| Chapter title |
Cullin-RING E3 Ubiquitin Ligases: Bridges to Destruction
|
|---|---|
| Chapter number | 12 |
| Book title |
Macromolecular Protein Complexes
|
| Published in |
Sub cellular biochemistry, March 2017
|
| DOI | 10.1007/978-3-319-46503-6_12 |
| Pubmed ID | |
| Book ISBNs |
978-3-31-946501-2, 978-3-31-946503-6
|
| Authors |
Henry C. Nguyen, Wei Wang, Yong Xiong, Nguyen, Henry C., Wang, Wei, Xiong, Yong |
| Editors |
J. Robin Harris, Jon Marles-Wright |
| Abstract |
Ubiquitination is a highly conserved post-translational modification in eukaryotes, well known for targeting proteins for degradation by the 26S proteasome. Proteins destined for proteasomal degradation are selected by E3 ubiquitin ligases. Cullin-RING E3 ubiquitin ligases (CRLs) are the largest superfamily of E3 ubiquitin ligases, with over 400 members known in mammals. These modular complexes are tightly regulated in the cell. In this chapter, we highlight recent structural and biochemical advances shedding light on the assembly and architecture of cullin-RING ligases, their dynamic regulation by a variety of host factors, and their manipulation by viral pathogens and small molecules. |
Mendeley readers
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 99 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 23 | 23% |
| Student > Bachelor | 13 | 13% |
| Researcher | 9 | 9% |
| Student > Master | 7 | 7% |
| Student > Doctoral Student | 2 | 2% |
| Other | 3 | 3% |
| Unknown | 42 | 42% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 32 | 32% |
| Chemistry | 6 | 6% |
| Agricultural and Biological Sciences | 6 | 6% |
| Immunology and Microbiology | 4 | 4% |
| Neuroscience | 3 | 3% |
| Other | 7 | 7% |
| Unknown | 41 | 41% |