Cargando…
Exposed hydrophobicity is a key determinant of nuclear quality control degradation
Protein quality control (PQC) degradation protects the cell by preventing the toxic accumulation of misfolded proteins. In eukaryotes, PQC degradation is primarily achieved by ubiquitin ligases that attach ubiquitin to misfolded proteins for proteasome degradation. To function effectively, PQC ubiqu...
Autores principales: | Fredrickson, Eric K., Rosenbaum, Joel C., Locke, Melissa N., Milac, Thomas I., Gardner, Richard G. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2011
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3128539/ https://www.ncbi.nlm.nih.gov/pubmed/21551067 http://dx.doi.org/10.1091/mbc.E11-03-0256 |
Ejemplares similares
-
The extent of Ssa1/Ssa2 Hsp70 chaperone involvement in nuclear protein quality control degradation varies with the substrate
por: Jones, Ramon D., et al.
Publicado: (2020) -
Hydrophobicity is a key determinant in the activity of arginine-rich cell penetrating peptides
por: Allen, Jason, et al.
Publicado: (2022) -
Nuclear Phosphoinositides as Key Determinants of Nuclear Functions
por: Vidalle, Magdalena C., et al.
Publicado: (2023) -
Exposure of bipartite hydrophobic signal triggers nuclear quality control of Ndc10 at the endoplasmic reticulum/nuclear envelope
por: Furth, Noa, et al.
Publicado: (2011) -
Mutation of exposed hydrophobic amino acids to arginine to increase protein stability
por: Strub, Caroline, et al.
Publicado: (2004)