FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis

Structure of Rpn10 and Its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12

(2010) Christiane Riedinger et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

USE1 is a bispecific conjugating enzyme for ubiquitin and FAT10, which FAT10ylates itself in cis

(2010) Annette Aichem et al.   Nature Communications

ALINE: a WYSIWYG protein-sequence alignment editor for publication-quality alignments

(2009) Charles Simon Bond et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome

(2009) Daniel Finley   Annual Review of Biochemistry

Jalview Version 2--a multiple sequence alignment editor and analysis workbench

(2009) A. M. Waterhouse et al.   BIOINFORMATICS

Quantitative Proteomics Reveals the Function of Unconventional Ubiquitin Chains in Proteasomal Degradation

(2009) Ping Xu et al.   CELL

Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L

(2009) Gunter Schmidtke et al.   FEBS LETTERS

Together, Rpn10 and Dsk2 Can Serve as a Polyubiquitin Chain-Length Sensor

(2009) Daoning Zhang et al.   MOLECULAR CELL

Structure of the S5a:K48-Linked Diubiquitin Complex and Its Interactions with Rpn13

(2009) Naixia Zhang et al.   MOLECULAR CELL

Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction

(2008) Patrick Schreiner et al.   NATURE

Proteasome subunit Rpn13 is a novel ubiquitin receptor

(2008) Koraljka Husnjak et al.   NATURE

Activating the ubiquitin family: UBA6 challenges the field

(2008) Marcus Groettrup et al.   TRENDS IN BIOCHEMICAL SCIENCES