Results 41 to 50 of about 197,780 (305)

The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells [PDF]

, 2019
The linear ubiquitin assembly complex (LUBAC) comprises 3 components: HOIP, HOIL-1, and Sharpin, of which HOIP and HOIL-1 are both members of the RBR subfamily of E3 ubiquitin ligases. HOIP catalyses the formation of Met1-linked ubiquitin oligomers (also
Axel Knebel, Cohen, Ian R. Kelsall, J. Simon C. Arthur, Jiazhen Zhang, Philip Cohen, Thorne, Wang   +7 more
core   +2 more sources

Genome-Wide Identification of the U-Box E3 Ubiquitin Ligase Gene Family in Cabbage (Brassica oleracea var. capitata) and Its Expression Analysis in Response to Cold Stress and Pathogen Infection

Plants, 2023
Plant U-box E3 ubiquitin ligases (PUBs) play an important role in growth, development, and stress responses in many species. However, the characteristics of U-box E3 ubiquitin ligase genes in cabbage (Brassica oleracea var.
Peiwen Wang, Lin Zhu, Ziheng Li, Mozhen Cheng, Xiuling Chen, Aoxue Wang, Chao Wang, Xiaoxuan Zhang   +7 more
doaj   +1 more source

Trim17, novel E3 ubiquitin-ligase, initiates neuronal apoptosis [PDF]

, 2010
Accumulating data indicate that the ubiquitin-proteasome system controls apoptosis by regulating the level and the function of key regulatory proteins. In this study, we identified Trim17, a member of the TRIM/RBCC protein family, as one of the critical ...
A Bobba, A Brunet, A Lipkin, A Reymond, AP Aalto, B Pettmann, CM Knudson, CM Pickart, DA Cross, DA Cross, DA Linseman, DP Martin, E Towers, F Jaudon, G Lutfalla, G Meroni, GV Putcha, I Lassot, I Robbins, J Gilley, J Ham, J Ham, J Whitfield, J Yuan, JX Comella, KA Wood, L Swainson, L Vanhille, M Broemer, M Kristiansen, M M Magiera, M Sardiello, MH Glickman, N Canu, R Bhat, R Rahmeh, R Sadoul, RJ Youle, S Desagher, S Desagher, S Mora, S Ogawa, SJ Riedl, SJ Thompson, SR D'Mello, SR Datta, T Urano, TM Miller, TM Miller, V Arce, V Hongisto, Y Du, Z Xia   +52 more
core   +5 more sources

Surface probing by fragment-based screening and computational methods identifies ligandable pockets on the von Hippel-Lindau (VHL) E3 ubiquitin ligase [PDF]

, 2018
Beyond the targeting of E3 ubiquitin ligases to inhibit protein homeostasis, E3 ligase binders can be repurposed as targeted protein degraders (PROTACs or molecular glues).
Ciulli, Alessio, Lucas, Xavier, van Molle, Inge   +2 more
core   +4 more sources

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

Ubiquitin E3 ligase activity of Ralstonia solanacearum effector RipAW is not essential for induction of plant defense in Nicotiana benthamiana

Frontiers in Microbiology, 2023
As one of the most destructive bacterial phytopathogens, Ralstonia solanacearum causes substantial annual yield losses of many important crops. Deciphering the functional mechanisms of type III effectors, the crucial factors mediating R.
Xue Ouyang, Jialan Chen, Zhimao Sun, Rongbo Wang, Xuan Wu, Benjin Li, Congfeng Song, Peiqing Liu, Meixiang Zhang   +8 more
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

Regulating the human HECT E3 ligases [PDF]

Cellular and Molecular Life Sciences, 2018
Ubiquitination, the covalent attachment of ubiquitin to proteins, by E3 ligases of the HECT (homologous to E6AP C terminus) family is critical in controlling diverse physiological pathways. Stringent control of HECT E3 ligase activity and substrate specificity is essential for cellular health, whereas deregulation of HECT E3s plays a prominent role in ...
Sluimer, Jasper, Distel, Ben
openaire   +4 more sources

A pathogen type III effector with a novel E3 ubiquitin ligase architecture.

PLoS Pathogens, 2013
Type III effectors are virulence factors of Gram-negative bacterial pathogens delivered directly into host cells by the type III secretion nanomachine where they manipulate host cell processes such as the innate immunity and gene expression.
Alexander U Singer, Sebastian Schulze, Tatiana Skarina, Xiaohui Xu, Hong Cui, Lennart Eschen-Lippold, Monique Egler, Tharan Srikumar, Brian Raught, Justin Lee, Dierk Scheel, Alexei Savchenko, Ulla Bonas   +12 more
doaj   +1 more source

Structural basis of high-order oligomerization of the cullin-3 adaptor SPOP. [PDF]

, 2013
Protein ubiquitination in eukaryotic cells is mediated by diverse E3 ligase enzymes that each target specific substrates. The cullin E3 ligase complexes are the most abundant class of E3 ligases; they contain various cullin components that serve as ...
Barbieri, Canning, Chen, Choo, Christopher M. Harrison, Cohen, Emsley, Errington, Espinás, Evans, Gareth O. Rosbrook, Helen J. Close, Kabsch, Kim, Kitagawa, Komander, Krissinel, Kwon, Laura K. van Geersdaele, Li, Li, Liu, Maiti, Mark A. Stead, McCoy, McNicholas, Murshudov, Nagai, Nalepa, Ogura, Pintard, Schneider, Sheldrick, Simon D. Connell, Stephanie C. Wright, Stephen B. Carr, Stogios, Stogios, Takahashi, Winter, Zhang, Zhang, Zheng, Zhuang, Zimmerman   +44 more
core   +1 more source