| Value |
10
%
|
| Organism |
Unspecified |
| Reference |
Yewdell JW, Reits E, Neefjes J. Making sense of mass destruction: quantitating MHC class I antigen presentation. Nat Rev Immunol. 2003 Dec3(12):952-61. DOI: 10.1038/nri1250 p.958 left column bottom paragraphPubMed ID14647477
|
| Primary Source |
[61] Notterpek, L., Ryan, M. C., Tobler, A. R. & Shooter, E. M. PMP22 accumulation in aggresomes: implications for CMT1A pathology. Neurobiol. Dis. 6, 450–460 (1999) DOI: 10.1006/nbdi.1999.0274 [64] Yedidia, Y., Horonchik, L., Tzaban, S., Yanai, A. & Taraboulos, A. Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. EMBO J. 20, 5383–5391 (2001) DOI: 10.1093/emboj/20.19.5383PubMed ID10527811, 11574470
|
| Method |
Primary source [61] abstract: "Double immunolabeling with an anti-ubiquitin antibody and various organelle markers indicates that the accumulated PMP22 is found in unique intracellular inclusions, called aggresomes." Primary source [64] abstract: "Using proteasome inhibitors, [investigators] now show that approximately 10% of nascent PrP(C) molecules are diverted into the ERAD [Endoplasmic-reticulum-associated protein degradation] pathway." |
| Comments |
P.958 left column 3rd paragraph: "Ten percent of newly synthesized prion protein is degraded by proteasomes [primary sources], although a recent report indicates that this is a result of prolonged treatment with proteasome inhibitors [ref 65]. (The reader might find it odd that nearly all of these specific examples of biosynthetic inefficiency [see BNID 113776, 113777, 113778, 113779] are membrane proteins. This does not reflect selective examples from the literature, but a real bias in the choice of proteins that have been studied, which probably reflects greater effort to understand the role of ER versus cytosolic chaperones)." |
| Entered by |
Uri M |
| ID |
113780 |