Histone deacetylase 8 (HDAC8) and its inhibitors with selectivity to other isoforms : An overview
Copyright © 2018 Elsevier Masson SAS. All rights reserved..
The histone deacetylases (HDACs) enzymes provided crucial role in transcriptional regulation of cells through deacetylation of nuclear histone proteins. Discoveries related to the HDAC8 enzyme activity signified the importance of HDAC8 isoform in cell proliferation, tumorigenesis, cancer, neuronal disorders, parasitic/viral infections and other epigenetic regulations. The pan-HDAC inhibitors can confront these conditions but have chances to affect epigenetic functions of other HDAC isoforms. Designing of selective HDAC8 inhibitors is a key feature to combat the pathophysiological and diseased conditions involving the HDAC8 activity. This review is concerned about the structural and positional aspects of HDAC8 in the HDAC family. It also covers the contributions of HDAC8 in the pathophysiological conditions, a preliminary discussion about the recent scenario of HDAC8 inhibitors. This review might help to deliver the structural, functional and computational information in order to identify and design potent and selective HDAC8 inhibitors for target specific treatment of diseases involving HDAC8 enzymatic activity.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2019 |
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| Erschienen: |
2019 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:164 |
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| Enthalten in: |
European journal of medicinal chemistry - 164(2019) vom: 15. Feb., Seite 214-240 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Banerjee, Suvankar [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 26.03.2019 Date Revised 26.03.2019 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.ejmech.2018.12.039 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM292237715 |
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| 500 | |a Date Revised 26.03.2019 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2018 Elsevier Masson SAS. All rights reserved. | ||
| 520 | |a The histone deacetylases (HDACs) enzymes provided crucial role in transcriptional regulation of cells through deacetylation of nuclear histone proteins. Discoveries related to the HDAC8 enzyme activity signified the importance of HDAC8 isoform in cell proliferation, tumorigenesis, cancer, neuronal disorders, parasitic/viral infections and other epigenetic regulations. The pan-HDAC inhibitors can confront these conditions but have chances to affect epigenetic functions of other HDAC isoforms. Designing of selective HDAC8 inhibitors is a key feature to combat the pathophysiological and diseased conditions involving the HDAC8 activity. This review is concerned about the structural and positional aspects of HDAC8 in the HDAC family. It also covers the contributions of HDAC8 in the pathophysiological conditions, a preliminary discussion about the recent scenario of HDAC8 inhibitors. This review might help to deliver the structural, functional and computational information in order to identify and design potent and selective HDAC8 inhibitors for target specific treatment of diseases involving HDAC8 enzymatic activity | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Review | |
| 650 | 4 | |a Cancer | |
| 650 | 4 | |a HDAC8 | |
| 650 | 4 | |a HDAC8 inhibitor | |
| 650 | 4 | |a Histone deacetylase | |
| 650 | 4 | |a Quantitative structure-activity relationship (QSAR) | |
| 650 | 4 | |a Structure-activity relationship (SAR) | |
| 650 | 7 | |a Histone Deacetylase Inhibitors |2 NLM | |
| 650 | 7 | |a Protein Isoforms |2 NLM | |
| 650 | 7 | |a Repressor Proteins |2 NLM | |
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| 650 | 7 | |a Histone Deacetylases |2 NLM | |
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| 700 | 1 | |a Adhikari, Nilanjan |e verfasserin |4 aut | |
| 700 | 1 | |a Amin, Sk Abdul |e verfasserin |4 aut | |
| 700 | 1 | |a Jha, Tarun |e verfasserin |4 aut | |
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