Results 31 to 40 of about 105,668 (286)
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 +5 more
core +1 more source
Progress on Poxvirus E3 Ubiquitin Ligases and Adaptor Proteins
Frontiers in Immunology, 2021 Poxviruses have evolved a variety of innate immunity evasion mechanisms, some of which involve poxvirus-encoded E3 ubiquitin ligases and adaptor proteins.
Haoran Cui +7 more
doaj +1 more source
Structure of the Human FANCL RING-Ube2T Complex Reveals Determinants of Cognate E3-E2 Selection [PDF]
, 2014 The combination of an E2 ubiquitin-conjugating enzyme with an E3 ubiquitin-ligase is essential for ubiquitin modification of a substrate. Moreover, the pairing dictates both the substrate choice and the modification type. The molecular details of generic
Miles, Jennifer Anne +3 more
core +1 more source
Scientific Reports, 2021 The sarcomere protein titin is a major determinant of cardiomyocyte stiffness and ventricular distensibility. The constant mechanical stress on titin requires well-controlled protein quality control, the exact mechanisms of which have not yet been fully ...
Erik Müller +5 more
doaj +1 more source
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
Mainak Guharoy +15 more
core +1 more source
IAPs as E3 ligases of Rac1 [PDF]
Small GTPases, 2012 Inhibitors of Apoptosis Proteins (IAPs) are well-studied E3 ubiquitin ligases predominantly known for regulation of apoptosis. We uncovered that IAPs can function as a direct E3 ubiquitin ligase of RhoGTPase Rac1. cIAP1 and XIAP directly conjugate polyubiquitin chains to Lysine 147 of activated Rac1 and target it for proteasomal degradation ...
Oberoi-Khanuja, Tripat Kaur +1 more
openaire +3 more sources
The Role of E3 Ligase Pirh2 in Disease
Cells, 2022 The p53-dependent ubiquitin ligase Pirh2 regulates a number of proteins involved in different cancer-associated processes. Targeting the p53 family proteins, Chk2, p27Kip1, Twist1 and others, Pirh2 participates in such cellular processes as proliferation, cell cycle regulation, apoptosis and cellular migration.
Alexandra Daks +5 more
openaire +3 more sources
Cereblon versus VHL: Hijacking E3 Ligases Against Each Other Using PROTACs [PDF]
, 2019 The von Hippel-Lindau (VHL) and cereblon (CRBN) proteins are substrate recognition subunits of two ubiquitously expressed and biologically important Cullin RING E3 ubiquitin ligase complexes.
Chiara, Maniaci +4 more
core +1 more source
New classes of E3 ligases illuminated by chemical probes [PDF]
, 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
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