| + |
H4C1 | up-regulates activity 
relocalization
|
BRDT |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262066 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27991587 |
BRDT interacts with acetylated nucleosomes via its BD1 domain. Binding may be initiated through non-specific interactions with DNA, which allow BRDT to localize to chromatin. Specificity is generated through recognition of tandem acetylated lysine residues (K5ac/K8ac) on the histone H4 tail, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRDT | up-regulates quantity
binding
|
EIF4EBP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262049 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33125143 |
It was revealed that eIF4EBP1 interacted with BRDT, a novel interacting protein. In addition, the present study further demonstrated that BRDT inhibitors PLX51107 and INCB054329 blocked the progression of RCC cells, along with suppressing eIF4EBP1 and c‑myc expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
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 |
3.0
BRDT
- 
- 