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Volumn 52, Issue 23, 2009, Pages 7836-7846

Discovery of potent and selective histone deacetylase inhibitors via focused combinatorial libraries of cyclic α3 β-tetrapeptides

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; HISTONE DEACETYLASE 6; HISTONE DEACETYLASE INHIBITOR; TETRAPEPTIDE;

EID: 72249094958     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm900850t     Document Type: Article
Times cited : (75)

References (91)
  • 1
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides, T. Chromatin modifications and their function. Cell 2007, 128, 693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 3
    • 20344392202 scopus 로고    scopus 로고
    • Epigenetics - An epicenter of gene regulation: Histones and histone-modifying enzymes
    • DOI 10.1002/anie.200461346
    • Biel, M.; Wascholowski, V.; Giannis, A. Epigenetics - an epicenter of gene regulation: histones and histone-modifying enzymes. Angew. Chem., Int. Ed. 2005, 44, 3186-3216. (Pubitemid 40778337)
    • (2005) Angewandte Chemie - International Edition , vol.44 , Issue.21 , pp. 3186-3216
    • Biel, M.1    Wascholowski, V.2    Giannis, A.3
  • 4
    • 0037406061 scopus 로고    scopus 로고
    • Class II histone deacetylases: Versatile regulators
    • Verdin, E.; Dequiedt, F.; Kasler, H. G. Class II histone deacetylases: versatile regulators. Trends Genet. 2003, 19, 286-293.
    • (2003) Trends Genet. , vol.19 , pp. 286-293
    • Verdin, E.1    Dequiedt, F.2    Kasler, H.G.3
  • 5
    • 12244251445 scopus 로고    scopus 로고
    • Stat3 dimerization regulated by reversible acetylation of a single lysine residue
    • Yuan, Z. L.; Guan, Y. J.; Chatterjee, D.; Chin, Y. E. Stat3 dimerization regulated by reversible acetylation of a single lysine residue. Science 2005, 307, 269-273.
    • (2005) Science , vol.307 , pp. 269-273
    • Yuan, Z.L.1    Guan, Y.J.2    Chatterjee, D.3    Chin, Y.E.4
  • 9
    • 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. 2008, 51, 1505-1529.
    • (2008) J. Med. Chem. , vol.51 , pp. 1505-1529
    • Paris, M.1    Porcelloni, M.2    Binaschi, M.3    Fattori, D.4
  • 10
    • 45749142120 scopus 로고    scopus 로고
    • Isoform-selective histone deacetylase inhibitors
    • Bieliauskas, A. V.; Pflum, M. K. Isoform-selective histone deacetylase inhibitors. Chem. Soc. Rev. 2008, 37, 1402-1413.
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 1402-1413
    • Bieliauskas, A.V.1    Pflum, M.K.2
  • 11
    • 51949111451 scopus 로고    scopus 로고
    • Chemical probes for histone-modifying enzymes
    • Cole, P. A. Chemical probes for histone-modifying enzymes. Nat. Chem. Biol. 2008, 4, 590-597.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 590-597
    • Cole, P.A.1
  • 13
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci, S.; Pelicci, P. G. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat. Rev. Cancer 2006, 6, 38-51.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 16
    • 33846122993 scopus 로고    scopus 로고
    • Dimethyl sulfoxide to vorinostat: Development of this histone deacetylase inhibitor as an anticancer drug
    • Marks, P. A.; Breslow, R. Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug. Nat. Biotechnol. 2007, 25, 84-90.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 84-90
    • Marks, P.A.1    Breslow, R.2
  • 17
    • 53249130741 scopus 로고    scopus 로고
    • Therapeutic application of histone deacetylase inhibitors for central nervous system disorders
    • Kazantsev, A. G.; Thompson, L. M. Therapeutic application of histone deacetylase inhibitors for central nervous system disorders. Nat. Rev. Drug. Discovery 2008, 7, 854-868.
    • (2008) Nat. Rev. Drug. Discovery , vol.7 , pp. 854-868
    • Kazantsev, A.G.1    Thompson, L.M.2
  • 18
    • 34248523169 scopus 로고    scopus 로고
    • Recovery of learning and memory is associated with chromatin remodelling
    • Fischer, A.; Sananbenesi, F.; Wang, X.; Dobbin, M.; Tsai, L. H. Recovery of learning and memory is associated with chromatin remodelling. Nature 2007, 447, 178-182.
