Novel substrates and functions for the ubiquitin-like molecule NEDD8
Author:
Affiliation:
1. Wellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, U.K.
Abstract
Publisher
Portland Press Ltd.
Subject
Biochemistry
Link
https://portlandpress.com/biochemsoctrans/article-pdf/36/5/802/545575/bst0360802.pdf
Reference56 articles.
1. Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein;Kamitani;J. Biol. Chem.,1997
2. Modification of proteins by ubiquitin and ubiquitin-like proteins;Kerscher;Annu. Rev. Cell Dev. Biol.,2006
3. DEN1 is a dual function protease capable of processing the C terminus of Nedd8 and deconjugating hyper-neddylated CUL1;Wu;J. Biol. Chem.,2003
4. Identification and characterization of DEN1, a deneddylase of the ULP family;Gan-Erdene;J. Biol. Chem.,2003
5. NEDP1, a highly conserved cysteine protease that deNEDDylates Cullins;Mendoza;J. Biol. Chem.,2003
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