# |
PMID |
Sentence |
1 |
6849935
|
Minor hemoglobins, namely AIa1, AIa2, AIb1, AIb2, AIb3, AIc, AId1, AId2 and AId3, have been separated and eluted in that order.
|
2 |
14645241
|
Interactions between activating signal cointegrator-2 and the tumor suppressor retinoblastoma in androgen receptor transactivation.
|
3 |
14645241
|
In this work, we showed that ASC-2 has an indirect, separate binding site for androgen receptor (AR).
|
4 |
14645241
|
Interactions between activating signal cointegrator-2 and the tumor suppressor retinoblastoma in androgen receptor transactivation.
|
5 |
14645241
|
In this work, we showed that ASC-2 has an indirect, separate binding site for androgen receptor (AR).
|
6 |
15764585
|
Characterization of activating signal cointegrator-2 as a novel transcriptional coactivator of the xenobiotic nuclear receptor constitutive androstane receptor.
|
7 |
15764585
|
In this report, we demonstrate that ASC-2 also serves as a coactivator of the xenobiotic nuclear receptor constitutive androstane receptor (CAR).
|
8 |
15764585
|
In support of this idea, DN1, a fragment of ASC-2 encompassing the first LXXLL motif, suppressed CAR transactivation, and coexpressed ASC-2 but not other LXXLL-type coactivators such as thyroid hormone receptor-associated protein 220 reversed this repression.
|
9 |
15764585
|
Characterization of activating signal cointegrator-2 as a novel transcriptional coactivator of the xenobiotic nuclear receptor constitutive androstane receptor.
|
10 |
15764585
|
In this report, we demonstrate that ASC-2 also serves as a coactivator of the xenobiotic nuclear receptor constitutive androstane receptor (CAR).
|
11 |
15764585
|
In support of this idea, DN1, a fragment of ASC-2 encompassing the first LXXLL motif, suppressed CAR transactivation, and coexpressed ASC-2 but not other LXXLL-type coactivators such as thyroid hormone receptor-associated protein 220 reversed this repression.
|
12 |
15764585
|
Characterization of activating signal cointegrator-2 as a novel transcriptional coactivator of the xenobiotic nuclear receptor constitutive androstane receptor.
|
13 |
15764585
|
In this report, we demonstrate that ASC-2 also serves as a coactivator of the xenobiotic nuclear receptor constitutive androstane receptor (CAR).
|
14 |
15764585
|
In support of this idea, DN1, a fragment of ASC-2 encompassing the first LXXLL motif, suppressed CAR transactivation, and coexpressed ASC-2 but not other LXXLL-type coactivators such as thyroid hormone receptor-associated protein 220 reversed this repression.
|
15 |
17021013
|
Activating signal cointegrator-2 (ASC-2), a coactivator of multiple transcription factors that include retinoic acid receptor (RAR), associates with histone H3-K4 methyltranferases (H3K4MTs) MLL3 and MLL4 in mixed-lineage leukemia.
|
16 |
17021013
|
Here, we show that mice expressing a SET domain mutant of MLL3 share phenotypes with isogenic ASC2+/- mice and that expression and H3-K4 trimethylation of RAR target gene RAR-beta2 are impaired in ASC-2-null mouse embryo fibroblasts (MEFs) or in MEFs expressing siRNAs against both MLL3 and MLL4.
|
17 |
17021013
|
We also show that MLL3 and MLL4 are found in distinct ASC-2-containing complexes rather than in a common ASC-2 complex, and they are recruited to RAR-beta2 by ASC-2.
|
18 |
17021013
|
These results suggest that ASC-2 confers target gene specificity to MLL3 and MLL4 H3K4MT complexes and that recruitment of H3K4MTs to their target genes generally involves interactions between integral components of H3K4MT complexes and transcription factors.
|
19 |
17021013
|
Activating signal cointegrator-2 (ASC-2), a coactivator of multiple transcription factors that include retinoic acid receptor (RAR), associates with histone H3-K4 methyltranferases (H3K4MTs) MLL3 and MLL4 in mixed-lineage leukemia.
|
20 |
17021013
|
Here, we show that mice expressing a SET domain mutant of MLL3 share phenotypes with isogenic ASC2+/- mice and that expression and H3-K4 trimethylation of RAR target gene RAR-beta2 are impaired in ASC-2-null mouse embryo fibroblasts (MEFs) or in MEFs expressing siRNAs against both MLL3 and MLL4.
|
21 |
17021013
|
We also show that MLL3 and MLL4 are found in distinct ASC-2-containing complexes rather than in a common ASC-2 complex, and they are recruited to RAR-beta2 by ASC-2.
|
22 |
17021013
|
These results suggest that ASC-2 confers target gene specificity to MLL3 and MLL4 H3K4MT complexes and that recruitment of H3K4MTs to their target genes generally involves interactions between integral components of H3K4MT complexes and transcription factors.
|
23 |
17021013
|
Activating signal cointegrator-2 (ASC-2), a coactivator of multiple transcription factors that include retinoic acid receptor (RAR), associates with histone H3-K4 methyltranferases (H3K4MTs) MLL3 and MLL4 in mixed-lineage leukemia.
|
24 |
17021013
|
Here, we show that mice expressing a SET domain mutant of MLL3 share phenotypes with isogenic ASC2+/- mice and that expression and H3-K4 trimethylation of RAR target gene RAR-beta2 are impaired in ASC-2-null mouse embryo fibroblasts (MEFs) or in MEFs expressing siRNAs against both MLL3 and MLL4.
