Results 31 to 40 of about 194,539 (300)

An ORFeome of rice E3 ubiquitin ligases for global analysis of the ubiquitination interactome

Genome Biology, 2022
Background Ubiquitination is essential for many cellular processes in eukaryotes, including 26S proteasome-dependent protein degradation, cell cycle progression, transcriptional regulation, and signal transduction.
Ruyi Wang, Xiaoman You, Chongyang Zhang, Hong Fang, Min Wang, Fan Zhang, Houxiang Kang, Xiao Xu, Zheng Liu, Jiyang Wang, Qingzhen Zhao, Xuli Wang, Zeyun Hao, Feng He, Hui Tao, Debao Wang, Jisong Wang, Liang Fang, Mengchao Qin, Tianxiao Zhao, Pingping Zhang, Hefei Xing, Yunping Xiao, Wende Liu, Qi Xie, Guo-Liang Wang, Yuese Ning   +26 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
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Structure-guided design and optimization of small molecules targeting the protein-protein interaction between the von hippel-lindau (VHL) E3 ubiquitin ligase and the hypoxia inducible factor (HIF) alpha subunit with in vitro nanomolar affinities [PDF]

, 2014
E3 ubiquitin ligases are attractive targets in the ubiquitin-proteasome system, however, the development of small-molecule ligands has been rewarded with limited success.
Dias, David M, Carles Galdeano (1305135), Galdeano, Carles, Dias, David M., David M. Dias (1340694), Van Molle, Inge, Gadd, Morgan Stuart, Ciulli, Alessio, Sarah Hewitt (1340700), Soares, Pedro, Galdeano , Carles, Pedro Soares (393566), Gadd, Morgan S., Salvatore Scaffidi (1340703), Inge Van Molle (1284120), Morgan S. Gadd (149371), Scaffidi, Salvatore, Ipek Birced (1340697), Alessio Ciulli (762789), Hewitt, Sarah, Birced, Ipek   +20 more
core   +1 more source

Functional Diversity and Structural Disorder in the Human Ubiquitination Pathway [PDF]

, 2013
The ubiquitin-proteasome system plays a central role in cellular regulation and protein quality control (PQC). The system is built as a pyramid of increasing complexity, with two E1 (ubiquitin activating), few dozen E2 (ubiquitin conjugating) and several
Mainak Guharoy, Rita Pancsa (173029), Pallab Bhowmick, Tompa, Péter, Pallab Bhowmick (416342), Peter Tompa, Bhowmick, Pallab, Pancsa Rita, Guharoy Mainak, Bhowmick Pallab, Tompa Peter, Guharoy, Majnak, Mainak Guharoy (416343), Peter Tompa (38445), Rita Pancsa, Pancsa, Rita   +15 more
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Exploration of Aberrant E3 Ligases Implicated in Alzheimer’s Disease and Development of Chemical Tools to Modulate Their Function

Frontiers in Cellular Neuroscience, 2021
The Ubiquitin Proteasome System (UPS) is responsible for the degradation of misfolded or aggregated proteins via a multistep ATP-dependent proteolytic mechanism. This process involves a cascade of ubiquitin (Ub) transfer steps from E1 to E2 to E3 ligase.
Frances M. Potjewyd, Alison D. Axtman
doaj   +1 more source

Trim17, novel E3 ubiquitin-ligase, initiates neuronal apoptosis [PDF]

, 2010
Accumulating data indicate that the ubiquitin-proteasome system controls apoptosis by regulating the level and the function of key regulatory proteins. In this study, we identified Trim17, a member of the TRIM/RBCC protein family, as one of the critical ...
Rahmeh, R, Magiera, M, Ham, Jonathan, M Kristiansen, Kristiansen, Mark, Ham, J, Desagher, Solange, Lipkin, A, Desagher, S., Rahmeh, Rita, Mora, Stéphan, M M Magiera, Vanhille, Laurent, Pettmann, B, Lipkin, Alexey, Mora, S, Lipkin, A., Kristiansen, M, Robbins, Ian, S Mora, Ham, J., R Rahmeh, Rahmeh, R., A Lipkin, Pettmann, Brigitte, Robbins, I., Mora, S., Lassot, I., Desagher, S, Lassot, I, Magiera, Maria Magdalena, Magiera, M. M., L Vanhille, Jaudon, F, I Lassot, Vanhille, L., Jaudon, F., S Desagher, Jaudon, Fanny, Lassot, Irina, Kristiansen, M., F Jaudon, Pettmann, B., Vanhille, L, Robbins, I, J Ham, I Robbins, B Pettmann   +47 more
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Cryo-EM structures of Gid12-bound GID E3 reveal steric blockade as a mechanism inhibiting substrate ubiquitylation

Nature Communications, 2022
The GID E3 ligase regulates glucose-induced degradation in yeast, and key physiology. This study unveils E3 ligase regulation by reshaping the substrate binding site, blocking substrate access to ubiquitination active sites, and a Cage-like assembly.
Shuai Qiao, Chia-Wei Lee, Dawafuti Sherpa, Jakub Chrustowicz, Jingdong Cheng, Maximilian Duennebacke, Barbara Steigenberger, Ozge Karayel, Duc Tung Vu, Susanne von Gronau, Matthias Mann, Florian Wilfling, Brenda A. Schulman   +12 more
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Genome-Wide Identification of the U-Box E3 Ubiquitin Ligase Gene Family in Cabbage (Brassica oleracea var. capitata) and Its Expression Analysis in Response to Cold Stress and Pathogen Infection

Plants, 2023
Plant U-box E3 ubiquitin ligases (PUBs) play an important role in growth, development, and stress responses in many species. However, the characteristics of U-box E3 ubiquitin ligase genes in cabbage (Brassica oleracea var.
Peiwen Wang, Lin Zhu, Ziheng Li, Mozhen Cheng, Xiuling Chen, Aoxue Wang, Chao Wang, Xiaoxuan Zhang   +7 more
doaj   +1 more source

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
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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