메뉴 건너뛰기




Volumn 14, Issue 19-20, 2009, Pages 942-948

Histone acetyl transferases as emerging drug targets

Author keywords

[No Author keywords available]

Indexed keywords

5 CHLOROISOTHIAZOLONE; ALPHA METHYLENE BUTYROLACTONE DERIVATIVE; ANACARDIC ACID; CURCUMIN; GARCINOL; HISTONE; HISTONE ACETYLTRANSFERASE; HISTONE ACETYLTRANSFERASE CBP; HISTONE ACETYLTRANSFERASE GCN5; HISTONE ACETYLTRANSFERASE INHIBITOR; HISTONE ACETYLTRANSFERASE P300; HISTONE ACETYLTRANSFERASE PCAF; ISOGARCINOL; ISOTHIAZOLONE; ISOTHIAZOLONE DERIVATIVE; LTK 14; TRANSFERASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 70349311616     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.drudis.2009.06.008     Document Type: Review
Times cited : (263)

References (65)
  • 1
    • 0035976787 scopus 로고    scopus 로고
    • Regulated assembly of transcription factors and control of transcription initiation
    • Beckett D. Regulated assembly of transcription factors and control of transcription initiation. J. Mol. Biol. 314 (2001) 335-352
    • (2001) J. Mol. Biol. , vol.314 , pp. 335-352
    • Beckett, D.1
  • 2
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. Chromatin modifications and their function. Cell 128 (2007) 693-705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 3
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., and Allis C.D. The language of covalent histone modifications. Nature 403 (2000) 41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 4
    • 34249337761 scopus 로고    scopus 로고
    • Perceptions of epigenetics
    • Bird A. Perceptions of epigenetics. Nature 447 (2007) 396-398
    • (2007) Nature , vol.447 , pp. 396-398
    • Bird, A.1
  • 5
    • 33947315736 scopus 로고    scopus 로고
    • Cancer epigenomics: DNA methylomes and histone-modification maps
    • Esteller M. Cancer epigenomics: DNA methylomes and histone-modification maps. Nat. Rev. Genet. 8 (2007) 286-298
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 286-298
    • Esteller, M.1
  • 6
    • 34547864553 scopus 로고    scopus 로고
    • Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global acetylation
    • Nagy Z., and Tora L. Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global acetylation. Oncogene 26 (2007) 5341-5357
    • (2007) Oncogene , vol.26 , pp. 5341-5357
    • Nagy, Z.1    Tora, L.2
  • 7
    • 0034707037 scopus 로고    scopus 로고
    • Global histone acetylation and deacetylation in yeast
    • Vogelauer M., et al. Global histone acetylation and deacetylation in yeast. Nature 408 (2000) 495-498
    • (2000) Nature , vol.408 , pp. 495-498
    • Vogelauer, M.1
  • 8
    • 21744457108 scopus 로고    scopus 로고
    • Global histone modification patterns predict risk of prostate cancer recurrence
    • Seligson D.B., et al. Global histone modification patterns predict risk of prostate cancer recurrence. Nature 435 (2005) 1262-1266
    • (2005) Nature , vol.435 , pp. 1262-1266
    • Seligson, D.B.1
  • 9
    • 55449096356 scopus 로고    scopus 로고
    • Crosstalk among histone modifications
    • Suganuma T., and Workman J.L. Crosstalk among histone modifications. Cell 135 (2008) 604-607
    • (2008) Cell , vol.135 , pp. 604-607
    • Suganuma, T.1    Workman, J.L.2
  • 10
    • 0033636595 scopus 로고    scopus 로고
    • Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation
    • Cheung P., et al. Synergistic coupling of histone H3 phosphorylation and acetylation in response to epidermal growth factor stimulation. Mol. Cell 5 (2000) 905-915
    • (2000) Mol. Cell , vol.5 , pp. 905-915
