| + |
PRKD1 |
phosphorylation
|
HDAC7 |
0.495 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249275 |
Ser155 |
FPLRKTVsEPNLKLR |
in vitro |
|
| pmid |
sentence |
| 15738054 |
We demonstrate that protein kinase D (PKD; also known as PKCmi), which is activated upon engagement of the TCR, stimulates HDAC7 nuclear export by direct phosphorylation on four serine residues. Conversely, selective PKD inhibition blocks TCR-induced HDAC7 nuclear export and Nur77 expression. In addition, an HDAC7 mutant specifically deficient in phosphorylation by PKD blocks TCR-mediated apoptosis. | PKD1 phosphorylates S155, S181, S321, and S449 of HDAC7 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249273 |
Ser181 |
NPLLRKEsAPPSLRR |
in vitro |
|
| pmid |
sentence |
| 15738054 |
We demonstrate that protein kinase D (PKD; also known as PKCmi), which is activated upon engagement of the TCR, stimulates HDAC7 nuclear export by direct phosphorylation on four serine residues. Conversely, selective PKD inhibition blocks TCR-induced HDAC7 nuclear export and Nur77 expression. In addition, an HDAC7 mutant specifically deficient in phosphorylation by PKD blocks TCR-mediated apoptosis. | PKD1 phosphorylates S155, S181, S321, and S449 of HDAC7 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249274 |
Ser358 |
WPLSRTRsEPLPPSA |
in vitro |
|
| pmid |
sentence |
| 15738054 |
We demonstrate that protein kinase D (PKD; also known as PKCmi), which is activated upon engagement of the TCR, stimulates HDAC7 nuclear export by direct phosphorylation on four serine residues. Conversely, selective PKD inhibition blocks TCR-induced HDAC7 nuclear export and Nur77 expression. In addition, an HDAC7 mutant specifically deficient in phosphorylation by PKD blocks TCR-mediated apoptosis. | PKD1 phosphorylates S155, S181, S321, and S449 of HDAC7 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249276 |
Ser486 |
RPLSRAQsSPAAPAS |
in vitro |
|
| pmid |
sentence |
| 15738054 |
We demonstrate that protein kinase D (PKD; also known as PKCmi), which is activated upon engagement of the TCR, stimulates HDAC7 nuclear export by direct phosphorylation on four serine residues. Conversely, selective PKD inhibition blocks TCR-induced HDAC7 nuclear export and Nur77 expression. In addition, an HDAC7 mutant specifically deficient in phosphorylation by PKD blocks TCR-mediated apoptosis. | PKD1 phosphorylates S155, S181, S321, and S449 of HDAC7 in vitro. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
PRKD3 | up-regulates activity 
phosphorylation
|
HDAC7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275932 |
Ser155 |
FPLRKTVsEPNLKLR |
|
|
| pmid |
sentence |
| 18692497 |
Histone deacetylase (HDAC) 5 and 7, two members of the class II of classical HDAC [62], are in vivo substrates of PKD3 and PKD [63]. In response to a variety of signals, including phorbol esters, T cell receptor engagement, vascular endothelial growth factor and angiotensin stimulation, the activity of HDAC5 and 7 are regulated by a mechanism that involves PKD3 and PKD-mediated phosphorylation of the highly conserved Ser259 and Ser498 residues that are located in N-terminus of class II HDACs [63–67]. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275934 |
Ser358 |
WPLSRTRsEPLPPSA |
|
|
| pmid |
sentence |
| 18692497 |
Histone deacetylase (HDAC) 5 and 7, two members of the class II of classical HDAC [62], are in vivo substrates of PKD3 and PKD [63]. In response to a variety of signals, including phorbol esters, T cell receptor engagement, vascular endothelial growth factor and angiotensin stimulation, the activity of HDAC5 and 7 are regulated by a mechanism that involves PKD3 and PKD-mediated phosphorylation of the highly conserved Ser259 and Ser498 residues that are located in N-terminus of class II HDACs [63–67]. |
|
| Publications: |
2 |
| + |
PRKD2 | up-regulates activity
phosphorylation
|
HDAC7 |
0.451 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275933 |
Ser155 |
FPLRKTVsEPNLKLR |
|
|
| pmid |
sentence |
| 18692497 |
Histone deacetylase (HDAC) 5 and 7, two members of the class II of classical HDAC [62], are in vivo substrates of PKD3 and PKD [63]. In response to a variety of signals, including phorbol esters, T cell receptor engagement, vascular endothelial growth factor and angiotensin stimulation, the activity of HDAC5 and 7 are regulated by a mechanism that involves PKD3 and PKD-mediated phosphorylation of the highly conserved Ser259 and Ser498 residues that are located in N-terminus of class II HDACs [63–67]. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275935 |
Ser358 |
WPLSRTRsEPLPPSA |
|
|
| pmid |
sentence |
| 18692497 |
Histone deacetylase (HDAC) 5 and 7, two members of the class II of classical HDAC [62], are in vivo substrates of PKD3 and PKD [63]. In response to a variety of signals, including phorbol esters, T cell receptor engagement, vascular endothelial growth factor and angiotensin stimulation, the activity of HDAC5 and 7 are regulated by a mechanism that involves PKD3 and PKD-mediated phosphorylation of the highly conserved Ser259 and Ser498 residues that are located in N-terminus of class II HDACs [63–67]. |
|
| Publications: |
2 |
| + |
