Publication for MTA1 and NCOR2
| Species | Symbol | Function* | Entrez Gene ID* | Other ID | Gene coexpression |
CoexViewer |
|---|---|---|---|---|---|---|
| hsa | MTA1 | metastasis associated 1 | 9112 | [link] | ||
| hsa | NCOR2 | nuclear receptor corepressor 2 | 9612 |
| Pubmed ID | Priority | Text |
|---|---|---|
| 23791785 | 0.98 | SMRT complex with that of HDAC1:MTA1 reveals key differences between the two HDACs and their corepressors that dictate the specificity of complex assembly (Figure 6). |
| 0.97 | MTA1 results in a significant increase in HDAC activity in a similar fashion to that observed for the HDAC3:SMRT complex (Figure 5F). | |
| 0.97 | MTA1 having one fewer Ins(1,4,5,6)P4-interacting lysine residues than SMRT. | |
| 0.97 | MTA1) and Arg36 (HDAC1) cause helix H3 in MTA1-SANT to be slightly tipped away from the HDAC compared with the SMRT-SANT. | |
| 0.97 | MTA1-ELM2 (cyan) and helix H0 of SMRT (orange) are indicated. | |
| 0.96 | MTA1-SANT and SMRT-SANT, whereas HDAC3 only binds SMRT-SANT efficiently. | |
| 0.96 | MTA1 and HDAC1, orange; SMRT and HDAC3, green). | |
| 0.94 | MTA1 by Ins(1,4,5,6)P4 is 5 muM:similar to that of the HDAC3:SMRT complex. | |
| 0.93 | MTA1 with the ELM2-specific-like motif (ESLM) of SMRT and NCoR. | |
| 0.92 | MTA1-SANT (green) and SMRT-SANT (orange) bound to HDAC1 and HDAC3, respectively. | |
| 0.91 | MTA1 and SMRT, we sought to determine whether HDAC1 and HDAC3 can discriminate between the SANT domains. | |
| 0.89 | MTA1-SANT domain and explains the specificity of HDAC3 for the SMRT-SANT. | |
| 0.53 | MTA1 and SMRT. | |
| 25352341 | 0.97 | SMRT, the addition of IP4 to HDAC1:MTA1 enhances HDAC activity, and mutation of the IP4 coordinating residues inhibits activation. |
| 0.67 | MTA1 is highly related to the first of two SANT domains from the nuclear receptor corepressor protein SMRT (also known as NCOR2). | |
| 0.54 | MTA1 in the same orientation as observed in the HDAC3:SMRT crystal structure. | |
| 27109927 | 0.96 | SMRT complex, the HDAC1:MTA1 complex can be activated by both Ins(1,3,4,5,6)P5 and InsP6, suggesting that the mode of inositol phosphate binding is likely to be similar (Fig. 3a). |
| 0.94 | SMRT and HDAC1:MTA1 complexes are reproducibly activated by inositol phosphates. | |
| 0.93 | SMRT:Ins(1,4,5,6)P4 structure or the position seen in the HDAC1:MTA1:InsP6 complex (Supplementary Fig. 10). | |
| 21814622 | 0.95 | SMRT and MTA1. |
| 26055705 | 0.94 | MTA1 and SMRT/NCoR has recently been established. |
| 25653165 | 0.62 | SMRT bound to HDAC3 and an ELM2-SANT domain from MTA1 in complex with HDAC1. |
The preparation time of this page was 0.0 [sec].
