Disordered Substrates of the 20S Proteasome Link Degradation with Phase Separation
Sign Up to like & getrecommendations! Published in 2018 at "PROTEOMICS"
DOI: 10.1002/pmic.201800276
Abstract: The 20S proteasome is known to degrade intrinsically disordered proteins (IDPs) via an ubiquitin‐independent, disorder‐driven mechanism. Unless protected within protein complexes or macromolecular assemblies, certain IDPs can undergo degradation mediated directly by the 20S core… read more here.
Keywords: degradation; phase; substrates 20s; 20s proteasome ... See more keywords
Structural and Functional Evidence for Citicoline Binding and Modulation of 20S Proteasome Activity: Novel Insights into its Pro-Proteostatic Effect.
Sign Up to like & getrecommendations! Published in 2020 at "Biochemical pharmacology"
DOI: 10.1016/j.bcp.2020.113977
Abstract: Citicoline or CDP-choline is a drug, made up by a cytidine 5'-diphosphate moiety and choline, which upon adsorption is rapidly hydrolyzed into cytidine 5'-diphosphate and choline, easily bypassing the blood-brain barrier. Once in the brain,… read more here.
Keywords: citicoline; functional evidence; structural functional; 20s proteasome ... See more keywords
Proteasome activity regulated by charged gold nanoclusters: Implications for neurodegenerative diseases
Sign Up to like & getrecommendations! Published in 2020 at "Nano Today"
DOI: 10.1016/j.nantod.2020.100933
Abstract: Abstract The 20S proteasome, the catalytic core particle of 26S proteasome, degrades a wide range of intracellular proteins, which is essential for many cellular processes. Herein, we have found that the 20S proteasome activity is… read more here.
Keywords: 20s proteasome; gold nanoclusters; proteasome activity; neurodegenerative diseases ... See more keywords
Design, Synthesis, and Biological Evaluation of Potent 20S Proteasome Activators for the Potential Treatment of α-Synucleinopathies.
Sign Up to like & getrecommendations! Published in 2022 at "Journal of medicinal chemistry"
DOI: 10.1021/acs.jmedchem.1c02158
Abstract: While neurodegenerative diseases affect millions of patients worldwide, there are insufficient available therapeutics to halt or slow down the progression of these diseases. A key pathological feature of several neurodegenerative diseases is the oligomerization and… read more here.
Keywords: 20s proteasome; design synthesis; synthesis biological; biological evaluation ... See more keywords
Nature of Irreversible Inhibition of Human 20S Proteasome by Salinosporamide A. The Critical Role of Lys–Asp Dyad Revealed from Electrostatic Effects Analysis
Sign Up to like & getrecommendations! Published in 2021 at "ACS Catalysis"
DOI: 10.1021/acscatal.0c05313
Abstract: 20S proteasome is the enzymatic core engine involved in the processes of cellular protein regulation, thus becoming a promising target inter alia in the therapy of many diseases. In this work, the ... read more here.
Keywords: nature irreversible; proteasome salinosporamide; inhibition human; 20s proteasome ... See more keywords
Comparative Structural Analysis of 20S Proteasome Ortholog Protein Complexes by Native Mass Spectrometry
Sign Up to like & getrecommendations! Published in 2020 at "ACS Central Science"
DOI: 10.1021/acscentsci.0c00080
Abstract: Ortholog protein complexes are responsible for equivalent functions in different organisms. However, during evolution, each organism adapts to meet its physiological needs and the environmental challenges imposed by its niche. This selection pressure leads to… read more here.
Keywords: protein; native mass; ortholog protein; protein complexes ... See more keywords
Competitive Metabolite Profiling of Natural Products Reveals Subunit Specific Inhibitors of the 20S Proteasome
Sign Up to like & getrecommendations! Published in 2020 at "ACS Central Science"
DOI: 10.1021/acscentsci.9b01170
Abstract: We have developed a syringolin-based chemical probe and explored its utility for the profiling of metabolite extracts as potent inhibitors of the 20S proteasome. Activity-guided fractionation by competitive labeling allowed us to isolate and identify… read more here.
Keywords: natural products; inhibitors 20s; competitive metabolite; profiling natural ... See more keywords
Small Molecule Enhancement of 20S Proteasome Activity Targets Intrinsically Disordered Proteins.
Sign Up to like & getrecommendations! Published in 2017 at "ACS chemical biology"
DOI: 10.1021/acschembio.7b00489
Abstract: The 20S proteasome is the main protease for the degradation of oxidatively damaged and intrinsically disordered proteins. When accumulation of disordered or oxidatively damaged proteins exceeds proper clearance in neurons, imbalanced pathway signaling or aggregation… read more here.
Keywords: small molecule; proteasome activity; 20s proteasome; disordered proteins ... See more keywords
Fluspirilene Analogs Activate the 20S Proteasome and Overcome Proteasome Impairment by Intrinsically Disordered Protein Oligomers.
Sign Up to like & getrecommendations! Published in 2021 at "ACS chemical neuroscience"
DOI: 10.1021/acschemneuro.1c00099
Abstract: Oligomerization of aggregation-prone intrinsically disordered proteins (IDPs), such as α-synuclein, amyloid β, and tau, has been shown to be associated with the pathogenesis of several neurodegenerative diseases, including Parkinson's and Alzheimer's disease. The proteasome is… read more here.
Keywords: accumulation; proteasome; fluspirilene analogs; neurodegenerative diseases ... See more keywords
Allosteric coupling between α-rings of the 20S proteasome
Sign Up to like & getrecommendations! Published in 2020 at "Nature Communications"
DOI: 10.1038/s41467-020-18415-7
Abstract: Proteasomal machinery performs essential regulated protein degradation in eukaryotes. Classic proteasomes are symmetric, with a regulatory ATPase docked at each end of the cylindrical 20S. Asymmetric complexes are also present in cells, either with a… read more here.
Keywords: coupling rings; atpase; allosteric coupling; opposite ends ... See more keywords
Structural insights into the human PA28–20S proteasome enabled by efficient tagging and purification of endogenous proteins
Sign Up to like & getrecommendations! Published in 2022 at "Proceedings of the National Academy of Sciences of the United States of America"
DOI: 10.1073/pnas.2207200119
Abstract: Significance We report an approach of combining CRISPR-Cas9 gene editing with florescence cell sorting to tag and purify human endogenous protein complexes from HEK cells for structural studies by single-particle cryogenic electron microscopy. This procedure… read more here.
Keywords: 20s proteasome; human pa28; structural insights; insights human ... See more keywords