Results 51 to 60 of about 248,165 (360)

Linear ubiquitin chains: enzymes, mechanisms and biology [PDF]

Open Biology, 2017
Ubiquitination is a versatile post-translational modification that regulates a multitude of cellular processes. Its versatility is based on the ability of ubiquitin to form multiple types of polyubiquitin chains, which are recognized by specific ...
Katrin Rittinger, Fumiyo Ikeda
doaj   +1 more source

The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells

Proceedings of the National Academy of Sciences of the United States of America, 2019
Significance The formation of isopeptide bonds between the C-terminal carboxylate of ubiquitin and ε-amino groups of lysine residues on another protein is a major mechanism for regulating protein function. Ubiquitin can also form peptide bonds with the N-
Ian R. Kelsall, Jiazhen Zhang, A. Knebel, J. Arthur, P. Cohen   +4 more
semanticscholar   +1 more source

RMND5 from Xenopus laevis is an E3 ubiquitin-ligase and functions in early embryonic forebrain development. [PDF]

PLoS ONE, 2015
In Saccharomyces cerevisiae the Gid-complex functions as an ubiquitin-ligase complex that regulates the metabolic switch between glycolysis and gluconeogenesis.
Thorsten Pfirrmann, Pablo Villavicencio-Lorini, Abinash K Subudhi, Ruth Menssen, Dieter H Wolf, Thomas Hollemann   +5 more
doaj   +1 more source

The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3

Nature Communications, 2016
The NLRP3 inflammasome has a fundamental role in host defence against microbial pathogens and its deregulation may cause diverse inflammatory diseases. NLRP3 protein expression is a rate-limiting step for inflammasome activation, thus its expression must
Hui Song, Bingyu Liu, Wanwan Huai, Zhongxia Yu, Wenwen Wang, Jing Zhao, Lihui Han, G. Jiang, Lining Zhang, Chengjiang Gao, Wei Zhao   +10 more
semanticscholar   +1 more source

Identification of a MicroRNA‐E3 Ubiquitin Ligase Regulatory Network for Hepatocyte Death in Alcohol‐Associated Hepatitis

Hepatology Communications, 2021
We aimed to identify a microRNA (miRNA)‐E3 ubiquitin ligase regulatory network for protein substrates enriched in cell death pathways and investigate the underlying molecular mechanisms in alcohol‐associated hepatitis (AH).
Xiude Fan, Jianguo Wu, Kyle L. Poulsen, Adam Kim, Xiaoqin Wu, Emily Huang, Tatsunori Miyata, Carlos Sanz‐Garcia, Laura E. Nagy   +8 more
doaj   +1 more source

An integrated bioinformatics platform for investigating the human E3 ubiquitin ligase-substrate interaction network

Nature Communications, 2017
The ubiquitination mediated by ubiquitin activating enzyme (E1), ubiquitin conjugating enzyme (E2), and ubiquitin ligase (E3) cascade is crucial to protein degradation, transcription regulation, and cell signaling in eukaryotic cells.
Yang Li, P. Xie, Liang Lu, Jian Wang, Lihong Diao, Zhongyang Liu, Feifei Guo, Yangzhige He, Yuan Liu, Qin Huang, Han Liang, Dong Li, F. He   +12 more
semanticscholar   +1 more source

G Protein Mono-ubiquitination by the Rsp5 Ubiquitin Ligase [PDF]

Journal of Biological Chemistry, 2009
Emerging evidence suggests that ubiquitination serves as a protein trafficking signal in addition to its well characterized role in promoting protein degradation. The yeast G protein α subunit Gpa1 represents a rare example of a protein that undergoes both mono- and poly-ubiquitination.
Brian Kuhlman, Michael J. Lee, Carrie Purbeck, Nikolay V. Dokholyan, Matthew P. Torres, Henrik G. Dohlman, Feng Ding   +6 more
openaire   +3 more sources

The E3 ubiquitin ligase RNF185 facilitates the cGAS-mediated innate immune response

PLoS Pathogens, 2017
The cyclic GMP-AMP synthase (cGAS), upon cytosolic DNA stimulation, catalyzes the formation of the second messenger 2′3′-cGAMP, which then binds to stimulator of interferon genes (STING) and activates downstream signaling. It remains to be elucidated how
Qiang Wang, Liyuan Huang, Ze Hong, Zhongshi Lv, Zhaomin Mao, Yijun Tang, X. Kong, Senlin Li, Ye Cui, Heng Liu, Lele Zhang, Xiaojie Zhang, Lindi Jiang, Chen Wang, Qin Zhou   +14 more
semanticscholar   +1 more source

Regulation of the CRL4Cdt2 Ubiquitin Ligase and Cell-Cycle Exit by the SCFFbxo11 Ubiquitin Ligase [PDF]

Molecular Cell, 2013
F-box proteins and DCAF proteins are the substrate binding subunits of the Skp1-Cul1-F-box protein (SCF) and Cul4-RING protein ligase (CRL4) ubiquitin ligase complexes, respectively. Using affinity purification and mass spectrometry, we determined that the F-box protein FBXO11 interacts with CDT2, a DCAF protein that controls cell-cycle progression ...
Moritz Horn, Shanshan Duan, Shanshan Duan, Adam Antebi, Michele Pagano, Michele Pagano, Anita Saraf, Michael P. Washburn, Michael P. Washburn, Mario Rossi, Laurence Florens, Yeon-Tae Jeong   +11 more
openaire   +5 more sources

RING Domain E3 Ubiquitin Ligases [PDF]

Annual Review of Biochemistry, 2009
E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate. The activity of most E3s is specified by a RING domain, which binds to an E2∼ubiquitin thioester and activates discharge of its ubiquitin cargo.
Deshaies, Raymond J., Joazeiro, Claudio A. P.   +1 more
openaire   +4 more sources