E., Schreiber, S.L. & Chory, J. Sir1, an upstream component in auxin signaling identified by chemical genetics. Science 301, 1107-1110 (2003).
    • (2003) Science , vol.301 , pp. 1107-1110
    • Zhao, Y.1    Dai, X.2    Blackwell, H.E.3    Schreiber, S.L.4    Chory, J.5
  • 50
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SirT1 activation prevent axonal degeneration
    • Araki, T., Sasaki, Y. & Milbrandt, J. Increased nuclear NAD biosynthesis and SirT1 activation prevent axonal degeneration. Science 305, 1010-1013 (2004).
    • (2004) Science , vol.305 , pp. 1010-1013
    • Araki, T.1    Sasaki, Y.2    Milbrandt, J.3
  • 51
    • 8844247034 scopus 로고    scopus 로고
    • Silent information regulator 2a, a longevity factor and class III histone deacetylase, is an essential endogenous apoptosis inhibitor in cardiac myocytes
    • Alcendor, R.R., Kirshenbaum, L.A., Imai, S., Vatner, S.F. & Sadoshima, J. Silent information regulator 2a, a longevity factor and class III histone deacetylase, is an essential endogenous apoptosis inhibitor in cardiac myocytes. Circ. Res. 95, 971-980 (2004).
    • (2004) Circ. Res , vol.95 , pp. 971-980
    • Alcendor, R.R.1    Kirshenbaum, L.A.2    Imai, S.3    Vatner, S.F.4    Sadoshima, J.5
  • 52
    • 34547599329 scopus 로고    scopus 로고
    • Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease
    • Outeiro, T.F. et al. Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease. Science 317, 516-519 (2007).
    • (2007) Science , vol.317 , pp. 516-519
    • Outeiro, T.F.1
  • 53
    • 34249828678 scopus 로고    scopus 로고
    • Small molecule modulators in epigenetics: Implications in gene expression and therapeutics
    • Swaminathan, V. et al. Small molecule modulators in epigenetics: implications in gene expression and therapeutics. Subcell. Biochem. 41, 397-428 (2007).
    • (2007) Subcell. Biochem , vol.41 , pp. 397-428
    • Swaminathan, V.1
  • 54
    • 1042300239 scopus 로고    scopus 로고
    • Selective HAT inhibitors as mechanistic tools for protein acetylation
    • Zheng, Y. et al. Selective HAT inhibitors as mechanistic tools for protein acetylation. Methods Enzymol. 376, 188-199 (2004).
    • (2004) Methods Enzymol , vol.376 , pp. 188-199
    • Zheng, Y.1
  • 55
    • 27644473204 scopus 로고    scopus 로고
    • Isothiazolones as inhibitors of PCAF and p300 histone acetyltransferase activity
    • Stimson, L. et al. Isothiazolones as inhibitors of PCAF and p300 histone acetyltransferase activity. Mol. Cancer Ther. 4, 1521-1532 (2005).
    • (2005) Mol. Cancer Ther , vol.4 , pp. 1521-1532
    • Stimson, L.1
  • 56
    • 34250308083 scopus 로고    scopus 로고
    • Specific inhibition of p300-HAT alters global gene expression and represses HIV replication
    • Mantelingu, K. et al. Specific inhibition of p300-HAT alters global gene expression and represses HIV replication. Chem. Biol. 14, 645-657 (2007).
    • (2007) Chem. Biol , vol.14 , pp. 645-657
    • Mantelingu, K.1
  • 57
    • 40549135974 scopus 로고    scopus 로고
    • The dietary compound curcumin inhibits p300 histone acetyltransferase activity and prevents heart failure in rats
    • Morimoto, T. et al. The dietary compound curcumin inhibits p300 histone acetyltransferase activity and prevents heart failure in rats. J. Clin. Invest. 118, 868-878 (2008).
    • (2008) J. Clin. Invest , vol.118 , pp. 868-878
    • Morimoto, T.1
  • 58
    • 0014443830 scopus 로고
    • Conditions for the self-catalysed inactivation of carnitine acetyltransferase
    • Chase, J.F.A. & Tubbs, P.K. Conditions for the self-catalysed inactivation of carnitine acetyltransferase. Biochem. J. 111, 225-235 (1969).
    • (1969) Biochem. J , vol.111 , pp. 225-235
    • Chase, J.F.A.1    Tubbs, P.K.2
  • 59
    • 0035165210 scopus 로고    scopus 로고
    • Mechanism-based design of a protein kinase inhibitor
    • Parang, K. et al. Mechanism-based design of a protein kinase inhibitor. Nat. Struct. Biol. 8, 37-41 (2001).
