Results 21 to 30 of about 13,489 (251)
The 20S Proteasome of Streptomyces coelicolor [PDF]
Journal of Bacteriology, 1998 ABSTRACT 20S proteasomes were purified from Streptomyces coelicolor A3(2) and shown to be built from one α-type subunit (PrcA) and one β-type subunit (PrcB). The enzyme displayed chymotrypsin-like activity on synthetic substrates and was sensitive to peptide aldehyde and peptide vinyl sulfone inhibitors ...
Nagy, I. +4 more
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Mechanism of Gate Opening in the 20S Proteasome by the Proteasomal ATPases [PDF]
Molecular Cell, 2008 Substrates enter the cylindrical 20S proteasome through a gated channel that is regulated by the ATPases in the 19S regulatory particle in eukaryotes or the homologous PAN ATPase complex in archaea. These ATPases contain a conserved C-terminal hydrophobic-tyrosine-X (HbYX) motif that triggers gate opening upon ATP binding.
Rabl, Julius +5 more
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Inhibitory Effect of b-AP15 on the 20S Proteasome
Biomolecules, 2014 The 26S proteasome is a cellular proteolytic complex containing 19S regulatory particles and the 20S core proteasome. It was reported that the small molecule b-AP15 targets the proteasome by inhibiting deubiquitination of the 19S regulatory particles of
Li Huang, Katherine Jung, Chin Ho Chen
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Changes in proteasome structure and function caused by HAMLET in tumor cells. [PDF]
PLoS ONE, 2009 Proteasomes control the level of endogenous unfolded proteins by degrading them in the proteolytic core. Insufficient degradation due to altered protein structure or proteasome inhibition may trigger cell death.
Lotta Gustafsson +5 more
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Circulating 20S proteasome is independently associated with abdominal muscle mass in hemodialysis patients. [PDF]
PLoS ONE, 2015 Protein-energy wasting is highly prevalent in hemodialysis patients, and it contributes to patient morbidity and mortality. The ubiquitin-proteasome system is the major pathway for intracellular protein degradation and it is involved in the regulation of
Hirotaka Fukasawa +6 more
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Assembly of the 20S proteasome
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2014 The proteasome is a cellular protease responsible for the selective degradation of the majority of the intracellular proteome. It recognizes, unfolds, and cleaves proteins that are destined for removal, usually by prior attachment to polymers of ubiquitin. This macromolecular machine is composed of two subcomplexes, the 19S regulatory particle (RP) and
Kunjappu, Mary J., Hochstrasser, Mark
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Redox regulation of the proteasome via S-glutathionylation
Redox Biology, 2014 The proteasome is a multimeric and multicatalytic intracellular protease responsible for the degradation of proteins involved in cell cycle control, various signaling processes, antigen presentation, and control of protein synthesis.
Marilene Demasi +9 more
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Biomolecules, 2022 Carfilzomib is a last generation proteasome inhibitor (PI) with proven clinical efficacy in the treatment of relapsed/refractory multiple myeloma. This drug is considered to be extremely specific in inhibiting the chymotrypsin-like activity of the 20S ...
Grazia Raffaella Tundo +14 more
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PLoS ONE, 2020 IntroductionIn cancer treatment an attempt has been made to pharmacologically regulate the proteasome functions, thus the aim was to test whether 20S proteasome chymotrypsin-like (ChT-L) activity has a role in glial brain tumors. Furthermore, we analyzed
Olga Martyna Koper-Lenkiewicz +7 more
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Communications Biology, 2023 Considering the link between neurodegenerative diseases and impaired proteasome function, and the neuro-protective impact of enhanced proteasome activity in animal models, it’s crucial to understand proteasome activation mechanisms.
Janelle J. Y. Chuah +2 more
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