(Q27933838)

English

Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway

scientific article published in June 2000

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scholarly article

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PubMed publication ID

1 December 2016

Peptides accelerate their uptake by activating a ubiquitin-dependent proteolytic pathway (English)

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PubMed publication ID

1 December 2016

1 reference

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GOA release 2020-03-11

author name string

G C Turner

1

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F Du

2

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A Varshavsky

3

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publication date

1 June 2000

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1 reference

PubMed publication ID

1 December 2016

405

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6786

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579-83

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Substrate targeting in the ubiquitin system

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The ubiquitin system

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The ubiquitin system

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The N-end rule pathway controls the import of peptides through degradation of a transcriptional repressor

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The recognition component of the N-end rule pathway

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How proteolysis drives the cell cycle

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The E2-E3 interaction in the N-end rule pathway: the RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain

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The N-end rule is mediated by the UBC2(RAD6) ubiquitin-conjugating enzyme

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A recognition component of the ubiquitin system is required for peptide transport in Saccharomyces cerevisiae

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Using ubiquitin to follow the metabolic fate of a protein

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Degradation signals in the lysine-asparagine sequence space

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PTR3, a novel gene mediating amino acid-inducible regulation of peptide transport in Saccharomyces cerevisiae

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The mouse and human genes encoding the recognition component of the N-end rule pathway

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The N-end rule in bacteria.

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Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae.

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Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression

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