Results 91 to 100 of about 72,591 (191)

The Acidic Tail of the Cdc34 Ubiquitin-conjugating Enzyme Functions in Both Binding to and Catalysis with Ubiquitin Ligase SCFC^(dc4*) [PDF]

, 2009
Ubiquitin ligases, together with their cognate ubiquitin-conjugating enzymes, are responsible for the ubiquitylation of proteins, a process that regulates a myriad of eukaryotic cellular functions. The first cullin-RING ligase discovered, yeast SCF^(Cdc4)
Bing Hao, Block, Cardozo, Creighton, Dane A. Mohl, Das, Deshaies, Dye, Eletr, Feldman, Frescas, Gary Kleiger, Gill, Gill, Hershko, Hofmann, Kamura, Kleiger, Kolman, Koppenol, Li, Li, Mathias, Nakayama, Ohta, Pan, Petroski, Petroski, Petroski, Pohl, Raymond J. Deshaies, Ruiz, Saha, Schoppink, Schreiber, Schreiber, Schwob, Seol, Silver, Skowyra, Skowyra, Tan, Thrower, Van Loon, Willems, Wu, Xie, Yang, Zheng   +48 more
core   +3 more sources

Repair or destruction: an intimate liaison between ubiquitin ligases and molecular chaperones in proteostasis [PDF]

, 2017
Cellular differentiation, developmental processes, and environmental factors challenge the integrity of the proteome in every eukaryotic cell. The maintenance of protein homeostasis, or proteostasis, involves folding and degradation of damaged proteins ...
Amerik, Anckar, Apaja, Arndt, Arndt, Aviram, Balch, Ballinger, Bar-Lavan, Barrott, Bartel, Bays, Becuwe, Behrends, Bengtson, Boban, Boban, Bodnar, Boomsma, Bordallo, Brandman, Brehme, Broersen, Buchner, Calderwood, Carra, Catlett, Choe, Christianson, Chu, Ciechanover, Ciocca, Ciryam, Commerford, Connell, Craig, Crippa, Crosas, Cuervo, Cuervo, Cyr, Dai, Davies, Defenouillere, Deng, Deyter, Donati, Douglas, Douglas, Dunker, Duttler, Ehrlich, Eisele, Ellis, Fan, Fang, Fang, Fang, Fang, Ferreira, Finley, Finley, Foresti, Fourie, Fredrickson, Gallagher, Gamerdinger, Gardner, Garrido, Goldberg, Guerriero, Guo, Han, Hartl, Hatakeyama, Heck, Hemmingsen, Hessa, Hettema, Higy, Hondele, Hondele, Hoppe, Iwata, Jana, Jego, Jiang, Jin, Joshi, Kahn, Kampinga, Kaplan, Katsogiannou, Kaushik, Kaushik, Keller, Kenyon, Kerscher, Kettern, Khmelinskii, Kim, Kitagawa, Koegl, Komander, Koren, Kraft, Kuhlbrodt, Kuhlbrodt, Kumar, Kuo, Kwon, Laba, Labbadia, Lakshmipathy, Lee, Lerch-Bader, Levine, Li, Li, Lopez, Lopez-Otin, MacGurn, Maier, Matsumura, Mattiroli, Maurer, McDonough, Meacham, Mehnert, Meng, Merz, Metzger, Min, Mishra, Mizushima, Morano, Morimoto, Morimoto, Morimoto, Morishima, Murata, Murata, Nahleh, Nillegoda, Nillegoda, Nillegoda, Park, Park, Paul, Petrucelli, Powers, Powers, Prasad, Qian, Ranford, Rape, Ravid, Rees, Roberts, Roberts, Rodina, Rodrigo-Brenni, Rosenbaum, Ruggiano, Russell, Rüb, Rüdiger, Saez, Saibil, Salminen, Samant, Schopf, Shahsavarani, Shao, Shiber, Shiga, Shin, Singh, Singh, Singh, Soss, Sowa, Spiechowicz, Stuttmann, Sulistio, Sultana, Summers, Sung, Swanson, Taipale, Takayama, Tasaki, Tasaki, Tawo, Taylor, Terman, Tzankov, Ulbricht, Urushitani, VanPelt, Venkatesh, Verma, Vilchez, Walther Dirk, Wang, Wang, Willhoft, Williams, Xie, Xu, Xu, Yonashiro, Yu, Zargari, Zhang, Zhang, Zhao, Zhao, Zhou, Zuehlke, Zuiderweg   +220 more
core   +1 more source