MAP3K7 | down-regulates 
phosphorylation
|
HDAC7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149579 |
Ser155 |
FPLRKTVsEPNLKLR |
Homo sapiens |
|
| pmid |
sentence |
| 16980613 |
We further show that emk and c-tak1 phosphorylate class iia hdacs on one of their multiple 14-3-3 binding sites and alter their subcellular localization and repressive function |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CA | up-regulates activity
dephosphorylation
|
HDAC7 |
0.322 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248646 |
Ser155 |
FPLRKTVsEPNLKLR |
Homo sapiens |
|
| pmid |
sentence |
| 18339811 |
Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. |Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs.|we demonstrate that PP2A constitutively dephosphorylates the class IIa member HDAC7 to control its biological functions as a regulator of T cell apoptosis and endothelial cell functions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248647 |
Ser181 |
NPLLRKEsAPPSLRR |
Homo sapiens |
|
| pmid |
sentence |
| 18339811 |
Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. |Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs.|we demonstrate that PP2A constitutively dephosphorylates the class IIa member HDAC7 to control its biological functions as a regulator of T cell apoptosis and endothelial cell functions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248648 |
Ser358 |
WPLSRTRsEPLPPSA |
Homo sapiens |
|
| pmid |
sentence |
| 18339811 |
Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. |Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs.|we demonstrate that PP2A constitutively dephosphorylates the class IIa member HDAC7 to control its biological functions as a regulator of T cell apoptosis and endothelial cell functions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248649 |
Ser486 |
RPLSRAQsSPAAPAS |
Homo sapiens |
|
| pmid |
sentence |
| 18339811 |
Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. |Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs.|we demonstrate that PP2A constitutively dephosphorylates the class IIa member HDAC7 to control its biological functions as a regulator of T cell apoptosis and endothelial cell functions. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
MARK2 | down-regulates
phosphorylation
|
HDAC7 |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149583 |
Ser155 |
FPLRKTVsEPNLKLR |
Homo sapiens |
|
| pmid |
sentence |
| 16980613 |
We further show that emk and c-tak1 phosphorylate class iia hdacs on one of their multiple 14-3-3 binding sites and alter their subcellular localization and repressive function |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMPK | down-regulates
phosphorylation
|
HDAC7 |
0.281 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216554 |
Ser155 |
FPLRKTVsEPNLKLR |
Homo sapiens |
|
| pmid |
sentence |
| 21892142 |
Another recently described set of transcriptional regulators targeted by ampk and its related family members across a range of eukaryotes are the class iia family of histone deacetylases (hdacs). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216558 |
Ser358 |
WPLSRTRsEPLPPSA |
Homo sapiens |
|
| pmid |
sentence |
| 21892142 |
Another recently described set of transcriptional regulators targeted by ampk and its related family members across a range of eukaryotes are the class iia family of histone deacetylases (hdacs). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKAA1 | down-regulates
phosphorylation
|
HDAC7 |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176487 |
Ser155 |
FPLRKTVsEPNLKLR |
Homo sapiens |
|
| pmid |
sentence |
| 21892142 |
Another recently described set of transcriptional regulators targeted by ampk and its related family members across a range of eukaryotes are the class iia family of histone deacetylases (hdacs). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176491 |
Ser358 |
WPLSRTRsEPLPPSA |
Homo sapiens |
|
| pmid |
sentence |
| 21892142 |
Another recently described set of transcriptional regulators targeted by ampk and its related family members across a range of eukaryotes are the class iia family of histone deacetylases (hdacs). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | down-regulates
phosphorylation
|
HDAC7 |
0.495 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-132894 |
Ser155 |
FPLRKTVsEPNLKLR |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 15623513 |
Protein kinase d1 (pkd1) was activated after tcr engagement, interacted with hdac7, and phosphorylated three serines (ser155, ser318, and ser448) at its n terminus, leading to its export from the nucleus. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-132898 |
Ser358 |
WPLSRTRsEPLPPSA |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 15623513 |
Protein kinase d1 (pkd1) was activated after tcr engagement, interacted with hdac7, and phosphorylated three serines (ser155, ser318, and ser448) at its n terminus, leading to its export from the nucleus. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178713 |
Ser486 |
RPLSRAQsSPAAPAS |
Homo sapiens |
|
| pmid |
sentence |
| 18509061 |
