Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases.
By N. Zheng, Ping Wang, P. Jeffrey, N. Pavletich. Cell, 2000
906 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/24f946b8b8acec9a072a74428e0e3bdd2fc5d4a9
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Molecular Biology
- Aaron Ciechanover
- C. Pickart
- C. Joazeiro
- A. Weissman
- M. Glickman
- M. Eddins
- Graciana Diez-Roux
- R. Deshaies
In Oncology
- Aaron Ciechanover
- M. Eddins
- M. Glickman
- C. Joazeiro
- A. Weissman
- C. Pickart
- Donna D. Zhang
- D. Komander
Citations in the corpus
- Ubiquitin: structures, functions, mechanisms. (2004, background): “(A) RING domain [45]; (B) PHD [92]; (C) U-box [110].”
- Functional Analysis of the RING-Type Ubiquitin Ligase Family of Arabidopsis1[w] (2005, background): “Trp-408 of c-CBL is also involved in E2 binding and is required for E3 ligase activity (Joazeiro et al., 1999; Zheng et al., 2000).”
- RING domain E3 ubiquitin ligases. (2009, background): “(42), the residues at the core of the c-Cbl-UbcH7 interface are sometimes completely different in other E3-E2 pairs.”