Zobrazeno 1 - 10
of 22
pro vyhledávání: '"C. M. Pickart"'
Autor:
R J Mayer, C M Pickart, Michael Landon, Robert Layfield, Robert Ramage, Andrew Alban, Y A Lam, C Jamieson
Publikováno v:
Proceedings of the National Academy of Sciences. 97:9902-9906
Alzheimer's disease is the most common cause of dementia in the elderly. Although several genetic defects have been identified in patients with a family history of this disease, the majority of cases involve individuals with no known genetic predispo
Publikováno v:
Cell. 105(6)
While the signaling properties of ubiquitin depend on the topology of polyubiquitin chains, little is known concerning the molecular basis of specificity in chain assembly and recognition. UEV/Ubc complexes have been implicated in the assembly of Lys
Autor:
C. M. Pickart
Publikováno v:
Stress Proteins ISBN: 9783642635199
Cells respond to stresses such as elevated temperature, heavy metals, and amino acid analogs by inducing the transcription of a set of genes whose products, known as stress proteins, enhance survival under stress conditions. The major shared property
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::967f7c72d79fb220be5e5df7a2eca3b2
https://doi.org/10.1007/978-3-642-58259-2_6
https://doi.org/10.1007/978-3-642-58259-2_6
Publikováno v:
The Journal of biological chemistry. 269(10)
Ubiquitin-mediated proteolysis proceeds via the formation and degradation of ubiquitin-protein conjugates. Ubiquitin (Ub)-activating enzyme (E1) catalyzes the first, MgATP-dependent step in the conjugative reaction sequence. With wild type ubiquitin,
Publikováno v:
The Journal of biological chemistry. 267(23)
Covalent ligation of multiubiquitin chains targets eukaryotic proteins for degradation. In such multiubiquitin chains, successive ubiquitins are linked by an isopeptide bond involving the side chain of Lys48 and the carboxyl group of Gly76. The cryst
Publikováno v:
The Journal of biological chemistry. 267(23)
Trivalent arsenoxides bind to vicinal thiol groups of proteins. We showed previously that the simplest trivalent arsenoxide, inorganic arsenite, inhibits ubiquitin-dependent protein degradation in rabbit reticulocyte lysate (Klemperer, N.S., and Pick
Publikováno v:
The Journal of biological chemistry. 267(20)
Covalent ligation of multiubiquitin chains targets eukaryotic proteins for degradation. Ubiquitin-conjugating enzyme E2(25K) utilizes isolated ubiquitin as the substrate for synthesis of such chains, in which successive ubiquitin units are linked by
Publikováno v:
The Journal of biological chemistry. 266(24)
The ubiquitin (Ub)-conjugating enzyme E2(25K) catalyzes the synthesis of multi-Ub chains in which successive Ub units are linked by an isopeptide bond involving the epsilon-amino group of Lys-48 of Ubn, and the COOH-terminal Gly residue of Ubn+1 (Che
Autor:
Z, Chen, C M, Pickart
Publikováno v:
The Journal of biological chemistry. 265(35)
Target protein multi-ubiquitination involving lysine 48 of ubiquitin (Ub) is known to occur during protein degradation in the ATP- and Ub-dependent proteolytic pathway (Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K.,
Autor:
I A Rose, C M Pickart
Publikováno v:
Journal of Biological Chemistry. 260:1573-1581
In the formation of covalent ubiquitin-protein conjugates that occurs during ATP- and ubiquitin-dependent proteolysis in reticulocyte extracts, ubiquitin (Ub) is activated to a thiol ester of the activating enzyme E1 (via the Ub carboxyl terminus), t