    • (2001) Nat. Struct. Biol , vol.8 , pp. 37-41
    • Parang, K.1
  • 60
    • 0033714888 scopus 로고    scopus 로고
    • HATs off: Selective synthetic inhibitors of the histone acetyltransferases p300 and PCAF
    • Lau, O.D. et al. HATs off: selective synthetic inhibitors of the histone acetyltransferases p300 and PCAF. Mol. Cell 5, 589-595 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 589-595
    • Lau, O.D.1
  • 61
    • 0034698144 scopus 로고    scopus 로고
    • PCAF Histone acetyltransferase processing of a peptide substrate: Kinetic analysis of the catalytic mechanism
    • Lau, O.D. et al. PCAF Histone acetyltransferase processing of a peptide substrate: kinetic analysis of the catalytic mechanism. J. Biol. Chem. 275, 21953-21959 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 21953-21959
    • Lau, O.D.1
  • 62
    • 0037195124 scopus 로고    scopus 로고
    • Structure of the GCN5 histone acetyltransferase bound to a bisubstrate inhibitor
    • Poux, A.N., Cebrat, M., Kim, C.M., Cole, P.A. & Marmorstein, R. Structure of the GCN5 histone acetyltransferase bound to a bisubstrate inhibitor. Proc. Natl. Acad. Sci. USA 99, 14065-14070 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14065-14070
    • Poux, A.N.1    Cebrat, M.2    Kim, C.M.3    Cole, P.A.4    Marmorstein, R.5
  • 63
    • 23244460580 scopus 로고    scopus 로고
    • Fluorescence analysis of a dynamic loop in the PCAF/GCN5 histone acetyltransferase
    • Zheng, Y. et al. Fluorescence analysis of a dynamic loop in the PCAF/GCN5 histone acetyltransferase. Biochemistry 44, 10501-10509 (2005).
    • (2005) Biochemistry , vol.44 , pp. 10501-10509
    • Zheng, Y.1
  • 64
    • 0035823497 scopus 로고    scopus 로고
    • Transcriptional coactivator protein p300. Kinetic characterization of its histone acetyltransferase activity
    • Thompson, P.R., Kurooka, H., Nakatani, Y. & Cole, P.A. Transcriptional coactivator protein p300. Kinetic characterization of its histone acetyltransferase activity. J. Biol. Chem. 276, 33721-33729 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 33721-33729
    • Thompson, P.R.1    Kurooka, H.2    Nakatani, Y.3    Cole, P.A.4
  • 65
    • 39149109887 scopus 로고    scopus 로고
    • The structural basis of protein acetylation by the p300/CBP transcriptional coactivator
    • Liu, X. et al. The structural basis of protein acetylation by the p300/CBP transcriptional coactivator. Nature 451, 846-850 (2008).
    • (2008) Nature , vol.451 , pp. 846-850
    • Liu, X.1
  • 66
    • 29044440879 scopus 로고    scopus 로고
    • Synthesis and evaluation of a potent and selective cell-permeable p300 histone acetyltransferase inhibitor
    • Zheng, Y. et al. Synthesis and evaluation of a potent and selective cell-permeable p300 histone acetyltransferase inhibitor. J. Am. Chem. Soc. 127, 17182-17183 (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 17182-17183
    • Zheng, Y.1
  • 67
    • 20744456118 scopus 로고    scopus 로고
    • Guidez, F. et al. Histone acetyltransferase activity of p300 is required for transcriptional repression by the promyelocytic zinc finger protein. Mol. Cell. Biol. 25, 5552-5566 (2005).
    • Guidez, F. et al. Histone acetyltransferase activity of p300 is required for transcriptional repression by the promyelocytic zinc finger protein. Mol. Cell. Biol. 25, 5552-5566 (2005).