    • (2007) Nature , vol.447 , pp. 178-182
    • Fischer, A.1    Sananbenesi, F.2    Wang, X.3    Dobbin, M.4    Tsai, L.H.5
  • 20
    • 33645357786 scopus 로고    scopus 로고
    • Sustained hippocampal chromatin regulation in a mouse model of depression and antidepressant action
    • Tsankova, N. M.; Berton, O.; Renthal, W.; Kumar, A.; Neve, R. L.; Nestler, E. J. Sustained hippocampal chromatin regulation in a mouse model of depression and antidepressant action. Nat. Neurosci. 2006, 9, 519-525.
    • (2006) Nat. Neurosci. , vol.9 , pp. 519-525
    • Tsankova, N.M.1    Berton, O.2    Renthal, W.3    Kumar, A.4    Neve, R.L.5    Nestler, E.J.6
  • 26
    • 0036161439 scopus 로고    scopus 로고
    • Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR
    • DOI 10.1016/S1097-2765(01)00429-4
    • Fischle, W.; Dequiedt, F.; Hendzel, M. J.; Guenther, M. G.; Lazar, M. A.; Voelter, W.; Verdin, E. Enzymatic activity associated with class IIHDACsis dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR. Mol. Cell 2002, 9, 45-57. (Pubitemid 34127770)
    • (2002) Molecular Cell , vol.9 , Issue.1 , pp. 45-57
    • Fischle, W.1    Dequiedt, F.2    Hendzel, M.J.3    Guenther, M.G.4    Lazar, M.A.5    Voelter, W.6    Verdin, E.7
  • 30
    • 33746228132 scopus 로고    scopus 로고
    • Histone deacetylase 7 maintains vascular integrity by repressing matrix metalloproteinase 10
    • Chang, S.; Young, B. D.; Li, S.; Qi, X.; Richardson, J. A.; Olson, E. N. Histone deacetylase 7 maintains vascular integrity by repressing matrix metalloproteinase 10. Cell 2006, 126, 321-334.
    • (2006) Cell , vol.126 , pp. 321-334
    • Chang, S.1    Young, B.D.2    Li, S.3    Qi, X.4    Richardson, J.A.5    Olson, E.N.6
  • 32
    • 45549101405 scopus 로고    scopus 로고
    • Control of endothelial cell proliferation and migration by VEGF signaling to histone deacetylase 7
    • Wang, S.; Li, X.; Parra, M.; Verdin, E.; Bassel-Duby, R.; Olson, E. N. Control of endothelial cell proliferation and migration by VEGF signaling to histone deacetylase 7. Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 7738-7743.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 7738-7743
    • Wang, S.1    Li, X.2    Parra, M.3    Verdin, E.4    Bassel-Duby, R.5    Olson, E.N.6
  • 34
    • 39049135494 scopus 로고    scopus 로고
    • Structure and activity of largazole, a potent antiproliferative agent from the Floridian marine cyanobacterium Symploca sp
    • Taori, K.; Paul, V. J.; Luesch, H. Structure and activity of largazole, a potent antiproliferative agent from the Floridian marine cyanobacterium Symploca sp. J. Am. Chem. Soc. 2008, 130, 1806-1807.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 1806-1807
    • Taori, K.1    Paul, V.J.2    Luesch, H.3
  • 35
    • 46049100010 scopus 로고    scopus 로고
    • Total synthesis and molecular target of largazole, a histone deacetylase inhibitor
    • Ying, Y.; Taori, K.; Kim, H.; Hong, J.; Luesch, H. Total synthesis and molecular target of largazole, a histone deacetylase inhibitor. J. Am. Chem. Soc. 2008, 130, 8455-8459.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 8455-8459
    • Ying, Y.1    Taori, K.2    Kim, H.3    Hong, J.4    Luesch, H.5
  • 36
    • 52049119362 scopus 로고    scopus 로고
    • Synthesis and biological activity of largazole and derivatives
    • Seiser, T.; Kamena, F.; Cramer, N. Synthesis and biological activity of largazole and derivatives. Angew. Chem., Int. Ed. 2008, 47, 6483-6485.