    • Cheung, P.1
  • 11
    • 42149189465 scopus 로고    scopus 로고
    • 14-3-3 interaction with histone H3 involves a dual modification pattern of phosphoacetylation
    • Walter W., et al. 14-3-3 interaction with histone H3 involves a dual modification pattern of phosphoacetylation. Mol. Cell. Biol. 28 (2008) 2840-2849
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 2840-2849
    • Walter, W.1
  • 12
    • 66149127693 scopus 로고    scopus 로고
    • The Gcn5 bromodomain of the SAGA complex facilitates cooperative and cross-tail acetylation of nucleosomes
    • Li S., and Shogren-Knaak M.A. The Gcn5 bromodomain of the SAGA complex facilitates cooperative and cross-tail acetylation of nucleosomes. J. Biol. Chem. 284 (2009) 9411-9417
    • (2009) J. Biol. Chem. , vol.284 , pp. 9411-9417
    • Li, S.1    Shogren-Knaak, M.A.2
  • 13
    • 0032948005 scopus 로고    scopus 로고
    • Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer
    • Cameron E.E., et al. Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer. Nat. Genet. 21 (1999) 103-107
    • (1999) Nat. Genet. , vol.21 , pp. 103-107
    • Cameron, E.E.1
  • 14
    • 34547911052 scopus 로고    scopus 로고
    • Chemistry of acetyl transfer by histone modifying enzymes: structure, mechanism and implications for effector design
    • Hodawadekar S.C., and Marmorstein R. Chemistry of acetyl transfer by histone modifying enzymes: structure, mechanism and implications for effector design. Oncogene 26 (2007) 5528-5540
    • (2007) Oncogene , vol.26 , pp. 5528-5540
    • Hodawadekar, S.C.1    Marmorstein, R.2
  • 15
    • 59449087016 scopus 로고    scopus 로고
    • Histone modifying enzymes: structures, mechanisms, and specificities
    • Marmorstein R., and Trievel R.C. Histone modifying enzymes: structures, mechanisms, and specificities. Biochim. Biophys. Acta 1789 (2009) 58-68
    • (2009) Biochim. Biophys. Acta , vol.1789 , pp. 58-68
    • Marmorstein, R.1    Trievel, R.C.2
  • 16
    • 0033556404 scopus 로고    scopus 로고
    • Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates
    • Schiltz R.L., et al. Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates. J. Biol. Chem. 274 (1999) 1189-1192
    • (1999) J. Biol. Chem. , vol.274 , pp. 1189-1192
    • Schiltz, R.L.1
  • 17
    • 34547896549 scopus 로고    scopus 로고
    • The MYST family of histone acetyltransferases and their intimate links to cancer
    • Avvakumov N., and Cote J. The MYST family of histone acetyltransferases and their intimate links to cancer. Oncogene 26 (2007) 5395-5407
    • (2007) Oncogene , vol.26 , pp. 5395-5407
    • Avvakumov, N.1    Cote, J.2
  • 18
    • 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 (2005) 212-226
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 212-226
    • Vetting, M.W.1
  • 19
    • 0034104047 scopus 로고    scopus 로고
    • Mutations truncating the EP300 acetylase in human cancers
    • Gayther S.A., et al. Mutations truncating the EP300 acetylase in human cancers. Nat. Genet. 24 (2000) 300-303
    • (2000) Nat. Genet. , vol.24 , pp. 300-303
    • Gayther, S.A.1
  • 20
    • 0036829085 scopus 로고    scopus 로고
    • Down-regulation of p300/CBP histone acetyltransferase activates a senescence checkpoint in human melanocytes
    • Bandyopadhyay D., et al. Down-regulation of p300/CBP histone acetyltransferase activates a senescence checkpoint in human melanocytes. Cancer Res. 62 (2002) 6231-6239
    • (2002) Cancer Res. , vol.62 , pp. 6231-6239
    • Bandyopadhyay, D.1
  • 21
