@article{8a0a4bc09e9111dd86a6000ea68e967b,
title = "Proteins interacting with the 26S proteasome.",
abstract = "The 26S proteasome is the multi-protein protease that recognizes and degrades ubiquitinylated substrates targeted for destruction by the ubiquitin pathway. In addition to the well-documented subunit organization of the 26S holoenzyme, it is clear that a number of other proteins transiently associate with the 26S complex. These transiently associated proteins confer a number of different roles such as substrate presentation, cleavage of the multi-ubiquitin chain from the protein substrate and turnover of misfolded proteins. Such activities are essential for the 26S proteasome to efficiently fulfill its intracellular function in protein degradation.",
author = "R Hartmann-Petersen and C Gordon",
note = "Keywords: Animals; Humans; Peptide Hydrolases; Proteasome Endopeptidase Complex; Protein Binding; Substrate Specificity; Ubiquitin; Ubiquitin-Conjugating Enzymes; Ubiquitin-Protein Ligases",
year = "2004",
doi = "10.1007/s00018-004-4132-x",
language = "English",
volume = "61",
pages = "1589--95",
journal = "Cellular and molecular life sciences : CMLS",
issn = "1420-682X",
publisher = "Springer Basel AG",
number = "13",
}