Structure of the Ubiquitin-interacting Motif of S5a Bound to the Ubiquitin-like Domain of HR23B
Open Access
- 1 February 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (6) , 4760-4767
- https://doi.org/10.1074/jbc.m309448200
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- Receptor downregulation and multivesicular-body sortingNature Reviews Molecular Cell Biology, 2002
- RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMONature, 2002
- Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeastNature, 2002
- Emerging Roles of Ubiquitin in Transcription RegulationScience, 2002
- From UBA to UBX: new words in the ubiquitin vocabularyTrends in Cell Biology, 2002
- A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteinsNature, 2002
- A New Ticket for Entry into Budding Vesicles—UbiquitinCell, 2001
- A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systemsTrends in Biochemical Sciences, 2001
- Protein regulation by monoubiquitinNature Reviews Molecular Cell Biology, 2001
- Characterization of Two Polyubiquitin Binding Sites in the 26 S Protease Subunit 5aJournal of Biological Chemistry, 1998