Cargando…
Heat shock and oxygen radicals stimulate ubiquitin-dependent degradation mainly of newly synthesized proteins
Accumulation of misfolded oxidant-damaged proteins is characteristic of many diseases and aging. To understand how cells handle postsynthetically damaged proteins, we studied in Saccharomyces cerevisiae the effects on overall protein degradation of shifting from 30 to 38°C, exposure to reactive oxyg...
Autores principales: | Medicherla, Balasubrahmanyam, Goldberg, Alfred L. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2518706/ https://www.ncbi.nlm.nih.gov/pubmed/18725537 http://dx.doi.org/10.1083/jcb.200803022 |
Ejemplares similares
-
26S proteasomes become stably activated upon heat shock when ubiquitination and protein degradation increase
por: Lee, Donghoon, et al.
Publicado: (2022) -
Inhibiting ubiquitination causes an accumulation of SUMOylated newly synthesized nuclear proteins at PML bodies
por: Sha, Zhe, et al.
Publicado: (2019) -
Microinjection of ubiquitin: changes in protein degradation in HeLa cells subjected to heat-shock
Publicado: (1987) -
Immuno- and Constitutive Proteasomes Do Not Differ in Their Abilities to Degrade Ubiquitinated Proteins
por: Nathan, James A., et al.
Publicado: (2013) -
Systematic quantification of the dynamics of newly synthesized proteins unveiling their degradation pathways in human cells
por: Tong, Ming, et al.
Publicado: (2020)