  • 68
    • 24744471838 scopus 로고    scopus 로고
    • Acetylation by P/CAF drives DEK into interchromatin granule clusters
    • Cleary, J. et al. Acetylation by P/CAF drives DEK into interchromatin granule clusters. J. Biol. Chem. 280, 31760-31767 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 31760-31767
    • Cleary, J.1
  • 69
    • 35448990859 scopus 로고    scopus 로고
    • Activation of Pol III transcription by c-Myc involves selective acetylation of histone H3 and recruitment of TRAPP, GCN5, and TFIIIB
    • Kenneth, N.S. et al. Activation of Pol III transcription by c-Myc involves selective acetylation of histone H3 and recruitment of TRAPP, GCN5, and TFIIIB. Proc. Natl. Acad. Sci. USA 104, 14917-14922 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 14917-14922
    • Kenneth, N.S.1
  • 70
    • 0036593394 scopus 로고    scopus 로고
    • Histone methyltransferases, diet nutrients and tumour suppressors
    • Huang, S. Histone methyltransferases, diet nutrients and tumour suppressors. Nat. Rev. Cancer 2, 469-476 (2002).
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 469-476
    • Huang, S.1
  • 71
    • 33947615716 scopus 로고    scopus 로고
    • Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases
    • Dirk, L.M. et al. Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases. Biochemistry 46, 3905-3915 (2007).
    • (2007) Biochemistry , vol.46 , pp. 3905-3915
    • Dirk, L.M.1
  • 72
    • 33846902276 scopus 로고    scopus 로고
    • The histone methyltransferase MLL is an upstream regulator of endothelial-cell sprout formation
    • Diehl, F., Rössig, L., Zeiher, A.M., Dimmeler, S. & Urbich, C. The histone methyltransferase MLL is an upstream regulator of endothelial-cell sprout formation. Blood 109, 1472-1478 (2007).
    • (2007) Blood , vol.109 , pp. 1472-1478
    • Diehl, F.1    Rössig, L.2    Zeiher, A.M.3    Dimmeler, S.4    Urbich, C.5
  • 73
    • 30644474460 scopus 로고    scopus 로고
    • Identification of a specific inhibitor of the histone methyltransferase SU(VAR)3-9
    • Greiner, D., Bonaldi, T., Eskeland, R., Roemer, E. & Imhof, A. Identification of a specific inhibitor of the histone methyltransferase SU(VAR)3-9. Nat. Chem. Biol. 1, 143-145 (2005).
    • (2005) Nat. Chem. Biol , vol.1 , pp. 143-145
    • Greiner, D.1    Bonaldi, T.2    Eskeland, R.3    Roemer, E.4    Imhof, A.5
  • 74
    • 33846783261 scopus 로고    scopus 로고
    • Reversal of H3K9me2 by a small-molecule inhibitor for the G9a histone methyltransferase
    • Kubicek, S. et al. Reversal of H3K9me2 by a small-molecule inhibitor for the G9a histone methyltransferase. Mol. Cell 25, 473-481 (2007).
    • (2007) Mol. Cell , vol.25 , pp. 473-481
    • Kubicek, S.1
  • 75
    • 33947214077 scopus 로고    scopus 로고
    • Chaetocin: A promising new antimyeloma agent with in vitro and in vivo activity mediated via imposition of oxidative stress
    • Isham, C.R. et al. Chaetocin: a promising new antimyeloma agent with in vitro and in vivo activity mediated via imposition of oxidative stress. Blood 109, 2579-2588 (2007).
    • (2007) Blood , vol.109 , pp. 2579-2588
    • Isham, C.R.1
  • 76
    • 0021192474 scopus 로고
    • Suicide substrates, mechanism-based enzyme inactivators: Recent developments
    • Walsh, C.T. Suicide substrates, mechanism-based enzyme inactivators: recent developments. Annu. Rev. Biochem. 53, 493-535 (1984).
    • (1984) Annu. Rev. Biochem , vol.53 , pp. 493-535
    • Walsh, C.T.1
  • 78
    • 24144462170 scopus 로고    scopus 로고
    • LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription
    • Metzger, E. et al. LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription. Nature 437, 436-439 (2005).
    • (2005) Nature , vol.437 , pp. 436-439
    • Metzger, E.1
  • 80
    • 33745187327 scopus 로고    scopus 로고
    • Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications
    • Lee, M.G., Wynder, C., Schmidt, D.M., McCafferty, D.G. & Shiekhatter, R. Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications. Chem. Biol. 13, 563-567 (2006).
    • (2006) Chem. Biol , vol.13 , pp. 563-567
    • Lee, M.G.1    Wynder, C.2    Schmidt, D.M.3    McCafferty, D.G.4    Shiekhatter, R.5
  • 81
    • 34147173308 scopus 로고    scopus 로고
    • trans-2-Phenylcyclopropylamine is a mechanism-based inactivator of the histone demethylase LSD1
    • Schmidt, D.M. & McCafferty, D.G. trans-2-Phenylcyclopropylamine is a mechanism-based inactivator of the histone demethylase LSD1. Biochemistry 46, 4408-4416 (2007).