Identification of suitable target/E3 ligase pairs for PROTAC development using a rapamycin-induced proximity assay (RiPA)

eLife
The development of proteolysis targeting chimeras (PROTACs), which induce the degradation of target proteins by bringing them into proximity with cellular E3 ubiquitin ligases, has revolutionized drug development. While the human genome encodes more than
Bikash Adhikari, Katharina Schneider, Mathias Diebold, Christoph Sotriffer, Elmar Wolf   +4 more
doaj   +1 more source

USP15 targets ALK3/BMPR1A for deubiquitylation to enhance bone morphogenetic protein signalling [PDF]

, 2014
Protein kinase ALK3/BMPR1A mediates bone morphogenetic protein (BMP) signalling through phosphorylation and activation of SMADs 1/5/8. SMAD6, a transcriptional target of BMP, negatively regulates the BMP pathway by recruiting E3 ubiquitin ligases and ...
Al-Salihi, Mazin A., Bruce, David, Cummins, Timothy D., Dingwell, Kevin S., Ewan, Richard, Herhaus, Lina, Macartney, Thomas, Sapkota, Gopal P., Smith, James C., Vogt, Janis, Wasmus, Lise, Weidlich, Simone   +11 more
core   +3 more sources

Arsenite binds to the RING finger domains of RNF20-RNF40 histone E3 ubiquitin ligase and inhibits DNA double-strand break repair. [PDF]

, 2014
Arsenic is a widespread environmental contaminant. However, the exact molecular mechanisms underlying the carcinogenic effects of arsenic remain incompletely understood.
Cai, Qian, Dai, Xiaoxia, Lin, Krystal, Paramasivam, Manikandan, Seidman, Michael M, Song, Jikui, Wang, Pengcheng, Wang, Yinsheng, Zhang, Fan   +8 more
core   +1 more source

E3 ubiquitin ligases in signaling, disease, and therapeutics

Trends in Biochemical Sciences
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 ...
Pirouz Ebadi, Caleb M. Stratton, Shaun K. Olsen   +2 more
openaire   +2 more sources

Targeting E3 ubiquitin ligases: a new frontier in idiopathic pulmonary fibrosis treatment

Frontiers in Immunology
Ubiquitination is a modification prevalent in eukaryotic cells. Disruptions in ubiquitination processes can have detrimental effects, potentially leading to diseases that endanger life.
Kun Zhang, Hui Yuan, Lin Shi
doaj   +1 more source

A multi-lock inhibitory mechanism for fine-tuning enzyme activities of the HECT family E3 ligases

Nature Communications, 2019
HECT type E3 ligases are key regulators of cell growth and proliferation. Here the authors present the crystal structures of the Nedd4 family E3 ligase WWP1 in a closed and semi-open state and in combination with mutagenesis experiments identify a multi ...
Zhen Wang, Ziheng Liu, Xing Chen, Jingyu Li, Weiyi Yao, Shijing Huang, Aihong Gu, Qun-Ying Lei, Ying Mao, Wenyu Wen   +9 more
doaj   +1 more source

Tomosyn Interacts with the SUMO E3 Ligase PIASγ

PLoS ONE, 2014
Protein modification by Small Ubiquitin-like MOdifier (SUMO) entities is involved in a number of neuronal functions, including synaptogenesis and synaptic plasticity. Tomosyn-1 (syntaxin-binding protein 5; STXPB5) binds to t-SNARE (Soluble NSF Attachment Protein Receptor) proteins to regulate neurotransmission and is one of the few neuronal SUMO ...
Geerts, C.J., Jacobsen, L., van de Bospoort, R., Verhage, M., Groffen, A.J.A.   +4 more
openaire   +5 more sources

E3 ubiquitin ligases: key regulators of osteogenesis and potential therapeutic targets for bone disorders

Frontiers in Cell and Developmental Biology
Ubiquitination is a crucial post-translational modification of proteins that mediates the degradation or functional regulation of specific proteins. This process participates in various biological processes such as cell growth, development, and signal ...
Heng-Rui Zhang, Heng-Rui Zhang, Yang-Hao Wang, Yang-Hao Wang, Zhen-Ping Xiao, Zhen-Ping Xiao, Guang Yang, Yun-Rong Xu, Zai-Tian Huang, Wei-Zhou Wang, Fei He   +10 more
doaj   +1 more source