    • 0034636450 scopus 로고    scopus 로고
    • CBP/p300 histone acetyl-transferase activity is important for the G1/S transition
    • Ait-Si-Ali S., et al. CBP/p300 histone acetyl-transferase activity is important for the G1/S transition. Oncogene 19 (2000) 2430-2437
    • (2000) Oncogene , vol.19 , pp. 2430-2437
    • Ait-Si-Ali, S.1
  • 22
    • 33846083491 scopus 로고    scopus 로고
    • p300 is required for orderly G1/S transition in human cancer cells
    • Iyer N.G., et al. p300 is required for orderly G1/S transition in human cancer cells. Oncogene 26 (2007) 21-29
    • (2007) Oncogene , vol.26 , pp. 21-29
    • Iyer, N.G.1
  • 23
    • 0035142070 scopus 로고    scopus 로고
    • Fusion of MOZ and p300 histone acetyltransferases in acute monocytic leukemia with a t(8;22)(p11;q13) chromosome translocation
    • Kitabayashi I., et al. Fusion of MOZ and p300 histone acetyltransferases in acute monocytic leukemia with a t(8;22)(p11;q13) chromosome translocation. Leukemia 15 (2001) 89-94
    • (2001) Leukemia , vol.15 , pp. 89-94
    • Kitabayashi, I.1
  • 24
    • 49749104565 scopus 로고    scopus 로고
    • Roles of the histone acetyltransferase monocytic leukemia zinc finger protein in normal and malignant hematopoiesis
    • Katsumoto T., et al. Roles of the histone acetyltransferase monocytic leukemia zinc finger protein in normal and malignant hematopoiesis. Cancer Sci. 99 (2008) 1523-1527
    • (2008) Cancer Sci. , vol.99 , pp. 1523-1527
    • Katsumoto, T.1
  • 25
    • 0035577668 scopus 로고    scopus 로고
    • Histone H3 specific acetyltransferases are essential for cell cycle progression
    • Howe L., et al. Histone H3 specific acetyltransferases are essential for cell cycle progression. Genes Dev. 15 (2001) 3144-3154
    • (2001) Genes Dev. , vol.15 , pp. 3144-3154
    • Howe, L.1
  • 26
    • 36849024085 scopus 로고    scopus 로고
    • Epigenetic regulation of airway inflammation
    • Adcock I.M., et al. Epigenetic regulation of airway inflammation. Curr. Opin. Immunol. 19 (2007) 694-700
    • (2007) Curr. Opin. Immunol. , vol.19 , pp. 694-700
    • Adcock, I.M.1
  • 27
    • 14744285888 scopus 로고    scopus 로고
    • Histone acetylation and deacetylation: importance in inflammatory lung diseases
    • Barnes P.J., et al. Histone acetylation and deacetylation: importance in inflammatory lung diseases. Eur. Respir. J. 25 (2005) 552-563
    • (2005) Eur. Respir. J. , vol.25 , pp. 552-563
    • Barnes, P.J.1
  • 28
    • 0036683630 scopus 로고    scopus 로고
    • Expression and activity of histone deacetylases in human asthmatic airways
    • Ito K., et al. Expression and activity of histone deacetylases in human asthmatic airways. Am. J. Respir. Crit. Care Med. 166 (2002) 392-396
    • (2002) Am. J. Respir. Crit. Care Med. , vol.166 , pp. 392-396
    • Ito, K.1
  • 29
    • 3142676314 scopus 로고    scopus 로고
    • Histone acetylase and deacetylase activity in alveolar macrophages and blood monocytes in asthma
    • Cosío B.G., et al. Histone acetylase and deacetylase activity in alveolar macrophages and blood monocytes in asthma. Am. J. Respir. Crit. Care Med. 170 (2004) 141-147
    • (2004) Am. J. Respir. Crit. Care Med. , vol.170 , pp. 141-147
    • Cosío, B.G.1
  • 30
    • 51549118740 scopus 로고    scopus 로고
    • PKCbetaII augments NF-kappaB-dependent transcription at the CCL11 promoter via p300/CBP-associated factor recruitment and histone H4 acetylation
    • Clarke D.L., et al. PKCbetaII augments NF-kappaB-dependent transcription at the CCL11 promoter via p300/CBP-associated factor recruitment and histone H4 acetylation. J. Immunol. 181 (2008) 3503-3514