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 6483-6485
    • Seiser, T.1    Kamena, F.2    Cramer, N.3
  • 37
    • 50249144006 scopus 로고    scopus 로고
    • Total synthesis and biological mode of action of largazole: A potent class I histone deacetylase inhibitor
    • Bowers, A.; West, N.; Taunton, J.; Schreiber, S. L.; Bradner, J. E.; Williams, R. M. Total synthesis and biological mode of action of largazole: a potent class I histone deacetylase inhibitor. J. Am. Chem. Soc. 2008, 130, 11219-11222.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11219-11222
    • Bowers, A.1    West, N.2    Taunton, J.3    Schreiber, S.L.4    Bradner, J.E.5    Williams, R.M.6
  • 38
    • 54049152858 scopus 로고    scopus 로고
    • A concise total synthesis of largazole, solution structure, and some preliminary structure-activity relationships
    • Nasveschuk, C. G.; Ungermannova, D.; Liu, X.; Phillips, A. J. A concise total synthesis of largazole, solution structure, and some preliminary structure-activity relationships. Org. Lett. 2008, 10, 3595-3598.
    • (2008) Org. Lett. , vol.10 , pp. 3595-3598
    • Nasveschuk, C.G.1    Ungermannova, D.2    Liu, X.3    Phillips, A.J.4
  • 39
    • 55949099039 scopus 로고    scopus 로고
    • Enantioselective total synthesis of (+)-largazole, a potent inhibitor of histone deacetylase
    • Ghosh, A. K.; Kulkarni, S. Enantioselective total synthesis of (+)-largazole, a potent inhibitor of histone deacetylase. Org. Lett. 2008, 10, 3907-3909.
    • (2008) Org. Lett. , vol.10 , pp. 3907-3909
    • Ghosh, A.K.1    Kulkarni, S.2
  • 40
    • 0027378351 scopus 로고
    • Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase
    • Kijima, M.; Yoshida, M.; Sugita, K.; Horinouchi, S.; Beppu, T. Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase. J. Biol. Chem. 1993, 268, 22429-22435.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22429-22435
    • Kijima, M.1    Yoshida, M.2    Sugita, K.3    Horinouchi, S.4    Beppu, T.5
  • 41
    • 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 1996, 272, 408-411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 43
    • 0023065338 scopus 로고
    • Analogues of the cytostatic and antimitogenic agents chlamydocin and HC-toxin: Synthesis and biological activity of chloromethyl ketone and diazomethyl ketone functionalized cyclic tetrapeptides
    • Shute, R. E.; Dunlap, B.; Rich, D. H. Analogues of the cytostatic and antimitogenic agents chlamydocin and HC-toxin: synthesis and biological activity of chloromethyl ketone and diazomethyl ketone functionalized cyclic tetrapeptides. J. Med. Chem. 1987, 30, 71-78.
    • (1987) J. Med. Chem. , vol.30 , pp. 71-78
    • Shute, R.E.1    Dunlap, B.2    Rich, D.H.3
  • 46
    • 33745314784 scopus 로고    scopus 로고
    • Solution, solid phase and computational structures of apicidin and its backbone-reduced analogs
    • Kranz, M.; Murray, P. J.; Taylor, S.; Upton, R. J.; Clegg, W.; Elsegood, M. R. Solution, solid phase and computational structures of apicidin and its backbone-reduced analogs. J. Pept. Sci. 2006, 12, 383-388.
    • (2006) J. Pept. Sci. , vol.12 , pp. 383-388
    • Kranz, M.1    Murray, P.J.2    Taylor, S.3    Upton, R.J.4    Clegg, W.5    Elsegood, M.R.6
  • 50
    • 33947586979 scopus 로고    scopus 로고
    • Total synthesis of azumamide a and azumamide E, evaluation as histone deacetylase inhibitors, and design of a more potent analogue
    • Wen, S.; Carey, K. L.; Nakao, Y.; Fusetani, N.; Packham, G.; Ganesan, A. Total synthesis of azumamide A and azumamide E, evaluation as histone deacetylase inhibitors, and design of a more potent analogue. Org. Lett. 2007, 9, 1105-1108.
