Results 71 to 80 of about 125,351 (338)
Parkin function in Parkinson's disease [PDF]
Parkinson's disease (PD) is the second most common neurodegenerative disease, and is characterized by involuntary shaking, muscle rigidity, and the progressive loss of dopaminergic neurons.
Arkinson, Connor, Walden, Helen
core +1 more source
PICALM::MLLT10 translocated leukemia
This comprehensive review of PICALM::MLLT10 translocated acute leukemia provides an in‐depth review of the structure and function of CALM, AF10, and the fusion oncoprotein (1). The multifaceted molecular mechanisms of oncogenesis, including nucleocytoplasmic shuttling (2), epigenetic modifications (3), and disruption of endocytosis (4), are then ...
John M. Cullen +7 more
wiley +1 more source
SCF-dependent proteolysis was first discovered via genetic screening of budding yeast almost 25 years ago. In recent years, more and more functions of SCF (Skp1-Cullin 1-F-box) ligases have been described, and we can expect the number of studies on this ...
Veronika Kinterová +3 more
doaj +1 more source
The Acidic Tail of the Cdc34 Ubiquitin-conjugating Enzyme Functions in Both Binding to and Catalysis with Ubiquitin Ligase SCFC^(dc4*) [PDF]
Ubiquitin ligases, together with their cognate ubiquitin-conjugating enzymes, are responsible for the ubiquitylation of proteins, a process that regulates a myriad of eukaryotic cellular functions. The first cullin-RING ligase discovered, yeast SCF^(Cdc4)
Bing Hao +48 more
core +3 more sources
At low cell density, SETDB1 and YAP1 accumulate in the nucleus. As cell density increases, the Hippo pathway is gradually activated, and SETDB1 is associated with increased YAP1 phosphorylation. At high cell density, phosphorylated YAP1 is sequestered in the cytoplasm, while SETDB1 becomes polyubiquitinated and degraded by the ubiquitin–proteasome ...
Jaemin Eom +3 more
wiley +1 more source
Bioinformatics analysis identifies several intrinsically disordered human E3 ubiquitin-protein ligases [PDF]
The ubiquitin-proteasome system targets misfolded proteins for degradation. Since the accumulation of such proteins is potentially harmful for the cell, their prompt removal is important.
Wouter Boomsma +4 more
doaj +2 more sources
Ubiquitination accomplished: E1 and E2 enzymes were not necessary [PDF]
Qiu et al. (2016) show that a mono-ADP-ribosyltransferase, SdeA, from Legionella pneumophila catalyzes ADP-ribosylation of ubiquitin, allowing SdeA to modify substrate with ubiquitin in the absence of E1 and E2 ...
Huang, Danny T., Nakasone, Mark
core +1 more source
β‐TrCP overexpression enhances cisplatin sensitivity by depleting BRCA1
Low levels of β‐TrCP (Panel A) allow the accumulation of BRCA1 and CtIP, which facilitate the repair of cisplatin‐induced DNA damage via homologous recombination (HR) and promote tumor cell survival. In contrast, high β‐TrCP expression (Panel B) leads to BRCA1 and CtIP degradation, impairing HR repair, resulting in persistent DNA damage and apoptosis ...
Rocío Jiménez‐Guerrero +8 more
wiley +1 more source
E3 Ubiquitin Ligases Neurobiological Mechanisms: Development to Degeneration
Cells regularly synthesize new proteins to replace old or damaged proteins. Deposition of various aberrant proteins in specific brain regions leads to neurodegeneration and aging.
Arun Upadhyay +6 more
doaj +1 more source
The proteasome lid triggers COP9 signalosome activity during the transition of Saccharomyces cerevisiae cells into quiescence. [PDF]
The class of Cullin–RING E3 ligases (CRLs) selectively ubiquitinate a large portion of proteins targeted for proteolysis by the 26S proteasome. Before degradation, ubiquitin molecules are removed from their conjugated proteins by deubiquitinating enzymes,
Bramasole, Lylan +8 more
core