    • (2007) Biochemistry , vol.46 , pp. 4408-4416
    • Schmidt, D.M.1    McCafferty, D.G.2
  • 82
    • 34447338875 scopus 로고    scopus 로고
    • Structural basis for inhibition of the LSD1 histone demethylase by the antidepressant trans-2-Phenylcyclopropylamine
    • Yang, M. et al. Structural basis for inhibition of the LSD1 histone demethylase by the antidepressant trans-2-Phenylcyclopropylamine. Biochemistry 46, 8058-8065 (2007).
    • (2007) Biochemistry , vol.46 , pp. 8058-8065
    • Yang, M.1
  • 84
    • 33646061354 scopus 로고    scopus 로고
    • A mechanism-based inactivator for histone demethylase LSD1
    • Culhane, J.C. et al. A mechanism-based inactivator for histone demethylase LSD1. J. Am. Chem. Soc. 128, 4536-4537 (2006).
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 4536-4537
    • Culhane, J.C.1
  • 85
    • 34250203607 scopus 로고    scopus 로고
    • Mechanistic analysis of a suicide inactivator of histone demethylase LSD1
    • Szewczuk, L.M. et al. Mechanistic analysis of a suicide inactivator of histone demethylase LSD1. Biochemistry 46, 6892-6902 (2007).
    • (2007) Biochemistry , vol.46 , pp. 6892-6902
    • Szewczuk, L.M.1
  • 86
    • 34249881352 scopus 로고    scopus 로고
    • Structural basis for histone demethylation by LSD1 revealed by suicide inactivation
    • Yang, M. et al. Structural basis for histone demethylation by LSD1 revealed by suicide inactivation. Nat. Struct. Mol. Biol. 14, 535-539 (2007).
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 535-539
    • Yang, M.1
  • 87
    • 18244376860 scopus 로고    scopus 로고
    • Modular synthesis of cyclic peptidomimetics inspired by γ-turns
    • Ramanathan, S.K. et al. Modular synthesis of cyclic peptidomimetics inspired by γ-turns. Org. Lett. 7, 1059-1062 (2005).
    • (2005) Org. Lett , vol.7 , pp. 1059-1062
    • Ramanathan, S.K.1
  • 88
    • 34547132094 scopus 로고    scopus 로고
    • Structural basis of LSD1-CoREST selectivity in histone H3 recognition
    • Forneris, F., Binda, C., Adamo, A., Battaglioli, E. & Mattevi, A. Structural basis of LSD1-CoREST selectivity in histone H3 recognition. J. Biol. Chem. 282, 20070-20074 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 20070-20074
    • Forneris, F.1    Binda, C.2    Adamo, A.3    Battaglioli, E.4    Mattevi, A.5
  • 89
    • 34249934238 scopus 로고    scopus 로고
    • Inhibition of lysine-specific demethylase 1 by polyamine analogues results in reexpression of aberrantly silenced genes
    • Huang, Y. et al. Inhibition of lysine-specific demethylase 1 by polyamine analogues results in reexpression of aberrantly silenced genes. Proc. Natl. Acad. Sci. USA 104, 8023-8028 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8023-8028
    • Huang, Y.1
  • 90
    • 41849105766 scopus 로고    scopus 로고
    • In situ generation of a bisubstrate analogue for protein arginine methyltransferase 1
    • Osborne, T., Roska, R.L., Rajski, S.R. & Thompson, P.R. In situ generation of a bisubstrate analogue for protein arginine methyltransferase 1. J. Am. Chem. Soc. 130, 4574-4575 (2008).
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 4574-4575
    • Osborne, T.1    Roska, R.L.2    Rajski, S.R.3    Thompson, P.R.4
  • 91
    • 33751010478 scopus 로고    scopus 로고
    • Activity-based protein profiling reagents for protein arginine deiminase 4 (PAD4): Synthesis and in vitro evaluation of a fluorescently labeled probe
    • Luo, Y., Knuckley, B., Bhatia, M., Pellechia, P.J. & Thompson, P.R. Activity-based protein profiling reagents for protein arginine deiminase 4 (PAD4): synthesis and in vitro evaluation of a fluorescently labeled probe. J. Am. Chem. Soc. 128, 14468-14469 (2006).