    • (2007) Org. Lett. , vol.9 , pp. 1105-1108
    • Wen, S.1    Carey, K.L.2    Nakao, Y.3    Fusetani, N.4    Packham, G.5    Ganesan, A.6
  • 51
    • 42949139951 scopus 로고    scopus 로고
    • Evaluation of antiangiogenic activity of azumamides by the in vitro vascular organization model using mouse induced pluripotent stem (iPS) cells
    • Nakao, Y.; Narazaki, G.; Hoshino, T.; Maeda, S.; Yoshida, M.; Maejima, H.; Yamashita, J. K. Evaluation of antiangiogenic activity of azumamides by the in vitro vascular organization model using mouse induced pluripotent stem (iPS) cells. Bioorg. Med. Chem. Lett. 2008, 18, 2982-2984.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 2982-2984
    • Nakao, Y.1    Narazaki, G.2    Hoshino, T.3    Maeda, S.4    Yoshida, M.5    Maejima, H.6    Yamashita, J.K.7
  • 52
    • 0035793107 scopus 로고    scopus 로고
    • Potent histone deacetylase inhibitors built from trichostatin a and cyclic tetrapeptide antibiotics including trapoxin
    • Furumai, R.; Komatsu, Y.; Nishino, N.; Khochbin, S.; Yoshida, M.; Horinouchi, S. Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin. Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 87-92.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 87-92
    • Furumai, R.1    Komatsu, Y.2    Nishino, N.3    Khochbin, S.4    Yoshida, M.5    Horinouchi, S.6
  • 56
    • 0029795991 scopus 로고    scopus 로고
    • Synthesis of natural and modified trapoxins, useful reagents for exploring histone deacetylase function
    • Taunton, J.; Collins, J. L.; Schreiber, S. L. Synthesis of natural and modified trapoxins, useful reagents for exploring histone deacetylase function. J. Am. Chem. Soc. 1996, 118, 10412-10422.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10412-10422
    • Taunton, J.1    Collins, J.L.2    Schreiber, S.L.3
  • 57
    • 0037034867 scopus 로고    scopus 로고
    • Solid-phase synthesis of apicidin A and a cyclic tetrapeptoid analogue
    • Berst, F.; Ladlow, M.; Holmes, A. B. Solid-phase synthesis of apicidin A and a cyclic tetrapeptoid analogue. Chem. Commun. 2002, 508-509.
    • (2002) Chem. Commun. , pp. 508-509
    • Berst, F.1    Ladlow, M.2    Holmes, A.B.3
  • 58
    • 35348816926 scopus 로고    scopus 로고
    • Molecular design of histone deacetylase inhibitors by aromatic ring shifting in chlamydocin framework
    • Shivashimpi, G. M.; Amagai, S.; Kato, T.; Nishino, N.; Maeda, S.; Nishino, T. G.; Yoshida, M. Molecular design of histone deacetylase inhibitors by aromatic ring shifting in chlamydocin framework. Bioorg. Med. Chem. 2007, 15, 7830-7839.
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 7830-7839
    • Shivashimpi, G.M.1    Amagai, S.2    Kato, T.3    Nishino, N.4    Maeda, S.5    Nishino, T.G.6    Yoshida, M.7
  • 60
    • 70349956393 scopus 로고    scopus 로고
    • Probing the bioactive conformation of an archetypal natural product HDAC inhibitor with conformationally homogeneous triazole-modified cyclic tetrapeptides
    • Horne, W. S.; Olsen, C. A.; Beierle, J. M.; Montero, A.; Ghadiri, M. R. Probing the bioactive conformation of an archetypal natural product HDAC inhibitor with conformationally homogeneous triazole-modified cyclic tetrapeptides. Angew. Chem., Int. Ed. 2009, 48, 4718-4724.
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 4718-4724
    • Horne, W.S.1    Olsen, C.A.2    Beierle, J.M.3    Montero, A.4    Ghadiri, M.R.5
  • 61
    • 55949094932 scopus 로고    scopus 로고
    • Synthesis and activity of largazole analogues with linker and macrocycle modification
    • Ying, Y.; Liu, Y.; Byeon, S. R.; Kim, H.; Luesch, H.; Hong, J. Synthesis and activity of largazole analogues with linker and macrocycle modification. Org. Lett. 2008, 10, 4021-4024.
