+ |
JWOGUUIOCYMBPV-GMFLJSBRSA-N | down-regulates activity
chemical inhibition
|
HDAC2 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261127 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
17868033 |
Apicidin inhibited rhHDACs 2 and 3 in the nanomolar range. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-257979 |
|
|
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-257914 |
|
|
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: |
3 |
Organism: |
Homo Sapiens, In Vitro |
+ |
JWOGUUIOCYMBPV-GMFLJSBRSA-N | down-regulates activity
chemical inhibition
|
HDAC3 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261128 |
|
|
Homo sapiens |
|
pmid |
sentence |
17868033 |
Apicidin inhibited rhHDACs 2 and 3 in the nanomolar range. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-257913 |
|
|
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-257978 |
|
|
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: |
3 |
Organism: |
Homo Sapiens, 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 |
+ |
JWOGUUIOCYMBPV-GMFLJSBRSA-N | down-regulates activity
chemical inhibition
|
HDAC1 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-257977 |
|
|
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 |