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 14468-14469
    • Luo, Y.1    Knuckley, B.2    Bhatia, M.3    Pellechia, P.J.4    Thompson, P.R.5
  • 92
    • 33845292279 scopus 로고    scopus 로고
    • Activity-based substrate profiling for Gcn5-related N-acetyltransferases: The use of chloroacetyl-coenzyme A to identify protein substrates
    • Yu, M., de Carvalho, L.P., Sun, G. & Blanchard, J.S. Activity-based substrate profiling for Gcn5-related N-acetyltransferases: the use of chloroacetyl-coenzyme A to identify protein substrates. J. Am. Chem. Soc. 128, 15356-15357 (2006).
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 15356-15357
    • Yu, M.1    de Carvalho, L.P.2    Sun, G.3    Blanchard, J.S.4
  • 93
    • 35048849835 scopus 로고    scopus 로고
    • Selective chemical probe for coenzyme A-requiring enzymes
    • Hwang, Y. et al. Selective chemical probe for coenzyme A-requiring enzymes. Angew. Chem. Int. Edn Engl. 46, 7621-7624 (2007).
    • (2007) Angew. Chem. Int. Edn Engl , vol.46 , pp. 7621-7624
    • Hwang, Y.1
  • 94
    • 30744456492 scopus 로고    scopus 로고
    • Target structure-based discovery of small molecules that block human p53 and CREB binding protein association
    • Sachchidanand et al. Target structure-based discovery of small molecules that block human p53 and CREB binding protein association. Chem. Biol. 13, 81-90 (2006).
    • (2006) Chem. Biol , vol.13 , pp. 81-90
    • Sachchidanand1
  • 95
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • Shogren-Knaak, M. et al. Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 311, 844-847 (2006).
    • (2006) Science , vol.311 , pp. 844-847
    • Shogren-Knaak, M.1
  • 96
    • 1842420646 scopus 로고    scopus 로고
    • Regulation of p300 HAT domain via a novel activation loop
    • Thompson, P.R. et al. Regulation of p300 HAT domain via a novel activation loop. Nat. Struct. Mol. Biol. 11, 308-315 (2004).
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 308-315
    • Thompson, P.R.1
  • 97
    • 33847386172 scopus 로고    scopus 로고
    • The site-specific installation of methyl-lysine analogs into recombinant histones
    • Simon, M.D. et al. The site-specific installation of methyl-lysine analogs into recombinant histones. Cell 128, 1003-1012 (2007).
    • (2007) Cell , vol.128 , pp. 1003-1012
    • Simon, M.D.1
  • 98
    • 44849100496 scopus 로고    scopus 로고
    • Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation
    • McGinty, R.K., Kim, J., Chatterjee, C., Roeder, R.G. & Muir, T.W. Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation. Nature 453, 812-816 (2008).
    • (2008) Nature , vol.453 , pp. 812-816
    • McGinty, R.K.1    Kim, J.2    Chatterjee, C.3    Roeder, R.G.4    Muir, T.W.5
  • 99
    • 2442570040 scopus 로고    scopus 로고
    • Genetically encoded fluorescent reporters of histone methylation in living cell
    • Lin, C.W., Jao, C.Y. & Ting, A.Y. Genetically encoded fluorescent reporters of histone methylation in living cell. J. Am. Chem. Soc. 126, 5982-5983 (2004).
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 5982-5983
    • Lin, C.W.1    Jao, C.Y.2    Ting, A.Y.3
  • 100
    • 0035233367 scopus 로고    scopus 로고
    • Recent advances in chemical approaches to the study of biological systems
    • Shogren-Knaak, M.A., Alaimo, P.J. & Shokat, K.M. Recent advances in chemical approaches to the study of biological systems. Annu. Rev. Cell Biol. 17, 405-433 (2001).
    • (2001) Annu. Rev. Cell Biol , vol.17 , pp. 405-433
    • Shogren-Knaak, M.A.1    Alaimo, P.J.2    Shokat, K.M.3
  • 101
    • 33644684486 scopus 로고    scopus 로고
    • Chemical rescue of a mutant enzyme in living cells
    • Qiao, Y., Molina, H., Pandey, A., Zhang, J. & Cole, P.A. Chemical rescue of a mutant enzyme in living cells. Science 311, 1293-1297 (2006).
    • (2006) Science , vol.311 , pp. 1293-1297
    • Qiao, Y.1    Molina, H.2    Pandey, A.3    Zhang, J.4    Cole, P.A.5


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