Results 41 to 50 of about 68,518 (300)

Genome-wide analysis of HECT E3 ubiquitin ligase gene family in Solanum lycopersicum

Scientific Reports, 2021
The E3 ubiquitin ligases have been known to intrigue many researchers to date, due to their heterogenicity and substrate mediation for ubiquitin transfer to the protein.
Bhaskar Sharma, Harshita Saxena, Harshita Negi   +2 more
doaj   +1 more source

The MALDI TOF E2/E3 ligase assay as universal tool for drug discovery in the ubiquitin pathway [PDF]

, 2017
In many diseases, components of the ubiquitin system - such as E2/E3 ligases and deubiquitylases - are dysregulated. The ubiquitin system has therefore become an emergent target for the treatment of a number of diseases, including cancer ...
Barlow, Victoria, De Cesare, Virginia, Hastie, Charles, Johnson, Clare, Knebel, Axel, Trost, Matthias   +5 more
core   +5 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

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 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

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

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

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

Activity-based E3 ligase profiling uncovers an E3 ligase with esterification activity [PDF]

, 2018
Ubiquitination is initiated by transfer of ubiquitin (Ub) from a ubiquitin-activating enzyme (E1) to a ubiquitin-conjugating enzyme (E2), producing a covalently linked intermediate (E2-Ub)(1). Ubiquitin ligases (E3s) of the 'really interesting new gene' (
A Borodovsky, A Hershko, A Plechanovová, AA Yunus, AF Alpi, Axel Knebel, B Grill, B Stieglitz, B Stieglitz, B Yang, BC Lechtenberg, Daan M. F. van Aalten, DM Wenzel, DS Hewings, E Babetto, G Langer, GN Murshudov, H Dou, HI Wan, J You, JE Brownell, JM Huibregtse, JN Pruneda, K Cadwell, Karim Rafie, Kay Hofmann, KC Pao, KK Dove, Kuan-Chuan Pao, L Conforti, M Scheffner, M Stanley, M Zhen, Mathew Stanley, MJ Niphakis, N Zheng, Nicola T. Wood, P Emsley, Peter D. Mabbitt, PY Wu, R Byrne, Ramasubramanian Sundaramoorthy, RJ Deshaies, S Milde, Satpal Virdee, SC Lovell, SK Olsen, X Wang, X Xiong, Y Shimizu, YO Ali   +50 more
core   +2 more sources

The structure and regulation of Cullin 2 based E3 ubiquitin ligases and their biological functions. [PDF]

, 2016
BACKGROUND: Cullin-RING E3 ubiquitin ligase complexes play a central role in targeting cellular proteins for ubiquitination-dependent protein turnover through 26S proteasome.
Cai, Weijia, Yang, Haifeng
core   +2 more sources