(2-Amino-phenyl)-amides of ω-substituted alkanoic acids as new histone deacetylase inhibitors

Vaisburg, A. F.; Bernstein, Naomy; Fréchette, Sylvie; Allan, Martin; Abou-Khalil, Elie; Leit, Silvana; Moradei, Oscar; Bouchain, Giliane; Wang, Jinru; Woo, Soon Hyung; Fournel, Marielle; Yan, Pu; Trachy-Bourget, Marie-Claude; Kalita, Ann; Beaulieu, Carole; Li, Zuomei; MacLeod, A. Robert; Besterman, Jeffrey M.; Delorme, Daniel

doi:10.1016/j.bmcl.2003.08.083

Cited by 31 publications

(14 citation statements)

References 22 publications

(5 reference statements)

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“…On the basis of this series of CHAPs and 3, Nishino and co-workers designed a set of inhibitors containing a sulfhydryl group [57]. Another set of inhibitors like MS-275 (15) is characterized by a benzamide substructure ( Figure 5) [58,59,60,61]. It is yet unclear whether 15 and its analogues complex the zinc ion in the catalytic site of the enzyme similar to hydroxamate inhibitors.…”

Section: Hdac Inhibitorsmentioning

confidence: 98%

Chromatin Modifications as Targets for New Anticancer Drugs

Schäfer

Jung

2005

Archiv der Pharmazie

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Chromatin proteins undergo diverse posttranslational modifications, esp. acetylation and methylation, that contribute to the control of transcriptional processes. The result of these modifications in its various states is called the histone code. This review presents an overview of those modifications of chromatin proteins that affect the side chains of lysines and arginines and define variations of the chromatin acetylome and methylome. The relevant enzymes are presented and the feasibility to influence their activity by inhibition or activation is discussed. The manipulation of these enzymes is an exciting strategy towards an increased understanding of their role in the functionality of a cell. Additionally, this may lead to new approaches for the treatment of diseases that are based on a dysregulation of transcription, especially cancer.

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Section: Hdac Inhibitorsmentioning

confidence: 98%

Chromatin Modifications as Targets for New Anticancer Drugs

Schäfer

Jung

2005

Archiv der Pharmazie

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“…Until very recently, known non-hydroxamate HDAC inhibitors were small fatty acids such as sodium butyrate and valproic acid, and o-aminoanilides such as MS-275 ( Fig. 3) [25][26][27][28][29][30][31][32][33][34]. However, most of these are less potent than hydroxamates.…”

Section: Introductionmentioning

confidence: 99%

Rational Design of Non-Hydroxamate Histone Deacetylase Inhibitors

Suzuki¹,

Miyata

2006

MRMC

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“…A variety of ω-substituted alkanoic acid (2-aminophenyl)-amides such as GG and HH were designed and synthesised [102]. These compounds were shown to inhibit recombinant human histone deacetylases (HDACs) with IC 50 values in the low micromolar range and induce hyperacetylation of histones in whole cells.…”

Section: Ortho-amino Anilidesmentioning

confidence: 99%

Histone Deacetylase Inhibitors: Latest Developments, Trends and Prospects

Moradei¹,

Maroun²,

Paquin³

et al. 2005

CMCACA

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Histone deacetylases (HDACs) and histone acetyltransferases (HATs) are enzymes that catalyze the deacetylation and acetylation of lysine residues located in the NH(2) terminal tails of histones and non-histone proteins. Perturbation of this balance is often observed in human cancers and inhibition of HDACs has emerged as a novel therapeutic strategy against cancer. To date, more that 30 groups, academic and industrial, are involved in research related to these target enzymes. Over the past year, dozens of research papers and patent applications describing new HDAC inhibitors belonging to different structural classes have been disclosed. The present review highlights the latest developments in design and synthesis of HDAC inhibitors -- potential anti-cancer drugs.

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(2-Amino-phenyl)-amides of ω-substituted alkanoic acids as new histone deacetylase inhibitors

Cited by 31 publications

References 22 publications

Chromatin Modifications as Targets for New Anticancer Drugs

Chromatin Modifications as Targets for New Anticancer Drugs

Rational Design of Non-Hydroxamate Histone Deacetylase Inhibitors

Histone Deacetylase Inhibitors: Latest Developments, Trends and Prospects

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