| + |
PRKACA | down-regulates 
phosphorylation
|
HDAC8 |
0.47 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120643 |
Ser39 |
AKIPKRAsMVHSLIE |
Homo sapiens |
|
| pmid |
sentence |
| 14701748 |
Negative regulation of histone deacetylase 8 activity by cyclic amp-dependent protein kinase athe pka phosphoacceptor site of hdac8 is ser(39) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
romidepsin | down-regulates activity
chemical inhibition
|
HDAC8 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257994 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
N-[4-[(hydroxyamino)-oxomethyl]phenyl]carbamic acid [6-(diethylaminomethyl)-2-naphthalenyl]methyl ester | down-regulates activity
chemical inhibition
|
HDAC8 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257972 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
N-hydroxy-3-[4-[[2-hydroxyethyl-[2-(1H-indol-3-yl)ethyl]amino]methyl]phenyl]-2-propenamide | down-regulates activity
chemical inhibition
|
HDAC8 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257985 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257928 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
(S)-N-Hydroxy-4-(3-methyl-2-phenylbutanamido)benzamide | down-regulates activity
chemical inhibition
|
HDAC8 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262248 |
|
|
Homo sapiens |
Esophageal Squamous Cell Carcinoma Cell Line |
| pmid |
sentence |
| 31908417 |
The present study aimed to detect HDAC1 expression in and around ESCC tissues and comprehensively assess the anti-ESCC effects of AR-42, a phenylbutyrate-derived pan-HDAC inhibitor with low nanomolar IC50s against HDACs including HDAC1. AR-42 developed by Chen et al is an orally bioavailable hydroxamate-tethered phenylbutyrate derivative with strong inhibitory activity against class I (HDAC 1, 2, 3 and 8) and class IIb (HDAC 6 and 10) HDACs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
belinostat | down-regulates activity
chemical inhibition
|
HDAC8 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257744 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257958 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
panobinostat | down-regulates activity
chemical inhibition
|
HDAC8 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257753 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
HDAC8 | up-regulates quantity by stabilization 
binding
|
SMG5 |
0.627 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272650 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16809764 |
Here, we report that the human ortholog of the yeast ever-shorter telomeres 1B (EST1B) binds HDAC8. This interaction is regulated by protein kinase A-mediated HDAC8 phosphorylation and protects human EST1B (hEST1B) from ubiquitin-mediated degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CUDC-101 | down-regulates activity
chemical inhibition
|
HDAC8 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262264 |
|
|
in vitro |
|
| pmid |
sentence |
| 20143778 |
By incorporating histone deacetylase (HDAC) inhibitory functionality into the pharmacophore of the epidermal growth factor receptor (EGFR) and human epidermal growth factor receptor 2 (HER2) inhibitors, we synthesized a novel series of compounds with potent, multiacting HDAC, EGFR, and HER2 inhibition and identified 7-(4-(3-ethynylphenylamino)-7-methoxyquinazolin-6-yloxy)-N-hydroxyheptanamide 8 (CUDC-101) as a drug candidate, which is now in clinical development. 8 displays potent in vitro inhibitory activity against HDAC, EGFR, and HER2 with an IC(50) of 4.4, 2.4, and 15.7 nM, respectively. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
vorinostat | down-regulates activity
chemical inhibition
|
HDAC8 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257920 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
trichostatin A | down-regulates activity
chemical inhibition
|
HDAC8 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258013 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257939 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
4-(4-chloro-2-methylphenoxy)-N-hydroxybutanamide | down-regulates
chemical inhibition
|
HDAC8 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191436 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
6-(1,3-dioxo-2-benzo[de]isoquinolinyl)-N-hydroxyhexanamide | down-regulates activity
chemical inhibition
|
HDAC8 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258001 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
JWOGUUIOCYMBPV-GMFLJSBRSA-N | down-regulates activity
chemical inhibition
|
HDAC8 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257976 |
|
|
in vitro |
|
| pmid |
sentence |
| 20139990 |
Collaboratively, we synthesized and assembled a panel of structurally-diverse small-molecule HDACi 1, 2, 7-20 that comprise most of the relevant literature-reported tool compounds and pharmaceutically developed clinical candidates (Supplementary Fig 3). We next conducted a high-throughput, precise profiling of HDACi potency against all Class I and II enzymes, in a miniaturized dose-ranging format (Supplementary Table 1). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257915 |
|
|
in vitro |
|
| pmid |
sentence |
| 17868033 |
Our findings suggest that hydroxamic acid-derived compounds such as TSA, NVP-LAQ824, panobinostat, ITF2357, vorinostat and belinostat act as potent pan-HDAC isoform inhibitors. A notable observation was the similarity between belinostat and vorinostat in the biochemical isoform assays; both compounds exhibit similar EC50 values in all but the HDAC8 assay. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
N-hydroxy-1-[(4-methoxyphenyl)methyl]-6-indolecarboxamide | down-regulates
chemical inhibition
|
HDAC8 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189684 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HDAC8 | down-regulates activity
deacetylation
|
TP53 |
0.468 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255738 |
|
|
Mus musculus |
32D Cell |
| pmid |
sentence |
| 26387755 |
HDAC8 mediates CM-induced deacetylation of p53.Collectively, these results indicate that although binding to p53 and HDAC8 occurs through distinct regions of the CM protein, simultaneous interaction with HDAC8 and p53 is required for aberrant deacetylation and inactivation of p53. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
HDAC8
- 
- 