Results 21 to 30 of about 149,506 (292)

TRIM56 coiled-coil domain structure provides insights into its E3 ligase functions

Computational and Structural Biotechnology Journal, 2023
Protein ubiquitination is a post-translation modification mediated by E3 ubiquitin ligases. The RING domain E3 ligases are the largest family of E3 ubiquitin ligases, they act as a scaffold, bringing the E2-ubiquitin complex and its substrate together to
Xiaohua Lou, Binbin Ma, Yuan Zhuang, Xiang Xiao, Laurie J. Minze, Junji Xing, Zhiqiang Zhang, Xian C. Li   +7 more
doaj   +1 more source

Structural studies of the coiled-coil domain of TRIM75 reveal a tetramer architecture facilitating its E3 ligase complex

Computational and Structural Biotechnology Journal, 2022
Protein ubiquitination plays a vital role in controlling the degradation of intracellular proteins and in regulating cell signaling pathways. Functionally, E3 ubiquitin ligases control the transfer of ubiquitin to the target substrates. As a major family
Xiaohua Lou, Binbin Ma, Yuan Zhuang, Xiang Xiao, Laurie J. Minze, Junji Xing, Zhiqiang Zhang, Xian C. Li   +7 more
doaj   +1 more source

E3 ubiquitin ligases in signaling, disease, and therapeutics. [PDF]

Trends Biochem Sci
The ubiquitin-proteasome system (UPS) is a central regulator of protein turnover and signaling, with E3 ubiquitin ligases conferring substrate specificity and chain-type control. Recent advances have revealed new mechanistic classes of E3 ligases and expanded our understanding of their roles in disease, including cancer, neurodegeneration, and immune ...
Ebadi P, Stratton CM, Olsen SK.
europepmc   +3 more sources

From Drosophila to Human: Biological Function of E3 Ligase Godzilla and Its Role in Disease

Cells, 2022
The ubiquitin–proteasome system is of fundamental importance in all fields of biology due to its impact on proteostasis and in regulating cellular processes.
Valérie C. Cabana, Marc P. Lussier
doaj   +1 more source

Activation of the E3 ubiquitin ligase Parkin [PDF]

Biochemical Society Transactions, 2015
The PINK1 (phosphatase and tensin homologue-induced putative kinase 1)/Parkin-dependent mitochondrial quality control pathway mediates the clearance of damaged organelles, but appears to be disrupted in Parkinson's disease (PD) [Springer and Kahle (2011) Autophagy 7, 266–278].
Thomas R, Caulfield, Fabienne C, Fiesel, Wolfdieter, Springer   +2 more
openaire   +2 more sources

E3 Ubiquitin Ligases in Breast Cancer Metastasis: A Systematic Review of Pathogenic Functions and Clinical Implications

Frontiers in Oncology, 2021
Female breast cancer has become the most commonly occurring cancer worldwide. Although it has a good prognosis under early diagnosis and appropriate treatment, breast cancer metastasis drastically causes mortality.
Yingshuang Wang, Yingshuang Wang, Jiawen Dai, Jiawen Dai, Youqin Zeng, Youqin Zeng, Jinlin Guo, Jinlin Guo, Jie Lan   +8 more
doaj   +1 more source

AIRE Functions As an E3 Ubiquitin Ligase [PDF]

The Journal of Experimental Medicine, 2004
Autoimmune regulator (AIRE) gene mutation is responsible for the development of autoimmune-polyendocrinopathy-candidiasis ectodermal dystrophy, an organ-specific autoimmune disease with monogenic autosomal recessive inheritance. AIRE is predominantly expressed in medullary epithelial cells of the thymus and is considered to play important roles in the ...
Uchida, Daisuke, Hatakeyama, Shigetsugu, Matsushima, Akemi, Han, Hongwei, Ishido, Satoshi, Hotta, Hak, Kudoh, Jun, Shimizu, Nobuyoshi, Doucas, Vassilis, Nakayama, Keiichi I., Kuroda, Noriyuki, Matsumoto, Mitsuru   +11 more
openaire   +2 more sources

WWP2 is an E3 ubiquitin ligase for PTEN [PDF]

Nature Cell Biology, 2011
PTEN, a lipid phosphatase, is one of the most frequently mutated tumour suppressors in human cancer. Several recent studies have highlighted the importance of ubiquitylation in regulating PTEN tumour-suppressor function, but the enzymatic machinery required for PTEN ubiquitylation is not clear.
Subbareddy, Maddika, Sridhar, Kavela, Neelam, Rani, Vivek Reddy, Palicharla, Jenny L, Pokorny, Jann N, Sarkaria, Junjie, Chen   +6 more
openaire   +2 more sources

Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases. [PDF]

, 2013
Cullin-RING ligases are multisubunit E3 ubiquitin ligases that recruit substrate-specific adaptors to catalyze protein ubiquitylation. Cul3-based Cullin-RING ligases are uniquely associated with BTB adaptors that incorporate homodimerization, Cul3 ...
Bullock, AN, Canning, P, Marsden, BD, Gileadi, Opher, Gileadi, O, Krojer, Tobias, Pike, AC, von Delft, F, Hojzan, V, Thangaratnarajah, C, Murray, James W., Cooper, CD, Keates, Tracy, Thangaratnarajah, Chancievan, Bullock, Alex N., Knapp, Stefan, Marsden, Brian D., Knapp, S, Hojzan, Viktorija, Murray, JW, von Delft, Frank, Chaikuad, A, Keates, T, Ayinampudi, Vikram, Ayinampudi, V, Pike, Ashley C.W., Chaikuad, Apirat, Krojer, T, Canning, Peter, Cooper, Christopher D.O., Bullock, Alexander   +30 more
core   +1 more source

SUMO chain-induced dimerization activates RNF4 [PDF]

, 2014
Dimeric RING E3 ligases interact with protein substrates and conformationally restrain the ubiquitin-E2-conjugating enzyme thioester complex such that it is primed for catalysis.
Hay, Ronald T, Rojas-Fernandez, Alejandro, Hattersley, Neil, Plechanovová, Anna, Tatham, Michael H, Jaffray, Ellis   +5 more
core   +1 more source