@article{f3d2c15095f311dd86a6000ea68e967b,
title = "Integral UBL domain proteins: a family of proteasome interacting proteins.",
abstract = "The family of ubiquitin-like (UBL) domain proteins (UDPs) comprises a conserved group of proteins involved in a multitude of different cellular activities. However, recent studies on UBL-domain proteins indicate that these proteins appear to share a common property in their ability to interact with 26S proteasomes. The 26S proteasome is a multisubunit protease which is responsible for the majority of intracellular proteolysis in eukaryotic cells. Before degradation commences most proteins are first marked for destruction by being coupled to a chain of ubiquitin molecules. Some UBL-domain proteins catalyse the formation of ubiquitin-protein conjugates, whereas others appear to target ubiquitinated proteins for degradation and interact with chaperones. Hence, by binding to the 26S proteasome the UBL-domain proteins seem to tailor and direct the basic proteolytic functions of the particle to accommodate various cellular substrates.",
author = "Rasmus Hartmann-Petersen and Colin Gordon",
note = "Keywords: Animals; Humans; Peptide Hydrolases; Proteasome Endopeptidase Complex; Protein Binding; Protein Structure, Tertiary; Ubiquitin-Protein Ligases; Ubiquitins",
year = "2004",
language = "English",
volume = "15",
pages = "247--59",
journal = "Seminars in Cell and Developmental Biology",
issn = "1084-9521",
publisher = "Academic Press",
number = "2",
}