We show for the first time that vegf stimulated phosphorylation of hdac7 at the sites of ser178, ser344, and ser479we found that phospholipase cgamma/protein kinase c/protein kinase d1 (pkd1)-dependent signal pathway mediated hdac7 phosphorylation and cytoplasmic accumulation by vegf. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-132902 |
Ser486 |
RPLSRAQsSPAAPAS |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 15623513 |
Protein kinase d1 (pkd1) was activated after tcr engagement, interacted with hdac7, and phosphorylated three serines (ser155, ser318, and ser448) at its n terminus, leading to its export from the nucleus. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179430 |
Ser486 |
RPLSRAQsSPAAPAS |
Homo sapiens |
|
| pmid |
sentence |
| 18617643 |
We show for the first time that vegf stimulated phosphorylation of hdac7 at the sites of ser178, ser344, and ser479we found that phospholipase cgamma/protein kinase c/protein kinase d1 (pkd1)-dependent signal pathway mediated hdac7 phosphorylation and cytoplasmic accumulation by vegf. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
PPP2CB | up-regulates activity
dephosphorylation
|
HDAC7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248603 |
Ser155 |
FPLRKTVsEPNLKLR |
Homo sapiens |
|
| pmid |
sentence |
| 18339811 |
Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. |Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248604 |
Ser181 |
NPLLRKEsAPPSLRR |
Homo sapiens |
|
| pmid |
sentence |
| 18339811 |
Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. |Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248605 |
Ser358 |
WPLSRTRsEPLPPSA |
Homo sapiens |
|
| pmid |
sentence |
| 18339811 |
Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. |Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248606 |
Ser486 |
RPLSRAQsSPAAPAS |
Homo sapiens |
|
| pmid |
sentence |
| 18339811 |
Phosphorylation of conserved serine residues triggers association with 14-3-3 proteins and cytoplasmic relocalization of class IIa HDACs, which leads to the derepression of their target genes. |Here we identify PP2A as a phosphatase responsible for dephosphorylating the 14-3-3 binding sites in class IIa HDACs. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
trichostatin A | down-regulates activity
chemical inhibition
|
HDAC7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257938 |
|
|
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-258014 |
|
|
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 |
| + |
N-[4-[(hydroxyamino)-oxomethyl]phenyl]carbamic acid [6-(diethylaminomethyl)-2-naphthalenyl]methyl ester | down-regulates activity
chemical inhibition
|
HDAC7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257964 |
|
|
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-257907 |
|
|
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 |
| + |
HDAC7 | down-regulates
deacetylation
|
PLAG1 |
0.258 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140950 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16207715 |
Plag1 and plagl2 are also regulated by acetylation. They are acetylated and activated by p300 and deacetylated and repressed by hdac7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
6-(1,3-dioxo-2-benzo[de]isoquinolinyl)-N-hydroxyhexanamide | down-regulates activity
chemical inhibition
|
HDAC7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258004 |
|
|
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 |
| + |
HDAC7 | down-regulates
deacetylation
|
PLAGL2 |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140953 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16207715 |
Plag1 and plagl2 are also regulated by acetylation. They are acetylated and activated by p300 and deacetylated and repressed by hdac7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
belinostat | down-regulates activity
chemical inhibition
|
HDAC7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257741 |
|
|
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-257954 |
|
|
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 |
| + |
romidepsin | down-regulates activity
chemical inhibition
|
HDAC7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257992 |
|
|
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
|
HDAC7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257927 |
|
|
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-257980 |
|
|
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 |
| + |
BCORL1 | up-regulates activity
binding
|
HDAC7 |
0.499 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259114 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17379597 |
BCoR-L1 interacts with Class II HDACs, HDAC4, HDAC5, and HDAC7, suggesting that they are involved in its function as transcriptional corepressor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
vorinostat | down-regulates activity
chemical inhibition
|
HDAC7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257919 |
|
|
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 |
| + |
panobinostat | down-regulates activity
chemical inhibition
|
HDAC7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257752 |
|
|
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 |
3.0
HDAC7
- 
- 