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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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

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

1 reference

Europe PubMed Central

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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

2

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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

4

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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

author name string

A L Eilers

1

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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

J Liu

3

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1 November 2019

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publication date

1 November 1999

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1 November 2019

Journal of Biological Chemistry

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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

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

Eukaryotic transcription: an interlaced network of transcription factors and chromatin-modifying machines

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Chromatin remodeling machines: similar motors, ulterior motives

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Chromatin remodeling and the control of gene expression

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HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription

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The Transcriptional Repressor Even-skipped Interacts Directly with TATA-Binding Protein

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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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Mot1, a global repressor of RNA polymerase II transcription, inhibits TBP binding to DNA by an ATP-dependent mechanism.

1 reference

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21 January 2018

Histone deacetylase activity is required for full transcriptional repression by mSin3A

1 reference

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21 January 2018

Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression

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Retinoblastoma protein recruits histone deacetylase to repress transcription

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Retinoblastoma protein represses transcription by recruiting a histone deacetylase

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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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Groucho is required for Drosophila neurogenesis, segmentation, and sex determination and interacts directly with hairy-related bHLH proteins

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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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21 January 2018

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

1 reference

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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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21 January 2018

Histone acetylation in chromatin structure and transcription

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21 January 2018

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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21 January 2018

Histone acetylation and transcriptional regulatory mechanisms

1 reference

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21 January 2018

Covalent modifications of histones: expression from chromatin templates

1 reference

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21 January 2018

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

1 reference

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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

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

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

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

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

1 reference

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

21 January 2018

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

1 reference

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21 January 2018

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

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

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

1 reference

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21 January 2018

Expression of the mad gene during cell differentiation in vivo and its inhibition of cell growth in vitro

1 reference

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21 January 2018

Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites

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Mnt, a novel Max-interacting protein is coexpressed with Myc in proliferating cells and mediates repression at Myc binding sites

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Inhibition of cell proliferation by the Mad1 transcriptional repressor

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Mad proteins contain a dominant transcription repression domain.

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SIN3-dependent transcriptional repression by interaction with the Mad1 DNA-binding protein

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Analysis of an activator:coactivator complex reveals an essential role for secondary structure in transcriptional activation

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Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein

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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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