Beyond K48 and K63: non-canonical protein ubiquitination
Abstract Protein ubiquitination has become one of the most extensively studied post-translational modifications. Originally discovered as a critical element in highly regulated proteolysis, ubiquitination is now regarded as essential for many other cellular processes. This results from the unique fe...
Main Authors: | Michal Tracz, Wojciech Bialek |
---|---|
Format: | Article |
Language: | English |
Published: |
BMC
2021-01-01
|
Series: | Cellular & Molecular Biology Letters |
Subjects: | |
Online Access: | https://doi.org/10.1186/s11658-020-00245-6 |
Similar Items
-
E3 Ubiquitin Ligase SPL2 Is a Lanthanide-Binding Protein
by: Michał Tracz, et al.
Published: (2021-05-01) -
Ubiquitination in the ERAD Process
by: Anna Lopata, et al.
Published: (2020-07-01) -
Hepatitis B Core Protein Is Post-Translationally Modified through K29-Linked Ubiquitination
by: Hana Langerová, et al.
Published: (2020-11-01) -
The poxvirus ubiquitin ligase p28 manipulates the ubiquitin proteasome system
by: Mottet, Kelly
Published: (2010) -
The Challenge of Producing Ubiquitinated Proteins for Structural Studies
by: Serena Faggiano, et al.
Published: (2014-06-01)