Cryo-EM Structure of the Plant 26S Proteasome
Plant Communications, 2022 Targeted proteolysis is a hallmark of life. It is especially important in long-lived cells that can be found in higher eukaryotes, like plants. This task is mainly fulfilled by the ubiquitin–proteasome system.
Alexander Schleiffer +2 more
exaly +4 more sources
Degradation of Intrinsically Disordered Proteins by the NADH 26S Proteasome
Biomolecules, 2020 The 26S proteasome is the endpoint of the ubiquitin- and ATP-dependent degradation pathway. Over the years, ATP was regarded as completely essential for 26S proteasome function due to its role in ubiquitin-signaling, substrate unfolding and ensuring its ...
Peter Tsvetkov +3 more
doaj +2 more sources
Mitochondrial Regulation of the 26S Proteasome [PDF]
Cell Reports, 2020 Summary: The proteasome is the main proteolytic system for targeted protein degradation in the cell and is fine-tuned according to cellular needs.
Thomas Meul +23 more
doaj +2 more sources
FAT10 and NUB1L cooperate to activate the 26S proteasome
Life Science Alliance, 2023 26S proteasome activation is achieved by the collective binding of the ubiquitin-like modifier FAT10 and its interaction partner NUB1L, causing gate opening in a USP14-independent way.
Florian Brockmann +6 more
doaj +2 more sources
The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro but not in cellulo
Life Science Alliance, 2023 The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro, whereas FAT10 degradation depends on the 26S proteasome in cellulo, shown by impairing 26S function via Rpt2 knockdown.
Franziska Oliveri +4 more
doaj +1 more source
Regulation of the proteasome by AMPK in endothelial cells: the role of O-GlcNAc transferase (OGT). [PDF]
PLoS ONE, 2012 26S proteasome is a macromolecular multi-subunit complex responsible for recognizing, unfolding, and ultimately destroying proteins. It remains poorly understood how 26S proteasome activity is regulated.
Jian Xu +3 more
doaj +1 more source
Tyrosine nitration of PA700 links proteasome activation to endothelial dysfunction in mouse models with cardiovascular risk factors. [PDF]
PLoS ONE, 2012 Oxidative stress is believed to cause endothelial dysfunction, an early event and a hallmark in cardiovascular diseases (CVD) including hypertension, diabetes, and dyslipidemia.
Jian Xu +5 more
doaj +1 more source
PiZ mouse liver accumulates polyubiquitin conjugates that associate with catalytically active 26S proteasomes. [PDF]
PLoS ONE, 2014 Accumulation of aggregation-prone human alpha 1 antitrypsin mutant Z (AT-Z) protein in PiZ mouse liver stimulates features of liver injury typical of human alpha 1 antitrypsin type ZZ deficiency, an autosomal recessive genetic disorder.
Christopher J Haddock +7 more
doaj +1 more source
20S and 26S proteasome-binding proteins of the rabbit brain: A proteomic dataset
Data in Brief, 2021 Fractions of 26S and 20S proteasomes isolated from the rabbit brain by the method of salt fractionation (salt-induced precipitation) contain intrinsic proteasome proteins responsible for assembly of the core particle and regulatory particle of proteasome
Olga Buneeva +4 more
doaj +1 more source
PLoS ONE, 2014 The 26S proteasome plays a fundamental role in almost all eukaryotic cells, including vascular endothelial cells. However, it remains largely unknown how proteasome functionality is regulated in the vasculature.
Hongtao Liu +3 more
doaj +1 more source