    • (2008) J. Immunol. , vol.181 , pp. 3503-3514
    • Clarke, D.L.1
  • 31
    • 47549109984 scopus 로고    scopus 로고
    • Beyond transcription factors: the role of chromatin modifying enzymes in regulating transcription required for memory
    • Barrett R.M., and Wood M.A. Beyond transcription factors: the role of chromatin modifying enzymes in regulating transcription required for memory. Learn. Mem. 15 (2008) 460-467
    • (2008) Learn. Mem. , vol.15 , pp. 460-467
    • Barrett, R.M.1    Wood, M.A.2
  • 32
    • 43649104766 scopus 로고    scopus 로고
    • Altered memory capacities and response to stress in p300/CBP-associated factor (PCAF) histone acetylase knockout mice
    • Maurice T., et al. Altered memory capacities and response to stress in p300/CBP-associated factor (PCAF) histone acetylase knockout mice. Neurophychopharmacology 33 (2008) 1584-1602
    • (2008) Neurophychopharmacology , vol.33 , pp. 1584-1602
    • Maurice, T.1
  • 33
    • 27144463461 scopus 로고    scopus 로고
    • Acetylation of HIV-1 integrase by p300 regulates viral integration
    • Cereseto A., et al. Acetylation of HIV-1 integrase by p300 regulates viral integration. EMBO J. 24 (2005) 3070-3081
    • (2005) EMBO J. , vol.24 , pp. 3070-3081
    • Cereseto, A.1
  • 34
    • 33747162419 scopus 로고    scopus 로고
    • The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention
    • Stevens M., et al. The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention. Med. Res. Rev. 26 (2006) 595-625
    • (2006) Med. Res. Rev. , vol.26 , pp. 595-625
    • Stevens, M.1
  • 35
    • 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 (2007) 645-657
    • (2007) Chem. Biol. , vol.14 , pp. 645-657
    • Mantelingu, K.1
  • 36
    • 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 (2000) 589-595
    • (2000) Mol. Cell , vol.5 , pp. 589-595
    • Lau, O.D.1
  • 37
    • 2542421889 scopus 로고    scopus 로고
    • Bisubstrate analogue structure-activity relationships for p300 histone acetyltransferase inhibitors
    • Sagar V., et al. Bisubstrate analogue structure-activity relationships for p300 histone acetyltransferase inhibitors. Bioorg. Med. Chem. 12 (2004) 3383-3390
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 3383-3390
    • Sagar, V.1
  • 38
    • 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 (2005) 17182-17183
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17182-17183
    • Zheng, Y.1
  • 39
    • 0037195124 scopus 로고    scopus 로고
    • Structure of the GCN5 histone acetyltransferase bound to a bisubstrate inhibitor
    • Poux A.N., et al. Structure of the GCN5 histone acetyltransferase bound to a bisubstrate inhibitor. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 14065-14070
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 14065-14070
    • Poux, A.N.1
  • 40
    • 10944243759 scopus 로고    scopus 로고
    • Curcumin, a novel p300/CREB-binding protein-specific inhibitor of acetyltransferase, represses the acetylation of histone/nonhistone proteins and histone acetyltransferase-dependent chromatin transcription
    • Balasubramanyam K., et al. Curcumin, a novel p300/CREB-binding protein-specific inhibitor of acetyltransferase, represses the acetylation of histone/nonhistone proteins and histone acetyltransferase-dependent chromatin transcription. J. Biol. Chem. 279 (2004) 51163-51171
    • (2004) J. Biol. Chem. , vol.279 , pp. 51163-51171
    • Balasubramanyam, K.1
