Results 41 to 50 of about 77,505 (293)

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.
Hay, Ronald T, Rojas-Fernandez, Alejandro, Hattersley, Neil, Plechanovová, Anna, Tatham, Michael H, Jaffray, Ellis   +5 more
core   +1 more source

Classification of barley U-box E3 ligases and their expression patterns in response to drought and pathogen stresses

BMC Genomics, 2019
Background Controlled turnover of proteins as mediated by the ubiquitin proteasome system (UPS) is an important element in plant defense against environmental and pathogen stresses.
Moon Young Ryu, Seok Keun Cho, Yourae Hong, Jinho Kim, Jong Hum Kim, Gu Min Kim, Yan-Jun Chen, Eva Knoch, Birger Lindberg Møller, Woo Taek Kim, Michael Foged Lyngkjær, Seong Wook Yang   +11 more
doaj   +1 more source

Functional analysis of proteasome-associated ubiquitin ligases in plants [PDF]

, 2022
Degradation of intracellular proteins by the ubiquitin-proteasome system (UPS) is a sophisticated mechanism that begins with anchoring ubiquitin molecules to a substrate and ends with proteasome-dependent proteolysis.
Wang, Zhishuo
core   +1 more source

Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases.

, 2013
Cullin-RING ligases are multisubunit E3 ubiquitin ligases that recruit substrate-specific adaptors to catalyze protein ubiquitylation. Cul3-based Cullin-RING ligases are uniquely associated with BTB adaptors that incorporate homodimerization, Cul3 ...
Bullock, AN, Canning, P, Marsden, BD, Gileadi, Opher, Gileadi, O, Krojer, Tobias, Pike, AC, von Delft, F, Hojzan, V, Thangaratnarajah, C, Murray, James W., Cooper, CD, Keates, Tracy, Thangaratnarajah, Chancievan, Bullock, Alex N., Knapp, Stefan, Marsden, Brian D., Knapp, S, Hojzan, Viktorija, Murray, JW, von Delft, Frank, Chaikuad, A, Keates, T, Ayinampudi, Vikram, Ayinampudi, V, Pike, Ashley C.W., Chaikuad, Apirat, Krojer, T, Canning, Peter, Cooper, Christopher D.O., Bullock, Alexander   +30 more
core   +1 more source

NAD+-dependent DNA ligases of Mycobacterium tuberculosis and Streptomyces coelicolor

, 2003
Sequencing of the genomes of Mycobacterium tuberculosis H37Rv and Streptomyces coelicolor A3(2) identified putative genes for an NAD+-dependent DNA ligase. We have cloned both open reading frames and overexpressed the protein products in Escherichia coli.
Bullard, Desmond, Smith, Andrew, Kieser, Tobias, Day, Jonathan, Sayer, Heather, Bowater, Richard, Wilkinson, Adam   +6 more
core   +1 more source

The role of NEDD4 related HECT-type E3 ubiquitin ligases in defective autophagy in cancer cells: molecular mechanisms and therapeutic perspectives

Molecular Medicine, 2023
The homologous to the E6-AP carboxyl terminus (HECT)-type E3 ubiquitin ligases are the selective executers in the protein ubiquitination, playing a vital role in modulation of the protein function and stability. Evidence shows the regulatory role of HECT-
Rui Zhang, Shaoqing Shi
doaj   +1 more source

The molecular basis of CRL4 ubiquitin ligase architecture, targeting and regulation [PDF]

, 2013
Members of the CUL4-RBX1-DDB1 (CRL4) E3 ubiquitin ligase family regulate multiple cellular processes including development, transcription, and DNA repair.
Fischer, Eric Sebastian
core   +1 more source

HECT ubiquitin ligases as accessory proteins of the plant proteasome [PDF]

, 2022
The proteasome plays vital roles in eukaryotic cells by orchestrating the regulated degradation of large repertoires of substrates involved in numerous biological processes.
Wang, Zhishuo, Spoel, Steven H, Spoel, Steven H.   +2 more
core   +1 more source

New classes of E3 ligases illuminated by chemical probes

, 2022
Specificity in the ubiquitin system depends on E3 ligases, largely belonging to a handful of families discovered more than a decade ago. However, the last two years brought a quantum leap in the identification and/or mechanistic characterization of ...
Horn-Ghetko, D., Schulman, B.
core   +1 more source

The enigma of the RING-UIM E3 ligases: its transformative impact on cancer research

Journal of Translational Medicine
RING-UIM E3 ligases, a subfamily within the RING-type E3 ligases, comprise four members: RNF114, RNF125, RNF138, and RNF166. These ligases are crucial in various biological processes, including immunity, inflammation, epigenetics, and homologous ...
Ye Wang, Yue Zhao, Qi Xin, Jihong Zhang
doaj   +1 more source