Results 271 to 280 of about 120,389 (309)

Ubiquitination on Nonlysine Residues by a Viral E3 Ubiquitin Ligase

Science, 2005
Ubiquitination controls a broad range of cellular functions. The last step of the ubiquitination pathway is regulated by enzyme type 3 (E3) ubiquitin ligases. E3 enzymes are responsible for substrate specificity and catalyze the formation of an isopeptide bond between a lysine residue of the substrate (or the N terminus of the ...
Ken, Cadwell, Laurent, Coscoy
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RNF220, an E3 ubiquitin ligase that targets Sin3B for ubiquitination

Biochemical and Biophysical Research Communications, 2010
Modification of proteins by ubiquitination plays important roles in various cellular processes. During this process, the target specificity is determined by ubiquitin ligases. Here we identify RNF220 (RING finger protein 220) as a novel ubiquitin ligase for Sin3B. As a conserved RING protein, RNF220 can bind E2 and mediate auto-ubiquitination of itself.
Qinghua, Kong, Wanli, Zeng, Jingyang, Wu, Wanling, Hu, Chaocui, Li, Bingyu, Mao   +5 more
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Structure of the human UBR5 E3 ubiquitin ligase

Structure, 2022
ABSTRACT The human UBR5 (also known as EDD) is a single polypeptide chain HECT-type E3 ubiquitin ligase essential for embryonic development in mammals. Although widely expressed, UBR5 is markedly amplified and overexpressed in breast, ovarian, prostate, gastric and pancreatic ...
Feng Wang, Qing He, Wenhu Zhan, Ziqi Yu, Efrat Finkin-Groner, Xiaojing Ma, Gang Lin, Huilin Li   +7 more
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HECT-Type E3 Ubiquitin Ligases in Cancer

Trends in Biochemical Sciences, 2019
Ubiquitination, a post-translational modification that involves a covalent attachment of ubiquitin to a protein substrate, is essential for cellular homeostatic maintenance. At the end of a three-enzyme cascade, E3 ubiquitin ligases (E3s) recruit substrates and promote or directly catalyze ubiquitin transfer to targets.
Francesca Bernassola, Giovanni Chillemi, Gerry Melino   +2 more
openaire   +5 more sources

Inhibitors for E3 ubiquitin ligases

Nature Biotechnology, 2010
Two studies show that specific cullin-RING E3 ubiquitin ligases can be targeted with small molecules.
John R Lydeard, J Wade Harper
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E3 ubiquitin ligase that recognizes sugar chains

Nature, 2002
N-glycosylation of proteins in the endoplasmic reticulum (ER) has a central role in protein quality control. Here we report that N-glycan serves as a signal for degradation by the Skp1-Cullin1-Fbx2-Roc1 (SCF(Fbx2)) ubiquitin ligase complex. The F-box protein Fbx2 (ref. 4) binds specifically to proteins attached to N-linked high-mannose oligosaccharides
Yukiko, Yoshida, Tomoki, Chiba, Fuminori, Tokunaga, Hiroshi, Kawasaki, Kazuhiro, Iwai, Toshiaki, Suzuki, Yukishige, Ito, Koji, Matsuoka, Minoru, Yoshida, Keiji, Tanaka, Tadashi, Tai   +10 more
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Role of E3 ubiquitin ligases in insulin resistance

Diabetes, Obesity and Metabolism, 2016
E3 ubiquitin ligases are a large family of proteins that catalyse the ubiquitination of many proteins for degradation by the 26S proteasome. E3 ubiquitin ligases play pivotal roles in the process of insulin resistance and diabetes.
X-D, Yang, D-X, Xiang, Y-Y, Yang
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E3 ubiquitin ligases in cancer and implications for therapies

Cancer and Metastasis Reviews, 2017
E3 ligases are a class of enzymes that can transfer ubiquitin to substrates for their degradation, which are of importance in cellular homeostasis. Since many oncogenic or tumor-suppressive proteins are reported to be regulated by the ubiquitin-proteasome system (UPS), E3 ligases, which function as substrate interacting modules, have been attracting ...
Dong, Wang, Leina, Ma, Bin, Wang, Jia, Liu, Wenyi, Wei   +4 more
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A portrayal of E3 ubiquitin ligases and deubiquitylases in cancer

International Journal of Cancer, 2013
E3 ubiquitin ligases and deubiquitylating enzymes (DUBs) are the key components of ubiquitin proteasome system which plays a critical role in cellular protein homeostasis. Any shortcoming in their biological roles can lead to various diseases including cancer.
Yatendra Kumar, Satija, Abhishek, Bhardwaj, Sanjeev, Das   +2 more
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E3 ubiquitin ligases and mitosis: embracing the complexity

Trends in Cell Biology, 2008
Faithful division of eukaryotic cells requires temporal and spatial coordination of morphological transitions, which ensures that the newly replicated copies of the genome are equally distributed into the two daughter cells during mitosis. One of the mechanisms ensuring the fidelity of mitotic progression is targeted, ubiquitin-dependent proteolysis of
Sumara I, Maerki S, Peter M
openaire   +3 more sources