Histone Deacetylases
Springer New York
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Timeline
Mendeley readers
| Chapter title |
A Sensitive and Flexible Assay for Determining Histone Deacetylase 1 (HDAC1) Activity
|
|---|---|
| Chapter number | 1 |
| Book title |
Histone Deacetylases
|
| Published in |
Methods in molecular biology, January 2016
|
| DOI | 10.1007/978-1-4939-3667-0_1 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-3665-6, 978-1-4939-3667-0
|
| Authors |
Mei-Yi Wu, Ray-Chang Wu, Wu, Mei-Yi, Wu, Ray-Chang |
| Abstract |
Histones acetylation and deacetylation constitute part of the so-called "histone code" and work in concert with other posttranslational modifications to determine the activity of genes. Deacetylation of histone is carried out by a class of enzymes, known as histone deacetylases (HDACs). The action of HDAC is countered by histone acetyltransferases. Although histone is the best characterized substrate of HDACs, increasing evidence also indicates that non-histone proteins are equally important subtract of HDACs. Since HDACs play an important role in normal physiological and pathophysiological conditions, a sensitive and flexible deacetylation assay that can reliably detect HDAC activity and identify potential novel targets of HDACs is critical. |
Mendeley readers
The data shown below were compiled from readership statistics for 3 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 3 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 1 | 33% |
| Lecturer > Senior Lecturer | 1 | 33% |
| Unknown | 1 | 33% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 2 | 67% |
| Unknown | 1 | 33% |