Results 41 to 50 of about 376,415 (308)
Keeping Cell Death in Check: Ubiquitylation-Dependent Control of TNFR1 and TLR Signaling
Frontiers in Cell and Developmental Biology, 2019 Pro-inflammatory signaling pathways, induced by pathogens, tissue damage or cytokines, depend on the ubiquitylation of various subunits of receptor signaling complexes, controlled by ubiquitin ligases and deubiquitinases.
Laura Griewahn +6 more
doaj +1 more source
Control of mitochondrial biogenesis and function by the ubiquitin–proteasome system [PDF]
Open Biology, 2017 Mitochondria are pivotal organelles in eukaryotic cells. The complex proteome of mitochondria comprises proteins that are encoded by nuclear and mitochondrial genomes. The biogenesis of mitochondrial proteins requires their transport in an unfolded state
Piotr Bragoszewski +2 more
doaj +1 more source
More Than Just Cleaning: Ubiquitin-Mediated Proteolysis in Fungal Pathogenesis
Frontiers in Cellular and Infection Microbiology, 2021 Ubiquitin-proteasome mediated protein turnover is an important regulatory mechanism of cellular function in eukaryotes. Extensive studies have linked the ubiquitin-proteasome system (UPS) to human diseases, and an array of proteasome inhibitors have been
Chengjun Cao +3 more
doaj +1 more source
Structural and biochemical analyses of monoubiquitinated human histones H2B and H4 [PDF]
Open Biology, 2016 Monoubiquitination is a major histone post-translational modification. In humans, the histone H2B K120 and histone H4 K31 residues are monoubiquitinated and may form transcriptionally active chromatin.
Shinichi Machida +4 more
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
Ubiquitin-dependent and -independent proteasomal protein degradation.
, 2023 A. UPS protein degradation resulting from (1) ubiquitin system targeting followed by (2) proteasomal protein degradation. B. Proteins with ubiquitin-independent degrons are directly bound and degraded by the proteasome without ubiquitin system targeting.
Frank W. Albert (7879037) +2 more
core +1 more source
Cells, 2019 The ubiquitin proteasome system (UPS) plays an important role in regulating numerous cellular processes, and a dysfunctional UPS is thought to contribute to motor neuron disease.
Monique Bax +12 more
doaj +1 more source
Resolving the Complexity of Ubiquitin Networks
Frontiers in Molecular Biosciences, 2020 Ubiquitination regulates nearly all cellular processes by coordinated activity of ubiquitin writers (E1, E2, and E3 enzymes), erasers (deubiquitinating enzymes) and readers (proteins that recognize ubiquitinated proteins by their ubiquitin-binding ...
Katarzyna Kliza, Koraljka Husnjak
doaj +1 more source
, 2011 In this chapter, we describe a method for detecting the ubiquitination status of G protein-coupled receptors (GPCRs). This involves co-expression of a GPCR with an epitope-tagged ubiquitin construct in a -heterologous mammalian expression system. Stimulus-dependent modification of the GPCR by -ubiquitin is detected by immunoprecipitation and subsequent
Adriana, Caballero, Adriano, Marchese
openaire +2 more sources
Ubiquitin-proteasome dependent mitochondrial protein quality control [PDF]
, 2014 Dysfunctional mitochondria cause many neurodegenerative disorders and with aging in general, mechanisms of mitochondrial quality control are essential for cellular function.
Benischke, Anne-Sophie
core +1 more source