Results 1 to 10 of about 197,780 (305)

Genome-wide identification and transcriptome profiling reveal that E3 ubiquitin ligase genes relevant to ethylene, auxin and abscisic acid are differentially expressed in the fruits of melting flesh and stony hard peach varieties

BMC Genomics, 2019
Background Ubiquitin ligases (E3) are the enzymes in the ubiquitin/26S proteasome pathway responsible for targeting proteins to the degradation pathway and play major roles in multiple biological activities. However, the E3 family and their functions are
Bin Tan, Xiaodong Lian, Jun Cheng, Wenfang Zeng, Xianbo Zheng, Wei Wang, Xia Ye, Jidong Li, Zhiqian Li, Langlang Zhang, Jiancan Feng   +10 more
doaj   +1 more source

Regulation of reactive oxygen species during plant immunity through phosphorylation and ubiquitination of RBOHD. [PDF]

, 2020
Production of reactive oxygen species (ROS) is critical for successful activation of immune responses against pathogen infection. The plant NADPH oxidase RBOHD is a primary player in ROS production during innate immunity. However, how RBOHD is negatively
Castro, Bardo, Coaker, Gitta, Dinesh-Kumar, Savithramma P, Lal, Neeraj K, Lee, DongHyuk, Lin, Zuh-Jyh Daniel, Liu, Jun, Ma, Shisong, Toruño, Tania   +8 more
core   +1 more source

Trim25 restricts rabies virus replication by destabilizing phosphoprotein

Cell Insight, 2022
Tripartite motif-containing protein 25 (Trim25) is an E3 ubiquitin ligase that activates retinoid acid-inducible gene I (RIG-I) and promotes the antiviral interferon response.
Yueming Yuan, An Fang, Zongmei Wang, Bin Tian, Yuan Zhang, Baokun Sui, Zhaochen Luo, Yingying Li, Ming Zhou, Huanchun Chen, Zhen F. Fu, Ling Zhao   +11 more
doaj   +1 more source

Structural analysis of MDM2 RING separates degradation from regulation of p53 transcription activity [PDF]

, 2017
MDM2–MDMX complexes bind the p53 tumor-suppressor protein, inhibiting p53's transcriptional activity and targeting p53 for proteasomal degradation. Inhibitors that disrupt binding between p53 and MDM2 efficiently activate a p53 response, but their use in
A Plechanovová, A Plechanovová, Andreas K Hock, CS Chen, D Migliorini, D Shi, Danny T Huang, DC Scott, DE Christensen, Dominika Kowalczyk, E Branigan, E Meulmeester, Gary J Sibbet, H Dou, H Dou, H Kawai, H Kawai, I Ray-Coquard, J Momand, J Parant, JC Badciong, JD Oliner, JG Sanchez, JN Pruneda, K Itahana, K Linke, Karen H Vousden, KH Khoo, Koji Nomura, L Buetow, L Buetow, L Huang, LA Tollini, LC Storoni, LK Linares, LT Vassilev, M Andreeff, M Argentini, M Bista, M Kostic, Marta Klejnot, MG Koliopoulos, MHG Kubbutat, ML Choong, MS Dai, MS Dai, MV Poyurovsky, MW Jackson, N Minsky, N Zheng, P Dolezelova, P Emsley, P Roxburgh, PD Adams, PS Brzovic, Q Cheng, Q Cheng, Q Ding, R Honda, R Montes de Oca Luna, R Stad, R Stad, RA Finch, RK Geyer, S Iyappan, S Shangary, S Uldrijan, SN Jones, UM Moll, V Pant, W Kabsch, Y Pan   +71 more
core   +1 more source

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

Nature Communications, 2017
Protein stability modulation by E3 ubiquitin ligases is an important layer of functional regulation, but screening for E3 ligase-substrate interactions is time-consuming and costly.
Yang Li, Ping Xie, Liang Lu, Jian Wang, Lihong Diao, Zhongyang Liu, Feifei Guo, Yangzhige He, Yuan Liu, Qin Huang, Han Liang, Dong Li, Fuchu He   +12 more
doaj   +1 more source

Roles of the TRAF6 and Pellino E3 ligases in MyD88 and RANKL signaling [PDF]

, 2017
It is widely accepted that the essential role of TRAF6 in vivo is to generate the Lys63-linked ubiquitin (K63-Ub) chains needed to activate the "master" protein kinase TAK1.
Arthur, J. Simon C., Cohen, Philip, Emmerich, Christoph H., Goh, Eddy T. H., Hastie, C. James, Kelsall, Ian R., Knebel, Axel, Macartney, Thomas, Marchesi, Francesco, Peggie, Mark, Strickson, Sam, Zhang, Jiazhen   +11 more
core   +3 more sources

Lafora disease offers a unique window into neuronal glycogen metabolism [PDF]

, 2018
Lafora disease (LD) is a fatal, autosomal recessive, glycogen-storage disorder that manifests as severe epilepsy. LD results from mutations in the gene encoding either the glycogen phosphatase laforin or the E3 ubiquitin ligase malin. Individuals with LD
Gentry, Matthew S., Guinovart, Joan J., Minassian, Berge A., Roach, Peter J., Serratosa, Jose M.   +4 more
core   +2 more sources

Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications [PDF]

, 2012
Conjugation of ubiquitin to proteins (ubiquitylation) has emerged to be one of the most crucial post-translational modifications controlling virtually all cellular processes.
Fulda, Simone, Rajalingam, Krishnaraj, Dikic, Ivan   +2 more
core   +2 more sources

Differential PROTAC substrate specificity dictated by orientation of recruited E3 ligase

Nature Communications, 2019
PROTACs enable targeted protein degradation by recruiting an E3 ligase to a specific substrate but the determinants of selectivity are not fully understood.
Blake E. Smith, Stephen L. Wang, Saul Jaime-Figueroa, Alicia Harbin, Jing Wang, Brian D. Hamman, Craig M. Crews   +6 more
doaj   +1 more source

A Cullin1-based SCF E3 ubiquitin ligase targets the InR/PI3K/TOR pathway to regulate neuronal pruning.

PLoS Biology, 2013
Pruning that selectively eliminates unnecessary axons/dendrites is crucial for sculpting the nervous system during development. During Drosophila metamorphosis, dendrite arborization neurons, ddaCs, selectively prune their larval dendrites in response to
Jack Jing Lin Wong, Song Li, Edwin Kok Hao Lim, Yan Wang, Cheng Wang, Heng Zhang, Daniel Kirilly, Chunlai Wu, Yih-Cherng Liou, Hongyan Wang, Fengwei Yu   +10 more
doaj   +1 more source