Cellular Functions of Ufd2 and Ufd3 in Proteasomal Protein Degradation Depend on Cdc48 Binding
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Title
Cellular Functions of Ufd2 and Ufd3 in Proteasomal Protein Degradation Depend on Cdc48 Binding
Authors
Keywords
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Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 31, Issue 7, Pages 1528-1539
Publisher
American Society for Microbiology
Online
2011-02-01
DOI
10.1128/mcb.00962-10
References
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Note: Only part of the references are listed.- Imbalances in p97 co-factor interactions in human proteinopathy
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- The Yeast E4 Ubiquitin Ligase Ufd2 Interacts with the Ubiquitin-like Domains of Rad23 and Dsk2 via a Novel and Distinct Ubiquitin-like Binding Domain
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- Ubiquitin Chain Elongation Enzyme Ufd2 Regulates a Subset of Doa10 Substrates
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- The AAA-ATPase Cdc48 and cofactor Shp1 promote chromosome bi-orientation by balancing Aurora B activity
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- The Salmonella Effector SptP Dephosphorylates Host AAA+ ATPase VCP to Promote Development of its Intracellular Replicative Niche
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- A ubiquitin-selective AAA-ATPase mediates transcriptional switching by remodelling a repressor–promoter DNA complex
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- An Armadillo motif in Ufd3 interacts with Cdc48 and is involved in ubiquitin homeostasis and protein degradation
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- Tyrosine phosphorylation of ATPase p97 regulates its activity during ERAD
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- Dissecting the ER-Associated Degradation of a Misfolded Polytopic Membrane Protein
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- UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97
- (2008) C. Schuberth et al. CELLULAR AND MOLECULAR LIFE SCIENCES
- DOA1/UFD3 Plays a Role in Sorting Ubiquitinated Membrane Proteins into Multivesicular Bodies
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