Results 11 to 20 of about 27,758 (248)
Reversible phosphorylation of the 26S proteasome [PDF]
Protein & Cell, 2017 The 26S proteasome at the center of the ubiquitin-proteasome system (UPS) is essential for virtually all cellular processes of eukaryotes. A common misconception about the proteasome is that, once made, it remains as a static and uniform complex with ...
Xing Guo, Xiuliang Huang, Mark J. Chen
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Proteasome in action: substrate degradation by the 26S proteasome. [PDF]
Biochem Soc Trans, 2021 Ubiquitination is the major criteria for the recognition of a substrate-protein by the 26S proteasome. Additionally, a disordered segment on the substrate — either intrinsic or induced — is critical for proteasome engagement. The proteasome is geared to interact with both of these substrate features and prepare it for degradation.
Sahu I, Glickman MH.
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The 26S Proteasome and Initiation of Gene Transcription [PDF]
Biomolecules, 2014 Transcription activation is the foremost step of gene expression and is modulated by various factors that act in synergy. Misregulation of this process and its associated factors has severe effects and hence requires strong regulatory control.
Geetha Durairaj, Peter Kaiser
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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
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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
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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
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The Hunt for Degrons of the 26S Proteasome [PDF]
Biomolecules, 2019 Since the discovery of ubiquitin conjugation as a cellular mechanism that triggers proteasomal degradation, the mode of substrate recognition by the ubiquitin-ligation system has been the holy grail of research in the field. This entails the discovery of recognition determinants within protein substrates, which are part of a degron, and explicit E3 ...
Hadar Ella, Yuval Reiss, Tommer Ravid
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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
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Mechanisms of substrate recognition by the 26S proteasome. [PDF]
Curr Opin Struct Biol, 2021 The majority of regulated protein degradation in eukaryotes is accomplished by the 26S proteasome, the large proteolytic complex responsible for removing regulatory proteins and damaged proteins. Proteins are targeted to the proteasome by ubiquitination, and degradation is initiated at a disordered region within the protein.
Davis C, Spaller BL, Matouschek A.
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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
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