Results 21 to 30 of about 67,820 (304)

RBR E3 ubiquitin ligases: new structures, new insights, new questions [PDF]

, 2014
The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain enzymes.
Shaw, Gary S., Spratt, Donald E., Walden, Helen   +2 more
core   +1 more source

The roles of E3 ubiquitin ligases in cancer progression and targeted therapy

Clinical and Translational Medicine, 2023
Ubiquitination is one of the most important post‐translational modifications which plays a significant role in conserving the homeostasis of cellular proteins.
Chibuzo Sampson, Qiuping Wang, Wuxiyar Otkur, Haifeng Zhao, Yun Lu, Xiaolong Liu, Hai‐long Piao   +6 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

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
A Arrigoni, A Hershko, A Mohan, AE Deffenbaugh, B Bothner, B Hao, B Hess, C Guda, C Haynes, CJ Cox, CM Pickart, D Ekman, D Szklarczyk, D Van Der Spoel, D Vuzman, DM Duda, DM Duda, DW Leung, ES Zimmerman, ET Powers, F Bernassola, F Tama, F. Gisou van der Goot, FU Hartl, G Bussi, G Moncalian, G Swaminathan, G Wu, H Daub, H Dinkel, H Dou, H Shimizu, H Zhu, HC van Leeuwen, HE Niessen, HJ Dyson, HM Berman, I Szymkiewicz, I von Ossowski, J Liu, J Ma, J Prilusky, JC Rosenbaum, JH Fong, JM Huibregtse, K Peng, K Suhre, L Aravind, L Yang, LM Iakoucheva, M Christen, M Cormont, M Fuxreiter, M Fuxreiter, M Guharoy, M Hochstrasser, M Kanehisa, M Kanehisa, M Kanehisa, M Vidal, M Zhao, MA McCoy, Mainak Guharoy, MD Petroski, MD Petroski, ME Sowa, N Foray, N Mathias, N Zheng, P Tompa, P Tompa, P Tompa, P Tompa, P Tompa, Pallab Bhowmick, PE Ryan, PE Wright, Peter Tompa, PW Hildebrand, R Kiss, RG Smock, Rita Pancsa, RJ Deshaies, S Fishbain, S Vucetic, S Wiesner, SC Kales, SJ Demarest, SJ van Wijk, T Hagai, T Inobe, T Mittag, T Ravid, U Emekli, VN Uversky, W Humphrey, W Li, WY Mark, X Zhong, Y Haupt, Y Sheng, Y Xie, Z Dosztanyi, Z Dosztanyi, Z Dosztanyi   +104 more
core   +6 more sources

Structure of the HHARI catalytic domain shows glimpses of a HECT E3 ligase. [PDF]

PLoS ONE, 2013
The ubiquitin-signaling pathway utilizes E1 activating, E2 conjugating, and E3 ligase enzymes to sequentially transfer the small modifier protein ubiquitin to a substrate protein.
Donald E Spratt, Pascal Mercier, Gary S Shaw   +2 more
doaj   +1 more source

Targeted Degradation of 53BP1 Using Ubiquitin Variant Induced Proximity

Biomolecules, 2022
In recent years, researchers have leveraged the ubiquitin-proteasome system (UPS) to induce selective degradation of proteins by E3 ubiquitin ligases, which has great potential as novel therapeutics for human diseases, including cancer and ...
Bayonle Aminu, Julia Fux, Evan Mallette, Nathaniel Petersen, Wei Zhang   +4 more
doaj   +1 more source

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

E3 Ubiquitin Ligases as Cancer Targets and Biomarkers

Neoplasia: An International Journal for Oncology Research, 2006
E3 ubiquitin ligases are a large family of proteins that are engaged in the regulation of the turnover and activity of many target proteins. Together with ubiquitinactivating enzyme El and ubiquitin-conjugating enzyme E2, E3 ubiquitin ligases catalyze ...
Yi Sun
doaj   +1 more source

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

Viral hijacking of cellular ubiquitination pathways as an anti-innate immunity strategy. [PDF]

, 2006
International audienceViruses are obligate parasites of host cells. Virus-host coevolution has selected virus for growth despite antiviral defenses set up by hosting cells and organisms. Ubiquitin conjugation onto proteins, through a cascade of reactions
Chen, Mingzhou, Gerlier, Denis
core   +3 more sources