Results 11 to 20 of about 176,319 (351)

RNF12 X-Linked Intellectual Disability Mutations Disrupt E3 Ligase Activity and Neural Differentiation [PDF]

Cell Reports, 2018
Summary: X-linked intellectual disability (XLID) is a heterogeneous syndrome affecting mainly males. Human genetics has identified >100 XLID genes, although the molecular and developmental mechanisms underpinning this disorder remain unclear.
Francisco Bustos, Anna Segarra-Fas, Viduth K. Chaugule, Lennart Brandenburg, Emma Branigan, Rachel Toth, Thomas Macartney, Axel Knebel, Ronald T. Hay, Helen Walden, Greg M. Findlay   +10 more
doaj   +9 more sources

Structural basis for the RING catalyzed synthesis of K63 linked ubiquitin chains [PDF]

, 2015
This work was supported by grants from Cancer Research UK (C434/A13067), the Wellcome Trust (098391/Z/12/Z) and Biotechnology and Biological Sciences Research Council (BB/J016004/1).The RING E3 ligase catalysed formation of lysine 63 linked ubiquitin ...
A Plechanovová, A Plechanovová, A Rojas-Fernandez, AA Yunus, AJ McCoy, Anna Plechanovová, AP VanDemark, CE Berndsen, CE Berndsen, CM Guzzo, D Reverter, DC Scott, E Krissinel, Ellis G Jaffray, Emma Branigan, G Winter, GN Murshudov, H Dou, James H Naismith, JN Pruneda, L Chang, L Spyracopoulos, M Scheffner, M Zhang, MB Metzger, MD Winn, MH Tatham, MH Tatham, MJ Eddins, MJ Lewis, P Emsley, P Evans, PY Wu, R Vyas, RM Hofmann, Ronald T Hay, S McKenna, S McKenna, TF Moraes, VB Chen, W Kabsch, Y Galanty, Y Yin   +42 more
core   +11 more sources

Research progress of E3 ubiquitin ligase regulating biological behavior of human placental trophoblast cells

Frontiers in Endocrinology, 2023
E3 ubiquitin ligases are important components of the ubiquitin protease system. This family includes many proteins, which can catalyze the ubiquitination of a variety of protein substrates and promote the degradation of them by the proteasome system ...
Jun Feng, Huimei Yin, Baturuhu, Yonghui Dai, Fuxiao Dai, Junjun Xu, Zhili Chen, Yanyan Liu   +7 more
doaj   +1 more source

Structural studies of the coiled-coil domain of TRIM75 reveal a tetramer architecture facilitating its E3 ligase complex

Computational and Structural Biotechnology Journal, 2022
Protein ubiquitination plays a vital role in controlling the degradation of intracellular proteins and in regulating cell signaling pathways. Functionally, E3 ubiquitin ligases control the transfer of ubiquitin to the target substrates. As a major family
Xiaohua Lou, Binbin Ma, Yuan Zhuang, Xiang Xiao, Laurie J. Minze, Junji Xing, Zhiqiang Zhang, Xian C. Li   +7 more
doaj   +1 more source

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

A Comprehensive Atlas of E3 Ubiquitin Ligase Mutations in Neurological Disorders

Frontiers in Genetics, 2018
Protein ubiquitination is a posttranslational modification that plays an integral part in mediating diverse cellular functions. The process of protein ubiquitination requires an enzymatic cascade that consists of a ubiquitin activating enzyme (E1 ...
Arlene J. George, Yarely C. Hoffiz, Antoinette J. Charles, Ying Zhu, Angela M. Mabb   +4 more
doaj   +1 more source

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

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

Inhibitors of ubiquitin E3 ligase as potential new antimalarial drug leads

BMC Pharmacology and Toxicology, 2017
Background Protein ubiquitylation is an important post-translational regulation, which has been shown to be necessary for life cycle progression and survival of Plasmodium falciparum.
Jagrati Jain, Surendra K. Jain, Larry A. Walker, Babu L. Tekwani   +3 more
doaj   +1 more source

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