Cellular functions and molecular mechanisms of non-lysine ubiquitination
Protein ubiquitination is of great cellular importance through its central role in processes such as degradation, DNA repair, endocytosis and inflammation. Canonical ubiquitination takes place on lysine residues, but in the past 15 years non-lysine ubiquitination on serine, threonine and cysteine ha...
Main Authors: | Amie J. McClellan, Sophie Heiden Laugesen, Lars Ellgaard |
---|---|
Format: | Article |
Language: | English |
Published: |
The Royal Society
2019-09-01
|
Series: | Open Biology |
Subjects: | |
Online Access: | https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.190147 |
Similar Items
-
Targeting of Ubiquitin E3 Ligase RNF5 as a Novel Therapeutic Strategy in Neuroectodermal Tumors
by: Elisa Principi, et al.
Published: (2022-04-01) -
Ubiquitin Ligase Redundancy and Nuclear-Cytoplasmic Localization in Yeast Protein Quality Control
by: Carolyn Allain Breckel, et al.
Published: (2021-12-01) -
Emerging roles of the HECT-type E3 ubiquitin ligases in hematological malignancies
by: Vincenza Simona Delvecchio, et al.
Published: (2021-10-01) -
Targeted Protein Degradation Systems: Controlling Protein Stability Using E3 Ubiquitin Ligases in Eukaryotic Species
by: Yoshitaka Ogawa, et al.
Published: (2024-01-01) -
The Ubiquitin Proteasome System and Nutrient Stress Response
by: Erin Mackinnon, et al.
Published: (2022-05-01)