+ |
JQ1 | down-regulates activity
chemical inhibition
|
BRD3 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261988 |
|
|
in vitro |
|
pmid |
sentence |
20871596 |
Enantiomerically pure (+)-JQ1 bound with a Kd of about 50 nM and 90 nM to the first and second bromodomains of BRD4, respectively (Fig. 1c, Supplementary Table 3). Comparable binding to both domains of BRD3 was observed, whereas the first bromodomains of BRDT and BRD2 revealed about 3-fold weaker binding.|Here, we present a first, thoroughly characterized inhibitor of the BET-family of bromodomains. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
JQ1 | down-regulates activity
chemical inhibition
|
BRDT |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261990 |
|
|
in vitro |
|
pmid |
sentence |
20871596 |
Enantiomerically pure (+)-JQ1 bound with a Kd of about 50 nM and 90 nM to the first and second bromodomains of BRD4, respectively (Fig. 1c, Supplementary Table 3). Comparable binding to both domains of BRD3 was observed, whereas the first bromodomains of BRDT and BRD2 revealed about 3-fold weaker binding.|Here, we present a first, thoroughly characterized inhibitor of the BET-family of bromodomains. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
JQ1 | down-regulates activity
chemical inhibition
|
BRD2 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261987 |
|
|
in vitro |
|
pmid |
sentence |
20871596 |
Enantiomerically pure (+)-JQ1 bound with a Kd of about 50 nM and 90 nM to the first and second bromodomains of BRD4, respectively (Fig. 1c, Supplementary Table 3). Comparable binding to both domains of BRD3 was observed, whereas the first bromodomains of BRDT and BRD2 revealed about 3-fold weaker binding.|Here, we present a first, thoroughly characterized inhibitor of the BET-family of bromodomains. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
JQ1 | down-regulates activity
chemical inhibition
|
BRD4 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261989 |
|
|
in vitro |
|
pmid |
sentence |
20871596 |
Enantiomerically pure (+)-JQ1 bound with a Kd of about 50 nM and 90 nM to the first and second bromodomains of BRD4, respectively (Fig. 1c, Supplementary Table 3). Comparable binding to both domains of BRD3 was observed, whereas the first bromodomains of BRDT and BRD2 revealed about 3-fold weaker binding.|Here, we present a first, thoroughly characterized inhibitor of the BET-family of bromodomains. |
|
Publications: |
1 |
Organism: |
In Vitro |