    • (2008) Org. Lett. , vol.10 , pp. 4021-4024
    • Ying, Y.1    Liu, Y.2    Byeon, S.R.3    Kim, H.4    Luesch, H.5    Hong, J.6
  • 63
    • 64049106355 scopus 로고    scopus 로고
    • Synthesis and histone deacetylase inhibitory activity of largazole analogs: Alteration of the zinc-binding domain and macrocyclic scaffold
    • Bowers, A. A.; West, N.; Newkirk, T. L.; Troutman-Youngman, A. E.; Schreiber, S. L.; Wiest, O.; Bradner, J. E.; Williams, R. M. Synthesis and histone deacetylase inhibitory activity of largazole 7846 Journal of Medicinal Chemistry, 2009, Vol.52, No.23 Olsen and Ghadiri analogs: alteration of the zinc-binding domain and macrocyclic scaffold. Org. Lett. 2009, 11, 1301-1304.
    • (2009) Org. Lett. , vol.11 , pp. 1301-1304
    • Bowers, A.A.1    West, N.2    Newkirk, T.L.3    Troutman-Youngman, A.E.4    Schreiber, S.L.5    Wiest, O.6    Bradner, J.E.7    Williams, R.M.8
  • 64
    • 0034614056 scopus 로고    scopus 로고
    • Are beta-amino acids gamma-turn mimetics? Exploring a new design principle for bioactive cyclopeptides
    • Schumann, F.; Muller, A.; Koksch, M.; Muller, G.; Sewald, N. Are beta-amino acids gamma-turn mimetics? Exploring a new design principle for bioactive cyclopeptides. J. Am. Chem. Soc. 2000, 122, 12009-12010.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12009-12010
    • Schumann, F.1    Muller, A.2    Koksch, M.3    Muller, G.4    Sewald, N.5
  • 65
    • 0037460144 scopus 로고    scopus 로고
    • Conformationally homogeneous cyclic tetrapeptides: Useful new threedimensional scaffolds
    • Glenn, M. P.; Kelso, M. J.; Tyndall, J. D.; Fairlie, D. P. Conformationally homogeneous cyclic tetrapeptides: useful new threedimensional scaffolds. J. Am. Chem. Soc. 2003, 125, 640-641.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 640-641
    • Glenn, M.P.1    Kelso, M.J.2    Tyndall, J.D.3    Fairlie, D.P.4
  • 66
    • 33750430831 scopus 로고    scopus 로고
    • Beta2-amino acids in the design of conformationally homogeneous cyclo-peptide scaffolds
    • Norgren, A. S.; Buttner, F.; Prabpai, S.; Kongsaeree, P.; Arvidsson, P. I. Beta2-amino acids in the design of conformationally homogeneous cyclo-peptide scaffolds. J. Org. Chem. 2006, 71, 6814-6821.
    • (2006) J. Org. Chem. , vol.71 , pp. 6814-6821
    • Norgren, A.S.1    Buttner, F.2    Prabpai, S.3    Kongsaeree, P.4    Arvidsson, P.I.5
  • 67
    • 67749142082 scopus 로고    scopus 로고
    • Design, synthesis, biological evaluation, and structural characterization of potent histone deacetylase inhibitors based on cyclic alpha/betatetrapeptide architectures
    • Montero, A.; Beierle, J. M.; Olsen, C. A.; Ghadiri, M. R. Design, synthesis, biological evaluation, and structural characterization of potent histone deacetylase inhibitors based on cyclic alpha/betatetrapeptide architectures. J. Am. Chem. Soc. 2009, 131, 3033-3041.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 3033-3041
    • Montero, A.1    Beierle, J.M.2    Olsen, C.A.3    Ghadiri, M.R.4
  • 68
    • 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.; Knapp, R. J. A new type of synthetic peptide library for identifying ligand-binding activity. Nature 1991, 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
  • 73
    • 33845925314 scopus 로고    scopus 로고
    • Design, synthesis, potency, and cytoselectivity of anticancer agents derived by parallel synthesis from alpha-aminosuberic acid
    • Kahnberg, P.; Lucke, A. J.; Glenn, M. P.; Boyle, G. M.; Tyndall, J. D.; Parsons, P. G.; Fairlie, D. P. Design, synthesis, potency, and cytoselectivity of anticancer agents derived by parallel synthesis from alpha-aminosuberic acid. J. Med. Chem. 2006, 49, 7611-7622.
