(Q43845830)

27 November 2017

title

The SANT domain of Ada2 is required for normal acetylation of histones by the yeast SAGA complex (English)

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27 November 2017

David E Sterner

1

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27 November 2017

Xun Wang

2

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27 November 2017

Melissa H Bloom

3

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27 November 2017

Gabriel M Simon

4

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27 November 2017

Shelley L Berger

5

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27 November 2017

language of work or name

English

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publication date

2 January 2002

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Journal of Biological Chemistry

27 November 2017

published in

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27 November 2017

volume

277

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27 November 2017

issue

10

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27 November 2017

page(s)

8178-8186

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Transcriptional coactivators in yeast and beyond

27 November 2017

cites work

1 reference

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Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex

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Transcriptional activators direct histone acetyltransferase complexes to nucleosomes

21 January 2018

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Activation domain-specific and general transcription stimulation by native histone acetyltransferase complexes

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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A positive selection for mutants lacking orotidine-5'-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance

21 January 2018

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Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae

21 January 2018

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Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14.

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Tra1p is a component of the yeast Ada.Spt transcriptional regulatory complexes.

21 January 2018

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Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M108601200

1 reference

27 November 2017

1 reference