(Q33930855)

30 July 2017

title

Evidence that proteolysis of Gal4 cannot explain the transcriptional effects of proteasome ATPase mutations (English)

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30 July 2017

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Russell SJ

1

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30 July 2017

Johnston SA

series ordinal

2

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30 July 2017

language of work or name

English

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publication date

4 January 2001

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Journal of Biological Chemistry

30 July 2017

published in

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30 July 2017

volume

276

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30 July 2017

issue

13

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30 July 2017

page(s)

9825-9831

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Alterations in a yeast protein resembling HIV Tat-binding protein relieve requirement for an acidic activation domain in GAL4.

30 July 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.M010889200

Isolation and characterization of SUG2. A novel ATPase family component of the yeast 26 S proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

A 200-amino acid ATPase module in search of a basic function

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

The regulatory particle of the Saccharomyces cerevisiae proteasome.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated transactivation, as subunit 7 of the 26 S protease

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

Tat-binding protein 7 is a subunit of the 26S protease

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

Sug1 modulates yeast transcription activation by Cdc68.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

Elevated recombination rates in transcriptionally active DNA

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

Sequence analysis of the AAA protein family

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

Subcellular localization, stoichiometry, and protein levels of 26 S proteasome subunits in yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

Proteolysis: The proteasome: a protein-degrading organelle?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

From the cradle to the grave: ring complexes in the life of a protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

Conformational constraints in protein degradation by the 20S proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

A new component of bacteriophage Mu replicative transposition machinery: the Escherichia coli ClpX protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

Disassembly of the Mu transposase tetramer by the ClpX chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

The base of the proteasome regulatory particle exhibits chaperone-like activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

Proteasome-mediated degradation of transcriptional activators correlates with activation domain potency in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

Erratum: A highly conserved ATPase protein as a mediator between acidic activation domains and the TATA-binding protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

The 19S Regulatory Complex of the Proteasome Functions Independently of Proteolysis in Nucleotide Excision Repair

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M010889200

21 January 2018

Identifiers

DOI

10.1074/JBC.M010889200

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30 July 2017

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