    • (2006) J. Med. Chem. , vol.49 , pp. 7611-7622
    • Kahnberg, P.1    Lucke, A.J.2    Glenn, M.P.3    Boyle, G.M.4    Tyndall, J.D.5    Parsons, P.G.6    Fairlie, D.P.7
  • 74
    • 0037864003 scopus 로고    scopus 로고
    • Automated mass spectrometric sequence determination of cyclic peptide library members
    • Redman, J. E.; Wilcoxen, K. M.; Ghadiri, M. R. Automated mass spectrometric sequence determination of cyclic peptide library members. J. Comb. Chem. 2003, 5, 33-40.
    • (2003) J. Comb. Chem. , vol.5 , pp. 33-40
    • Redman, J.E.1    Wilcoxen, K.M.2    Ghadiri, M.R.3
  • 75
    • 0038522853 scopus 로고    scopus 로고
    • Multidimensional chemical genetic analysis of diversity-oriented synthesis-derived deacetylase inhibitors using cell-based assays
    • Haggarty, S. J.; Koeller, K. M.; Wong, J. C.; Butcher, R. A.; Schreiber, S. L. Multidimensional chemical genetic analysis of diversity-oriented synthesis-derived deacetylase inhibitors using cell-based assays. Chem. Biol. 2003, 10, 383-396.
    • (2003) Chem. Biol. , vol.10 , pp. 383-396
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3    Butcher, R.A.4    Schreiber, S.L.5
  • 76
    • 0344640906 scopus 로고    scopus 로고
    • Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation
    • Haggarty, S. J.; Koeller, K. M.; Wong, J. C.; Grozinger, C. M.; Schreiber, S. L. Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation. Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 4389-4394.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 4389-4394
    • Haggarty, S.J.1    Koeller, K.M.2    Wong, J.C.3    Grozinger, C.M.4    Schreiber, S.L.5
  • 78
    • 33746894565 scopus 로고    scopus 로고
    • Highly potent and selective histone deacetylase 6 inhibitors designed based on a small-molecular substrate
    • Suzuki, T.; Kouketsu, A.; Itoh, Y.; Hisakawa, S.; Maeda, S.; Yoshida, M.; Nakagawa, H.; Miyata, N. Highly potent and selective histone deacetylase 6 inhibitors designed based on a small-molecular substrate. J. Med. Chem. 2006, 49, 4809-4812.
    • (2006) J. Med. Chem. , vol.49 , pp. 4809-4812
    • Suzuki, T.1    Kouketsu, A.2    Itoh, Y.3    Hisakawa, S.4    Maeda, S.5    Yoshida, M.6    Nakagawa, H.7    Miyata, N.8
  • 79
    • 35848945959 scopus 로고    scopus 로고
    • Design, synthesis, structureselectivity relationship, and effect on human cancer cells of a novel series of histone deacetylase 6-selective inhibitors
    • Itoh, Y.; Suzuki, T.; Kouketsu, A.; Suzuki,N.;Maeda, S.; Yoshida, M.; Nakagawa, H.; Miyata, N. Design, synthesis, structureselectivity relationship, and effect on human cancer cells of a novel series of histone deacetylase 6-selective inhibitors. J. Med. Chem. 2007, 50, 5425-5438.
    • (2007) J. Med. Chem. , vol.50 , pp. 5425-5438
    • Itoh, Y.1    Suzuki, T.2    Kouketsu, A.3    Suzuki, N.4    Maeda, S.5    Yoshida, M.6    Nakagawa, H.7    Miyata, N.8
  • 81
    • 72249097070 scopus 로고    scopus 로고
    • 50 = 343 nM), which further confirmed the HDAC8/HDAC6 selectivity for compound 23
    • 50 = 343 nM), which further confirmed the HDAC8/HDAC6 selectivity for compound 23.
