Results 31 to 40 of about 67,820 (304)

How to Inactivate Human Ubiquitin E3 Ligases by Mutation

Frontiers in Cell and Developmental Biology, 2020
E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to substrate proteins, a process that determines the fate of the modified protein.
Cristina Garcia-Barcena, Nerea Osinalde, Juanma Ramirez, Ugo Mayor, Ugo Mayor   +4 more
doaj   +1 more source

A general strategy for discovery of inhibitors and activators of RING and U-box E3 ligases with ubiquitin variants [PDF]

, 2017
RING and U-box E3 ubiquitin ligases regulate diverse eukaryotic processes and have been implicated in numerous diseases, but targeting these enzymes remains a major challenge.
Ahmed, Syed Feroj, Buetow, Lori, Gabrielsen, Mads, Huang, Danny T., Nakasone, Mark A., Sibbet, Gary J., Sidhu, Sachdev S., Smith, Brian O., Zhang, Wei   +8 more
core   +3 more sources

Research Progress on the Role of E3 Ubiquitin Ligases in Regulating the Growth, Development and Stress Response of Fruits and Vegetables [PDF]

Shipin Kexue
Protein ubiquitination, an important post-translational modification, plays a wide role in the life activities of eukaryotic cells. E3 ubiquitin ligases specifically recognize target proteins in the ubiquitin-proteasome degradation system and play a ...
DING Jun, LI Fujun, LI Xiao’an, ZHANG Xinhua
doaj   +1 more source

A Generic Platform for Cellular Screening Against Ubiquitin Ligases [PDF]

, 2016
Ubiquitin signalling regulates most aspects of cellular life, thus deregulation of ubiquitylation has been linked with a number of diseases. E3 ubiquitin ligases provide substrate selectivity in ubiquitylation cascades and are therefore considered to be ...
AD Capili, CA Hong, CH Emmerich, D Kang, DF Ceccarelli, E Varfolomeev, F Mattiroli, I Dikic, J Bothos, JJ Sims, JR Skaar, JWM Nissink, K Acs, LT Vassilev, M Pulvino, MD Petroski, MF Murray, MS Luijsterburg, MSY Huen, N Mailand, P Cohen, P de Bie, Q Yin, R Hjerpe, R Verma, S Fields, S Orlicky, SJL van Wijk, SP Davies, T Hunter, V Plans, Y Sui   +31 more
core   +2 more sources

Ubiquitination, Biotech Startups, and the Future of TRIM Family Proteins: A TRIM-Endous Opportunity

Cells, 2021
Ubiquitination is a post-translational modification that has pivotal roles in protein degradation and diversified cellular processes, and for more than two decades it has been a subject of interest in the biotech or biopharmaceutical industry. Tripartite
Utsa Bhaduri, Giuseppe Merla
doaj   +1 more source

Genetically engineered mouse models for functional studies of SKP1-CUL1-F-box-protein (SCF) E3 ubiquitin ligases [PDF]

, 2013
The SCF (SKP1 (S-phase-kinase-associated protein 1), Cullin-1, F-box protein) E3 ubiquitin ligases, the founding member of Cullin-RING ligases (CRLs), are the largest family of E3 ubiquitin ligases in mammals.
Sun, Yi, Wei, Wenyi, Zhou, Weihua
core   +1 more source

RING Domain E3 Ubiquitin Ligases

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   +3 more sources

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.
Alejandro Rojas-Fernandez, Anna Plechanovová, Brzovic, Buchwald, Budhidarmo, Calderon-Villalobos, de Bie, Deshaies, Desterro, Desterro, Dou, Dou, Dueber, Ellis Jaffray, Feltham, Galanty, Geiss-Friedlander, Geoffroy, Geoffroy, Goddard, Goddard, Golebiowski, Guzzo, Haas, Hattersley, Hay, Hecker, Hickey, Johnson, Kang, Kravtsova-Ivantsiv, Lallemand-Breitenbach, Liew, Linke, Mace, Martin, Melchior, Michael H. Tatham, Mu, Mukhopadhyay, Mukhopadhyay, Neil Hattersley, Perry, Plechanovová, Plechanovová, Pruneda, Rodriguez, Ronald T. Hay, Saitoh, Sampson, Scheffner, Schermelleh, Shen, Song, Spencer, Sun, Tatham, Tatham, Tatham, Tatham, Vyas, Wenzel, Yin, Yin, Zhang   +64 more
core   +3 more sources

Homo-PROTACs:bivalent small-molecule dimerizers of the VHL E3 ubiquitin ligase to induce self-degradation [PDF]

, 2017
E3 ubiquitin ligases are key enzymes within the ubiquitin proteasome system which catalyze the ubiquitination of proteins, targeting them for proteasomal degradation.
A Grosfeld, A Hergovich, A Rapisarda, A Schoenfeld, AC Lai, AC Lai, AR Schoenfeld, B Vu, C Galdeano, C Galdeano, C Loenarz, CE Stebbins, CH Arrowsmith, CM Pickart, CM Robinson, D Komander, DC Swinney, DE Feldman, DL Buckley, DL Buckley, DM Spencer, DP Bondeson, E Bulatov, EF Douglass, EK Schrader, ES Fischer, ET Mack, FE Morreale, G Chessari, G Lu, G Minervini, G Nalepa, G Petzold, GE Winter, H Lebraud, H Sun, I Molle Van, IJ Frew, J Frost, J Krönke, J Lu, JR Skaar, K Raina, L Gossage, LT Vassilev, M Li, M Tanaka, M Toure, M Zengerle, MD Petroski, ME Matyskiela, MR Arkin, MS Gadd, N Ohoka, N Zheng, PH Maxwell, RE Barry, T Han, T Ito, T Kamura, T Uehara, TA Soucy, TB Durham, TG Davies, TK Oost, TW Corson, V Bangiyeva, V Wittmann, WG Kaelin, X Huang, X Lucas, X Tan, Y Itoh, Z-Y Jiang   +73 more
core   +3 more sources

E3 Ubiquitin Ligases: Potential Therapeutic Targets for Skeletal Pathology and Degeneration

Stem Cells International, 2022
The ubiquitination-proteasome system (UPS) is crucial in regulating a variety of cellular processes including proliferation, differentiation, and survival. Ubiquitin protein ligase E3 is the most critical molecule in the UPS system.
Ruiyin Zeng, Yuan Xiong, Ze Lin, Adriana C. Panayi, Yun Sun, Faqi Cao, Guohui Liu   +6 more
doaj   +1 more source