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The winged-helix/forkhead protein myocyte nuclear factor beta (MNF-beta) forms a co-repressor complex with mammalian sin3B
scientific journal article
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scholarly article
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PubMed
PubMed ID
10620510
retrieved
24 January 2017
title
The winged-helix/forkhead protein myocyte nuclear factor beta (MNF-beta) forms a co-repressor complex with mammalian sin3B
(English)
1 reference
stated in
PubMed
PubMed ID
10620510
retrieved
24 January 2017
main subject
Forkhead box K1
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GOA release 2020-03-11
author name string
Q. Yang
series ordinal
1
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PubMed
PubMed ID
10620510
retrieved
24 January 2017
Y. Kong
series ordinal
2
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PubMed
PubMed ID
10620510
retrieved
24 January 2017
B. Rothermel
series ordinal
3
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stated in
PubMed
PubMed ID
10620510
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24 January 2017
D. J. Garry
series ordinal
4
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PubMed
PubMed ID
10620510
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24 January 2017
R. Bassel-Duby
series ordinal
5
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PubMed
PubMed ID
10620510
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24 January 2017
R. S. Williams
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6
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PubMed
PubMed ID
10620510
retrieved
24 January 2017
language of work or name
English
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publication date
15 January 2000
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PubMed
PubMed ID
10620510
retrieved
24 January 2017
published in
Biochemical Journal
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PubMed
PubMed ID
10620510
retrieved
24 January 2017
volume
345 Pt 2
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PubMed
PubMed ID
10620510
retrieved
24 January 2017
page(s)
335–343
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PubMed
PubMed ID
10620510
retrieved
24 January 2017
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The Fork head transcription factor DAF-16 transduces insulin-like metabolic and longevity signals in C. elegans
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Transient expression of a winged-helix protein, MNF-beta, during myogenesis
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Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters
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Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex
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Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression
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Histone deacetylase activity is required for full transcriptional repression by mSin3A
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A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression
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Myocyte nuclear factor, a novel winged-helix transcription factor under both developmental and neural regulation in striated myocytes
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19 March 2017
An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3
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19 March 2017
Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3
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Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase
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29 September 2017
Activity of the rat liver-specific aldolase B promoter is restrained by HNF3.
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29 September 2017
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29 September 2017
MyoD-induced expression of p21 inhibits cyclin-dependent kinase activity upon myocyte terminal differentiation
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29 September 2017
GAL4 interacts with TATA-binding protein and coactivators
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29 September 2017
Cell cycle exit upon myogenic differentiation
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2 June 2018
Salivary duct determination in Drosophila: roles of the EGF receptor signalling pathway and the transcription factors fork head and trachealess
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2 June 2018
p53-independent expression of p21Cip1 in muscle and other terminally differentiating cells
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2 June 2018
Inhibition of myogenic differentiation in proliferating myoblasts by cyclin D1-dependent kinase
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2 June 2018
Correlation of terminal cell cycle arrest of skeletal muscle with induction of p21 by MyoD.
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2 June 2018
v-Myc, but not Max, possesses domains that function in both transcription activation and cellular transformation
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2 June 2018
Regionalization of Sonic hedgehog transcription along the anteroposterior axis of the mouse central nervous system is regulated by Hnf3-dependent and -independent mechanisms.
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27 November 2018
Persistent expression of MNF identifies myogenic stem cells in postnatal muscles.
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27 November 2018
Mnt, a novel Max-interacting protein is coexpressed with Myc in proliferating cells and mediates repression at Myc binding sites.
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27 November 2018
Identifiers
DOI
10.1042/0264-6021:3450335
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4829058
OpenCitations bibliographic resource ID
4829058
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4829058
PMCID
1220762
0 references
PubMed ID
10620510
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4829058
ResearchGate publication ID
247447698
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