  • 82
    • 49449113465 scopus 로고    scopus 로고
    • Use of the nitrile oxide cycloaddition (NOC) reaction for molecular probe generation: A new class of enzyme selective histone deacetylase inhibitors (HDACIs) showing picomolar activity at HDAC6
    • Kozikowski, A. P.; Tapadar, S.; Luchini, D. N.; Kim, K. H.; Billadeau, D. D. Use of the nitrile oxide cycloaddition (NOC) reaction for molecular probe generation: a new class of enzyme selective histone deacetylase inhibitors (HDACIs) showing picomolar activity at HDAC6. J. Med. Chem. 2008, 51, 4370-4373.
    • (2008) J. Med. Chem. , vol.51 , pp. 4370-4373
    • Kozikowski, A.P.1    Tapadar, S.2    Luchini, D.N.3    Kim, K.H.4    Billadeau, D.D.5
  • 83
    • 44949231404 scopus 로고    scopus 로고
    • The activity of HDAC8 depends on local and distal sequences of its peptide substrates
    • DOI 10.1021/bi800053v
    • Gurard-Levin, Z. A.; Mrksich, M. The activity ofHDAC8depends on local and distal sequences of its peptide substrates. Biochemistry 2008, 47, 6242-6250. (Pubitemid 351812837)
    • (2008) Biochemistry , vol.47 , Issue.23 , pp. 6242-6250
    • Gurard-Levin, Z.A.1    Mrksich, M.2
  • 84
    • 58149089923 scopus 로고    scopus 로고
    • Pimelic diphenylamide 106 is a slow, tight-binding inhibitor of class I histone deacetylases
    • Chou, C. J.; Herman, D.; Gottesfeld, J. M. Pimelic diphenylamide 106 is a slow, tight-binding inhibitor of class I histone deacetylases. J. Biol. Chem. 2008, 283, 35402-35409.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35402-35409
    • Chou, C.J.1    Herman, D.2    Gottesfeld, J.M.3
  • 85
    • 0141849191 scopus 로고    scopus 로고
    • Improved fluorogenic histone deacetylase assay for high-throughput screening applications
    • Wegener, D.; Hildmann, C.; Riester, D.; Schwienhorst, A. Improved fluorogenic histone deacetylase assay for high-throughput screening applications. Anal. Biochem. 2003, 321, 202-208.
    • (2003) Anal. Biochem. , vol.321 , pp. 202-208
    • Wegener, D.1    Hildmann, C.2    Riester, D.3    Schwienhorst, A.4
  • 86
    • 33846649707 scopus 로고    scopus 로고
    • Activity-based probes for proteomic profiling of histone deacetylase complexes
    • Salisbury, C. M.; Cravatt, B. F. Activity-based probes for proteomic profiling of histone deacetylase complexes. Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 1171-1176.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 1171-1176
    • Salisbury, C.M.1    Cravatt, B.F.2
  • 87
    • 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. 2008, 130, 2184-2194.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2184-2194
    • Salisbury, C.M.1    Cravatt, B.F.2
  • 88
    • 0000577984 scopus 로고    scopus 로고
    • The "One-bead-one - Compound" combinatorial library method
    • Lam, K. S.; Lebl, M.; Krchnak, V. The "One-bead-one - compound" combinatorial library method. Chem. Rev. 1997, 97, 411-448.
    • (1997) Chem. Rev. , vol.97 , pp. 411-448
    • Lam, K.S.1    Lebl, M.2    Krchnak, V.3
  • 91
    • 34250313965 scopus 로고    scopus 로고
    • A combinatorial approach to the discovery of biocidal sixresidue cyclic D,L-alpha-peptides against the bacteria methicillinresistant Staphylococcus aureus (MRSA) and E. coli and the biofouling algae Ulva linza and Navicula perminuta
    • Fletcher, J. T.; Finlay, J. A.; Callow, M. E.; Callow, J. A.; Ghadiri, M. R. A combinatorial approach to the discovery of biocidal sixresidue cyclic D,L-alpha-peptides against the bacteria methicillinresistant Staphylococcus aureus (MRSA) and E. coli and the biofouling algae Ulva linza and Navicula perminuta. Chem. - Eur. J. 2007, 13, 4008-4013.
    • (2007) Chem. - Eur. J. , vol.13 , pp. 4008-4013
    • Fletcher, J.T.1    Finlay, J.A.2    Callow, M.E.3    Callow, J.A.4    Ghadiri, M.R.5


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