Protein degradation: recognition of ubiquitinylated substrates.
Research output: Contribution to journal › Journal article › Research › peer-review
A cell-free system has been developed in budding yeast that provides direct evidence that the Dsk2/Dph1, Rad23/Rhp23 and Rpn10/Pus1 multi-ubiquitin-binding proteins, long implicated in substrate recognition and presentation to the 26S proteasome, actually fulfil such a role.
| Original language | English |
|---|---|
| Journal | Current Biology |
| Volume | 14 |
| Issue number | 18 |
| Pages (from-to) | R754-6 |
| ISSN | 0960-9822 |
| DOIs | |
| Publication status | Published - 2004 |
Bibliographical note
Keywords: Carrier Proteins; Cell Cycle Proteins; DNA-Binding Proteins; Models, Biological; Proteasome Endopeptidase Complex; Protein Binding; Proteins; Saccharomyces cerevisiae Proteins; Schizosaccharomyces pombe Proteins; Ubiquitins; Yeasts
ID: 6493136