  • 41
    • 34247281570 scopus 로고    scopus 로고
    • Cinnamoyl compounds as simple molecules that inhibit p300 histone acetyltransferase
    • Costi R., et al. Cinnamoyl compounds as simple molecules that inhibit p300 histone acetyltransferase. J. Med. Chem. 50 (2007) 1973-1977
    • (2007) J. Med. Chem. , vol.50 , pp. 1973-1977
    • Costi, R.1
  • 42
    • 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 (2008) 868-878
    • (2008) J. Clin. Invest. , vol.118 , pp. 868-878
    • Morimoto, T.1
  • 43
    • 4043146501 scopus 로고    scopus 로고
    • Polyisoprenylated benzophenone, garcinol, a natural histone acetyltransferase inhibitor, represses chromatin transcription and alters global gene expression
    • Balasubramanyam K., et al. Polyisoprenylated benzophenone, garcinol, a natural histone acetyltransferase inhibitor, represses chromatin transcription and alters global gene expression. J. Biol. Chem. 279 (2004) 33716-33726
    • (2004) J. Biol. Chem. , vol.279 , pp. 33716-33726
    • Balasubramanyam, K.1
  • 44
    • 60549106446 scopus 로고    scopus 로고
    • Mechanism of p300 specific histone acetyltransferase inhibition by small molecules
    • Arif M., et al. Mechanism of p300 specific histone acetyltransferase inhibition by small molecules. J. Med. Chem. 52 (2009) 267-277
    • (2009) J. Med. Chem. , vol.52 , pp. 267-277
    • Arif, M.1
  • 45
    • 0037805679 scopus 로고    scopus 로고
    • Small molecule modulators of histone acetyltransferase p300
    • Balasubramanyam K., et al. Small molecule modulators of histone acetyltransferase p300. J. Biol. Chem. 278 (2003) 19134-19140
    • (2003) J. Biol. Chem. , vol.278 , pp. 19134-19140
    • Balasubramanyam, K.1
  • 46
    • 54849423666 scopus 로고    scopus 로고
    • Synthesis of benzamides related to anacardic acid and their histone acetyltransferase HAT inhibitory activities
    • Souto J.A., et al. Synthesis of benzamides related to anacardic acid and their histone acetyltransferase HAT inhibitory activities. ChemMedChem 3 (2008) 1435-1442
    • (2008) ChemMedChem , vol.3 , pp. 1435-1442
    • Souto, J.A.1
  • 47
    • 42949089945 scopus 로고    scopus 로고
    • Identification of long alkylidenemalonates as novel small molecule modulators of histone acetyltransferases
    • Sbardella G., et al. Identification of long alkylidenemalonates as novel small molecule modulators of histone acetyltransferases. Bioorg. Med. Chem. Lett. 18 (2008) 2788-2792
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 2788-2792
    • Sbardella, G.1
  • 48
    • 46749127067 scopus 로고    scopus 로고
    • Anacardic acid (6-nonadecyl salicylic acid), an inhibitor of histone acetyltransferase, suppresses expression of nuclear factor-kappaB-regulated gene products involved in cell survival, proliferation, invasion, and inflammation through inhibition of the inhibitory subunit of nuclear factor-kappaBalpha kinase, leading to potentiation of apoptosis
    • Sung B., et al. Anacardic acid (6-nonadecyl salicylic acid), an inhibitor of histone acetyltransferase, suppresses expression of nuclear factor-kappaB-regulated gene products involved in cell survival, proliferation, invasion, and inflammation through inhibition of the inhibitory subunit of nuclear factor-kappaBalpha kinase, leading to potentiation of apoptosis. Blood 111 (2008) 4880-4891
    • (2008) Blood , vol.111 , pp. 4880-4891
    • Sung, B.1
  • 49
    • 4544318283 scopus 로고    scopus 로고
    • Design, synthesis and biological evaluation of a small-molecule inhibitor of the histone acetyltransferase Gcn5
