A 13-amino acid amphipathic alpha-helix is required for the functional interaction between the transcriptional repressor Mad1 and mSin3A (Q73157313)

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scientific article published on 01 November 1999

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English	A 13-amino acid amphipathic alpha-helix is required for the functional interaction between the transcriptional repressor Mad1 and mSin3A	scientific article published on 01 November 1999

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scholarly article

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10551834%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

A 13-amino acid amphipathic alpha-helix is required for the functional interaction between the transcriptional repressor Mad1 and mSin3A (English)

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Europe PubMed Central

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1 November 2019

2

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1 November 2019

4

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1 November 2019

author name string

A L Eilers

1

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1 November 2019

J Liu

3

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1 November 2019

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1 November 1999

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1 November 2019

Journal of Biological Chemistry

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1 November 2019

274

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1 November 2019

46

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1 November 2019

32750-32756

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1 November 2019

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Structure-function analysis of the TBP-binding protein Dr1 reveals a mechanism for repression of class II gene transcription

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Histone deacetylase activity is required for full transcriptional repression by mSin3A

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21 January 2018

Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression

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Rb interacts with histone deacetylase to repress transcription

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Methylated DNA and MeCP2 recruit histone deacetylase to repress transcription

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21 January 2018

Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex

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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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Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain

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Solution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of CREB: A Model for Activator:Coactivator Interactions

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Induced alpha helix in the VP16 activation domain upon binding to a human TAF

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Histone acetylation in chromatin structure and transcription

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Targeting chromatin disruption: Transcription regulators that acetylate histones

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21 January 2018

Nuclear histone acetylases and deacetylases and transcriptional regulation: HATs off to HDACs.

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The SAGA unfolds: convergence of transcription regulators in chromatin-modifying complexes.

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Histone acetylation and transcriptional regulatory mechanisms

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Covalent modifications of histones: expression from chromatin templates

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21 January 2018

Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3

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21 January 2018

An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3

1 reference

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21 January 2018

Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.46.32750

21 January 2018

SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors

1 reference

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21 January 2018

A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.46.32750

21 January 2018

Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase

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21 January 2018

The Saccharomyces cerevisiae SIN3 gene, a negative regulator of HO, contains four paired amphipathic helix motifs

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21 January 2018

Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression

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21 January 2018

Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity

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Suppression of Myc, but not E1a, transformation activity by Max-associated proteins, Mad and Mxi1

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Identifiers

10.1074/JBC.274.46.32750

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10551834%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10551834%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

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