The ETS family member ERM contains an alpha-helical acidic activation domain that contacts TAFII60.
about
Exon 4-encoded acidic domain in the epithelium-restricted Ets factor, ESX, confers potent transactivating capacity and binds to TATA-binding protein (TBP)Analysis of transcriptional modulation of the presenilin 1 gene promoter by ZNF237, a candidate binding partner of the Ets transcription factor ERMCharacterization of the human and mouse ETV1/ER81 transcription factor genes: role of the two alternatively spliced isoforms in the humanHepatocyte growth factor/scatter factor activates the ETS1 transcription factor by a RAS-RAF-MEK-ERK signaling pathwayPea3 transcription factor cooperates with USF-1 in regulation of the murine bax transcription without binding to an Ets-binding siteCharacterization of ERM transactivation domain binding to the ACID/PTOV domain of the Mediator subunit MED25A small ubiquitin-related modifier-interacting motif functions as the transcriptional activation domain of Krüppel-like factor 4.Conservation and divergence of NF-Y transcriptional activation function.Transactivation, dimerization, and DNA-binding activity of white spot syndrome virus immediate-early protein IE1The C-terminal region of CHD3/ZFH interacts with the CIDD region of the Ets transcription factor ERM and represses transcription of the human presenilin 1 gene.The PEA3 Ets transcription factor comprises multiple domains that regulate transactivation and DNA binding.Different domains of the transcription factor ELF3 are required in a promoter-specific manner and multiple domains control its binding to DNA.The Mediator complex subunit MED25 is targeted by the N-terminal transactivation domain of the PEA3 group membersFEV acts as a transcriptional repressor through its DNA-binding ETS domain and alanine-rich domain.ERM transactivation is up-regulated by the repression of DNA binding after the PKA phosphorylation of a consensus site at the edge of the ETS domain.The activity of the activation function 2 of the human hepatocyte nuclear factor 4 (HNF-4alpha) is differently modulated by F domains from various origins.The possible functions of duplicated ets (GGAA) motifs located near transcription start sites of various human genesDioxin-inducible transactivation in a chromosomal setting. Analysis of the acidic domain of the Ah receptor.
P2860
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P2860
The ETS family member ERM contains an alpha-helical acidic activation domain that contacts TAFII60.
description
1997 nî lūn-bûn
@nan
1997 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
The ETS family member ERM cont ...... domain that contacts TAFII60.
@ast
The ETS family member ERM cont ...... domain that contacts TAFII60.
@en
The ETS family member ERM cont ...... domain that contacts TAFII60.
@nl
type
label
The ETS family member ERM cont ...... domain that contacts TAFII60.
@ast
The ETS family member ERM cont ...... domain that contacts TAFII60.
@en
The ETS family member ERM cont ...... domain that contacts TAFII60.
@nl
prefLabel
The ETS family member ERM cont ...... domain that contacts TAFII60.
@ast
The ETS family member ERM cont ...... domain that contacts TAFII60.
@en
The ETS family member ERM cont ...... domain that contacts TAFII60.
@nl
P2093
P2860
P356
P1476
The ETS family member ERM cont ...... domain that contacts TAFII60.
@en
P2093
Defossez PA
de Launoit Y
P2860
P304
P356
10.1093/NAR/25.22.4455
P407
P577
1997-11-01T00:00:00Z