    • Biel M., et al. Design, synthesis and biological evaluation of a small-molecule inhibitor of the histone acetyltransferase Gcn5. Angew. Chem. Int. Ed. 43 (2004) 3974-3976
    • (2004) Angew. Chem. Int. Ed. , vol.43 , pp. 3974-3976
    • Biel, M.1
  • 50
    • 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 (2005) 1521-1532
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 1521-1532
    • Stimson, L.1
  • 51
    • 0142184439 scopus 로고    scopus 로고
    • Isothiazoles. Part 14: new 3-aminosubstituted isothiazole dioxides and their mono- and dihalogeno derivatives
    • Clerici F., et al. Isothiazoles. Part 14: new 3-aminosubstituted isothiazole dioxides and their mono- and dihalogeno derivatives. Tetrahedron 59 (2003) 9399-9408
    • (2003) Tetrahedron , vol.59 , pp. 9399-9408
    • Clerici, F.1
  • 52
    • 58549087523 scopus 로고    scopus 로고
    • Inhibition of the PCAF histone acetyl transferase and cell proliferation by isothiazolones
    • Dekker F.J., et al. Inhibition of the PCAF histone acetyl transferase and cell proliferation by isothiazolones. Bioorg. Med. Chem. 17 (2009) 460-466
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 460-466
    • Dekker, F.J.1
  • 53
    • 58549083339 scopus 로고    scopus 로고
    • Synthesis of isothiazol-3-one derivatives as inhibitors of histone acetyltransferases (HATs)
    • Gorsuch S., et al. Synthesis of isothiazol-3-one derivatives as inhibitors of histone acetyltransferases (HATs). Bioorg. Med. Chem. 17 (2009) 467-474
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 467-474
    • Gorsuch, S.1
  • 54
    • 3242755097 scopus 로고    scopus 로고
    • Synthesis and antibacterial activity of 2-(4-substituted phenyl)-3(2H)-isothiazolones
    • Khalaj A., et al. Synthesis and antibacterial activity of 2-(4-substituted phenyl)-3(2H)-isothiazolones. Eur. J. Med. Chem. 39 (2004) 699-705
    • (2004) Eur. J. Med. Chem. , vol.39 , pp. 699-705
    • Khalaj, A.1
  • 55
    • 27744492467 scopus 로고    scopus 로고
    • Structure-activity relationships in 3-isothiazolones
    • Morley J.O., et al. Structure-activity relationships in 3-isothiazolones. Org. Biomol. Chem. 3 (2005) 3713-3719
    • (2005) Org. Biomol. Chem. , vol.3 , pp. 3713-3719
    • Morley, J.O.1
  • 56
    • 0033028448 scopus 로고    scopus 로고
    • Skin sensitization risk assessment: a comparative evaluation of 3 isothiazolinone biocides
    • Basketter D., et al. Skin sensitization risk assessment: a comparative evaluation of 3 isothiazolinone biocides. Contact Dermatitis 40 (1999) 150-154
    • (1999) Contact Dermatitis , vol.40 , pp. 150-154
    • Basketter, D.1
  • 57
    • 0037568064 scopus 로고    scopus 로고
    • Studies of chemical selectivity of haptens, reactivity, and skin sensitization potency. 3. Synthesis and studies on the reactivity towards model nucleophiles of the 13C labeled skin sensitizers, 5-chloro-2-methylisothiazol-3-one (MCI) and 2-methylisothiazol-3-one (MI)
    • Alvarez-Sánchez R., et al. Studies of chemical selectivity of haptens, reactivity, and skin sensitization potency. 3. Synthesis and studies on the reactivity towards model nucleophiles of the 13C labeled skin sensitizers, 5-chloro-2-methylisothiazol-3-one (MCI) and 2-methylisothiazol-3-one (MI). Chem. Res. Toxicol. 16 (2003) 627-638
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 627-638
    • Alvarez-Sánchez, R.1
  • 58
    • 34247191294 scopus 로고    scopus 로고
    • Kinetic studies on the reactions of 3-isothiazolones with 2-methyl-2-propanethiol
