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Keywords {🔍}

proteasome, doi, prp, gate, pubmed, google, scholar, disease, prion, ups, protein, opening, misfolded, proteins, βsheetrich, proteasomes, substrate, pmc, entry, inhibit, function, cellular, activity, diseases, proteolytic, diseaseassociated, particle, atpases, mechanism, article, neurodegenerative, pathogenesis, substrates, free, nature, oligomers, ubiquitin, dysfunction, impairment, cells, cell, mice, aggregates, nlm, system, degradation, activators, model, neurodegeneration, core,

Topics {✒️}

toxic β-sheet-rich isoforms β-sheet-rich conformation demonstrate β-sheet-rich prp acts lysine-48-linked poly-ubiquitin chains aggregated β-sheet-rich prp β-sheet-rich prp impairs β-sheet-rich prp species β-sheet-rich prp binding cell-produced alpha-synuclein oligomers β-sheet-rich prp pmc beta search b-sheet-rich prp α3δn open-gated 20s accumulating amyloid β-protein normal host-encoded protein selective small-molecule inhibitor wild-type 20s proteasomes intracellular protein-degradation pathways 11s-activated 20s proteasomes α3-subunit n-terminus proteasome-11s activator complex short-lived regulatory proteins ctrpt5-activated 20s proteasomes proteasome-pan/pa700 interactions allowing free access eukaryotic proteasome-atpase interactions ubiquitin-proteasome proteolytic pathway ubiquitin-proteasome system impairment impairment remain unknown atp-dependent process α-ring intersubunit pockets publisher site pdf constitutively open gate underlying cellular events hollow cylindrical core wild-type proteasomes alpha-synuclein filaments 20s proteasome α-subunits stimulate gate opening prp amyloid fibrils small-molecule inhibitor 20s proteasome barrel impaired proteasome function gate-opening properties cellular prion protein misfolded prp impairs induce gate opening proteolytic active sites wild-type counterparts selectively degrade damaged

Questions {❓}

• Taken together, these observations raise an obvious question—how do disease-associated misfolded PrP conformers bind to and inhibit the 20S proteasome?

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