Title : Characterization of C-terminal adaptors, UFD-2 and UFD-3, of CDC-48 on the polyglutamine aggregation in C. elegans.

Pub. Date : 2015 Mar 27

PMID : 25721663






4 Functional Relationships(s)
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1 We also found that the number of polyglutamine (polyQ) aggregates was reduced in the ufd-3 deletion mutant but not in the ufd-2 deletion mutant. polyglutamine PUL domain-containing protein;Ubiquitin fusion degradation protein 3 homolog Caenorhabditis elegans
2 We also found that the number of polyglutamine (polyQ) aggregates was reduced in the ufd-3 deletion mutant but not in the ufd-2 deletion mutant. polyglutamine PUL domain-containing protein;Ubiquitin fusion degradation protein 3 homolog Caenorhabditis elegans
3 Taken together, we propose that UFD-3 may promote the formation of polyQ aggregates to reduce the polyQ toxicity in C. elegans. polyglutamine PUL domain-containing protein;Ubiquitin fusion degradation protein 3 homolog Caenorhabditis elegans
4 Taken together, we propose that UFD-3 may promote the formation of polyQ aggregates to reduce the polyQ toxicity in C. elegans. polyglutamine PUL domain-containing protein;Ubiquitin fusion degradation protein 3 homolog Caenorhabditis elegans