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Dependence of Proteasome Processing Rate on Substrate Unfolding
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Structural Models for Interactions between the 20S Proteasome and Its PAN/19S Activators
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The C Terminus of Rpt3, an ATPase Subunit of PA700 (19 S) Regulatory Complex, Is Essential for 26 S Proteasome Assembly but Not for Activation
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Foot-and-Mouth Disease Virus 2C Is a Hexameric AAA plus Protein with a Coordinated ATP Hydrolysis Mechanism
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ATP-Dependent Steps in the Binding of Ubiquitin Conjugates to the 26S Proteasome that Commit to Degradation
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Getting to First Base in Proteasome Assembly
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Subcomplexes of PA700, the 19 S Regulator of the 26 S Proteasome, Reveal Relative Roles of AAA Subunits in 26 S Proteasome Assembly and Activation and ATPase Activity
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The 20S Proteasome as an Assembly Platform for the 19S Regulatory Complex
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Chaperone-mediated pathway of proteasome regulatory particle assembly
Jeroen Roelofs et al.
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Hexameric assembly of the proteasomal ATPases is templated through their C termini
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Polyubiquitin substrates allosterically activate their own degradation by the 26S proteasome
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Sequence analysis of the AAA protein family
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Differential Roles of the COOH Termini of AAA Subunits of PA700 (19 S Regulator) in Asymmetric Assembly and Activation of the 26 S Proteasome
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Relative structural and functional roles of multiple deubiquitylating proteins associated with mammalian 26S proteasome
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Proteasomes and their associated ATPases: A destructive combination
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ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins
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Rebuilt AAA plus motors reveal operating principles for ATP-fuelled machines
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Molecular machines for protein degradation
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Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome
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A cryptic protease couples deubiquitination and degradation by the proteasome
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Proteasome subunit Rpn1 binds ubiquitin-like protein domains
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Rad23 promotes the targeting of proteolytic substrates to the proteasome
L Chen et al.
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The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release
A Köhler et al.
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ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
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A gated channel into the proteasome core particle
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