Results 51 to 60 of about 72,591 (191)
Frontiers in Cell and Developmental BiologyE3 ubiquitin ligases are key determinants of substrate specificity within the ubiquitin–proteasome system and have emerged as important regulators of skeletal biology.
Yutong Zhao +4 more
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Dynamic control of selectivity in the ubiquitination pathway revealed by an ASP to GLU substitution in an intra-molecular salt-bridge network [PDF]
, 2012 Ubiquitination relies on a subtle balance between selectivity and promiscuity achieved through specific interactions between ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s).
Bonvin, Alexandre M. J. J. +4 more
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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. +1 more
openaire +3 more sources
A screen for E3 ubiquitination ligases that genetically interact with the adaptor protein Cindr during Drosophila eye patterning. [PDF]
PLoS ONE, 2017 Ubiquitination is a crucial post-translational modification that can target proteins for degradation. The E3 ubiquitin ligases are responsible for recognizing substrate proteins for ubiquitination, hence providing specificity to the process of protein ...
Kwami F Ketosugbo +2 more
doaj +1 more source
SCF E3 Ligase Substrates Switch from CAN-D to Can-ubiquitylate
, 2018 Liu et al. (2018) report a mathematical model predicting how the cellular repertoire of SCF E3 ligases is assembled by “adaptive exchange on demand,” with the limited pool of CUL1 scanning the vast sea of F-box proteins for those with substrates ...
Schulman, B., Scott, D.
core +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 +31 more
core +2 more sources
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
A Bacterial Platform for Studying Ubiquitination Cascades Anchored by SCF-Type E3 Ubiquitin Ligases
BiomoleculesUbiquitination is one of the most important post-translational modifications in eukaryotes. The ubiquitination cascade includes ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). The E3 ligases, responsible
Zuo-Xian Pu +9 more
doaj +1 more source
HECT E3 Ligases: A Tale With Multiple Facets [PDF]
Frontiers in Physiology, 2019 Ubiquitination plays a pivotal role in several cellular processes and is critical for protein degradation and signaling. E3 ubiquitin ligases are the matchmakers in the ubiquitination cascade, responsible for substrate recognition. In order to achieve selectivity and specificity on their substrates, HECT E3 enzymes are tightly regulated and exert their
Janine Weber +3 more
openaire +4 more sources
Frontiers in Molecular BiosciencesThe Ubiquitin-Proteasome System (UPS) is a key mechanism of cellular homeostasis. A central part of this mechanism is E3 ubiquitin ligases, which selectively direct proteins to be ubiquitinated for degradation via the UPS.
Srineevas Sriram +2 more
doaj +1 more source