    • Morley J.O., et al. Kinetic studies on the reactions of 3-isothiazolones with 2-methyl-2-propanethiol. Int. J. Chem. Kinet. 39 (2006) 254-260
    • (2006) Int. J. Chem. Kinet. , vol.39 , pp. 254-260
    • Morley, J.O.1
  • 59
    • 20444409179 scopus 로고    scopus 로고
    • Protein structure similarity clustering (PSSC) and natural product structure as inspiration sources for drug development and chemical genomics
    • Dekker F.J., et al. Protein structure similarity clustering (PSSC) and natural product structure as inspiration sources for drug development and chemical genomics. Curr. Opin. Chem. Biol. 9 (2005) 232-239
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 232-239
    • Dekker, F.J.1
  • 60
    • 28944443244 scopus 로고    scopus 로고
    • Design of compound libraries based on natural product scaffolds and protein structure similarity clustering (PSSC)
    • Balamurugan R., et al. Design of compound libraries based on natural product scaffolds and protein structure similarity clustering (PSSC). Mol. Biosyst. 1 (2005) 36-45
    • (2005) Mol. Biosyst. , vol.1 , pp. 36-45
    • Balamurugan, R.1
  • 61
    • 0037424691 scopus 로고    scopus 로고
    • Amino propynyl benzoic acid building block in rigid spacers of divalent ligands binding to the Syk SH2 domains with equally high affinity as the natural ligand
    • Dekker F.J., et al. Amino propynyl benzoic acid building block in rigid spacers of divalent ligands binding to the Syk SH2 domains with equally high affinity as the natural ligand. Bioorg. Med. Chem. Lett. 13 (2003) 1241-1244
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 1241-1244
    • Dekker, F.J.1
  • 62
    • 0037333328 scopus 로고    scopus 로고
    • Role of solution conformation and flexibility of short peptide ligands that bind to the p56(lck) SH2 domain
    • Dekker F.J., et al. Role of solution conformation and flexibility of short peptide ligands that bind to the p56(lck) SH2 domain. Bioorg. Med. Chem. 11 (2003) 941-949
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 941-949
    • Dekker, F.J.1
  • 63
    • 0036523477 scopus 로고    scopus 로고
    • Replacement of the intervening amino acid sequence of a Syk-binding diphosphopeptide by a nonpeptide spacer with preservation of high affinity
    • Dekker F.J., et al. Replacement of the intervening amino acid sequence of a Syk-binding diphosphopeptide by a nonpeptide spacer with preservation of high affinity. Chembiochem 3 (2002) 238-242
    • (2002) Chembiochem , vol.3 , pp. 238-242
    • Dekker, F.J.1
  • 64
    • 0034698144 scopus 로고    scopus 로고
    • p300/CBP-associated factor histone acetyltransferase processing of a peptide substrate. Kinetic analysis of the catalytic mechanism
    • Lau O.D., et al. p300/CBP-associated factor histone acetyltransferase processing of a peptide substrate. Kinetic analysis of the catalytic mechanism. J. Biol. Chem. 275 (2000) 21953-22159
    • (2000) J. Biol. Chem. , vol.275 , pp. 21953-22159
    • Lau, O.D.1
  • 65
    • 0038692967 scopus 로고    scopus 로고
    • Synthesis and analysis of potential prodrugs of coenzyme A analogues for the inhibition of the histone acetyltransferase p300
    • Cebrat M., et al. Synthesis and analysis of potential prodrugs of coenzyme A analogues for the inhibition of the histone acetyltransferase p300. Bioorg. Med. Chem. 11 (2003) 3307-3313
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 3307-3313
    • Cebrat, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.