|
25 |
17021013
|
We also show that MLL3 and MLL4 are found in distinct ASC-2-containing complexes rather than in a common ASC-2 complex, and they are recruited to RAR-beta2 by ASC-2.
|
26 |
17021013
|
These results suggest that ASC-2 confers target gene specificity to MLL3 and MLL4 H3K4MT complexes and that recruitment of H3K4MTs to their target genes generally involves interactions between integral components of H3K4MT complexes and transcription factors.
|
27 |
17021013
|
Activating signal cointegrator-2 (ASC-2), a coactivator of multiple transcription factors that include retinoic acid receptor (RAR), associates with histone H3-K4 methyltranferases (H3K4MTs) MLL3 and MLL4 in mixed-lineage leukemia.
|
28 |
17021013
|
Here, we show that mice expressing a SET domain mutant of MLL3 share phenotypes with isogenic ASC2+/- mice and that expression and H3-K4 trimethylation of RAR target gene RAR-beta2 are impaired in ASC-2-null mouse embryo fibroblasts (MEFs) or in MEFs expressing siRNAs against both MLL3 and MLL4.
|
29 |
17021013
|
We also show that MLL3 and MLL4 are found in distinct ASC-2-containing complexes rather than in a common ASC-2 complex, and they are recruited to RAR-beta2 by ASC-2.
|
30 |
17021013
|
These results suggest that ASC-2 confers target gene specificity to MLL3 and MLL4 H3K4MT complexes and that recruitment of H3K4MTs to their target genes generally involves interactions between integral components of H3K4MT complexes and transcription factors.
|
31 |
17500065
|
PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex.
|
32 |
17500065
|
Here we show that while ectopically expressed PTIP is capable of interacting with DNA damage response proteins including 53BP1, endogenous PTIP, and a novel protein PA1 are both components of a Set1-like histone methyltransferase (HMT) complex that also contains ASH2L, RBBP5, WDR5, hDPY-30, NCOA6, SET domain-containing HMTs MLL3 and MLL4, and substoichiometric amount of JmjC domain-containing putative histone demethylase UTX.
|
33 |
17500065
|
Furthermore, PA1 binds PTIP directly and requires PTIP for interaction with the rest of the complex.
|
34 |
17500065
|
The evolutionarily conserved hDPY-30, ASH2L, RBBP5, and WDR5 likely constitute a subcomplex that is shared by all human Set1-like HMT complexes.
|
35 |
17500065
|
In contrast, PTIP, PA1, and UTX specifically associate with the PTIP complex.
|
36 |
19047629
|
Activating signal cointegrator-2 (ASC-2), a transcriptional coactivator of multiple transcription factors that include the adipogenic factors peroxisome proliferator-activated receptor gamma (PPARgamma) and C/EBPalpha, is associated with histone H3-Lys-4-methyltransferase (H3K4MT) MLL3 or its paralogue MLL4 in a complex named ASCOM (ASC-2 complex).
|
37 |
19047629
|
However, the specific roles for MLL3 and MLL4 in adipogenesis remain undefined.
|
38 |
19047629
|
Third, ASC-2, MLL3, and MLL4 are recruited to the PPARgamma-activated aP2 gene during adipogenesis, and PPARgamma is shown to interact directly with the purified ASCOM.
|
39 |
19047629
|
Moreover, although H3K4 methylation of aP2 is readily induced in WT MEFs, it is not induced in ASC-2(-/-) MEFs and only partially induced in MLL3(Delta/Delta) MEFs.
|
40 |
19047629
|
Activating signal cointegrator-2 (ASC-2), a transcriptional coactivator of multiple transcription factors that include the adipogenic factors peroxisome proliferator-activated receptor gamma (PPARgamma) and C/EBPalpha, is associated with histone H3-Lys-4-methyltransferase (H3K4MT) MLL3 or its paralogue MLL4 in a complex named ASCOM (ASC-2 complex).
|
41 |
19047629
|
However, the specific roles for MLL3 and MLL4 in adipogenesis remain undefined.
|
42 |
19047629
|
Third, ASC-2, MLL3, and MLL4 are recruited to the PPARgamma-activated aP2 gene during adipogenesis, and PPARgamma is shown to interact directly with the purified ASCOM.
|
43 |
19047629
|
Moreover, although H3K4 methylation of aP2 is readily induced in WT MEFs, it is not induced in ASC-2(-/-) MEFs and only partially induced in MLL3(Delta/Delta) MEFs.
|
44 |
19047629
|
Activating signal cointegrator-2 (ASC-2), a transcriptional coactivator of multiple transcription factors that include the adipogenic factors peroxisome proliferator-activated receptor gamma (PPARgamma) and C/EBPalpha, is associated with histone H3-Lys-4-methyltransferase (H3K4MT) MLL3 or its paralogue MLL4 in a complex named ASCOM (ASC-2 complex).
|
45 |
19047629
|
However, the specific roles for MLL3 and MLL4 in adipogenesis remain undefined.
|
46 |
19047629
|
Third, ASC-2, MLL3, and MLL4 are recruited to the PPARgamma-activated aP2 gene during adipogenesis, and PPARgamma is shown to interact directly with the purified ASCOM.
|
47 |
19047629
|
Moreover, although H3K4 methylation of aP2 is readily induced in WT MEFs, it is not induced in ASC-2(-/-) MEFs and only partially induced in MLL3(Delta/Delta) MEFs.
|