Cellular quality control by the ubiquitin-proteasome system and autophagy
Science, 2019 To achieve homeostasis, cells evolved dynamic and self-regulating quality control processes to adapt to new environmental conditions and to prevent prolonged damage.
C. Pohl, I. Dikič
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Poxvirus Exploitation of the Ubiquitin-Proteasome System
Viruses, 2010 Ubiquitination plays a critical role in many cellular processes. A growing number of viruses have evolved strategies to exploit the ubiquitin-proteasome system, including members of the Poxviridae family. Members of the poxvirus family have recently been
Alastair Teale +5 more
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Ubiquitination in Plant Meiosis: Recent Advances and High Throughput Methods
Frontiers in Plant Science, 2021 Meiosis is a specialized cell division which is essential to sexual reproduction. The success of this highly ordered process involves the timely activation, interaction, movement, and removal of many proteins. Ubiquitination is an extraordinarily diverse
Jamie N. Orr +4 more
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A quantitative assay to monitor HSV-1 ICP0 ubiquitin ligase activity in vitro [PDF]
, 2015 The ubiquitin–proteasome system is an essential cellular process that plays a fundamental role in the regulation of protein stability. This pathway is tightly controlled by a sequential cascade of enzymatic steps that culminates in the formation of a ...
Boutell, Chris, Davido, David J.
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NEDD8 nucleates a multivalent cullin-RING-UBE2D ubiquitin ligation assembly
Nature, 2020 Eukaryotic cell biology depends on cullin–RING E3 ligase (CRL)-catalysed protein ubiquitylation 1 , which is tightly controlled by the modification of cullin with the ubiquitin-like protein NEDD8 2 – 6 . However, how CRLs catalyse ubiquitylation, and the
Kheewoong Baek +8 more
semanticscholar +1 more source
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
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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
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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
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Site-specific identification and quantitation of endogenous SUMO modifications under native conditions. [PDF]
, 2017 Small ubiquitin-like modifier (SUMO) modification regulates numerous cellular processes. Unlike ubiquitin, detection of endogenous SUMOylated proteins is limited by the lack of naturally occurring protease sites in the C-terminal tail of SUMO proteins ...
Ahmad, Alla S +8 more
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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
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