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https://www.nature.com/articles/ncb0805-742
Aug 01, 2005 · One family of receptors delivers the ubiquitinated proteins to the proteasome resulting in ATP-dependent substrate unfolding and proteolysis.Author: Suzanne Elsasser, Daniel Finley
https://www.researchgate.net/publication/7690391_Elsasser_S_Finley_D_Delivery_of_ubiquitinated_substrates_to_protein-unfolding_machines_Nat_Cell_Biol_7_742-749
Ubiquilins (Ubqlns) are a family of ubiquitin receptors that promote the delivery of hydrophobic and aggregated ubiquitinated proteins to the proteasome for degradation.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1618115/
Oct 18, 2006 · Elsasser S, Finley D (2005) Delivery of ubiquitinated substrates to protein-unfolding machines. Nat Cell Biol 7 : 742–749 [ PubMed ] Glickman MH, Ciechanover A (2002) The ubiquitin–proteasome proteolytic pathway: destruction for the sake of construction .
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4927277/
Jul 01, 2016 · Here we used a misfolded huntingtin exon I containing a 103-polyglutamine expansion (Htt103QP) as a model substrate for the functional study of ubiquilin proteins. We found that yeast ubiquilin mutant ( dsk2 δ) is sensitive to Htt103QP overexpression and has a defect in the formation of Htt103QP inclusion bodies.Author: Kun-Han Chuang, Fengshan Liang, Ryan Higgins, Yanchang Wang
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1697804/
In Saccharomyces cerevisiae Rad23, Ddi1 and Dsk2 are the three UBL-UBA proteins, which are hypothesized to shuttle ubiquitinated substrates to the proteasome for degradation [6-11] due to their ability to interact with the proteasome through their UBL domains [12-15] as well as with ubiquitin and polyubiquitinated substrates through their UBA domains [7,8,16-18].Author: Laura A Díaz-Martínez, Yang Kang, Kylie J Walters, Duncan J Clarke
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3647454/
Apr 01, 2010 · The best-studied protein modification targeting proteins for degradation in eukaryotes is ubiquitin. Ubiquitin is a highly conserved, 76 amino acid protein that covalently attaches to substrate lysines though its C-terminal di-glycine (GG) motif.Author: Kristin E. Burns, K. Heran Darwin
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